ID A0A7G2FGQ9_ARATH Unreviewed; 1048 AA. AC A0A7G2FGQ9; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 19-JAN-2022, entry version 5. 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 ORFNames=AT9943_LOCUS21307 {ECO:0000313|EMBL:CAD5333972.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:CAD5333972.1, ECO:0000313|Proteomes:UP000516314}; RN [1] {ECO:0000313|EMBL:CAD5333972.1, ECO:0000313|Proteomes:UP000516314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Cdm-0 {ECO:0000313|Proteomes:UP000516314}; RA Ashkenazy H.; RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Nucleus {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; LR881470; CAD5333972.1; -; Genomic_DNA. DR OMA; DEMFVEL; -. DR Proteomes; UP000516314; Chromosome 5. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:InterPro. DR Gene3D; 3.30.1490.100; -; 1. DR Gene3D; 3.30.70.270; -; 1. DR Gene3D; 3.40.50.10190; -; 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; IPR012112; REV1. DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase. DR InterPro; IPR001126; UmuC. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF00817; IMS; 1. DR Pfam; PF11799; IMS_C; 1. DR PIRSF; PIRSF036573; REV1; 2. DR SMART; SM00292; BRCT; 1. DR SUPFAM; SSF100879; SSF100879; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR SUPFAM; SSF56672; SSF56672; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS50173; UMUC; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|PIRNR:PIRNR036573}; KW DNA repair {ECO:0000256|PIRNR:PIRNR036573}; KW DNA synthesis {ECO:0000256|ARBA:ARBA00022634, KW ECO:0000256|PIRNR:PIRNR036573}; KW DNA-binding {ECO:0000256|PIRNR:PIRNR036573}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR036573}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036573}; KW Transferase {ECO:0000256|PIRNR:PIRNR036573}. FT DOMAIN 26..117 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT DOMAIN 318..499 FT /note="UmuC" FT /evidence="ECO:0000259|PROSITE:PS50173" FT REGION 141..205 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 234..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 718..746 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 877..902 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..156 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 160..181 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 187..202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 886..902 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1048 AA; 116288 MW; 5C120CAA661EAE8C CRC64; MEVKNRKLQN QFETEASAAS RGVSGSEKLI FQGVSIFVDG FTIPSHQELK GYMMKYGGRF ENYFSRRSVT HIICSNLPDS KVKNLRTFSR GLPVVKPTWI VDSISANRLL GWVPYQLDQL NDTQPKLSAF FAPRSHLTPQ MASPVTSFQP DTGYSEAEEG SSIRADDSEE ARDHIDDEID GVYIENTTPE LTEQTGTGDL KSSEMNAEGL GNYDIEEKEV SSELQSTTIL HSTSDNKSVH ANGKNGGKSI ATAAGSSTRR HSTLEDPNFV ENYFKNSRLH FIGTWRNRYR KRFHGSSNGL KWADSGQNTA EMAKKSTIIH IDLDCFFVSV VIKNRLELHD KPVAVCHSDN PKGTAEISSA NYPARAYGVK AGMFVRHAKD LCPQLVIVPY NFEAYEEVAD QFYDILHRHC RKVQALSCDE AFLDVSDLSD VETEVLASTI RNEILETTGC SASAGIGGTM LMARLATRVA KPAGQLYISA EKVEEFLDQL PVGTLPGVGS VLKEKLVKQN IQTCGQLRLI SKDSLQKDFG VKTGEMLWSY SRGLDLRSVT AVQESKSIGA EVNWGVRFRD QQDVFILVQH FLQCLCKEVS LRLQGCEMIG RTFTLKIKKR KKDAEEPTKY MGCGDCDNLS RSITVPAATD DIEVLQRISK KLFGSFCLDV KEVRGVGLQV SKLDSADPSN KGSRTLKSWL SSAPAVVQIE QDDNVFAAKV RENSDCNRPV TGGVSRLRES NSEESSIQSG DTNSSLPPMC YLDMEVLENL PPELLSELDG TYGGKLFELI EKKRGKRRIN CNSPHVSLDG TAASIKELKS LSVKIHGLST SGEKEYKEPY VPHPSIARTS NQHTIEMTDL LPSSLSQVDV SVLQELPEEL RADVLGAFPS HRRQQSSSDV PKETCKKQDE EPIDLKGTEN EIGLSFSSLW FGNPPLWTEK FKVSGNCTME KLSAIYFKVA QSRPMLSLVL QHAISEMSSF PDAASASDLD KAIYDVCELL KQYINLKVGG DIEEIYLCFR LLKRLAARSQ LFLQVYEILS PFIQASISEH YGGSLSIP //