ID Q654Y6_ORYSJ Unreviewed; 1125 AA. AC Q654Y6; DT 25-OCT-2004, integrated into UniProtKB/TrEMBL. DT 25-OCT-2004, sequence version 1. DT 27-NOV-2024, entry version 136. DE RecName: Full=DNA repair protein REV1 {ECO:0000256|ARBA:ARBA00020399, ECO:0000256|PIRNR:PIRNR036573}; DE EC=2.7.7.- {ECO:0000256|PIRNR:PIRNR036573}; GN OrderedLocusNames=Os06g0691000 {ECO:0000313|EMBL:BAS99233.1}; GN ORFNames=OSNPB_060691000 {ECO:0000313|EMBL:BAS99233.1}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:BAS99233.1, ECO:0000313|Proteomes:UP000059680}; RN [1] {ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=16100779; DOI=10.1038/nature03895; RG International rice genome sequencing project (IRGSP); RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N., RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y., RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N., RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M., RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N., RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H., RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S., RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y., RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H., RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M., RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A., RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S., RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R., RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J., RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X., RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S., RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A., RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R., RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S., RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M., RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S., RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H., RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C., RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S., RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S., RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K., RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A., RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R., RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S., RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K., RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D., RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I., RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A., RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H., RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S., RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T., RA Kadowaki K., Sugiura M., Burr B., Sasaki T.; RT "The map-based sequence of the rice genome."; RL Nature 436:793-800(2005). RN [2] {ECO:0000313|EMBL:BAS99233.1, ECO:0000313|Proteomes:UP000059680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000059680}; RX PubMed=24280374; DOI=10.1186/1939-8433-6-4; RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R., RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L., RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H., RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.; RT "Improvement of the Oryza sativa Nipponbare reference genome using next RT generation sequence and optical map data."; RL Rice 6:4-4(2013). CC -!- FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a CC dCMP residue from dCTP to the 3'-end of a DNA primer in a template- CC dependent reaction. May assist in the first step in the bypass of CC abasic lesions by the insertion of a nucleotide opposite the lesion. CC Required for normal induction of mutations by physical and chemical CC agents. {ECO:0000256|PIRNR:PIRNR036573}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR036573-2}; CC Note=Binds 2 magnesium ions. {ECO:0000256|PIRSR:PIRSR036573-2}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|PIRNR:PIRNR036573}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. CC {ECO:0000256|ARBA:ARBA00010945, ECO:0000256|PIRNR:PIRNR036573}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP014962; BAS99233.1; -; Genomic_DNA. DR RefSeq; XP_015643387.1; XM_015787901.1. DR AlphaFoldDB; Q654Y6; -. DR SMR; Q654Y6; -. DR STRING; 39947.Q654Y6; -. DR PaxDb; 39947-Q654Y6; -. DR EnsemblPlants; Os06t0691000-01; Os06t0691000-01; Os06g0691000. DR GeneID; 4341904; -. DR Gramene; Os06t0691000-01; Os06t0691000-01; Os06g0691000. DR KEGG; osa:4341904; -. DR eggNOG; KOG2093; Eukaryota. DR InParanoid; Q654Y6; -. DR OMA; QPRLNFG; -. DR OrthoDB; 169741at2759; -. DR Proteomes; UP000059680; Chromosome 6. DR ExpressionAtlas; Q654Y6; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0017125; F:deoxycytidyl transferase activity; IBA:GO_Central. 