ID R7Z5X0_CONA1 Unreviewed; 1111 AA.
AC R7Z5X0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 13-SEP-2023, entry version 56.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_08763 {ECO:0000313|EMBL:EON69503.1};
OS Coniosporium apollinis (strain CBS 100218) (Rock-inhabiting black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Coniosporium.
OX NCBI_TaxID=1168221 {ECO:0000313|EMBL:EON69503.1, ECO:0000313|Proteomes:UP000016924};
RN [1] {ECO:0000313|Proteomes:UP000016924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 100218 {ECO:0000313|Proteomes:UP000016924};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Gorbushina A., Noack S., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Coniosporium apollinis CBS 100218.";
RL Submitted (JUN-2012) 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; JH767616; EON69503.1; -; Genomic_DNA.
DR RefSeq; XP_007784820.1; XM_007786630.1.
DR AlphaFoldDB; R7Z5X0; -.
DR STRING; 1168221.R7Z5X0; -.
DR GeneID; 19906074; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OMA; VHDYQFF; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000016924; 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; 1.10.1040.30; 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:UP000016924}.
FT DOMAIN 192..357
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 488..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 853..905
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 127432 MW; 077420D3AAE68798 CRC64;
MAPADVSMAD SDMNGRDADD AMQGYQDTPD YTDSDTNPNT TASSVAGDAA PIDGRKRRAQ
DQQLRKSMFG RKHDRLGESK EDDSIRRFRY LLGLTDLFRH FIETNPNPRI KEIMAEIDRQ
NQEEEEKAKK GHTRKGGAAG ERRRKTEQEE DKELVRDEKR GGESATVFRD SPAFIKGGQM
RDYQVAGLNW LISLHENGIS GILADEMGLG KTLQTISFLG YLRFVCGITG PHLVVVPKST
LDNWKREFGR WIPEINVLVL QGAKEERNNL INERLVDEKF DVCITSYEMI LREKTHLKKF
AWEYIIIDEA HRIKNEESSL AQIIRLFNSR NRLLITGTPL QNNLHELWAL LNFLLPDVFG
DSEAFDQWFS SQEEDQDTVV QQLHKVLRPF LLRRVKSDVE KSLLPKKEIN LYVGMSEMQV
RWYQKILEKD IDAVNGAAGK KESKTRLLNI VMQLRKCCNH PYLFEGAEPG PPYTTDEHLV
NNAAKMVMLD RLLKRMKAQG SRVLIFSQMS RVLDILEDYS VMRGYQYCRI DGSTAHEDRI
AAIDDYNKPG SEKFLFLLTT RAGGLGINLT SADIVVLFDS DWNPQADLQA MDRAHRIGQT
KQVMVFRFVT ENAIEEKVLE RAAQKLRLDQ LVIQQGRAQQ PAKNAASKDE LLNMIQHGAE
KVFQSQGGIG VVGGKADLTD DDFEAILSRG EERTAELNAK YEKLGIDDLQ KFTSDSAYEW
NGQSFVPSKK EIGINWINPA KRERKEQSYS MDKYYRAALQ TGGRTADTKP RVPRAPKHVS
IHDYQFYPEK LKVLQDKELA WYRKENGIKA PLLEGTEEDL VEREADRDLV QLDIDNAEPL
TEAEKEEKER LTEQGFDWNR RDFQQFINGS AKYGRNNYHL IEDEVDGKNA EEIKAYAKVF
WQRYTDIPGW EKFVKAVEEG ENAIRTRERH QKLLRKKISM YRVPLQQMKI NYTVSTTNKK
VYTEEEDRFI LVCLDKFGID SEGLYERIRD EIRESPLFRF DWFFLSRTPV EISRRCTTLV
TTVVREFEDR NGSIPNGTSK SKRTLDEEEE EEEEETAPVK KRAKNGVKNK QLDNVKGTAS
KATSASTSRA GSVVSNGSAV PQKSKAKSKK K
//