ID A0A9P5Z6J2_9AGAR Unreviewed; 1477 AA.
AC A0A9P5Z6J2;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=BDN70DRAFT_973495 {ECO:0000313|EMBL:KAF9481513.1};
OS Pholiota conissans.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Pholiota.
OX NCBI_TaxID=109636 {ECO:0000313|EMBL:KAF9481513.1, ECO:0000313|Proteomes:UP000807469};
RN [1] {ECO:0000313|EMBL:KAF9481513.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIRM-BRFM 674 {ECO:0000313|EMBL:KAF9481513.1};
RG DOE Joint Genome Institute;
RA Ahrendt S., Riley R., Andreopoulos W., Labutti K., Pangilinan J.,
RA Ruiz-Duenas F.J., Barrasa J.M., Sanchez-Garcia M., Camarero S.,
RA Miyauchi S., Serrano A., Linde D., Babiker R., Drula E.,
RA Ayuso-Fernandez I., Pacheco R., Padilla G., Ferreira P., Barriuso J.,
RA Kellner H., Castanera R., Alfaro M., Ramirez L., Pisabarro A.G., Kuo A.,
RA Tritt A., Lipzen A., He G., Yan M., Ng V., Cullen D., Martin F.,
RA Rosso M.-N., Henrissat B., Hibbett D., Martinez A.T., Grigoriev I.V.;
RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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|ARBA:ARBA00049360,
CC 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}.
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:KAF9481513.1}.
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DR EMBL; MU155177; KAF9481513.1; -; Genomic_DNA.
DR OrthoDB; 48943at2759; -.
DR Proteomes; UP000807469; 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 GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:TreeGrafter.
DR CDD; cd07542; P-type_ATPase_cation; 1.
DR FunFam; 1.20.1110.10:FF:000032; Cation-transporting ATPase; 1.
DR FunFam; 3.40.1110.10:FF:000057; Cation-transporting ATPase; 1.
DR FunFam; 3.40.50.1000:FF:000068; Cation-transporting ATPase; 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; IPR059000; ATPase_P-type_domA.
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; 1.
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; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000807469};
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 319..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 488..507
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 694..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 730..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1233..1251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1257..1276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1297..1319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1350..1368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1380..1399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1419..1435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 302..431
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 553..675
FT /note="P-type ATPase A"
FT /evidence="ECO:0000259|Pfam:PF00122"
FT DOMAIN 1257..1427
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..139
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..189
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1477 AA; 164404 MW; E320E07CC53318CB CRC64;
MAPIVGSSSN PEESNYDYTE GASLLEIDQA LDNNLRTRRD SQYNSYYDDS GDGSTFAGPG
HTVNPSSISR MSHMELGRRS SDLRLSRRKS MESRTSYRRR RDSKDSQVSH QTVEGANGYH
LEDGGESGSP SDNDAISSSS RRRRAKSPPS PTQRASVFGN IAHLFGRAGP SDTSPYRRPS
ISQRSSTSRV SRRSSRSAAS EHALDTEDED EERWGYSSGE EASENESQRS MDFTPDNQSI
TASMTYDSEP PSPTEGTQNL PLLNLDPIFG GESRIDMDTS FTLLAPPPSG PPSRQTVHIP
DEDSTVRFVG YETIPWRVGL WRVCFVLSFG ILGLLGHWFP HLWLRWVARE KAFIDSRNGF
LVVESSYKAI SLLPIRTIHY PYHISTVFPA TLSIIPGTEA ELIKPSHDEY IIENDMLKSL
LITDYRHSRF AVDPRTGLFD LIRRDWRDSN WNSVTAAQIP LDEQTREQRR LIFGKNEIDI
EGKSTISLLV DEVIHPFYVF QIASIILWSL DDYYYYAFCI ALISIISITT TLIETKKTVA
RMREMSRLVC SMDVLKAGSW VECDSTELVP GDIVNLSTSR LSLMPTDLFL LSGDAIVNES
MLTGESVPVS KIPIKDDDIL KWRDDKTENP KTFLYGGTRV VRIRGAFTTE GQGRPAMAIV
ARTGRFNTTK GALIRSMLFP KPIGFKFYRD SVRFIGVLAG IAGLGFCFSA IEFIKISLPW
QTIVVRALDL ITVVVPPALP ATLSIGTSFA IGRLRKLGIY CISPSRVNVA GKINVCCFDK
TGTLTEDGLD ILGVRSLDRT EHRFGELLED VHDMPLSKDK ATFLHALATC HSLKMVDGEM
IGDPLDVKMF GFTRWTLEEG RVAGTGNIKA KGTVIEQTAL VQTVVRPPGS AQFRLEDALK
GASKHAHFLE LGVIRAFDFV SSLRRMSVIV KRLKSTSMEI YVKGAPEVIV NICEKSSFPQ
DYDDLLSYYT KRGYRVIAIA GKSIEGLSWL KAQRMKREQA ESGLRFLGLV IFENRLKPGT
APAIQALRSA HLACRMITGD NPLTAVSVAR ECSLINQAAH VFSPAFLRGN ASTPNSKLVW
SSMDDLSWKL DSYSLKPMTP PPHHTIEADE INYQDYSLVI TGDIFRWMLN YAPLETVQRM
LVKTQIFARM SPDEKNEVVE RLQTLGYTVL MCGDGANDCA ALKAADVGIS LSEAEASVAA
PFTTSTPDIG CVIEVIKEGR SALVTSFSCF KYMALYSMIQ FTSVTLLYSF ASSLGDFQFL
YIDLFIIIPI AVTMGRTLPY PRIYPKRPTA SLVSKKVLAS IIGQIVITAA VQFWVYFWVR
RQEWYTPPPP NLPSEGGDNK LESTNYENTV LFLISCFQYI LVAAVFSIGP PYRKSMWTNG
WLMCSMVLLS GFNILVLLAP PKTVGNLLTL MNLPQAARYT LLLATAINVI VSLGFEQWGT
QGVSTIIGGA ISWWHRGRRR VRDGKAYKVV EGGMRSS
//
