ID A0A0D2DF97_9EURO Unreviewed; 1123 AA.
AC A0A0D2DF97;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 43.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z517_11122 {ECO:0000313|EMBL:KIW76376.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW76376.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW76376.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76376.1,
RC ECO:0000313|Proteomes:UP000053029};
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 Fonsecaea pedrosoi CBS 271.37.";
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; KN846975; KIW76376.1; -; Genomic_DNA.
DR RefSeq; XP_013280184.1; XM_013424730.1.
DR AlphaFoldDB; A0A0D2DF97; -.
DR STRING; 1442368.A0A0D2DF97; -.
DR GeneID; 25310612; -.
DR VEuPathDB; FungiDB:Z517_11122; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000053029; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053029}.
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 149..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1040..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 920..947
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
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 1040..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1123 AA; 128646 MW; 3EFC86C64711FFD6 CRC64;
MAPSKPQQPD SETSSVAETP MTDGPDYIRP HRPSFGHLNR PVDDTPDYTD SDTNPNTTAS
SVAGDTPLAD GRKKRSEAFQ LRKSILGKKH GQLDESKEDD TLRRFKYLLG LTDLFRHFID
ASPNPKIREV LQQIDQENAE EEAKARKVVS RKGGAAGAAK RKTEQEEDAE LLRDEKRGTA
SQTVFRDSPA FIKGGEMRDY QVAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFLGYLR
HICGIKGPHL ITVPKSTLDN WRREFEKWTP DVDVLVLQGA KEDRHALINE RLIDEKFDVC
ITSYEMILRE KSHLKKFAWE YIIVDEAHRI KNEESSLAQI IRMFSSRNRL LITGTPLQNN
LHELWALLNF LLPDVFGDSE AFDSWFSSQN EDQDTVVQQL HRVLRPFLLR RVKSDVEKSL
LPKKEVNLYV GMSEMQVKWY KKILEKDIDA VNGAGGKRES KTRLLNIVMQ LRKCCNHPYL
FEGAEPGPPY TTDEHLVFNS GKMIILDKIL KRMKDEGSRV LIFSQMSRVL DILEDYCVFR
GHQYCRIDGG TAHEDRIAAI DEYNKPGSEK FVFLLTTRAG GLGINLTSAN IVILYDSDWN
PQADLQAMDR AHRIGQTKQV VVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRAQQQVK
QAASKDELLT MIQHGAEKVF ETKGTTGELD DIDEILRRGE ARTAELSAKY EKLGIDDLQK
FSSENAYEWN GEDFTNRKKD ISLHWINPSK RERKEQSYSM DKYYKQALST GGRPADTKPK
IPRAPKQVVV HDWQFFPPGL QELQEKETAY YHKEIGFKVP LTDGTEEDLS DREADQRLAQ
NEIDNAEPLT EEEKQLKAEM QEHGFGNWNR RDFQQFINGS AKFGRTNYEG IATEVDSKEP
DEVEKYAKVF WKRYTEIAEF DKYIKNIEAG EEKLRKTERQ RKMLRKKMEM YRVPLQQLKI
NYTVSTTNKK VYTEEEDRFL LVMLDKYGVD GEGLYERIRD EIRESPLFRF DWFFLSRTPV
EIGRRCTTLL NTVSREFGET EEKLTNGHAP GKGRGRDRDD EEDEENDSEA PPVKKKAKNG
IVNKQVKAVK SGRGSKATSP ATSRAQSVSS TTPTASKSKG KKK
//