ID   REV3L_HUMAN             Reviewed;        3130 AA.
AC   O60673; O43214; Q5TC33;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   22-FEB-2023, entry version 193.
DE   RecName: Full=DNA polymerase zeta catalytic subunit;
DE            EC=2.7.7.7;
DE   AltName: Full=Protein reversionless 3-like;
DE            Short=REV3-like;
DE            Short=hREV3;
GN   Name=REV3L; Synonyms=POLZ, REV3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-1224.
RC   TISSUE=Fetal brain;
RX   PubMed=9618506; DOI=10.1073/pnas.95.12.6876;
RA   Gibbs P.E.M., McGregor W.G., Maher V.M., Nisson P., Lawrence C.W.;
RT   "A human homolog of the Saccharomyces cerevisiae REV3 gene, which encodes
RT   the catalytic subunit of DNA polymerase zeta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:6876-6880(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-1224.
RC   TISSUE=Bone marrow, and Leukocyte;
RX   PubMed=10102035; DOI=10.1016/s0921-8777(98)00065-2;
RA   Lin W., Wu X., Wang Z.;
RT   "A full-length cDNA of hREV3 is predicted to encode DNA polymerase zeta for
RT   damage-induced mutagenesis in humans.";
RL   Mutat. Res. 433:89-98(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-1224.
RA   Murakumo Y., Rasio D., Roth T., Negrini M., Croce C.M., Fishel R.;
RT   "Cloning and characterization of hREV3, the human homolog of S. cerevisiae
RT   REV3.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-231; CYS-1156;
RP   ILE-1224 AND GLU-1540.
RC   TISSUE=Testis;
RX   PubMed=9925914; DOI=10.1159/000015157;
RA   Morelli C., Mungall A.J., Negrini M., Barbanti-Brodano G., Croce C.M.;
RT   "Alternative splicing, genomic structure, and fine chromosome localization
RT   of REV3L.";
RL   Cytogenet. Cell Genet. 83:18-20(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-397; THR-693; GLN-962;
RP   CYS-1156; ILE-1224; THR-1302; HIS-1309; THR-1339; PRO-1469; LEU-1576;
RP   ASN-1713; THR-1724; SER-1791; HIS-1812; ARG-1923; HIS-1970; VAL-2015;
RP   MET-2075; GLN-2762 AND ILE-3064.
RG   NIEHS SNPs program;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 70-3130 (ISOFORM 1), VARIANTS HIS-231;
RP   CYS-1156; ILE-1224 AND GLU-1540, AND INTERACTION WITH MAD2L2.
RX   PubMed=10660610; DOI=10.1074/jbc.275.6.4391;
RA   Murakumo Y., Roth T., Ishii H., Rasio D., Numata S., Croce C.M., Fishel R.;
RT   "A human REV7 homolog that interacts with the polymerase zeta catalytic
RT   subunit hREV3 and the spindle assembly checkpoint protein hMAD2.";
RL   J. Biol. Chem. 275:4391-4397(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1030 AND THR-1041, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1724 AND SER-1967, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   FUNCTION, IDENTIFICATION IN POL-ZETA COMPLEX, AND MUTAGENESIS OF ASP-2614
RP   AND ASP-2783.
RX   PubMed=24449906; DOI=10.1073/pnas.1324001111;
RA   Lee Y.S., Gregory M.T., Yang W.;
RT   "Human Pol zeta purified with accessory subunits is active in translesion
RT   DNA synthesis and complements Pol eta in cisplatin bypass.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:2954-2959(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1847-1898 IN COMPLEX WITH MAD2L2.
RX   PubMed=20164194; DOI=10.1074/jbc.m109.092403;
RA   Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S.,
RA   Akashi S., Takeda S., Shimizu T., Sato M.;
RT   "Crystal structure of human REV7 in complex with a human REV3 fragment and
RT   structural implication of the interaction between DNA polymerase zeta and
RT   REV1.";
RL   J. Biol. Chem. 285:12299-12307(2010).
CC   -!- FUNCTION: Catalytic subunit of the DNA polymerase zeta complex, an
CC       error-prone polymerase specialized in translesion DNA synthesis (TLS).
