ID A0A2T5M915_9EURO Unreviewed; 1040 AA.
AC A0A2T5M915;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA excision repair protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=P175DRAFT_0471798 {ECO:0000313|EMBL:PTU25026.1};
OS Aspergillus ochraceoroseus IBT 24754.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU25026.1, ECO:0000313|Proteomes:UP000244073};
RN [1] {ECO:0000313|EMBL:PTU25026.1, ECO:0000313|Proteomes:UP000244073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU25026.1,
RC ECO:0000313|Proteomes:UP000244073};
RX PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT "Linking secondary metabolites to gene clusters through genome sequencing
RT of six diverse Aspergillus species.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTU25026.1}.
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DR EMBL; MSFN02000001; PTU25026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5M915; -.
DR VEuPathDB; FungiDB:P175DRAFT_0471798; -.
DR OrthoDB; 5399336at2759; -.
DR Proteomes; UP000244073; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR029256; Heliccase-ass-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF14773; VIGSSK; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242}.
FT DOMAIN 254..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 625..779
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 117818 MW; E15A2B204259C921 CRC64;
MGSRQDLDAV DAITIDSDDD DDLDFTRPIT KSVSAHPTTP TTTPHRDAVK FEKISPPIRS
STPPPDVAVK QPSPDQKTTG ESSSDDGSMN EGEAVYQEFK NRKSRKRKRS SVNVGKNNKA
TKVATPNSIV GRIPKQESKA SRPRRSREYR EDVQSEDELM EFTLPDYLQK RRLLFDRRVE
QLTQAGLKLP PDYDQVDFSD DERLEFLQEK PAFKEISPCN EYKDILLPFS LGLIPAPVAQ
WLRQYQVDGA AFLHELFVYQ RGGILGDDMG LGKTVQVIAF LTAAYGKTGD ERDAKRMRKM
RRNEREKWYP RTLIICPGTL IQNWMSELSR WGWWHIDTYH GDNKDLALHA AKSGRVEILI
TTYSTYLHNK DSVNMVDWDC VIADECHAIK ERTSETTKAM NDINALCRIG LTGTALQNKY
EELWTLLNWT NPGKLGPVTT WKRTISEPLR VGQSHDATIY QLRRARITAK KLVENLLPQF
FLRRMKTLIA DQLPKKVDRV VFCALTETQA EAYENFLNSD IIRYIKTSSE RCDCGSGKKA
GWCCQRKLPS GALWQSYVFP AIAVLQKLSN HLAILIPQGG DSYEKQEKDK EMLEIAVPGQ
WENLYRTRDS IVNYANPEFC GKWKVLRRLL KWWHSNGDKV LVFSHSVRLL KMLQMLFHYT
SYNVSYLDGS MSYEDRTKVV DDFNADPRQF VFLISTRSGG VGLNITSANK VVIVDPNWNP
SHDLQAQDRA YRIGQSRDVE VFRLISAGTI EEIVYARQIY KQQQANIGYN ASSERRYFKG
VQEKKDQKGE IFGLANIFEY QNNNIVLRDI VNKTNIAESK AGVQVIGIDL DADADADTPL
PPLAPTPDAS SKVKTQAPKD NDEVMSQLAA MIRGDQDASA SVSKTSASPP GKHDPIQAIL
AGAGVEYSHL NNEVVGSSKV EEHLSRRAEL AGDNMANHQV FGGCPQSDRR GTVASAFLQR
NGRVVRFKYH PPGEVMKRQF CSMARWFGFP NATEFALVVE SMTQAQRRAY LEKWYQERRR
VLLEGSDEGS DEQSDEGLSA
//