ID A0A284QM73_ARMOS Unreviewed; 1476 AA.
AC A0A284QM73;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=ARMOST_00824 {ECO:0000313|EMBL:SJK97572.1};
OS Armillaria ostoyae (Armillaria root rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=47428 {ECO:0000313|EMBL:SJK97572.1, ECO:0000313|Proteomes:UP000219338};
RN [1] {ECO:0000313|Proteomes:UP000219338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C18/9 {ECO:0000313|Proteomes:UP000219338};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; FUEG01000001; SJK97572.1; -; Genomic_DNA.
DR STRING; 47428.A0A284QM73; -.
DR OMA; FSCFQYM; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000219338; 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; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
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; IPR047821; P5B-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; PF00690; Cation_ATPase_N; 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|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:UP000219338};
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 498..518
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 679..703
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 715..736
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1235..1254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1260..1279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1300..1322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1352..1370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1382..1401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1421..1453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 289..418
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 441..493
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT DOMAIN 1260..1431
FT /note="Cation-transporting P-type ATPase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00689"
FT REGION 1..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1476 AA; 163400 MW; 6DFC23D1397FA624 CRC64;
MAPVAGPSKA TSSHDYTEGA STVDIEEAVT SSRRARRDSQ HSAIYGEDGE GAIFSGPGHS
DFVNPSSVSR MSHIEHGRRS SEGHSRSRRL SQDSRVSGRQ KVSRRDSEVS RQSIEDVSDE
DNHSTLSWEG RRTRAVSPAP KPSVFENIAN LFGRTSSPDH LRRPSLSQRS SRSMSRRSRR
SRQSDAGSDY AVDTEDDEEE RWGYSSGEED SDDDSESIMN TLPDNISVSA SMDYDSDPPS
PGMSQGLPLL ASDQIFAGES RIDMEIPFAL LQPPPPGPPS RQTIHIPDED STIRLIGYET
VPWRQWVWRI GCLFSLDILG LLGHWFPTLW LRWCAREKAF IDANNGFVVV ESAYRDIAIF
PIHTIKYPYP LSTVFSAPLD PSSIIDSSLK TADGPDAGED GLLRKLFILD YRYSRFALDP
RTGLFGVVRD WRDSSLHGVA SIQNGLQDDV RKQRGTLFGP NAIDIEGKST LALLVEEVIH
PFYVFQIASI VLWSLDDYYY YAFCILLISV ISVTTTLMET KKTIARMREM SRLSCKMDTL
VNGVWTERDS TNLVPGDIVN LSSSDFTLIP ADMFLLSGDA IVNESMLTGE SVPVSKTPVK
DEDLMSWKEN QPENPKTYMY GGTRVIRIRG ALGSDAGPGR PALAMVARTG FNTTKGALIR
SMLFPKPIGF KFYRDSVRFI FVLAGIAALG FSASAVQFIR IGLKWQTIII RALDLITVVV
PPALPATLSI GTSFAIGRLR KLGIYCISPS RVNVGGKVNV CCFDKTGTLT EDGLDILGVR
ALDRNNRRFG ELLDDVHDMP LGKDKATFLH ALATCHSLKM VDGEPLGDPL DMKMFSFTKW
TLEEGRVSGT GVIKSKSGAI MEQAALVQIV VRPPGSAQFR LEDALKGATK HAHFLELGVI
RTFEFVSGLR RMSVIVKRLK SNSMEIYVKG APEVMGDICD KDSFPEDYDD LLSYYTKRGY
RVIAIAGKSI EGLSWLKAQR MKREQAESGL RFLGLVIFEN KIKPGTGPAI HALRSAHLAC
RMITGDNPLT AASVARECGL INQAAHIFYP VFARGSYSVN LSFSRAHVDM VGNTLTPESR
LEWPCTDDPS WMLDSYSLKP LVPPAHHTVE AIELDYHDYA LVVTGDVFRW MINYAPLETL
QRMLVKTQIF ARMSPDEKNE VVERLQALGY TVLMCGDGAN DCAALKAADV GISLSEAEAS
VAAPFTASTP DIGCVIELIK EGRASLVTSF SCFKYMALYS MIQFTTVTLL YSFASSLGDF
QFLYIDLFII IPVAVTMGRT LPYPRIHPQR PTASLVSKKV LSSIIGQIVI TCVVQIWAYV
WVRGQEWYTP PREDEPSQDS NKLESRNFEN SVLFLVSCFQ YILVAAVFSI GPPYRKAMST
NVLLMLAIGV LSAFNLVILL FPPAVLTDWL TLMALPAHAR MVLLIAVVVN IGVSLLFEQY
GAHTVATVIG IVLSWRRGRR RDRDGKVYKA VEGGMR
//
