ID R7YRA1_CONA1 Unreviewed; 1186 AA.
AC R7YRA1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Adenosinetriphosphatase {ECO:0008006|Google:ProtNLM};
GN ORFNames=W97_03391 {ECO:0000313|EMBL:EON64161.1};
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:EON64161.1, 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}.
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DR EMBL; JH767567; EON64161.1; -; Genomic_DNA.
DR RefSeq; XP_007779478.1; XM_007781288.1.
DR AlphaFoldDB; R7YRA1; -.
DR STRING; 1168221.R7YRA1; -.
DR GeneID; 19900702; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_2_1; -.
DR OMA; ELQAYND; -.
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:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
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 633..800
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 987..1137
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 132036 MW; BCFA518A78D01070 CRC64;
MACPLSDAIS DWSQEQKKEQ DATGAYNSAD DSGDDLFNDI HETQATLPLS RPYGHGPSIS
YRDLKSQISS PARHVTQPTQ ILDTPVARRT DPSSVVQVAA SSPTHSPAPP SPAPPRMSLG
YAMAPPGTSF RPFAAAPPPR PPPILSDSPV EHYSSDDDVT ITRANIKPTS FTSGGRSQAM
RAADAQDSSI GRMQELASKY TYDEKVSNQL RPQKRTTDDM ASAYANSGRP KKQPRQTGPS
RAQPVAPDMS LQDIGDLEVQ RKVGRMKSVY PQKRIIELRD ALMIKRGNEE DALEFIAGLE
EAVNDKQPID LTTSDDELAP DKSAVAAPKP TAKRHVKAPN MSIKDKWSST QHVAQQAPAK
ALPVGSSPLP ATPPRPRRRL VQGRRVPSSP SPPASPIAPA PPVQKPVPVK HKVICLESDE
EPEFSDSGVS SASDVGEENT SELEEGLLKF INSCSAAELA DLSHQSPDVA AAIIAARPFR
SLGQVRAVSV DAPPVPQRGK QKTTRKLTSD KVVDICLEMW TGYQAVDELV SRCEKLGEQI
TTEMKKWGFN IFGIAKGGEL ELTSLDDAQS DSSSLRDSGI GTPSSTTADE DDDADVKIVE
PRRGKTQLLK KPGIMAEDTE LKDYQVLGLN WLNLLWSKKL SCILADDMGL GKTCQVISFL
SHLKETRVRG PHLIIVPGST LENWLREFKT FSPSLVVEPY YGSQKERADQ RAQLEDDIRK
IDVIVTTYDI ARPPDDNKFL RRIKPTVCVY DEGHMLKNSM SARYTQLMRI PAQFRLLLTG
TPLQNNLQEL ASLLAFIMPD LFAERHEDLA YIFKYKAKTT DADHASLLSV QRIARARSMM
TPFILRRKKH QVLKYLPTKT RRVERCPMTP EQQEIYNEHL SEQRKILADR AAGRPNKNNA
NNMMKLRQAA IHPLLLRHIY DDEKIRKMSR ACIKEPELSK SDPNVVFEEM QFYSDWSLHK
LCEKYPKTLK RYALQNEEWM RSGKVQKLAE LLKKHVKDGD RTLIFSQFTS MMDILEQVLE
TLDIQFFRLD GATPISERQD MIDEFYADDS IPVFMLSTKS GGAGINLACA NKVVIFDSSF
NPQEDVQAEN RAHRVGQKRE VEVVRLISTG TIEEQIYKLG ESKLALDERV AGEAGSEDSA
KKVEKEGQAM VEKMLLEDME QEKSTGDLKE DFKSGMKKKG FDISAA
//