CC       Lacks an intrinsic 3'-5' exonuclease activity and thus has no
CC       proofreading function. {ECO:0000269|PubMed:24449906}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P14284};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P14284};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.71 uM for dATP (for Pol-zeta2);
CC         KM=1.17 uM for dATP (for Pol-zeta4);
CC         Note=kcat is 0.31 min(-1) for DNA synthesis by Pol-zeta4. kcat is
CC         0.05 min(-1) for DNA synthesis by Pol-zeta2.
CC         {ECO:0000269|PubMed:24449906};
CC   -!- SUBUNIT: Heterodimer with MAD2L2. This dimer forms the minimal DNA
CC       polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA polymerase
CC       catalytic activity, although its activity is very low in this context.
CC       Component of the tetrameric Pol-zeta complex (Pol-zeta4), which
CC       consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the fully
CC       active form of DNA polymerase zeta. {ECO:0000269|PubMed:10660610,
CC       ECO:0000269|PubMed:20164194, ECO:0000269|PubMed:24449906}.
CC   -!- INTERACTION:
CC       O60673; Q9UI95: MAD2L2; NbExp=5; IntAct=EBI-2871302, EBI-77889;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60673-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60673-2; Sequence=VSP_024121;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DOMAIN: Its C-terminal part could serve as the catalytic domain during
CC       nucleotide polymerization, while its N-terminal part could provide
CC       sites for protein-protein interactions with other factors during
CC       translesion DNA synthesis.
CC   -!- DOMAIN: The CysB motif binds 1 4Fe-4S cluster and is required for the
CC       formation of polymerase complexes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/rev3l/";
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DR   EMBL; AF058701; AAC24357.1; -; mRNA.
DR   EMBL; AF071798; AAC24009.1; -; mRNA.
DR   EMBL; AF157476; AAD40184.1; -; mRNA.
DR   EMBL; AF179428; AAG09402.1; -; mRNA.
DR   EMBL; AF179429; AAG09403.1; -; mRNA.
DR   EMBL; AF078695; AAC28460.1; -; mRNA.
DR   EMBL; AY684169; AAT74627.1; -; Genomic_DNA.
DR   EMBL; AL080317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL136310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL512325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF035537; AAB88486.1; -; mRNA.
DR   CCDS; CCDS5091.2; -. [O60673-1]
DR   CCDS; CCDS69177.1; -. [O60673-2]
DR   RefSeq; NP_001273360.1; NM_001286431.1. [O60673-2]
DR   RefSeq; NP_001273361.1; NM_001286432.1. [O60673-2]
DR   RefSeq; NP_002903.3; NM_002912.4. [O60673-1]
DR   PDB; 3ABD; X-ray; 1.90 A; X/Y=1847-1898.
DR   PDB; 3ABE; X-ray; 2.60 A; Z=1847-1898.
DR   PDB; 3VU7; X-ray; 2.80 A; Z=1847-1898.
DR   PDB; 4EXT; X-ray; 1.90 A; B=1873-1895.
DR   PDB; 4GK0; X-ray; 2.70 A; C/D=1847-1898.
DR   PDB; 4GK5; X-ray; 3.21 A; C/D=1847-1898.
DR   PDB; 5O8K; X-ray; 1.80 A; B=1873-1898.
DR   PDB; 6BC8; X-ray; 1.68 A; B=1987-2014.
DR   PDB; 6BCD; X-ray; 1.43 A; B=1987-2014.
DR   PDB; 6BI7; X-ray; 2.80 A; B/D/F/H=1987-2014.
DR   PDB; 6EKM; X-ray; 2.76 A; B=1989-2014.
DR   PDB; 6KEA; X-ray; 2.35 A; A/B/C/D=1850-1872, A/B/C/D=1887-1894.
DR   PDB; 6WS0; X-ray; 2.24 A; ZZZ=1847-1898.
DR   PDB; 6WS5; X-ray; 2.47 A; ZZZ=1847-1898.
DR   PDBsum; 3ABD; -.
DR   PDBsum; 3ABE; -.
DR   PDBsum; 3VU7; -.
DR   PDBsum; 4EXT; -.
DR   PDBsum; 4GK0; -.
DR   PDBsum; 4GK5; -.
DR   PDBsum; 5O8K; -.
DR   PDBsum; 6BC8; -.
DR   PDBsum; 6BCD; -.
DR   PDBsum; 6BI7; -.
DR   PDBsum; 6EKM; -.
DR   PDBsum; 6KEA; -.
DR   PDBsum; 6WS0; -.
DR   PDBsum; 6WS5; -.
