ID H6C2S2_EXODN Unreviewed; 1120 AA.
AC H6C2S2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Adenosinetriphosphatase {ECO:0000313|EMBL:EHY58796.1};
GN ORFNames=HMPREF1120_06799 {ECO:0000313|EMBL:EHY58796.1};
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:EHY58796.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58796.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58796.1};
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}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; JH226134; EHY58796.1; -; Genomic_DNA.
DR RefSeq; XP_009159257.1; XM_009161009.1.
DR AlphaFoldDB; H6C2S2; -.
DR STRING; 858893.H6C2S2; -.
DR GeneID; 20311438; -.
DR VEuPathDB; FungiDB:HMPREF1120_06799; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; H6C2S2; -.
DR OMA; TAFYRKE; -.
DR OrthoDB; 5482994at2759; -.
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:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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}.
FT DOMAIN 209..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 505..656
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 863..915
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1120 AA; 128395 MW; 4C32E8EE3F750EB9 CRC64;
MTPSKLAQPD SETSSMVDTP MTDANELVQP RRPSFGHLNR YVDDTPDYTD SDTNPNTTAS
SVAGDVAQTD GRKKRSEALQ LRKSILGKKH GQLDESKEDD TIRRFKYLLG LTDLFRHFIE
TNPNPKIREV MAEIDRQNAE EEEKAKKGVS RKGGAAAIGK RKTEQEEDAE LLRDEKRGTA
SQTVFRESPA FIKGGEMRDY QIAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFLGYLR
HICGIKGPHL IIVPKSTLDN WAREFKKWTP DVDVLVLQGA KDERHALIND RLVDEKFDVC
ITSYEMILRE KAHLKKFAWE YIIVDEAHRI KNEESSLAQI IRVFSSRNRL LITGTPLQNN
LHELWALLNF LLPDVFGDSE AFDSWFSNQN EDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
LPKKELNLYV GMSEMQVRWY KKILEKDIDA VNGAGGKRES KTRLLNIVMQ LRKCCNHPYL
FEGAEPGPPY TTDEHLVYNS GKMIILDKIL KRMKEEGSRV LIFSQMSRVL DILEDYCVFR
GHQYCRIDGG TAHEDRIAAI DEYNKPGSEK FVFLLTTRAG GLGINLTTAD IVILYDSDWN
PQADLQAMDR AHRIGQTKQV KVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQAK
QAASKDELLN MIQHGAEKVF ETKGAVGELD DIDEILRRGE ARTAELNAKY ENLGIDDLQK
FSSENAYEWN GEDFTQKKKD VGLAWINPSK RERKEQSYSM DKYYKQALST GGRPAETKPK
VPRAPKQVNI HDWQFFPPGL QELQEKETAY YHKEIGYKVP LAEGTEEDLS DREADQRLNQ
DEIDNAEPLT EEEKQRKAEM QQHGFGNWNR RDFQQFINGS AKFGRTNYEG IATEVDSKEP
HEIEEYAKVF WKRYTEIADY DKYIKTIEAG EEKLRKTNLQ RKMLRKKMEM YRVPLQQLKI
NYTVSTTNKK VYTEEEDRFL LVMLDKHGVD GEGLYEKIRD EIRESPLFRF DWFFLSRTPV
EIGRRCTTLL NTVLREFGDP EEKLTNGHGP GKGRGRDRDE DEDEENDSEA APAKKKAKNG
VVNKQVKAIK SGRGSKASSP VSRAQSVSST TASRSKGRKK
//
