ID A0A1X7RW30_ZYMTR Unreviewed; 1206 AA.
AC A0A1X7RW30;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=ZT3D7_G6748 {ECO:0000313|EMBL:SMQ51595.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ51595.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ51595.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; LT853697; SMQ51595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RW30; -.
DR STRING; 1276538.A0A1X7RW30; -.
DR Proteomes; UP000215127; 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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:UniProt.
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; 6.10.250.1630; -; 2.
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; PF16589; BRCT_2; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR Pfam; PF16727; REV1_C; 1.
DR Pfam; PF14377; UBM; 3.
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:UP000215127};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036573}.
FT DOMAIN 61..149
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 411..609
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 190..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1206 AA; 132959 MW; 0F9B059C2E9B4540 CRC64;
MGSRLEEKSK LVRKRIEGHT FQDEGGEEYE GSKFGGFSDY FRRKKIKLQN LDAEVRAQTS
DKPQIFKGVT CHVNGYTQPS LNDLHTMIVQ HGGGFLQYLD GKTMVTHIIA SNLTPKKKEE
FRRYRIVKPA WVVDSVKAGK LLPWNEYRML DEGVAQKVLG FENGQVVTQA NRRTQGYREQ
TDASWYTSQF NAASSTAGPS KPAFATQTVT PSEEIEDDDD FPLPEVTSSI EEALDEASRL
HSKQQAEPLP AEPSTDLQTP PPTSPPPHHS PATRDEPAQT VEAATATPEK PKDAALGLLS
NGKRKREWEG LEPDYSMAVV KNSNVWDSVS PSKLAAMTAE QHNSLILSDP NIRKSTVVNP
GFLQQYYDQS RLHHLSTWKA DLKSQLQAIA AETSASQKSR QKRLPGQRRY VMHVDFDSFF
AAVSLKKHPE YNDKPTVVAH GNGSGSEIAS CNYPARKFGI SNGMWMKRAL ELCPELKILP
YDFPAYEDAS RKFYDAIMAT GGLVQSVSID EALIDISTIC IAESGQDGVK RSEGAVHREQ
SKADELGQRL RDEVLEKTGC AVSVGIGANI LQAKVALRKA KPAGQYQLKP EDVLDFIGQL
EVQKLPGVAW SIGGKLEEIG IKLVKDIRDV SRERLINTLG PKTGEKIWEY ARGIDKTEVG
DQVVRKSVSA EVNWGVRFEN NDQVDEFMQG LCGELNKRLV KERVKGKQLT MKVMRRAANA
PLDPPKHLGH GKCDVYNKSS QLGVATNDPS VITKEAIAML RSFKISPGEL RGIGVQMQKL
EPIKSGVDGV DQGSQRRLQF KAGPVAKPVV EDEPSKAVED AIVDDIKTPQ KARIPAANRP
SAAFTPIEPG TPSRKPLNTL GTQFILPTQV DPAVLAELPE DIRAKLAKHV PKPEAKKLDL
LPTANVPSRA QSPAVGLPTL TQIDPDILSA LPDDVRDEIL GFYNQPAPAK RPEQAVLPQS
PRKTRTLPAP RQPVKRGRGR PRGGSLLSNR LRSAAGESST LTQSNFVSRP SVPTTTSATT
TDNELEDIDP EVLAALPEDL RLEVLAQQRS AKLQRTGGID LSLHARPKTG KTKKLTSHIP
GEVLATGDRH FLLPPHAPKP SFTSRKLTEV EELRTAIKAW FEEFRDEGPY GEDVEALGKY
LGEVVGSEGD LEKAVKVAKW VGFVVEEGVE EWDEEDVIGR WRDAVARVEE CVRLKARERG
IEGVVF
//
