ID B8B1U1_ORYSI Unreviewed; 1100 AA.
AC B8B1U1;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 72.
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=OsI_24262 {ECO:0000313|EMBL:EEC81221.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC81221.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC81221.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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; CM000131; EEC81221.1; -; Genomic_DNA.
DR AlphaFoldDB; B8B1U1; -.
DR STRING; 39946.B8B1U1; -.
DR EnsemblPlants; BGIOSGA020637-TA; BGIOSGA020637-PA; BGIOSGA020637.
DR Gramene; BGIOSGA020637-TA; BGIOSGA020637-PA; BGIOSGA020637.
DR HOGENOM; CLU_003901_0_0_1; -.
DR OMA; QPRLNFG; -.
DR Proteomes; UP000007015; Chromosome 6.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:EnsemblPlants.
DR GO; GO:0042276; P:error-prone translesion synthesis; IEA:InterPro.
DR GO; GO:0010224; P:response to UV-B; IEA:EnsemblPlants.
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; 2.
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 Pfam; PF21704; POLH-Rev1_HhH; 1.
DR PIRSF; PIRSF036573; REV1; 3.
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:UP000007015};
KW Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 83..167
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 346..553
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 120832 MW; 873C51BA4419DC72 CRC64;
MSASSSGGRG APPPATAASP GQKRPRGDDP ASPSNRSESA PAKNPRRAFS SSPFADFGSY
MAAKNSKLAA QFEADASTSA AEVTGGVFAG VSIFVDGFTV PSSQELKEIM LNNGGRFVNY
FSRNTVTHII CTHLPNSKMS NLRAFSKGLP VVKPAWVVDS LAENRLLSCS FSSPSLTNSL
LLEGSQDHNS GCEKEGSLLK EEASKDSLSS DDHKASMFEE QDSEDFVDEA GNAYETACSE
RRDNDMDGKL HVAESPDIRS RCSNLCSTSS TGSHLSLDSL DRNATKSSSR THSTLTDPNF
VENYFKYSRL HFIGTWRNRY RKRFSNLLGD KSSKGNRDHS GKNNTIIHID MDCFFVSVVI
RNKPELHDKP VAVCHSDNPK GTAEISSANY PARNYGIKAG MFVREAKARC PHLMIVPYDF
DAYGEVADQF YGILHKYCSK VQALSCDEAF LDMTECLHDN PEEVTQKIRN EIFGTTKCSA
SAGISGNMLI ARLATRSAKP NGQCFISSEK ITPGDPAFSK KAHKQGSVTT KQTKKKVDGY
LNTLSIKALP GIGHTVSDKL KSKEVEYCGQ LRNIPKESLH KDFGKKIGDM LWNYCRGIDH
SVVEAVQETK SVGAEVNWGV RFNDNKDAEN FLVNLSKELK TRRKGAGEPI KFMGCGDCET
VSRSMTIAGA TDNPVTLQRI AKQLFSSFFV DVKEVRGVGL KISRLEHADL ARGAPQGNML
ESWLASPSDK LKKHSTEKAC LLKNRDDAAT SERRGFGSIR PSGIGGTSRS SEVNPPSDRS
TRVGVELPPL SELDLEVLKN LPPEIIYEMN DMYKGELHGF LGITSGDKAR ESNTKSLVFP
AVDQNLVPVL DTKLHGDGKH KDSIHFKKEA DIKGPSGEQL SELKQANAPR SIASELVDIP
TKSVIQHDFM PNSLSQADVT VLQELPEDVK ADLFNALPLH RSGDPTCSTS HVSENKFPQD
GRSDDPKQHP QICHLPGNSQ KWIEEFRVSH CLILNVIAEQ HTDSISSRPL SSVLEPVISY
LPLCPNSGTE EWNEAFASLS ELLTQYIHQK VESDIEELHK CFRLLKRLSS GSELFLELHD
SILPLLQDSV RQHYGGILHL
//
