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Database: UniProt
Entry: A0A0D9RX98_CHLSB
LinkDB: A0A0D9RX98_CHLSB
Original site: A0A0D9RX98_CHLSB 
ID   A0A0D9RX98_CHLSB        Unreviewed;      1248 AA.
AC   A0A0D9RX98;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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   Name=REV1 {ECO:0000313|Ensembl:ENSCSAP00000013237.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000013237.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000013237.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000013237.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   EMBL; AQIB01138544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008006365.1; XM_008008174.1.
DR   AlphaFoldDB; A0A0D9RX98; -.
DR   STRING; 60711.ENSCSAP00000013237; -.
DR   Ensembl; ENSCSAT00000015293.1; ENSCSAP00000013237.1; ENSCSAG00000017200.1.
DR   GeneID; 103241114; -.
DR   CTD; 51455; -.
DR   eggNOG; KOG2093; Eukaryota.
DR   GeneTree; ENSGT00940000156374; -.
DR   OMA; IKNGMWM; -.
DR   OrthoDB; 169741at2759; -.
DR   BioGRID-ORCS; 103241114; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 14.
DR   Bgee; ENSCSAG00000017200; Expressed in adrenal cortex and 7 other cell types or tissues.
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; IEA:Ensembl.
DR   GO; GO:0042276; P:error-prone translesion synthesis; IEA:Ensembl.
DR   GO; GO:0009411; P:response to UV; IEA:Ensembl.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT   DOMAIN          44..131
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          419..652
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          204..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          252..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1054
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1248 AA;  137757 MW;  A63A09ED7047A23B CRC64;
     MRRGGWRKRA ENDGWEKWGG YMAAKVQKLE EQFRSDAALQ KDGTSSTIFS GVAIYVNGYT
     DPSAEELRKL MMLHGGQYHV YYSRSKTTHI IATNLPNAKI KELKGEKVIR PEWIVESIKA
     GRLLSYIPYQ LYTKQSSVQK GLSFNPVCRP EDPVPGPSNI AKQFNNRVNH IVKKIETENE
     VKVNGMNSWN EEDENNDFSF VDLEQTSPGR KQNGIPHPRG STAIFNGHTS SSNGALKTQD
     CLVPMVNSVA SRLSPASSQE EDKAEKSSTD FRDCTLQQLQ QSTRNTDALR NPHRTNSVSL
     SPLHSNTKIN GAHHSTVQGP SSTKSTSSVS TLSKTAPSVP SKPSDCNFIS NFYSHSRLHH
     ISMWKCELTE FVNTLQRQSN GIFPGREKLK KMKTGRSALV VTDTGDVSVL SSPRHQSCIM
     HVDMDCFFVS VGIRNRPDLK GKPVAVTSNR GTGRAPLRPG ANPQLEWQYY QNKILKGKAD
     IPDSSLWENP DSAQANGIDS VLSKAEIASC SYEARQLGIK NGMFFGHAKQ LCPNLQAVPY
     DFHAYKEVAR TLYETLASYT HNIEAVSCDE ALVDITEILA ETKLTPDEFA NAVRMEIKDQ
     TKCAASVGIG SNILLARMAT RKAKPDGQYH LKPEEVDDFI RGQLVTNLPG VGCSMESKLA
     SLGIKTCGDL QYMTMAKLQK EFGPKTGQML YRFCRGLDDR PVRTEKERKS VSAEINYGIR
     FTQPKEAEAF LLSLSEEIQR RLEATGMKGK RLTLKIMVRK AGAPVETAKF GGHGICDNVA
     RTVTLDQATD NAKIIGKAML NMFHTMKLNI SDMRGVGIHV NQLVPTNMNP STCPSRPSVQ
     SSHFPGGSYS VRDIFQVQKA KKSTEEEHKE VFRTAVDLEI PSASRTCTLP PFPTHLPTSP
     DTNKAESSGK WNGLHSPVSV QSRLNLSIEV PSPSQLDQSV LEALPPDLRE QVEQVCAIQQ
     AEAHGDKRKE PVNGCNTGIL PQPVGTVLLQ IPEPQESNSD TGINVIALPA FSQVDPEVFA
     ALPAELQREL KAAYDQRQRQ GENSSHQQSA GASVPKNPLL HLKAAVKEKK RNKKKPIGSP
     KRIQSPLRNK LPNSPAKTLP GACGSPQKLI DGFLKHEGTP AEKPLEELSA STSGVPGLSS
     LQSDPAGCVR PPAPNLAGAV EFNDVKTLLR EWITTISDPM EEDILQVVKY CTDLIEEKDL
     EKLDLVIKYM KRLMQQSVES VWNMAFDFIL DNVQVVLQQT YGSTLKVT
//
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