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Database: UniProt
Entry: A0A2T5M915_9EURO
LinkDB: A0A2T5M915_9EURO
Original site: A0A2T5M915_9EURO 
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
//
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