DR   SASBDB; O60673; -.
DR   SMR; O60673; -.
DR   BioGRID; 111912; 39.
DR   ComplexPortal; CPX-994; DNA polymerase zeta complex.
DR   CORUM; O60673; -.
DR   IntAct; O60673; 14.
DR   MINT; O60673; -.
DR   STRING; 9606.ENSP00000351697; -.
DR   GlyGen; O60673; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60673; -.
DR   PhosphoSitePlus; O60673; -.
DR   BioMuta; REV3L; -.
DR   CPTAC; CPTAC-3252; -.
DR   CPTAC; CPTAC-3253; -.
DR   CPTAC; CPTAC-944; -.
DR   EPD; O60673; -.
DR   jPOST; O60673; -.
DR   MassIVE; O60673; -.
DR   MaxQB; O60673; -.
DR   PaxDb; O60673; -.
DR   PeptideAtlas; O60673; -.
DR   ProteomicsDB; 49517; -. [O60673-1]
DR   ProteomicsDB; 49518; -. [O60673-2]
DR   Antibodypedia; 32376; 108 antibodies from 23 providers.
DR   DNASU; 5980; -.
DR   Ensembl; ENST00000358835.7; ENSP00000351697.3; ENSG00000009413.16. [O60673-1]
DR   Ensembl; ENST00000368802.8; ENSP00000357792.3; ENSG00000009413.16. [O60673-1]
DR   Ensembl; ENST00000435970.5; ENSP00000402003.1; ENSG00000009413.16. [O60673-2]
DR   GeneID; 5980; -.
DR   KEGG; hsa:5980; -.
DR   MANE-Select; ENST00000368802.8; ENSP00000357792.3; NM_001372078.1; NP_001359007.1.
DR   UCSC; uc003puy.6; human. [O60673-1]
DR   AGR; HGNC:9968; -.
DR   CTD; 5980; -.
DR   DisGeNET; 5980; -.
DR   GeneCards; REV3L; -.
DR   HGNC; HGNC:9968; REV3L.
DR   HPA; ENSG00000009413; Tissue enhanced (brain).
DR   MalaCards; REV3L; -.
DR   MIM; 602776; gene.
DR   neXtProt; NX_O60673; -.
DR   OpenTargets; ENSG00000009413; -.
DR   Orphanet; 570; Moebius syndrome.
DR   PharmGKB; PA34337; -.
DR   VEuPathDB; HostDB:ENSG00000009413; -.
DR   eggNOG; KOG0968; Eukaryota.
DR   GeneTree; ENSGT00940000156226; -.
DR   HOGENOM; CLU_000203_1_0_1; -.
DR   InParanoid; O60673; -.
DR   OMA; PVSSCEN; -.
DR   OrthoDB; 211439at2759; -.
DR   PhylomeDB; O60673; -.
DR   TreeFam; TF101072; -.
DR   PathwayCommons; O60673; -.
DR   Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR   Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR   Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR   SignaLink; O60673; -.
DR   BioGRID-ORCS; 5980; 475 hits in 1159 CRISPR screens.
DR   ChiTaRS; REV3L; human.
DR   EvolutionaryTrace; O60673; -.
DR   GeneWiki; REV3L; -.
DR   GenomeRNAi; 5980; -.
DR   Pharos; O60673; Tbio.
DR   PRO; PR:O60673; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; O60673; protein.
DR   Bgee; ENSG00000009413; Expressed in calcaneal tendon and 204 other tissues.
DR   ExpressionAtlas; O60673; baseline and differential.
DR   Genevisible; O60673; HS.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IDA:UniProtKB.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006261; P:DNA-templated DNA replication; TAS:ProtInc.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IDA:ComplexPortal.
