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Database: UniProt
Entry: H6BRC5_EXODN
LinkDB: H6BRC5_EXODN
Original site: H6BRC5_EXODN 
ID   H6BRC5_EXODN            Unreviewed;      1904 AA.
AC   H6BRC5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Adenosinetriphosphatase {ECO:0000313|EMBL:EHY54706.1};
GN   ORFNames=HMPREF1120_02871 {ECO:0000313|EMBL:EHY54706.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY54706.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY54706.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY54706.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., 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., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; JH226131; EHY54706.1; -; Genomic_DNA.
DR   RefSeq; XP_009155167.1; XM_009156919.1.
DR   STRING; 858893.H6BRC5; -.
DR   GeneID; 20307510; -.
DR   VEuPathDB; FungiDB:HMPREF1120_02871; -.
DR   eggNOG; KOG0392; Eukaryota.
DR   HOGENOM; CLU_000315_1_1_1; -.
DR   InParanoid; H6BRC5; -.
DR   OMA; WYSDIAC; -.
DR   OrthoDB; 180798at2759; -.
DR   Proteomes; UP000007304; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   CDD; cd17999; DEXHc_Mot1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
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; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR044972; Mot1.
DR   InterPro; IPR044078; Mot1_ATP-bd.
DR   InterPro; IPR022707; Mot1_central_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR   Pfam; PF12054; DUF3535; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1330..1503
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1678..1826
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          184..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          240..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..744
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1904 AA;  211038 MW;  029A0F19E2A857F1 CRC64;
     MAASRLDRLV TLLDKGSTQL IRNTAAAQLA DIQKQNPDNL FALLGRVLPY LQSKSWETRT
     AAAKAIGGIV SNVPKFDPNA DEAEIKDEVP KSEDGELKVE VKTEDKVQEA DDLLQLATLD
     IKMILRHGKK LLGSAGKEYE YSMAGMTPAQ RLHHQKQSLT ARLGLGGEYM EEDLVTENDF
     AATSQHKLAQ TPGPPRVDTK SAGQRTDSIG APSPYSAMSP SENGQPFLEE SGLSKRQLNQ
     LKRKNKSAAK VGASKMRVVD LSGRRPSEPG QTPVSATPHP VKLNGQDESN GDSKQDYFSI
     KREGPDDNTA LISEFKGDVV EEKPLIQPDE EHSHDWPFEV MCDFLSIDLF DPNWEVRHGA
     AMGLREVLRV HGRGAGRRYG RSRAENDLAN RRWLDDMACR LLCVLMLDRF GDYVSDTVVA
     PIRESIGQTL GALLTQLPDD TAVSVYNFLQ QMINQSDTGL KQPIWEVCHG GMIGLRYFVA
     VRKDLLLQHN ALIDGVVSAV IRGLAHPDDD VKSVSAATLV PVAGELTTIR PQSLGQLIGV
     VWDCLLDMQD DLSASTGAVM DLLATLCSYD ATLEAMRKNA AEDPEQSFEM LVPRLYPFLR
     HTITSVRLAV LKALVTFLNL SNVNNMEWVG GRVTRLLFQN MLLERNEGVL RMSFEVWEAL
     VAFMERQGMA KFAPNLDPHI MPMLKATIQP VGQSRSPIPM DASLLIKPSG TPMATSAPRQ
     GSASDADQQP KKRRKVDKAD KADANQQPSH NTDGHMLHGE VDLVGMEVIL RTRITCSRAL
     GLLLGKQNEA AVASYWTSLL PIINSNHSSS RLFTGMILEE LARNQSIKPT DTASCVAQLQ
     SVLDDDGHHW YSDIVSSLQA ARGQCQSLIS AFQNNAHVSR DKLPAIAVVC QGENGAGPKA
     FSLADAEKIV TTDFDRLLKS LTPAQRVSGT QYLNDARTNA MTAVEEARKI KEGRDLAIKA
     AVASVLVRLG EIPKKPGQLI KCIMDSIKGE EFEELQARSA SAVAALIDFY TRGAKKGPVD
     KLVSNLVKFT CVDTSETPEF GPNAKFEDIV LSLRKEEDRK DHPDAAKFEQ EAKEARIMRR
     GAKRALDELA QSYGGELLEK LPVLKSLIEN PIGELVEPAD PATLQVDEER GQSLIDAFSI
     LRTLSPTLHP TLHPWILSLS PLIGKAMRSR LSVVRYSAAK CFATICSVIP IEGMTMLVQD
     ILPNISNPLD LRDRQGITEC VYHLIWVMGD RILPYVIFLI VPVLGRMSDA NHDIRLLATT
     SFATLVKLVP LEAGIPDPPG MPESLLQGRE RERKFMAQML DPKKVEPFQI PVAIKAELRS
     YQQEGVNWLA FLNKYNLHGV LCDDMGLGKT LQTLCIVASD HHMRAEEYAK TKAPDMRRLP
     SLIVCPPTLS GHWQQEIKQY APFLSCVAYV GNPMERNSRL HLLEQADVVI TSYDVCRNDN
     DVLAPITWNY CVLDEGHLIK NPKAKITQAV KKLVSNHRLI LSGTPIQNNV LELWSLFDFL
     MPGFLGTEKV FQDRFAKPIA ASRNAKSSSK EQEAGALAIE ALHKQVLPFL LRRLKEEVLN
     DLPPKILQNY YCDLSDLQKR LFEDFFKKER KTVENSIGAA DKEAKQHIFQ ALQYMRKLCN
     SPALVVKEGT KQYETISKQL AASKSSLRDV AHAPKLTALR DLLVDCGIGV SNDSNEMSAS
     NYVSQHRALI FCQMKEMLDM VQNEVLAKLL PSVQFLRLDG SVEATKRQNI VNQFNNDPSY
     DCLLLTTSVG GLGLNLTGAD TVIFVEHDWN PQKDIQAMDR AHRIGQKKVV NVYRLITRGT
     LEEKIMSLQR FKIDVASTVV NQQNAGLGSM ETDQILDLFN LGEGTDTGGE SGGAGKEEDM
     VDLETGEVKK KGEKGWLDDV GELWDERQYE EEFNLDSFVQ NLQK
//
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