ID C1G8X8_PARBD Unreviewed; 1147 AA.
AC C1G8X8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 60.
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=PADG_03714 {ECO:0000313|EMBL:EEH47630.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47630.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47630.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47630.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275960; EEH47630.2; -; Genomic_DNA.
DR RefSeq; XP_010759152.1; XM_010760850.1.
DR AlphaFoldDB; C1G8X8; -.
DR STRING; 502780.C1G8X8; -.
DR GeneID; 22582976; -.
DR KEGG; pbn:PADG_03714; -.
DR VEuPathDB; FungiDB:PADG_03714; -.
DR eggNOG; KOG2093; Eukaryota.
DR HOGENOM; CLU_003901_1_1_1; -.
DR InParanoid; C1G8X8; -.
DR OMA; IKNGMWM; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000001628; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 47..135
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 354..552
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 189..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 988..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 126626 MW; 505040013655D8DC CRC64;
MSAADVFDNE DGEEYEGSSF GGFGDYFRRK KLKLQNLDAE VRASSPNNPP IFRGVVAHVN
GYTQPSLNDL HRLIVSHGGG FLQYLDGKTS ATHILASVLT PKKREEFRKY RIVKPGWVVE
SVKAGRLLPW DKFRVVDEGQ SQKVLTFGGD GRVQSQANIQ FRNYRDHTET SWYTSQIKSG
FADITEKMET TGAISPSGTK DTAAISPSSR DPNLAVESDL GNDMFPTQND GIPDEAIAGS
DPQGELGITP SQRMSPISEE TKRQGPVYDL QNHVDTKSSM TPEVYNAKLL SDPHYQNSSV
VNSKFIQQFY CESRLHHLST WKAELKAQIQ SAAQDKGSTR KPARQRVPGV RRYIMHVDFD
SFFAAVSIRK HPELADQPVA IAHGTGPGSE IASCNYPARS FGIKNGMWMK GALQMCPNLK
VLPYDFAAYE EASRNFYDVI LSIDGIVQSV SIDEALVDIT NICLDAGGSD GIGISEGSIY
REQAKADEIA QKLRDSVKEQ TGCNISVGIG GNVLQARVAL RKAKPAGQFQ LKPDAVQDFI
GELTVKDLPG VAHSLGGKLE ELGVVFVKDI RELSKEKLTS SLGPKTGAKL WNYARGIDNT
EVGIQVPRKS VSAEISWGIR FVSQTQAEEF VQSLCDELHR RLVENLVKGK QLTMRIMKRS
TDAPLEPVKH LGHGKCDTFN KSVALGVATN ASDIIGREAI SILRGFKFSP GDLRGLGVQM
TKLEPVKQSN VRKVESSQRQ LSFKPSSPSP KMEIPVDPDE ISTPRKGDPS SKYLPASFKG
SPFLTDSSQK PLNLTGTKFM LPTQVDPKVV AELPMDIRSK LAPRQKHNQS PRPESPSRAA
AQLPPQSQLD PEMLAELPED VRAEVLGYYK RPLSPRPESP QFGTPRRNRT AASRASKRVP
TPTKTRTGRA RGRPSNKLTG NTTLLQSSFI KSHPSTTPAF VQESLYAPSF PQAELGGISA
DFLAALPEDI RREVLKEHKR SRLQKRAGLN LPPPTRRSLF HKPTPRIPEQ KKLTLPPRPE
KPTFTSKKLS TLPDLRIALD EWYGAFETEP PYEEDVAALA KYLKRVVLEE KDIAKAVAVV
GWLAWLIDNP TTEAPKTDHG GSSEKLDVCN TIVHTETREV WIKALQSLRD NISDAVQERG
LPPVEFT
//