DR   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   IDEAL; IID00259; -.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR032757; DUF4683.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
DR   Pfam; PF15735; DUF4683; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Alternative splicing; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Iron;
KW   Iron-sulfur; Metal-binding; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..3130
FT                   /note="DNA polymerase zeta catalytic subunit"
FT                   /id="PRO_0000046468"
FT   ZN_FING         3042..3057
FT                   /note="CysA-type"
FT   REGION          263..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..510
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          697..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          817..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1537..1600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1845..1882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1847..1898
FT                   /note="Mediates interaction with MAD2L2"
FT                   /evidence="ECO:0000269|PubMed:10660610"
FT   REGION          1962..1984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2017..2050
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2080..2150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2216..2236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           3086..3104
FT                   /note="CysB motif"
FT   COMPBIAS        700..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        843..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1060
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1195..1231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1537..1565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1574..1588
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1845..1876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1962..1983
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2080..2096
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2222..2236
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         3042
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3045
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3054
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3057
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3086
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3089
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3099
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   BINDING         3104
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P15436"
FT   MOD_RES         1030
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1041
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1724
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1967
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..78
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9925914"
FT                   /id="VSP_024121"
FT   VARIANT         231
FT                   /note="Q -> H (in dbSNP:rs1053911)"
FT                   /evidence="ECO:0000269|PubMed:10660610,
FT                   ECO:0000269|PubMed:9925914"
FT                   /id="VAR_008516"
FT   VARIANT         389
FT                   /note="S -> T"
FT                   /id="VAR_008517"
FT   VARIANT         397
FT                   /note="Q -> P (in dbSNP:rs3218579)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022226"
FT   VARIANT         633
FT                   /note="S -> G (in dbSNP:rs3218598)"
FT                   /id="VAR_048883"
FT   VARIANT         693
FT                   /note="M -> T (in dbSNP:rs3218593)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022227"
FT   VARIANT         962
FT                   /note="R -> Q (in dbSNP:rs17539588)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022228"
FT   VARIANT         1156
FT                   /note="Y -> C (in dbSNP:rs458017)"
FT                   /evidence="ECO:0000269|PubMed:10660610,
FT                   ECO:0000269|PubMed:9925914, ECO:0000269|Ref.5"
FT                   /id="VAR_022229"
FT   VARIANT         1220
FT                   /note="S -> L (in dbSNP:rs3218600)"
FT                   /id="VAR_048884"
FT   VARIANT         1224
FT                   /note="T -> I (in dbSNP:rs462779)"
FT                   /evidence="ECO:0000269|PubMed:10102035,
FT                   ECO:0000269|PubMed:10660610, ECO:0000269|PubMed:9618506,
FT                   ECO:0000269|PubMed:9925914, ECO:0000269|Ref.3,
FT                   ECO:0000269|Ref.5"
FT                   /id="VAR_022230"
FT   VARIANT         1284
FT                   /note="T -> P (in dbSNP:rs3218578)"
FT                   /id="VAR_048885"
FT   VARIANT         1302
FT                   /note="S -> T (in dbSNP:rs3218597)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022231"
FT   VARIANT         1309
FT                   /note="Q -> H (in dbSNP:rs3218595)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022232"
FT   VARIANT         1339
FT                   /note="P -> T (in dbSNP:rs17539616)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022233"
FT   VARIANT         1469
FT                   /note="Q -> P (in dbSNP:rs3218572)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022234"
FT   VARIANT         1540
FT                   /note="K -> E (in dbSNP:rs1053913)"
FT                   /evidence="ECO:0000269|PubMed:10660610,
FT                   ECO:0000269|PubMed:9925914"
FT                   /id="VAR_008518"
FT   VARIANT         1576
FT                   /note="S -> L (in dbSNP:rs3218582)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022235"
FT   VARIANT         1713
FT                   /note="D -> N (in dbSNP:rs3218585)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022236"
FT   VARIANT         1724
FT                   /note="S -> T (in dbSNP:rs17539644)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022237"
FT   VARIANT         1791
FT                   /note="P -> S (in dbSNP:rs17539651)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022238"
FT   VARIANT         1812
FT                   /note="D -> H (in dbSNP:rs3218599)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022239"
FT   VARIANT         1923
FT                   /note="G -> R (in dbSNP:rs3218604)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022240"
FT   VARIANT         1970
FT                   /note="R -> H (in dbSNP:rs3218606)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022241"
FT   VARIANT         2015
FT                   /note="E -> V (in dbSNP:rs17539692)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022242"
FT   VARIANT         2075
FT                   /note="I -> M (in dbSNP:rs17510963)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022243"
FT   VARIANT         2607
FT                   /note="S -> T"
FT                   /id="VAR_008519"
FT   VARIANT         2762
FT                   /note="R -> Q (in dbSNP:rs3218592)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_022244"
FT   VARIANT         3064
FT                   /note="V -> I (in dbSNP:rs3204953)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_016147"
FT   MUTAGEN         2614
FT                   /note="D->N: Loss of DNA polymerase catalytic activity;
FT                   when associated with N-2783."
