ID C5MCF2_CANTT Unreviewed; 1121 AA.
AC C5MCF2;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=CTRG_03903 {ECO:0000313|EMBL:EER32232.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER32232.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER32232.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; GG692399; EER32232.1; -; Genomic_DNA.
DR RefSeq; XP_002549606.1; XM_002549560.1.
DR AlphaFoldDB; C5MCF2; -.
DR STRING; 294747.C5MCF2; -.
DR EnsemblFungi; CTRG_03903-t43_1; CTRG_03903-t43_1-p1; CTRG_03903.
DR GeneID; 8297958; -.
DR KEGG; ctp:CTRG_03903; -.
DR VEuPathDB; FungiDB:CTRG_03903; -.
DR eggNOG; KOG2093; Eukaryota.
DR HOGENOM; CLU_003901_1_0_1; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000002037; 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; 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 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; IPR012112; REV1.
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 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:UP000002037};
KW Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 156..244
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 399..587
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 42..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..285
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 128347 MW; 8B05BA1520E9C868 CRC64;
MDNANSEDIT NADVTETSQY QDFLMSLDDD KLISHVQNIG KQQELHHHHP SFHPSFQEVS
TPRKNASFNS NISSDPFNDG LDDEIMNIGG SKTTEVRADI ENESEENEAE KSVGELHKFG
DYGTYFRSKH LKQQRQDEEY VKWDLKRRKL QNLDSEPKQI FQGCSIYVNG HTDPSINEIH
RLVILHGGKF ISYLVNKSSA THIVCDRLTP RKSIEYKNCR VVKAQWIVDS VAKQELLDWK
EYRLIAEVAY NQKRLDFIKQ NPIHEADEDQ DEDGDGLLQE DDDDDDNNEF FRKSQELEQV
ISTTDKVENE DDDIELSVFE GEITEDQKGV HKVRNKLVLD ARHPDFLPNF FKNSRLHHLS
MWKSDLRLKF LRRIVKEELH QSQSKLDNPF LDSVKEKVIM HIDFDCFFAT ASCLLRPDLD
INKHPIAVTH GGRTSDIASC NYVARSFGLK NGMWLGSAKK MCPNLITLPY DFDSYEKYSS
EFYNYLLSSK YFDSIFPVSI DEVLVDATTY CNSQIGGIHT VVEELSSRIR QDVFTLTKCS
VSVGASTNVL LAKLALRKAK PNGQFQLFDN VESFLQTISI RDLPGFGRGI MEKLQNHTSA
TNPEIKDILH LSKAALIESL GEKTGCKLYE YCRGIDETKI EIDTKNPEAM LGRKSVSVDV
NFGIRFDTVE ELDDFLVRLS KELYQRLVTL GICGSSLSLR LAKRAAGAPV NPPKFLGMGY
CDYVNKSSRL GVPTNDWGII GNEVKSLYRS VNIQVSELRG VSITMAKLKD TESVKNSRQM
RLPFAKAKDK LQINDELKRI AKDASPGKPK TPERLFFKKN MSENKSSKIS TSDPSFDIEN
FDWEVLDALP YDIKLELKGE LRRRGLIPET SPTKGKVYRQ QLLPTQAGSA PKYIRVVDSP
PKKATTSPRK RKSSTPSPVK PKQKQKPQPM YQESQSYDSS VLNELPSSIK ESVLKDMEYR
KKIKKFDLAP MKDKLVRKID ETKVKVTEIT DSWINQQEKL VDDPLFLNQR LSTRDLSKRI
DDWVSSSLDQ AGPHEEDMKL FAGFISELLH QNQLNRVLIL IKQIKSKLVY QKSIMSLQEL
TEEDRLFKQE GIDDWNSQLD NQIEPLIVEY CKKRNITSIV Y
//
