ID A0A2J5HJH6_9EURO Unreviewed; 1148 AA.
AC A0A2J5HJH6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=BDW42DRAFT_6957 {ECO:0000313|EMBL:PLN77207.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN77207.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) 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; KZ559600; PLN77207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HJH6; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000235023; Unassembled WGS sequence.
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:0070987; P:error-free translesion synthesis; IEA:UniProt.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:InterPro.
DR CDD; cd17719; BRCT_Rev1; 1.
DR CDD; cd01701; PolY_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; 6.10.250.1630; -; 2.
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; IPR024728; PolY_HhH_motif.
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 PANTHER; PTHR45990; DNA REPAIR PROTEIN REV1; 1.
DR PANTHER; PTHR45990:SF1; DNA REPAIR PROTEIN REV1; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF11798; IMS_HHH; 1.
DR Pfam; PF16727; REV1_C; 1.
DR Pfam; PF14377; UBM; 2.
DR PIRSF; PIRSF036573; REV1; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 61..149
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 368..566
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 190..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..917
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1014
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 126466 MW; D308695EED736640 CRC64;
MGSLLDEKSN SVRKRIENHV FEDEVGEEYE ASAFGGFGDY MRRKKIKLQN LDAEIRSSSA
DCLPIFRGVV VHVNGYTQPS LQDLHRMIVS HGGGFLQYLD GKTSATHIVA SSLTPKKREE
FRRYRIVKPA WVVESVKAKR LLPWDAFRVV DEGQNQKVLK FDNGRVLNES NTPQSSYRDQ
TNSSWYTSQL KASTQAQNGR PISGTPDMDP AVDQAVAPPT QSDYGDFPSF TSLDEPNEIS
NKSARSGPEA VEERPRTPTP LVHSLEAIHT PSKSPPVVSQ APSPSRRDAS APEVTSEEYN
AQLLSDPRMR NNSVVNPEFI QQYYRESRLH HLSTWKAELK AQLQLAAKEK SQSRLSRRKQ
IPGARRYIMH VDFDCFFAAV AVLKHPDLDG KPVAVAHGTG SGSEIASCNY TARAKGVKNG
MWMKGALQSC PDLNVLPYDF PAYEDASRKF YSAILSVEGI VQSVSIDEAL VDITGQCLEA
GGSDGRGVSE GSIYREQAKA DEIAERLRHA IRSETGCSVS VGIGGNILQA KVALRKAKPA
GQFQLKPDMV LEFIGNLTVQ DLPGVGYSLG AKLEELGIKF VKDVRDQSKE RLTSALGPKT
GARIWDYARG IDRTEVGNEV MRKSVSAEVN WGIRFVNQSQ AEDFVRSLCE ELHRRLVENL
VKGKQLTLKV MRRSADAPLE PVKHLGHGKC DTFNKSVLLG VASNSTDVLG KEAVSMLKSF
AISPGDLRGI GVQMTKLEPL KPATGGSIEA SQKQLNFKAS PARKKAQHTH DPDDLESPRK
EETDTVNYGP SLNDSNQKPL NISGTQFIMP SQTDPQVVAE LPNDIRSKLV AQGKQAPRGE
RSTSPCPPPR RSQPPVAAEL PPQSQLDPDT LAALPEDLRA EVLDYYNQRD PAGPQTAPAP
APLAAPPPPP NPLRFKKPTS PPKKKRGRPS TKSTGTTTLR QANFLFPRPA TPTLSEERRE
PSPQPDTADE VSPEFLAALP EDIRREVLEE HRRARTRQRP SSATQRTAGQ QQTRPFGAPP
APAQERRLRL PPLPERPTFT SQKLSALSDL RDAVQSWHAA FTEEGPFAED VEALALYVKR
VVVDERDLDK AVSVTKWLMW LVEDSRPTEA GGQRGSPNGV SWDEAVRSLQ RSVAEGVEER
GLPPVDFS
//
