ID A0A0H1BR20_9EURO Unreviewed; 1168 AA.
AC A0A0H1BR20;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=EMPG_11585 {ECO:0000313|EMBL:KLJ13482.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ13482.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLJ13482.1}.
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DR EMBL; LDEV01000319; KLJ13482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1BR20; -.
DR STRING; 2060906.A0A0H1BR20; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000053573; 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; -; 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; 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; 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:UP000053573};
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 369..567
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 193..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 128501 MW; 24EF499F49775809 CRC64;
MGSRLESGSN AVRKRIENHV FDNEDGEEYQ GSSFGGFGDY FRRKKLKLQN LDAELRASSP
QNPPIFRGVV AHVNGYTQPS LKDLRHLVVS HGGGFLQYLD GKTSATHIIA STLTPKKREE
FRKYRIVKPA WVVESVKAGR LLPWDSFRVV DEGQSQKVLM FGGDGQVQSQ VNTQSRSYKD
QTDTSWYTSQ IQSKSLDNDD HMEITGATSS AHGGTPAPTP HNELQGTHSD AAMAAFPALD
TTLNTDVADQ AITRSSSCEN LEDPEPPDET GTADQVTLPK PVFDKYKESD AHSSMTPEEY
NAQLLSAPHM RNSSVVNPEF IQQFYRESRL HHLSTWKAEL KAKLQSAAQE KGISRAAKKP
HVPGARRYIM HVDFDSFFAA VSIRKHPELV DQPVAIAHGT GPGSEIASCN YPARSFGIKN
GMWMKGALQM CPNLKVLPYD FAAYEQASRT LYEVILSIDG IVQSVSIDEA LVDITGVCLD
AGGSDGRGIS EGSIWREQEK ADEIAQNLRN SVKDQTGCNI SVGIGGNVLQ ARVALRKAKP
AGQFQLKPDA VLDFMGTLAV KDLPGVAHSL GARLEELGVT FVKDIRDLSR EKLTSSLGPK
TGAKLWDFAR GIDNTEVGVQ APRKSVSAEI NWGIRFVNQA QAEEFVQNLC DELHRRLVEN
LVKGKQLTMR IMKRSADAPL EPVKHLGHGK CDTFNKSVNL GVATNASDII GREAISILRA
FKFSPGDLRG LGVQMTKLEP VKQNHARELD SSQRQISFKP ASPTRQRETP TDPDEISTPR
KGDATSEYLH KSLQSAPSLT DTSQKPLNLT GTQFVMPTQV DPKLLAELPM DIRSKFAHRQ
THSQGFQFHG ESPRADSPPP AAHLPPQSQL DPDMLAELPE DVRAEVLGYY KRPLSPRSES
PQLGTPRHNK PVISKAIKKA ITPTKARAGR ARGRPNKKLA GNSTLMQSNF ILTRPSTDPT
SVQADVASPG SPQAEADGIS DEFLAALPDD IRREVLEEHK RSRLQKRAGL NLPPPTRRSL
FPKPTARTPE QKTISLLPRP EKPTFTSKKL SSLPELRKAL DEWHGAFETE APYEEDVAAL
AKYLKRVVLE EKDIAKAVAV VGWLEWLIGS SIVEEIQPDQ GGSSPEVGTS STVKNVQARE
GWVKALWSLR DNISDAVQER GLPPVEFT
//