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:0070987; P:error-free translesion synthesis; IBA:GO_Central. DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central. DR GO; GO:0010224; P:response to UV-B; IEA:EnsemblPlants. DR CDD; cd17719; BRCT_Rev1; 1. DR CDD; cd01701; PolY_Rev1; 1. DR FunFam; 3.30.1490.100:FF:000001; DNA repair protein REV1; 1. DR FunFam; 3.30.70.270:FF:000019; DNA repair protein REV1; 1. DR FunFam; 3.40.1170.60:FF:000004; DNA repair protein REV1; 1. DR FunFam; 3.40.50.10190:FF:000011; DNA repair protein REV1; 1. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 3.40.1170.60; -; 1. DR Gene3D; 6.10.250.1490; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR043502; DNA/RNA_pol_sf. DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf. DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger. DR InterPro; IPR053848; IMS_HHH_1. DR InterPro; IPR012112; REV1. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR001126; UmuC. DR PANTHER; PTHR45990; DNA REPAIR PROTEIN REV1; 1. DR PANTHER; PTHR45990:SF1; DNA REPAIR PROTEIN REV1; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR Pfam; PF21999; IMS_HHH_1; 1. DR PIRSF; PIRSF036573; REV1; 1. DR SMART; SM00292; BRCT; 1. DR SUPFAM; SSF52113; BRCT domain; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS50173; UMUC; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR036573}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR036573}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, KW ECO:0000256|PIRNR:PIRNR036573}; KW DNA-binding {ECO:0000256|PIRNR:PIRNR036573}; KW Magnesium {ECO:0000256|PIRSR:PIRSR036573-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR036573-2}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, KW ECO:0000256|PIRNR:PIRNR036573}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036573}; KW Reference proteome {ECO:0000313|Proteomes:UP000059680}; KW Transferase {ECO:0000256|PIRNR:PIRNR036573}. FT DOMAIN 83..174 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT DOMAIN 379..560 FT /note="UmuC" FT /evidence="ECO:0000259|PROSITE:PS50173" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 199..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 302..326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 776..811 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 968..994 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..46 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..220 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..254 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 788..803 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 383 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036573-2" FT BINDING 480 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036573-2" FT BINDING 481 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR036573-2" SQ SEQUENCE 1125 AA; 123768 MW; 0B5903FCD290D390 CRC64; MSASSSGGRG APPPATAASP GQKRPRGDDP ASPSNRSESA PAKNPRRAFS SSPFADFGSY MAAKNSKLAA QFEADASTSA AEVTGGVFAG VSIFVDGFTV PSSQELKEIM LNNGGRFVNY FSRNTVTHII CTHLPNSKMS NLRAFSKGLP VVKPAWVVDS LAENRLLSCV PYQISQHNSS SRKQTKLSSF FSGRHYQGEL NDQSNSHELQ SSSVQEGSQD HNSGCEKEGS LLKEEASKDS LSSDDHKASM FEEQDSEDFV DEAGNAYETA CSERRDNDMD GKLHVAESPD IRSRCSNLCS TSSTGSHLSL DSLDRNATKS SSRTHSTLTD PNFVENYFKY SRLHFIGTWR NRYRKRFSNL LGDKSSKGNR DHSGKNNTII HIDMDCFFVS VVIRNKPELH DKPVAVCHSD NPKGTAEISS ANYPARNYGI KAGMFVREAK ARCPHLMIVP YDFDAYGEVA DQFYGILHKY CSKVQALSCD EAFLDMTECL HDNPEEVTQK IRNEIFGTTK CSASAGISGN MLIARLATRS AKPNGQCFIS SEKVDGYLNT LSIKALPGIG HTVSDKLKSK EVEYCGQLRN IPKESLHKDF GKKIGDMLWN YCRGIDHSVV EAVQETKSVG AEVNWGVRFN DNKDAENFLV NLSKEVCLRL EGCGVQGRTI TLKLKTRRKG AGEPIKFMGC GDCETVSRSM TIAGATDNPV TLQRIAKQLF SSFCVDVKEV RGVGLKISRL EHADLARGAP QGNMLESWLA SPSDKLKKHS TEKACLLKNR DDAATSERRG FGSIRPSGIG GTSRSSEVNP PSDRSTRVGV ELPPLSELDL EVLKNLPPEI IYEMNDMYKG ELHGFLGITS GDKAKESNTK SLVFPAVDQN LVPVLDTKLH GDGKHKDSIH FKKEADIKGP SGEQLSELKQ ANAPRSIASE LVDIPTKSVI QHDFMPNSLS QADVTVLQEL PEDVKADLFN ALPLHRSGDP TCSTSHVSEN KFPQDGRSDD PKQHPQICHL PGNSQKWIEE FRVSHCLILN VIAEQHTDSI SSRPLSSVLE PVISYLPLCP NSGTEEWNEA FASLSELLTQ YIHQKVESDI EELHKCFRLL KRLSSGSELF LELHDSILPL LQDSVRQHYG GILHL //