ID E2B6G0_HARSA Unreviewed; 1155 AA.
AC E2B6G0;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 28-JUN-2023, entry version 49.
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=EAI_03268 {ECO:0000313|EMBL:EFN88704.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN88704.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN88704.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL445973; EFN88704.1; -; Genomic_DNA.
DR RefSeq; XP_011151758.1; XM_011153456.2.
DR RefSeq; XP_011151764.1; XM_011153462.2.
DR AlphaFoldDB; E2B6G0; -.
DR STRING; 610380.E2B6G0; -.
DR EnsemblMetazoa; XM_011153456.3; XP_011151758.1; LOC105190625.
DR EnsemblMetazoa; XM_011153462.3; XP_011151764.1; LOC105190625.
DR GeneID; 105190625; -.
DR KEGG; hst:105190625; -.
DR InParanoid; E2B6G0; -.
DR OMA; YADCTKI; -.
DR OrthoDB; 169741at2759; -.
DR PhylomeDB; E2B6G0; -.
DR Proteomes; UP000008237; 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; -; 1.
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; IPR012112; REV1.
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 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:UP000008237};
KW Transferase {ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 43..134
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 301..497
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 688..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 130397 MW; E11FA2BD3B162F20 CRC64;
MSRKKRDHAW GENGFEDWGG YMAAKKAKLE EQFRDKATKE FKESSKLFEG IAIFVNGYTD
PTSDELRHLM MMHGGIYHHY MRPRITTHII ASNLPHSKIV LYRRSQNPIP ICKPQWITES
IAAGKILNFQ NYLLYSNSTN AQPQLAYKLN IKNGKFNIES VTQDKMDAEV STNTVNNKNS
TIDINVLDEG TNNDTRIHDK INIPQSSSAR INAQSTRDTE FLSAFYSNSR LHYIATMGTT
FKDYVNELRD KSDGTFPELE RLTKSRKVRG TSSLAGRESD SEDDTIGFDN SKACNKREFV
IMHIDMDCFF VSVGIRKRPE LQGLPVAVAH AKGNVHSTSH DGKEEFGSMS EVASCSYAAR
KAGVKNGMFL GEALKMCPNL KTIQYDFEGY KEVSYALYDT VASYTLSIEA VSCDEMYADC
TKVLETSGLS PLEFATVIRE KIKRKTGCPV STGFGSNKLL ARLATRKAKP DNQFYLSGRN
AEPYIRTLNV RDLPGVGGTT THKLHEMNVR TCEQLQMVSL GLLQKEFGRK TGEQLHKMCR
GLDDTKLNLE HVRKSVSAEV NYGIRFRDNE DAVNFLSKLS TEVCSRLTAA RVKGRCVTLK
LMIRAKEAPK ETAKFMGHGL CNYITKSRNL IASVDDVGII RKEVVSIWNQ LHLTPEDMRG
IGIQISRLEI CKNKGSLKNF FDKTEKVRTC ENTSGDNNKK NQHDSKLSEA HKKNSPETPQ
TTKSATENAS SAKIDNQSSR SAQSFEFEHT AVPLAILQTD PSSLAIEAKN ETSHDRKRAN
KNIIHAAETK DPSGKSSKKT AQKQTSQENF FKHIKPSSGK SSKYEMPPRI QDLDMSVLIE
LPQDIRNEIF DEYKRSKERS RVDTETAAKN TTPLEEMNTR DEETPKTQES FSQVDPDVLS
ALMGSDLHPD VRRDVQMYCN MKREAYGVSS KETNKKEGSS DRSVEQSQEA AASSSSEICR
DGGDARHKDE TKAACGISQD VKPHAENQPC MKDDTEETES AMHRTNRIEI SRNNVAMDKA
DTFILQNLSI LHNNENVDKH QEMLINLVNH LFTLPLQQVK MQIQTWVTKS NAVNEVDFLS
LATFLSMLPQ KKRIADLHIL LKTMHRCTTK TGNCIWHRTY RRTVRHVQRY MQIEYNSNLM
VPSIGCNDSR CNNGD
//
