ID A0A1J9Q5K1_9EURO Unreviewed; 1130 AA.
AC A0A1J9Q5K1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AJ78_07980 {ECO:0000313|EMBL:OJD11204.1};
OS Emergomyces pasteurianus Ep9510.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD11204.1, ECO:0000313|Proteomes:UP000182235};
RN [1] {ECO:0000313|EMBL:OJD11204.1, ECO:0000313|Proteomes:UP000182235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD11204.1,
RC ECO:0000313|Proteomes:UP000182235};
RG The Broad Institute Genomics Platform;
RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA McEwen J.G.;
RT "Emmonsia species relationships and genome sequence.";
RL Submitted (JUL-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}.
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:OJD11204.1}.
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DR EMBL; LGRN01000590; OJD11204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9Q5K1; -.
DR STRING; 1447872.A0A1J9Q5K1; -.
DR VEuPathDB; FungiDB:AJ78_07980; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000182235; 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:UP000182235}.
FT DOMAIN 211..376
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 507..658
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 873..925
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1130 AA; 129252 MW; C935E6D6FC7DDBA1 CRC64;
MAPSLSHLSG SESPSQVDTP MADANGYPSN TVVGSRDEDR SMMDYQDTPD YTDSDTNPNT
TASSIAGDLA QQDGRKRRSE AFQLRKSVLG RKHGRLDESK EDDSIRRFRY LLGLTDLFRH
FIETNPNPRI KEIMAEIDRQ NEAEANARKG LTRKGGASGE RRRRTEQEED AELLKDEKRG
GQAETVFRES PAFIKGGEMR DYQVAGLNWL ISLHENGISG ILADEMGLGK TLQTIAFLGY
LRHIAGITGP HLITVPKSTL DNWHREFSKW TPDVNVLVLQ GAKDDRHKLI NERLVDEKFD
VCITSYEMVL REKSHLKKFA WEYIIIDEAH RIKNEESSLA QIIRVFHSRN RLLITGTPLQ
NNLHELWALL NFLLPDVFGD SDAFDQWFSN QEADQDTVVQ QLHRVLRPFL LRRVKSDVEK
SLLPKKEVNL YVGMSDMQVK WYQKILEKDI DAVNGAQGKR ESKTRLLNIV MQLRKCCNHP
YLFEGAEPGP PYTTDEHLVD NAGKMVILDK ILKRMKNQGS RVLIFSQMSR VLDILEDYCV
FREHQYCRID GSTAHEDRIA AIDEYNRPGS EKFIFLLTTR AGGLGINLTS ADIVILYDSD
WNPQADLQAM DRAHRIGQTK QVVVFRFVTE NAIEEKVLER AAQKLRLDQL VIQQGRAQQQ
VKNAASKDEL LSMIQHGAAS VFGTKGPTGA LAKGNDISED DIDEILKKGE ERTAELNKKY
EKLGIDDLQK FTSDNAYEWN GEDFTNRKKD IGINWINPAK RERKEQSYSM DQYYRQALAT
GGRTADPKPK VPRAPKQIAI HDWQFFPPKL QELQEKETAY FHKEIGYKAV LPDGPDEELS
DREAERELEQ QEIDNAVPLT EEEQEQKAAL SEQGFGHWNR RDFQQFINGS AKFGRTNYNE
IATEVDSKDP EEIKEYAKVF WKRYTEIQDY PKHIRVIEQG EEKMRKMNHQ RKMLRKKMEM
YRVPLQQLKV NYTVSTTNKK VYTEEEDRFL LVMLDRHGVD GEGLYEKIRE EIRESPLFRF
DWFFLSRTPV EIGRRCTTLL NTVAKEFEVD GTKIPNGDSG GKGRGRDRDD VENEEVEAPA
KKKTKNGAVN KQLKAVQSAS GSRATSTATS RAGSVSSSTP ATSKSKGKKK
//
