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Database: UniProt
Entry: W2M8P3_PHYPR
LinkDB: W2M8P3_PHYPR
Original site: W2M8P3_PHYPR 
ID   W2M8P3_PHYPR            Unreviewed;       900 AA.
AC   W2M8P3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=L914_20610 {ECO:0000313|EMBL:ETM31889.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM31889.1};
RN   [1] {ECO:0000313|EMBL:ETM31889.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM31889.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica IAC_01/95.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KI696455; ETM31889.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2M8P3; -.
DR   EnsemblProtists; ETM31889; ETM31889; L914_20610.
DR   VEuPathDB; FungiDB:PPTG_06195; -.
DR   Proteomes; UP000054532; 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: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; 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   Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT   DOMAIN          28..118
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          242..421
FT                   /note="UmuC"
FT                   /evidence="ECO:0000259|PROSITE:PS50173"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          141..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..162
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        672..687
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   900 AA;  99715 MW;  C1D9CB1AC8BFAB88 CRC64;
     MSHKVQKLRS QNESFTAAAS PDRASSGNNA GIFQGIHVYV DGYTVPSKED IRQLMLLYGG
     GFEHYETGRV THIVATHLPA SKLLQLKKAR KPLPVVHPEW VVQSIEQHKL LPVQSFLYAG
     FTDPTQNNIF SLSGSYNFAQ LEDKPSSNEE PDDEDDELDV PEDPPASPPQ VASNKNSTTT
     LKLRTNSTKD GPEFVRHFFA KSRLHHIGTW RATFQQKAAE FQAKYKGAPI NRAPASSSDR
     VILHVDMDCF FVAVAVRDKP ELHKVPVAVA HSGNAGSSEI SSCNYLARAK GVGAGMFMQT
     AKELCPELIV LPYQFDDIQR VSFQIYDIFF LHTPYVQAMS CDEAFLEFGR GTNGMEKAKA
     IRNEIFEQTG CSASVGVSFN VLLAKLSSKK AKPDGIFEIS NVSQAEEFVL QLTIRDLPGA
     GHMTSAKLEA LGVENVRQLV SMTKGELIQS LGKASGEMLY NYARGIDIRP LSMESNMMRK
     SVSAVVNFGI RFEKWEDATV FLMALGEELS QRLRNLNVRA KCLTLLIKKR AGGAPVEPAK
     FMGHGVCDNF SKSQILAQPT DDEVVIGKAC IELLQQFNFP SEELRGVGVQ ATKLISDTPG
     NQRSGQLFKA WLKDTTGNAK NQEECEAKAE DPITETSTNA FAATSFSQIN IGVLGELPKQ
     LQQEILASYG RGASATTTQT NYQPPPRRKT NGKAPLRRKH PARNIFDSKS NSRLARNVHL
     LGTGDSGKED ALDDIRMSQV DSEVYHSLPL TIRREIDRYA KKRRPTSTVA PIPRPRASSI
     SSPEQPVKKK LTPVVLPRIE DLYADLVESL HDEYPTTGTR AQTAAFDPIY SRILVEVEDR
     ALDQALRMLR FVRRKCSSVA TPTELAEQLK RGFNHVLNLV NQDIRRQFNG ALSLRLVTPL
//
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