ID A0A0D1Y828_9EURO Unreviewed; 1122 AA.
AC A0A0D1Y828;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 44.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_10406 {ECO:0000313|EMBL:KIW11106.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW11106.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW11106.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW11106.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) 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; KN847499; KIW11106.1; -; Genomic_DNA.
DR RefSeq; XP_016231322.1; XM_016384720.1.
DR AlphaFoldDB; A0A0D1Y828; -.
DR STRING; 91928.A0A0D1Y828; -.
DR GeneID; 27337489; -.
DR VEuPathDB; FungiDB:PV08_10406; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000053328; 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; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; ISW-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:UP000053328}.
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..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1122
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..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Basic and acidic 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 1092..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 128422 MW; D42FBA9EEBF67D0F CRC64;
MAPTKPQQTD SENSSIADTS MIDAHSVLQP RRPSFGHLNR YMDDTPDYTD SDTNPNTTAS
SVAGDSVAPD GRKRRSEAFQ LRKSILGRKH GQLDESKEDD TVRRFKYLLG LTDLFRHFIE
TNPNPKIREV MEEIDRQNAE DAAKAKKGVS RKGGAAAGAK RKTEQEEDAE LLRDEKRGTA
SQTIFRESPA FIQGGEMRDY QVAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFLGYLR
HICDIKGPHL VAVPKSTLDN WAREFKKWTP EVDVLVLQGA KDDRHALIND RLIEEKFDVC
ITSYEMILRE KSHLKKFAWE YIIVDEAHRI KNEESSLAQI IRMFTSRNRL LITGTPLQNN
LHELWALLNF LLPDVFGDSE AFDSWFSSQN NDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
LPKKEVNLYV GMSEMQVKWY QRILEKDIDA VNGAGGKRES KTRLLNIVMQ LRKCCNHPYL
FEGAEPGPPY TTDEHLVYNS GKMIILDKIL NRMKEEGSRV LIFSQMSRVL DILEDYCVFR
GHKYCRIDGG TAHEDRIAAI DEYNKPGSEK FVFLLTTRAG GLGINLTTAN IVVLYDSDWN
PQADLQAMDR AHRIGQTKQV KVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQVK
QAASKDDLLN MIQHGAEKVF ETKGATGALD DIDEILQRGE ARTAELNKKY EKLGIDDLQK
FSSENAYEWN GEDFTNRRKD IGINWINPAK RERKEQSYSM DKYYKQALST GGKPAETKPK
VPRAPKQVNV HDWQFFPPGL QELQEKETAY YHKEIGYKVP LAEGTEEDLS DREADQRLNQ
DEIDNAEPLT EEEKQRKAEM QEHGFGNWNR RDFQQFINGS AKFGRTNYEG IANEVDSKEP
DEIEEYAKVF WKRYTEIADY DKHIKTIEAG EEKLRKTNLQ RKLLRKKMEM YRVPLQQLKI
NYTVSTTNKK VYTEEEDRFL LVMLDKHGVD GEGLYDKIRD EIRDSPLFRF DWFFLSRTPV
EIGRRCTTLL NTVLREFGDP EEKLTNGHGS GKGRGRDRDD DDDDDNESEA PPVKKKAKNG
IVNKAVKAVK SGRGSKNTSP ATSRAQSVSS STPASKSKGR KK
//