ID A0A178APP9_9PLEO Unreviewed; 1222 AA.
AC A0A178APP9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=IQ06DRAFT_306669 {ECO:0000313|EMBL:OAK99616.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK99616.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK99616.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK99616.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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}.
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; KV441714; OAK99616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178APP9; -.
DR STRING; 765868.A0A178APP9; -.
DR InParanoid; A0A178APP9; -.
DR OrthoDB; 169741at2759; -.
DR Proteomes; UP000077206; 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: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; 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:UP000077206};
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 397..595
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 190..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1100
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1222 AA; 134595 MW; 855F012AB514DF24 CRC64;
MGSRLDKNSD SVRKRIEKHT FDGEDGEEYK GSAFGGFTDY FRRKKIKLQN LDADIRAQAG
DKPQIFKGIV AHVNGYTQPS LNDLHTLIVQ HGGGFMQYLD GKTTVTHIIA SSLTPKKVVE
FRKYRIVKPA WVVNSIQAGK LLPWNEYRVV DEGEKQNVLA FDNGKVMSQA NVKARGYRDQ
TDASWYTGQL RASQAGPSST PTPSGSMRSH FSKQRLPTPD DDIDDGEDLP PSHQPESDPI
EQAPVTSEKP QDLVTPPKSS PTIAAQDDPF ADDELDADAA FHDSLYDAPP PDPPNAAQGM
VDDRVMDFIA AAGTTAAADG RQLTAEEHNA ILLRDPKIRK STVVDPNFLE QYYRESRLHH
LSTWKADLKS QLQALAAEKT STQKAKQKRP QGARTYVLHV DFDSFFAAVS LKKNPQFKDK
PAVVAHGQGS GSEIASCNYP ARKFGVKNGM WMRRAQELCP DLKILPYDFP AYEEASRAFY
DAILATGGLV QSVSIDEALI DVSSMCIAAG GSDGRKASEG SNYREQAKAD EIAQALRTEV
KAKTGCDVSV GIGGNVLLAK VALRKAKPAG QHQIKPEEVL DFIGELQVQD LPGVAWSIGG
KLEEIGVKYV KDIRELSREK LVQTLGPKTG EKLWEYARGI DRQEVGEQVV RKSVSAEVNW
GVRFENQEQA DEFITSLCGE LQKRLIKERV KGKQFTMKIM RRSPDAPLDP PKHLGHGKCD
THNKSMVLGV ATNAKEVLTK EALSMLRGFG FTPGELRGIG IQMTKLEPMK SATDGSLEGS
QRRLQFKVGN TEPVSARKIE KVVDEDPIQD EPETPRKPKV MTEEEQLAFG ASELNHSTPS
RRPLNVLGTQ FIMPSQVDPK VLAELPEDIR SKLLRQTRQT SPSPAARSPA RNAVTTTPTK
ALPFAMTALP AQSQLDPDIL AALPPEVRAE VLAQYAAGAT PASPSRRPRN ADQTLLPQSP
RKNRLIGIPA KKPIVPVKRG RGRPPRSAML AAAAQTTSLS KTGKTLTQAN FISRKNPIRE
DGGRETPAGT AADGIATAAH RPKDDDLDTD FLSALPPELR AEVVAEHKRK KLQAFRLALN
KSKPKHIPAP PRPAQRIKVP RPPCPTFTTQ KLSQTPDLRK AMKEWVKEFA DEGPYVEDVG
ALCKYLGKVV REERDLGKAV GVVRWLEWVV DDEEEVDESI VMKYMNRYAV SCAYPIDPNP
AGEVLGYMPC VVSCRVIDYN RV
//
