ID X0AVL8_FUSOX Unreviewed; 1139 AA.
AC X0AVL8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=FOMG_01044 {ECO:0000313|EMBL:EXK47820.1};
OS Fusarium oxysporum f. sp. melonis 26406.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089452 {ECO:0000313|EMBL:EXK47820.1};
RN [1] {ECO:0000313|EMBL:EXK47820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK47820.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum melonis.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EXK47820.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=26406 {ECO:0000313|EMBL:EXK47820.1};
RG The Broad Institute Genomics Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "Annotation of the Genome Sequence of Fusarium oxysporum f. sp. melonis
RT 26406.";
RL Submitted (MAY-2012) 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; JH659329; EXK47820.1; -; Genomic_DNA.
DR AlphaFoldDB; X0AVL8; -.
DR VEuPathDB; FungiDB:FOMG_01044; -.
DR HOGENOM; CLU_003901_1_1_1; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 2.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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 60..148
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 357..555
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..945
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 126771 MW; C156A39678416827 CRC64;
MGSVLEKNSS QVRKRIETHK FEDEGGEEYE GSEFNGFNDY FRRKKIKLQN LDAEIRANSD
KPQIFKGIVA HVTGYTQPPL HVLHREIVQH GGGFLQYLDS KTMATHIVAS TLPPKKSVDF
SRYRIVKPAW IIDSIKAGQI LPWSNYRVLD EGPRQKVLKF DGGSGLSPST PRSKQGYREQ
TENSFYANQF KASSLPSQSL SQVVEKARTP LRPTNGADTT PLMADVNSLC FKKPATPPGV
SPKDQLVVAS LDLEATDGEM LGPETGILPV PVAQFTHPDT SKPMTSEEHN AMLLSDPRLR
KSSTANPDFL RQFYSESRLH HLSTWKAELK SKMQRLAAEK GQSCQKAKKR LGARRYVMHV
DFDSFFCAVS LKKNPEYIDK PAVVAHSTGS GSEIASCNYP AREFGVKNGM WMKSALEMCP
ELKVLPYDFP AYEEASRLFY ESILDIGGLV QSVSIDEALV DITPIVLTNS NSEGTGSDAE
NTAREHDMAD KLAKDLRDKV KSLTGCHVSV GIGANILQAK VALRKAKPAG QYQLKSENVL
HIMGDLKVDQ LPGVARSIGG KLEDIGVTHV KDLREVSKER LTSILGPKTG EKLREYARGI
DRSEVGEQPP RKSVSAEVNW GIRFISQPEA EEFVCNLCKE LEKRLSNENV KGRQLTMKIM
RRAIDAPLDP PKSLGHGKCD TFNKSITFGV ATNDGQAIGK EAVNILRSYK FSPGDLRGLG
VQMTKLEPVK INFAAPDGSQ KKLAFGTFTK PSPAREASST EQIDEIESPG KQRQTPSREI
CQDPIADDPL TPRKQKIHPA MALTKASDDD VKAKTHLNIS GTQFIIPSNA DATILAELPN
TIRRKLMAQG SRMSDIHVES PITESRSQSP MPSDACPTQV DPEVFNALPD EMKTEILATY
GRKTRQTTPL KSPHKDSAME SRKPPTPSKR GRPRGLFGKA QRQRDAQAGL LQTNFRSLNQ
VGDAFEDEDI EELDPEFLAE LPEEMRKEVI EQHRKRQRAR ETSLETPLRR NSTPNPEGLL
PGGQCRIQFP VVPRKISFST SGVTSTREIK DMIDAWHSET RRLGPHRRDL AVLEDFLVKV
IQEERDLEKA TKLVKWLDVI VEQDGRKGRG QEVWRRSVEA IKVIVQDAVK QLGMAPLKL
//