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 24-JAN-2024, entry version 91.
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.ENSGALP00000066817; -.
DR PaxDb; 9031-ENSGALP00000027018; -.
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; Unassembled WGS sequence.
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 CDD; cd17719; BRCT_Rev1; 1.
DR CDD; cd01701; PolY_Rev1; 1.
DR CDD; cd12145; Rev1_C; 1.
DR CDD; cd19318; Rev1_UBM2; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 6.10.250.1490; -; 1.
DR Gene3D; 6.10.250.1630; -; 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 Gene3D; 1.20.58.1280; DNA repair protein Rev1, C-terminal 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; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR012112; REV1.
DR InterPro; IPR031991; Rev1_C.
DR InterPro; IPR038401; Rev1_C_sf.
DR InterPro; IPR047346; Rev1_UBM1/2.
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; 2.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF21704; POLH-Rev1_HhH; 1.
DR Pfam; PF16727; REV1_C; 1.
DR Pfam; PF14377; UBM; 2.
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 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
//
