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REV1_CHICK
ID   REV1_CHICK              Reviewed;        1255 AA.
AC   Q4KWZ7;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=DNA repair protein REV1;
DE            EC=2.7.7.-;
DE   AltName: Full=Rev1-like terminal deoxycytidyl transferase;
GN   Name=REV1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=15988022; DOI=10.1128/mcb.25.14.6103-6111.2005;
RA   Okada T., Sonoda E., Yoshimura M., Kawano Y., Saya H., Kohzaki M.,
RA   Takeda S.;
RT   "Multiple roles of vertebrate REV genes in DNA repair and recombination.";
RL   Mol. Cell. Biol. 25:6103-6111(2005).
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 (By similarity). May play a role in homologous recombination and
CC       immunoglobulin gene conversion. {ECO:0000250,
CC       ECO:0000269|PubMed:15988022}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal domain is necessary for protein interactions.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR   EMBL; AY675169; AAV80844.1; -; mRNA.
DR   RefSeq; NP_001025982.2; NM_001030811.2.
DR   AlphaFoldDB; Q4KWZ7; -.
DR   SMR; Q4KWZ7; -.
DR   BioGRID; 679901; 1.
DR   STRING; 9031.ENSGALP00000027018; -.
DR   PaxDb; Q4KWZ7; -.
DR   PRIDE; Q4KWZ7; -.
DR   GeneID; 418703; -.
DR   KEGG; gga:418703; -.
DR   CTD; 51455; -.
DR   VEuPathDB; HostDB:geneid_418703; -.
DR   eggNOG; KOG2093; Eukaryota.
DR   InParanoid; Q4KWZ7; -.
DR   PhylomeDB; Q4KWZ7; -.
DR   Reactome; R-GGA-353503; Translesion synthesis by Pol kappa.
DR   PRO; PR:Q4KWZ7; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
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:0006302; P:double-strand break repair; IMP:UniProtKB.
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:0002206; P:gene conversion of immunoglobulin genes; IMP:UniProtKB.
DR   Gene3D; 1.20.58.1280; -; 1.
DR   Gene3D; 3.30.1490.100; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
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; IPR025527; HUWE1/Rev1_UBM.
DR   InterPro; IPR012112; REV1.
DR   InterPro; IPR031991; Rev1_C.
DR   InterPro; IPR038401; Rev1_C_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR001126; UmuC.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF00817; IMS; 1.
DR   Pfam; PF11799; IMS_C; 1.
DR   Pfam; PF16727; REV1_C; 1.
DR   Pfam; PF14377; UBM; 2.
DR   PIRSF; PIRSF036573; REV1; 1.
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   2: Evidence at transcript level;
KW   DNA damage; DNA repair; DNA synthesis; DNA-binding; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1255
FT                   /note="DNA repair protein REV1"
FT                   /id="PRO_0000405249"
FT   DOMAIN          47..134
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          423..664
FT                   /note="UmuC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   REGION          287..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..367
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          664..667
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          720..728
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          1073..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1134..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1255
FT                   /note="Protein interaction domain"
FT                   /evidence="ECO:0000250"
FT   MOTIF           1079..1085
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1073..1087
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1136..1153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         362
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         427..431
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         427
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         521..527
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         533
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         581
FT                   /ligand="dCTP"
FT                   /ligand_id="ChEBI:CHEBI:61481"
FT                   /evidence="ECO:0000250"
FT   BINDING         581
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         581
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   BINDING         582
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT   SITE            781
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            794
FT                   /note="Interaction with target DNA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1255 AA;  138065 MW;  A8B151298C80682C CRC64;
     MRRGGWRKRA GEGDGWGGWG GYMSAKVKKL EDQFRSDSAI QHQRDGNSSS IFSGVAIYVN
     GFTDPSADEL RRLMMLHGGQ YHVYYSRSKT THIIATNLPN AKIKELKGEK VVRPEWIVES
     IKAGRLLSHI PYQLYTKQSS VQKGLSFNSI CKPEDAMPGP SNIAKDLNRV NHIKQCEMES
     EITPNGISSW NEEEEEDSDG LGFTKLDQIL PERKQNGIQS HKDSTAIFNG HTHNTCISAL
     KTQDCLVPSS NSVASRFSPG PVQEEGKPEK GIVDFRDCTM QQLQQSNKNT DFSWNPHRTM
     SNSSSSSSLH SNTKINGAHH STVQGPSSTK STSVPTPSKA ASLSVSKPSD CSFISDFYSR
     SRLHHISTWK CELTEFVNSL QRKNSGVFPG REKLKKWKAG RSALKTDTGN VSVASSAKPQ
     SCIMHVDMDC FFVSVAIRNR PDLKGKPVAV TSNRGAGKAP LRPGANPQLE WQYYQNKLLN
     GKAEIRIPDK LDSLVWEHSD SAHMNGVDCD LTVLSMAEIA SCSYEARQAG IKNGMFFGQA
     KKLCPNLQAV SYDFNAYKEV AQTVYEILAS YTHNIEAVSC DEALVDITEI LTETRLTPDE
     LANAIRDEIK AQTKCTASVG MGSNILLARM ATRKAKPDGQ YHLKPEEVDD FIRGQLVTNL
     PGVGRSMESK LASLGIRTCG DLQCASMSKL QKEFGPKTGQ MLYRFCRGLD DRPVRTEKER
     KSVSAEINYG IRFTQPKEAE AFLLSLSEEI QRRLEAAGMK GKRLTLKIMV RKAGAPVEPA
     KYGGHGICDN IARTVTLDHA TDSAKVIGKE TLNMFHTMKL NISDMRGVGI QVQQLVPISK
     TTSAQSAVQS GRLPGGSHSV IDLLHVQKAK KCSEEEHKEV FVAAMDLEIS SDSRTCTVLP
     SRGTHLTAGL NSNVSKTDSA VKLNGLHSPI SVKSRLNLSI EVPSASQLDK SVLEALPPDL
     REQVEQIYTI QQGETYGDSK REPINGCNTA LLSQPVGTVL LQVPELQEPN ANMGINVIAL
     PAFSQVDPEV FAALPAELQA ELKDAYDQRQ KQPEQQPANA FVSKNPCLQL KHATTKNKKK
     IRKKNPVSPV KKIQSPLKNK LLGSPAKNMP AASGSPQKLI DGFLKQEGAA AQLEAVPSTS
     DASDPSALQT EQCGSFRPQA PNLAGAVEFN DVKTLLKEWI TTISDPMEED ILQVVKYCTD
     LIEEKDLEKL DLVVKYMKRL MQSSVESVWN MAFDFILDNV QVVLQQTYGS TLKVI
 
 
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