ID A0A0J9HDZ4_AJEDA Unreviewed; 1129 AA.
AC A0A0J9HDZ4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Adenosinetriphosphatase, variant {ECO:0000313|EMBL:KMW67279.1};
GN ORFNames=BDDG_03366 {ECO:0000313|EMBL:KMW67279.1};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:KMW67279.1};
RN [1] {ECO:0000313|EMBL:KMW67279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:KMW67279.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) 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; GG749420; KMW67279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9HDZ4; -.
DR Proteomes; UP000007802; 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}.
FT DOMAIN 208..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 504..655
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 870..922
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..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1129
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 46..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 129181 MW; 7C68383509ED4316 CRC64;
MAPSLSHLSG SESPAQADTP MADANGYPSN TMEGTRDEDQ SMVDTPDYTD SDTNPNTTAS
SIAGDIAQQD GRKRRSEAFQ LRKSVLGRKH GRLDESKEDD SIRRFRYLLG LTDLFRHFIE
TNPNPRIKEI MAEIDRQNEA EANSRKGLTR KGGASGERRR RTEQEEDAEL LKDEKRGGQA
ETVFRESPAF VKGGEMRDYQ VAGLNWLVSL HENGISGILA DEMGLGKTLQ TIAFLGYLRH
LRGITGPHLI TVPKSTLDNW HREFSKWTPD VNVLVLQGAK EDRHKLINER LVDEKFDVCI
TSYEMVLREK SHLKKFAWEY IIIDEAHRIK NEESSLAQII RVFHSRNRLL ITGTPLQNNL
HELWALLNFL LPDVFGDSDA FDQWFSNQEA DQDTVVQQLH RVLRPFLLRR VKSDVEKSLL
PKKEMNLYVG MSDMQVKWYQ KILEKDIDAV NGAQGKRESK TRLLNIVMQL RKCCNHPYLF
EGAEPGPPYT TDEHLIDNAG KMVILDKILK RMKNQGSRVL IFSQMSRVLD ILEDYCVFRE
HQYCRIDGST AHEDRIAAID EYNRPGSEKF IFLLTTRAGG LGINLTSADI VILYDSDWNP
QADLQAMDRA HRIGQTKQVI VFRFVTENAI EEKVLERAAQ KLRLDQLVIQ QGRAQQQVKN
AASKDELLSM IQHGAASVFS TKGPTGALAK GNDISEDDID EILRKGEERT AELNKKYEKL
GIDDLQKFTS DNAYEWNGED FTNRKKDIGI NWINPAKRER KEQSYSMDQY YRQALATGGR
TADPKPKVPR APKQIAVHDW QFFPPKLQEL QEKETAYFHK EIGYKAVLPD GPDEELSDRE
AERELEQQEI DNAVPLTEEE QEQKAALSEE GFGNWNRRDF QQFINGSAKF GRTNYTEIAT
EVDSKDPDEI KEYAKVFWKR YTEIQDYPKY IRVIEQGEEK MRKMNHQRKM LRKKMEMYRV
PLQQLKVNYT VSTTNKKVYT EEEDRFLLVM LDRHGVDGEG LYEKIREEIR ESPLFRFDWF
FLSRTPVEIG RRCTTLLNTV AKEFEVDGGK IPNGDTGSGK GRGRDRDDDV ENEEVEAPAK
KKTKNGAVNK QLKAVQSASG SRATSTATSR AGSVSSSAPA TSKLKGKRK
//
