ID A7E7M1_SCLS1 Unreviewed; 1255 AA.
AC A7E7M1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
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=SS1G_01299 {ECO:0000313|EMBL:EDN96373.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN96373.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(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; CH476622; EDN96373.1; -; Genomic_DNA.
DR RefSeq; XP_001597105.1; XM_001597055.1.
DR AlphaFoldDB; A7E7M1; -.
DR STRING; 665079.A7E7M1; -.
DR EnsemblFungi; EDN96373; EDN96373; SS1G_01299.
DR GeneID; 5493677; -.
DR KEGG; ssl:SS1G_01299; -.
DR VEuPathDB; FungiDB:sscle_01g009860; -.
DR eggNOG; KOG2093; Eukaryota.
DR HOGENOM; CLU_003901_1_1_1; -.
DR InParanoid; A7E7M1; -.
DR OMA; IKNGMWM; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000001312; 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:0017125; F:deoxycytidyl transferase activity; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0070987; P:error-free translesion synthesis; IBA:GO_Central.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
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; -; 3.
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; 3.
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:UP000001312};
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 437..635
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 139437 MW; 3FC6DCB1AA3EE8E8 CRC64;
MGSRLDKNSE SIRKRIESHT FQNEGGEEYE GSKFGGFSDY FRRKRIKLQN LDAEVRSTST
GNPNIFRGVV AHVNGYTQPS LNDLHHLIVT HGGGFMQYLD GKTTVTHIIA STLTPRKAIE
FKRYRIVKPA WVVDSVKAGK CLPWDSYRVL DEGVGQRLLG FSDGKVVSHS NTPQRGYRDQ
TNASWYTSQV KTVAGNIDDD DGPQFPSSQV QRIMPHKTGA FAPSPTDQLV ESLEEVDQIP
VDDPISSTGS FEVTSSLEEA LKHAADIPTP TSREALKSTR TAKDSFLMNN SPSPSPALQT
SSSPAQVTPK RPEFLLGNTK ILHDVEASRY AEEVPVERRL FSNAKKRPHN EETYNSPKKA
QVETAEEHNA MLLADPHTRK SSTANPDFIK QYYSESRLHH LSAWKADLKS KFQQMASEKS
ASQKQSMKWK PGSRRYIMHV DFDSFFCAVS LKSAPEYFDK PAVVAHGNGT GSEIASCNYP
ARVFGVKNGM WMKNAIKLCP DIKVLPYDFP AYEEASKAFY EAILDVGGIF QSVSVDEAFV
DITSLCLAAG GTDGVGIREG SIWREQERAE EIGNALRKVI REKTGCNVSV GIGGNILLAK
VALRKAKPAG QYQIKPEEVL DFVGELDVQN LPGVAYSIGG KLEEIGVKFV KDVRQLSKDR
LMTVLGPKTG EKIWDYSRGI DRAEVGEQVV RKSVSAEVNW GIRFISQVEA EEFVQNLCIE
LQRRLIDQRV KGRQMTMKIM RKAADAPLDP PKFLGHGNCD TFNKSIVLGV ATNDATIIGR
EAVSILRSYG FSPGELRGLG VQMTKLEPVK SSNGTPFDGS QRKINFGAPV VSKPVKQVVE
DPIVDDPETP TKRRTTPRAQ PTNPLSEGIH DPVTPTKPKS IMKSIHTEDP IDESSPLKAK
PTPAHPATFI ARTNAGDQSA RKLNLTGTQF IIPSQIDPEV LKELPQNIRS KLMAQSKSVP
VSREQTPVTA MPESLSKSPS RLKTSHMPSQ LDPEVFDALP EEMKAEILAS YKPQIANSIP
GAQSILPQSP RRNRTITGKK PPTPVKKRGR GRPPGPRIKS EPPHGPLQSK FVANPRAREV
SVDATDDTEV LDPEFLAALP EDMREEIMAE HRRKRLQKRG NLMTSTVKKV KKPDPPPLGP
RKIRLPPRPI KPTFTTQELS TLEELRETLT IWFREFESEG PHPDDVAAME RYLRRVILDE
RDLAKVVGVV KWLEWLKDDS EIVGKGKELW ENAFEDVKSK VQEAVKERGL GILDI
//
