ID A0A182JNL6_9DIPT Unreviewed; 1178 AA.
AC A0A182JNL6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=DNA repair protein REV1 {ECO:0000256|ARBA:ARBA00020399, ECO:0000256|PIRNR:PIRNR036573};
DE EC=2.7.7.- {ECO:0000256|PIRNR:PIRNR036573};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR000100-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR000100-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR000100-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 AlphaFoldDB; A0A182JNL6; -.
DR STRING; 43041.A0A182JNL6; -.
DR EnsemblMetazoa; ACHR000100-RA; ACHR000100-PA; ACHR000100.
DR VEuPathDB; VectorBase:ACHR000100; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000075881; 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 CDD; cd12145; Rev1_C; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 6.10.250.1490; -; 1.
DR Gene3D; 6.10.250.1630; -; 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 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; PF00533; BRCT; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF16727; REV1_C; 1.
DR Pfam; PF14377; UBM; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 41..127
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 352..580
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 187..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1178 AA; 131907 MW; 94C9ECA6AE29A38D CRC64;
MKRKEKKESE TGFEGWGDYM DAKIAKLEDQ FRYSTANVGE KQSDLFAGVS IFVNGYTNPS
ADELKRLMML HGGVYHHYKR PNTTYTIASN LPDVKVRSIT SEIIISPRWV VDCLNEGKLL
DYSRYLLYTQ HKPSQPKLAF AKLAPSTSRA IDITKPVLKN DGDPNDISRS ECLNVLGMLK
NFTNPASEWS VPSVQQPQSE TPIGGDTPID PKPTNVVTGA SSPPMSNEQE KESQLSPQCS
PDVFPEDDPP SVDTSVQSSA IMKSPHKPAP TKQSLTATDP NFLAEFFNNS RLHHIATLGA
GFKQYVAELR EKSTGSFPAR DTLVQQLGCG RVGTRERERE CEFTNEPNAR YIMHIDMDCF
FVSVGLRKYP HLRGLPVAVT HSRGSEARVP SHPGQNRALE IELYHKRLEQ RYKAPDIPIE
SRLAAIDEHN SLSEIASCSY EARRCGVKNG MFVGAALKLC PELKTIPYDF EGYREVAHQL
YDTIAQYTLD IEAVSCDEMF VDLTELVQST GIDVMEFVSY VRNEISSATG CDCSAGIGAN
RLQARMATKK AKPNGQFHLA PSAVEEYMRA IPIAELPGVG PSTSHRLKKM TYVSCADLQT
IPKNVLQTEF GKKFGETLYN ACRGIDEKPL VYDRGRKSVS VDVNYGIRFS TDQEVDRFMR
QLTEEIHRRL VELRQRGKLV TVKLLVRSPE APVETAKFMG HGLCDVVTKS QPLRQFTDDR
CVIEGAVLGL MRTLAIAPSE LRGIGIQISK FEGTKHTADN EAGNRLKSMF QKVEDKKKPS
EEMARMDPDS AMGTESNRQR LPEFHQPDDQ QPCTSYNHNT VHTIPAAVRQ SYITPTKADY
NGTIISPKRS DNAAYSPSSR KAAGGSKSST RGRRGRPPKW ASISGRKDPA KTAQSVGVMR
KFLTGSVGSS CFGSELPAGL DPEVLAALPE DIREEAIRDY RRQQQQQQLL TANNRVHQPP
AEKTPVKNSP ARDASHREWK SPVALQNTGS GAEQDQKIKV ELKFLQALPL ELRLEVEKQI
ELNKDNMVVT CNEPEIDEPL LVTPENSPVK EQTPVQGNLT AVPDIELTEP ARDPNILRRR
NWRELVEEWI DSTEQPYEYD VLLLATNGQE LCEDKSLDQL YLFLRCLHRL VQETGNCYWH
QAFGKVVRPI QERMFAIYGR RLAVPAKIMC NLCNNNMV
//
