ID A1CBH1_ASPCL Unreviewed; 723 AA.
AC A1CBH1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE SubName: Full=XPG N-terminal domain protein {ECO:0000313|EMBL:EAW13089.1};
GN ORFNames=ACLA_015270 {ECO:0000313|EMBL:EAW13089.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW13089.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW13089.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family.
CC {ECO:0000256|ARBA:ARBA00024023}.
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DR EMBL; DS027049; EAW13089.1; -; Genomic_DNA.
DR RefSeq; XP_001274515.1; XM_001274514.1.
DR AlphaFoldDB; A1CBH1; -.
DR STRING; 344612.A1CBH1; -.
DR EnsemblFungi; EAW13089; EAW13089; ACLA_015270.
DR GeneID; 4706356; -.
DR KEGG; act:ACLA_015270; -.
DR VEuPathDB; FungiDB:ACLA_015270; -.
DR eggNOG; ENOG502QVHA; Eukaryota.
DR HOGENOM; CLU_378548_0_0_1; -.
DR OMA; FYQTKVI; -.
DR OrthoDB; 6876at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd09902; H3TH_MKT1; 1.
DR CDD; cd09858; PIN_MKT1; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR InterPro; IPR022039; MKT1_C.
DR InterPro; IPR037314; MKT1_H3TH.
DR InterPro; IPR022040; MKT1_N.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR PANTHER; PTHR11081; FLAP ENDONUCLEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR11081:SF32; POST-TRANSCRIPTIONAL REGULATOR MKT1; 1.
DR Pfam; PF12246; MKT1_C; 1.
DR Pfam; PF12247; MKT1_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845}.
FT DOMAIN 1..99
FT /note="XPG N-terminal"
FT /evidence="ECO:0000259|SMART:SM00485"
SQ SEQUENCE 723 AA; 81207 MW; 41FAC515CF57888D CRC64;
MPIRPLGEWA AARTQSLPLS ALKGAVVGID ASHYISQHLL HHSTREPLLV ALGGFPFALK
SNIEKELQIF KELGVGCLFV FNGLDFGKKD QRPQAQAESV RAFEQAWELY DQQQADQVVD
AFSSAGTPRP GSLYKFLQRI LYQNGVDFIV APYSAAAQLS YLAQGSNPVI DTIFGPSEVL
LFDVDKLITR IDIEPSQFLW ITKQSCQEEL GRLSSDQFLD FCLLLGSSFL RTIPAFENPA
FPGKAVTVRD ALPVFNQAGR NALALCAQFE EDRRMQDIQY TDLYKRAFMT VKHHVIMDVD
GKVAPMDSDN APSDMHELIG QRLPEELYFY LSRGVLGPEI PNNLTSGEVK ISLPLGVEDT
EIYRQTASTT LTPIRTQSIC LLSNSLHRFY QTKMINVRTW FDEKSDTSIN LKTLPSVKET
IQAWKIHSHQ LPDELKKLQS TTSPLKFAVQ SLKDGDVISK SFTASKDSQK PLSTQEEILA
NVYWRFLQLR GYIDEKNQLT PWGVCLEQAL SVLDPSGNLE EATLLAIEMA RFGLLNSRQW
FSHVSGGPMR GSDEDKKFNI LISRVACIAK LQHKNIGYSG PLSRQLLCYR SLISEVRSTL
RDLIEVVLTG LLLSGDAVRD RNDWSELSLK LPFIDDNDCG LGIAVRTYLD DLPLQADPTS
PEARAEVKSK GKEWFQHSDS FAGNLDKAFK LWDAVYKGTQ NAGRDFKDAQ QWKDANNWLA
ERR
//