ID A0A2R6QEF4_9APHY Unreviewed; 1443 AA.
AC A0A2R6QEF4;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=PHLCEN_2v3691 {ECO:0000313|EMBL:PSS06524.1};
OS Hermanssonia centrifuga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Meruliaceae; Hermanssonia.
OX NCBI_TaxID=98765 {ECO:0000313|EMBL:PSS06524.1, ECO:0000313|Proteomes:UP000186601};
RN [1] {ECO:0000313|EMBL:PSS06524.1, ECO:0000313|Proteomes:UP000186601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBCC195 {ECO:0000313|EMBL:PSS06524.1,
RC ECO:0000313|Proteomes:UP000186601};
RA Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA Riley R.;
RT "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT centrifuga.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PSS06524.1}.
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DR EMBL; MLYV02000363; PSS06524.1; -; Genomic_DNA.
DR STRING; 98765.A0A2R6QEF4; -.
DR Proteomes; UP000186601; 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:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd15863; SNARE_GS27; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; 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; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-ATPase; 1.
DR Pfam; PF12352; V-SNARE_C; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000186601};
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 533..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 695..714
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 904..928
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 516..640
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 663..715
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 94..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1443 AA; 160163 MW; 50E226C71D98474B CRC64;
MNSLYTLGVR QTNSIQADLE RLRNGDTSAA LLGQISASLA AMGRTVDDYD SMAKREIIKA
KQEKAMMRVQ KFRSDYAELR TQFEKIKGER ETASRSELFS ASSSSTVPLS PAHGDSRRRF
LTGQQPSSEV SESPFRGPTP LPQSSLREDY ALREHSFIHN TDARLDDFLA QGRAVLDDLV
DQRTVLKGTQ KRLLDAANTL GLSRDVIGWI ERRRLRSPSE WVDMVSDSSS SQNHDYTEGA
SAVDIQDVLN SNRRSRRDSQ YGEGGYMFDG PGHTVNPSSV SRMTLSEHGR RSSEGRSRGS
QSRRRSEDRG RDTSSSRSLR ASRDSLPSLA RSEDEYTDPG HEVEDEGDHA TLRRSRRKST
TSPQRQSVFG NIASMFGRAV PTTESPPRSR RPSLSSRSSR TGLLRRTSSR RSDAGSDYAI
ESDDEDERWG YASEEEDDSE SDITDDHRQG DSDSVDFHSI EEDSYPPSPG LALHTMTGPG
DPIFGDEARI DMGELDLHDP PPPGPPSRQT IYITDEDVHI RFIGFETVTI RHFLWRMACV
LTFGILGLLG HWFPRLWLRW VAKEKAFKDM EHGFVVIETA YRDIALFPVR KLHYPYHITT
VFPAQVDTLS RPPSRTNGDA NIGILEHLLV VDYRYARFAL DPRTGLFNIV RNWRDPSWTG
IQSVSNGLTQ SEEEQRLALF GPNVIDIEGK STVSLLIDEV IHPFYVFQIA SIVLWSLDDY
YYYAFCIALI SAISITTTLI ETKKTISRMR EMSRFSCPVN VFTDGIWKRR ESTDLVPGDI
VNLMDPPLAV FPADIFLLSG DTIVNESMLT GESVPVSKVP IRDEDIALWK EAIDVSSDVS
KSFLYAGTRV IRVRGALTAD GSSGAPALGL VVRTGFNTTK GALVRSMLFP KPIGFKFYRD
SIRFILVLAG LAGLGFCASA VQFVRLGIKW HTIMLRALDL ITVVVPPALP ATLSIGTSFA
IGRLRKLGIF CISPSRVNVG GRVNVCCFDK TGTLTEDGLD ILGVRALERN AHRFGELIED
VHDLPSSRDK ANFLHALATC HSLKMVDGNI IGDPLDVKMF DFTKWTLEEG HVAGTGVVKS
RIGGARPAAL VQTVVRPPGT AQFRVEDALR GSSKHAHFLE LGVIRTFEFV SALRRMSVIV
KRLKSSSMEI YVKGAPEVMG EICEPDSFPD DYDDLLSYYT KRGYRVIAMA GKSLEGLSWL
KAQKMKREHA ESGLKFLGLI IFENKLKPGT TPAIQSLRAA HLMCRMITGD NPLTAVSVAR
ECGLVNQAAH IFSPVFVRGN SATPMSKLEW SCTDEPAWKL DDYSLKPLSP PAHHTVESDN
VDVHDYTLVV TGDVFRWIIN HAALETVQRM LVKAQIFARM SPDEKNEVVE RLQGLGYTVL
MCGDGANDCA ALKAADVGLS LSEAEASVAA PFTSRTPDIS CVIEVIKEGR AALVTSFSCF
KYM
//
