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Database: UniProt
Entry: A0A0H1BR20_9EURO
LinkDB: A0A0H1BR20_9EURO
Original site: A0A0H1BR20_9EURO 
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
//
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