FT                   /evidence="ECO:0000269|PubMed:24449906"
FT   MUTAGEN         2783
FT                   /note="D->N: Loss of DNA polymerase catalytic activity;
FT                   when associated with N-2614."
FT                   /evidence="ECO:0000269|PubMed:24449906"
FT   CONFLICT        237
FT                   /note="E -> Q (in Ref. 4; AAC28460 and 7; AAB88486)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1877..1882
FT                   /evidence="ECO:0007829|PDB:5O8K"
FT   HELIX           1887..1894
FT                   /evidence="ECO:0007829|PDB:5O8K"
FT   STRAND          1991..1998
FT                   /evidence="ECO:0007829|PDB:6BCD"
FT   HELIX           2003..2012
FT                   /evidence="ECO:0007829|PDB:6BCD"
SQ   SEQUENCE   3130 AA;  352776 MW;  4FBAA214639DF3C6 CRC64;
     MFSVRIVTAD YYMASPLQGL DTCQSPLTQA PVKKVPVVRV FGATPAGQKT CLHLHGIFPY
     LYVPYDGYGQ QPESYLSQMA FSIDRALNVA LGNPSSTAQH VFKVSLVSGM PFYGYHEKER
     HFMKIYLYNP TMVKRICELL QSGAIMNKFY QPHEAHIPYL LQLFIDYNLY GMNLINLAAV
     KFRKARRKSN TLHATGSCKN HLSGNSLADT LFRWEQDEIP SSLILEGVEP QSTCELEVDA
     VAADILNRLD IEAQIGGNPG LQAIWEDEKQ RRRNRNETSQ MSQPESQDHR FVPATESEKK
     FQKRLQEILK QNDFSVTLSG SVDYSDGSQE FSAELTLHSE VLSPEMLQCT PANMVEVHKD
     KESSKGHTRH KVEEALINEE AILNLMENSQ TFQPLTQRLS ESPVFMDSSP DEALVHLLAG
     LESDGYRGER NRMPSPCRSF GNNKYPQNSD DEENEPQIEK EEMELSLVMS QRWDSNIEEH
     CAKKRSLCRN THRSSTEDDD SSSGEEMEWS DNSLLLASLS IPQLDGTADE NSDNPLNNEN
     SRTHSSVIAT SKLSVKPSIF HKDAATLEPS SSAKITFQCK HTSALSSHVL NKEDLIEDLS
     QTNKNTEKGL DNSVTSFTNE STYSMKYPGS LSSTVHSENS HKENSKKEIL PVSSCESSIF
     DYEEDIPSVT RQVPSRKYTN IRKIEKDSPF IHMHRHPNEN TLGKNSFNFS DLNHSKNKVS
     SEGNEKGNST ALSSLFPSSF TENCELLSCS GENRTMVHSL NSTADESGLN KLKIRYEEFQ
     EHKTEKPSLS QQAAHYMFFP SVVLSNCLTR PQKLSPVTYK LQPGNKPSRL KLNKRKLAGH
     QETSTKSSET GSTKDNFIQN NPCNSNPEKD NALASDLTKT TRGAFENKTP TDGFIDCHFG
     DGTLETEQSF GLYGNKYTLR AKRKVNYETE DSESSFVTHN SKISLPHPME IGESLDGTLK
     SRKRRKMSKK LPPVIIKYII INRFRGRKNM LVKLGKIDSK EKQVILTEEK MELYKKLAPL
     KDFWPKVPDS PATKYPIYPL TPKKSHRRKS KHKSAKKKTG KQQRTNNENI KRTLSFRKKR
     SHAILSPPSP SYNAETEDCD LNYSDVMSKL GFLSERSTSP INSSPPRCWS PTDPRAEEIM
     AAAEKEAMLF KGPNVYKKTV NSRIGKTSRA RAQIKKSKAK LANPSIVTKK RNKRNQTNKL
