ID A0A4V4HHD4_DENBC Unreviewed; 1459 AA.
AC A0A4V4HHD4;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=K435DRAFT_775570 {ECO:0000313|EMBL:THV02356.1};
OS Dendrothele bispora (strain CBS 962.96).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricales incertae sedis; Dendrothele.
OX NCBI_TaxID=1314807 {ECO:0000313|EMBL:THV02356.1, ECO:0000313|Proteomes:UP000297245};
RN [1] {ECO:0000313|EMBL:THV02356.1, ECO:0000313|Proteomes:UP000297245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 962.96 {ECO:0000313|EMBL:THV02356.1,
RC ECO:0000313|Proteomes:UP000297245};
RX PubMed=30886374; DOI=.1038/s41559-019-0834-1;
RA Varga T., Krizsan K., Foldi C., Dima B., Sanchez-Garcia M.,
RA Sanchez-Ramirez S., Szollosi G.J., Szarkandi J.G., Papp V., Albert L.,
RA Andreopoulos W., Angelini C., Antonin V., Barry K.W., Bougher N.L.,
RA Buchanan P., Buyck B., Bense V., Catcheside P., Chovatia M., Cooper J.,
RA Damon W., Desjardin D., Finy P., Geml J., Haridas S., Hughes K., Justo A.,
RA Karasinski D., Kautmanova I., Kiss B., Kocsube S., Kotiranta H.,
RA LaButti K.M., Lechner B.E., Liimatainen K., Lipzen A., Lukacs Z.,
RA Mihaltcheva S., Morgado L.N., Niskanen T., Noordeloos M.E., Ohm R.A.,
RA Ortiz-Santana B., Ovrebo C., Racz N., Riley R., Savchenko A., Shiryaev A.,
RA Soop K., Spirin V., Szebenyi C., Tomsovsky M., Tulloss R.E., Uehling J.,
RA Grigoriev I.V., Vagvolgyi C., Papp T., Martin F.M., Miettinen O.,
RA Hibbett D.S., Nagy L.G.;
RT "Megaphylogeny resolves global patterns of mushroom evolution.";
RL Nat. Ecol. Evol. 3:668-678(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
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DR EMBL; ML179077; THV02356.1; -; Genomic_DNA.
DR Proteomes; UP000297245; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR CDD; cd07542; P-type_ATPase_cation; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006544; P-type_TPase_V.
DR InterPro; IPR047819; P5A-ATPase_N.
DR InterPro; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000297245};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 717..735
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1217..1235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1241..1260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1281..1303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1333..1351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1363..1382
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1402..1418
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 290..416
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 1241..1416
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1459 AA; 163248 MW; 4C2B47CF8BB892D1 CRC64;
MTSVPGPSTR TRSSFDYTEG ASPIDIDTAL ANNRKSRRDS QFSSYIDDDE GTMFSGPGHS
VNPSSVTRMS NVEPGRRSSE GWSRTRRRSM DSGRRSVERR LSQDSQVSQQ SRESMDGEES
EEQDDEARTS RGRRRQRPPT SQHSGVLGSI ANLFQGKTQS PEARRLSFSR RSTDSLSRHS
RRISRSDAGS DYAVTTDDEQ ERWGYSSGEE DSEEEETSLL PVRDDMSITE SMAAYDSEPP
SPNMSQTLPL LASDQIFGGE SRIDMEMPFA SMKPPPPGAP SRQDIYIQEE DTTVRFVGYA
VALWKQFTWR LGCTLTFGLL GLVGHWFPRL WLRWVAQEKA FKDIRSGFVV VETAYRDIAL
FPMKQIDYSY HISTVFHSVV SPDEILTEES PDLYDKEHGM LRSLLTVDYR YSRFLLDPRT
GLFSMIRDWR DPSWNSGAAV QSGLTEDIRK QRKILFEQNE IDIQGKSVVS LLIEEVIHPF
YVFQIASIIL WSLDDYYYYA ITIALISIVS ITTTLMDTRK TIARMREMSH FCCQVDVFVN
GTWIERDSTD LVAGDVVNMT SSQLSVIPAD MFLLSGDAIV NESMLTGESI PVSKIPAKDE
DLVTWKDVKQ ENPKSFMYGG TKVVRIRGAI ANDGNMSKPA LALVARTGFN TTKGALIRSM
LFPKPIGFKF YRDSVRFIGV LAGIAMLGFS ISAVQFIKMG LKWQTILVRA LDLITVVVPP
ALPATLSIGT SFAIARLRRS NIYCISPSRV NVAGKINVCC FDKTGTLTED GLDILGVRGL
DRNVHRFGEL LEDVHDLPLA KEKASFLHAL ATCHSLKMVD GTVVGDPLDV KMFEFTKWTL
EEGQIAGTGV IKAKSGAVVE QTSLVQTVVR PPGSARFKLE DALKGGAKRA HFLELGVIRM
FEFVSSLRRM SVIVKRLKST SMEIYVKGAP EVMSEICEKD SFPEDYDDLL SYYTKRGYRV
IAIAGKSVEG LTWLKAQRMK REQAESQLRF LGLIIFENKL KPGTTPAIQA LRSAHLACRM
ITGDNPLTAV SVARECGLIG QEAYVFGPAF ARGDASIPES QLEWTCMDEP SWRLDNYSLK
PLEPPLHHTV ESDELDYHDF SLVITGDIFR WMINYAPLET LQRMLVKAQI FARMSPDEKN
EIVERLQGLG YTVLMCGDGA NDCAALKAAD VGISLSEAEA SVAAPFTSST PDISCVIELI
KEGRAALVTS FSCFKYMALY SLIQFTTVTL LYSFASSLGD FQFLYIDLFI IIPIAVTMGR
TLPFPKIFPT RPTASLVSKK VLASIIGQII ITSAVQIWAY VWVRSQEWYI PPPTDEPGDH
GNHLESQNYE NTVLFLGSCF QYILVAAVFS IGPPYRKPMW TNVWLMISLV VLTGFNLLVL
LAPPKAITNI LELMPLPIDG RQKLLVAVVI NIICCWMYEQ YGALRIGEGV GRIIRWRRQL
RRTRESEGKT YKAVLGGTR
//
