ID R0F1C1_9BRAS Unreviewed; 1098 AA.
AC R0F1C1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=CARUB_v10028416mg {ECO:0000313|EMBL:EOA15056.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA15056.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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; KB870812; EOA15056.1; -; Genomic_DNA.
DR RefSeq; XP_006282158.1; XM_006282096.1.
DR AlphaFoldDB; R0F1C1; -.
DR STRING; 81985.R0F1C1; -.
DR GeneID; 17876822; -.
DR KEGG; crb:17876822; -.
DR eggNOG; KOG2093; Eukaryota.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000029121; 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; 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:UP000029121};
KW Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 83..174
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 373..554
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 121925 MW; 00CEC35A511FC390 CRC64;
MKRSFGSNSS NNSGSGSNKK SKKKNNPSNQ KTLGAAWGAA SSRSSFRSAP FSDFGSYMEV
KNRKLQNQFE TEASATSHGV SGSEKLIFQG VSIFVDGFTI PSHQELKGYM MKYGGRFENY
FSRRSVTHII CSNLPDSKVK NLRAFSRGLP VVKPTWIVDS ISANRLLGWV PYQLDQLNDT
QPKLSAFFSP GSHLTPQMAS PVTSCQPDTG YSEAEEGSSI RAEDSEEARD NVNDEIDGVF
IENTTAELTE ETGTGDLKSS ETNPERLCNY DIEEKEVTSE IQSTTNLHSA SDNKSFHANG
KNAGKATVAG SSTRRHSTLE DPNFVENYFK NSRLHFIGTW RNRYRKRFHG SSNGLKWADS
GQNTAEVDKK STIIHIDLDC FFVSVVIKNR LELHDKPVAV CHSDNPKGTA EISSANYPAR
AYGVKAGMFV RHAKDLCPQL VIVPYNFEAY EEVADQFYDI LHRHCRKVQA LSCDEAFLDV
SDLRDVEPEF LASTIRNEIL ETTGCSASAG IGGTMLMARL ATRVAKPAGQ LYISAEKVEE
FLDQLPVGTL PGVGSVLKEK LVKQNIQTCG QLRLISKDSL QKDFGVKTGE MLWSYSRGLD
LRSVTAVQES KSIGAEVNWG VRFRDQQDVQ HFLQCLCKEV SLRLQGCEMI GRTFTLKIKK
RKKDAEEPTK YMGCGDCDNL SRSITVPAAT DDVEVLQRIS KKLFGSFCLD VKEVRGVGLQ
VSKLDSADLS NKGSRTLKSW LSSAPASVQI EQDDNVFSAV VRENSDRNRH VAGGVSRLRE
SNSAESSIQS GDTNSSLPPM CHLDMEVLEN LPPELLSELD GTYGGKLYEL IEKKRGKRKI
NNSSPHVSLD GTTAGIKELK PLSVKIHGLS TSGEKEYKKP FVPHLSTARA SIQHTIDMTD
LMPSSLSQVD VSVLQELPEE LRADVLGAFP AHRRQQSSSD VPMETCKKQD EEPIDIKGTE
NENGFSYRSL WFGNPPLWTE KFKVSGNCTL EFFSETYYKV AQSRPMLSPV LQHAISEIGI
FHDASANDLD EAINNMCELL KQYIKLKVEG DIEEIYLCFR LLKRLAARSQ FFLQVYEILS
PFIQATINEH YGGSLSIP
//
