ID V7CGH7_PHAVU Unreviewed; 1133 AA.
AC V7CGH7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=PHAVU_002G053200g {ECO:0000313|EMBL:ESW29219.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW29219.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002289; ESW29219.1; -; Genomic_DNA.
DR RefSeq; XP_007157225.1; XM_007157163.1.
DR AlphaFoldDB; V7CGH7; -.
DR STRING; 3885.V7CGH7; -.
DR EnsemblPlants; ESW29219; ESW29219; PHAVU_002G053200g.
DR GeneID; 18637020; -.
DR Gramene; ESW29219; ESW29219; PHAVU_002G053200g.
DR KEGG; pvu:PHAVU_002G053200g; -.
DR eggNOG; KOG2093; Eukaryota.
DR OMA; QPRLNFG; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000000226; Chromosome 2.
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: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; PF00533; BRCT; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
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:UP000000226};
KW Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 95..186
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 396..577
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 125924 MW; 5E4954A5865C310D CRC64;
MSLDSSRSAN SKRSFSNSIS SNRSNDSSKK NSKKTKTITN QKTLGAAWGS NASSRSSSRN
SAFSGFTSYM TEKNRKLHNQ FDAEASTSSL SDSASGKPIF SGVSIFVDGF TVPSSQELRS
YMLKYGGRFE NYFSRHRVTH IICSNLPDSK VKNLRAFSAG LPVVKPTWIL DSVAANRLLS
WVPYQLDQLA NKQSKLSAFF TFKSSKMSED ALTNSLCQVV SDVEDSSIRV GQTDSEDRNL
SKVGEMSEHS GQISAASDDI VLENSNAIMT EELNSVRIKF DEDQAAGSNA ATKDESNVKG
ELESTNQAPS TSFSSHCSEE QNAREFPSSS GTKPFKQCHS TFADPNFVEN YFKSSRLHFI
GTWRNRYRKR FSASSSGIKN ENSIISGSSI SHNSVIIHVD MDCFFVSVVI RNHPELSDQP
VAVCHSNNSN GTSEISSANY PARSHGIRAG MFVRDAKALY PDLVIFPYNF EAYEEVADQF
YSILHQHCNK VQAVSCDEAF LDVTDLEVED PKLLASSIRE EIYKTTGCTA SAGIAGNMLM
ARIATRTAKP NGQYHITTEK VEDHLYQLPI NSLPGIGHVL QEKLKKQNIY TCGQLRIISK
ASLQRDYGIK TGEMLWNYSR GIDNRLVGNF QESKTVGADV NWGVRFKDTK DCEHFLINLC
KEVSLRLQCC GVQGRTFTLK IKKRRKGADE PVKFMGCGDC ENLSHSVTVP LATDNVEILQ
RIVKQLFGCF YIDVKEIRGI GLQVSRLESA EASKQGTTKY TLKSWLTSGC ASVGNQKYPI
GHDKQSRDNT SRHASVNLPE SSVEMDNKIP NNEASTDPIS TPPPLCNLDM EVIRNLPPEV
FSELNEIYRG KLIDYIANWK DTSESSSPSG NSFLEQKAIN NEEELSYSGP IPQSNLLSKN
KAKQYVSGTS EGEDITYSVC GPSFKVTHHS SFENNDLLPS SLSQVDGSVF QQLPEDLKAD
IVEQLPAHRR PEICSNVVIP PLENNLLSVG VEISDNSPIS SYNDSLWVGN PPNWVGKFKG
SSCLILKKLA EMYFRSGLES TLSSVLHQNI SEFCELNLAQ QFSDETVNIM CELLRQYIKV
KIERDIEEIY ICFRLLKRFA AMSQFFLQVY NSVYPYLQAA VEDNYGGTLL LPS
//