     VDDGKKKPRA KQKTNEKGTS RKHTTLKDEK IKSQSGAEVK FVLKHQNVSE FASSSGGSQL
     LFKQKDMPLM GSAVDHPLSA SLPTGINAQQ KLSGCFSSFL ESKKSVDLQT FPSSRDDLHP
     SVVCNSIGPG VSKINVQRPH NQSAMFTLKE STLIQKNIFD LSNHLSQVAQ NTQISSGMSS
     KIEDNANNIQ RNYLSSIGKL SEYRNSLESK LDQAYTPNFL HCKDSQQQIV CIAEQSKHSE
     TCSPGNTASE ESQMPNNCFV TSLRSPIKQI AWEQKQRGFI LDMSNFKPER VKPRSLSEAI
     SQTKALSQCK NRNVSTPSAF GEGQSGLAVL KELLQKRQQK AQNANTTQDP LSNKHQPNKN
     ISGSLEHNKA NKRTRSVTSP RKPRTPRSTK QKEKIPKLLK VDSLNLQNSS QLDNSVSDDS
     PIFFSDPGFE SCYSLEDSLS PEHNYNFDIN TIGQTGFCSF YSGSQFVPAD QNLPQKFLSD
     AVQDLFPGQA IEKNEFLSHD NQKCDEDKHH TTDSASWIRS GTLSPEIFEK STIDSNENRR
     HNQWKNSFHP LTTRSNSIMD SFCVQQAEDC LSEKSRLNRS SVSKEVFLSL PQPNNSDWIQ
     GHTRKEMGQS LDSANTSFTA ILSSPDGELV DVACEDLELY VSRNNDMLTP TPDSSPRSTS
     SPSQSKNGSF TPRTANILKP LMSPPSREEI MATLLDHDLS ETIYQEPFCS NPSDVPEKPR
     EIGGRLLMVE TRLANDLAEF EGDFSLEGLR LWKTAFSAMT QNPRPGSPLR SGQGVVNKGS
     SNSPKMVEDK KIVIMPCKCA PSRQLVQVWL QAKEEYERSK KLPKTKPTGV VKSAENFSSS
     VNPDDKPVVP PKMDVSPCIL PTTAHTKEDV DNSQIALQAP TTGCSQTASE SQMLPPVASA
     SDPEKDEDDD DNYYISYSSP DSPVIPPWQQ PISPDSKALN GDDRPSSPVE ELPSLAFENF
     LKPIKDGIQK SPCSEPQEPL VISPINTRAR TGKCESLCFH STPIIQRKLL ERLPEAPGLS
     PLSTEPKTQK LSNKKGSNTD TLRRVLLTQA KNQFAAVNTP QKETSQIDGP SLNNTYGFKV
     SIQNLQEAKA LHEIQNLTLI SVELHARTRR DLEPDPEFDP ICALFYCISS DTPLPDTEKT
     ELTGVIVIDK DKTVFSQDIR YQTPLLIRSG ITGLEVTYAA DEKALFHEIA NIIKRYDPDI
     LLGYEIQMHS WGYLLQRAAA LSIDLCRMIS RVPDDKIENR FAAERDEYGS YTMSEINIVG
     RITLNLWRIM RNEVALTNYT FENVSFHVLH QRFPLFTFRV LSDWFDNKTD LYRWKMVDHY
     VSRVRGNLQM LEQLDLIGKT SEMARLFGIQ FLHVLTRGSQ YRVESMMLRI AKPMNYIPVT
     PSVQQRSQMR APQCVPLIME PESRFYSNSV LVLDFQSLYP SIVIAYNYCF STCLGHVENL
     GKYDEFKFGC TSLRVPPDLL YQVRHDITVS PNGVAFVKPS VRKGVLPRML EEILKTRFMV
     KQSMKAYKQD RALSRMLDAR QLGLKLIANV TFGYTSANFS GRMPCIEVGD SIVHKARETL
     ERAIKLVNDT KKWGARVVYG DTDSMFVLLK GATKEQSFKI GQEIAEAVTA TNPKPVKLKF
     EKVYLPCVLQ TKKRYVGYMY ETLDQKDPVF DAKGIETVRR DSCPAVSKIL ERSLKLLFET
     RDISLIKQYV QRQCMKLLEG KASIQDFIFA KEYRGSFSYK PGACVPALEL TRKMLTYDRR
     SEPQVGERVP YVIIYGTPGV PLIQLVRRPV EVLQDPTLRL NATYYITKQI LPPLARIFSL
     IGIDVFSWYH ELPRIHKATS SSRSEPEGRK GTISQYFTTL HCPVCDDLTQ HGICSKCRSQ
     PQHVAVILNQ EIRELERQQE QLVKICKNCT GCFDRHIPCV SLNCPVLFKL SRVNRELSKA
     PYLRQLLDQF
//