ID A0A2J6TQ33_9HELO Unreviewed; 1605 AA.
AC A0A2J6TQ33;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=K444DRAFT_640774 {ECO:0000313|EMBL:PMD65119.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD65119.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD65119.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD65119.1,
RC ECO:0000313|Proteomes:UP000235371};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (APR-2016) 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}.
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DR EMBL; KZ613747; PMD65119.1; -; Genomic_DNA.
DR STRING; 1095630.A0A2J6TQ33; -.
DR InParanoid; A0A2J6TQ33; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000235371; 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; cd02440; AdoMet_MTases; 1.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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 InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF02353; CMAS; 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 SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 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:UP000235371};
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 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 567..595
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1109..1128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1149..1171
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1196..1214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1226..1244
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 168..287
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1605 AA; 180634 MW; 976560E5B5D6BB8B CRC64;
MDESNGMPIH RGLRSSSRRN GSSNGQYGPV YRRDSNLTNA SVSSFLDDVE MAQDEVFSGP
MGESVPTSNS SFLHRRERAD STTSFTFYDE EPLQPSDDSA ILDDESELNF EEEEEEADLE
AGELSTMRRT SSGHSRASVH DRLLRSDSNG SNFGRGHRTS QKIYIVTEDL TIVVAGFTTS
TSGLALYTTI CVLTFGLGYL LFRWLPRWQV RIVGTPCPMR SCSWVVIENQ WGEMVVQGID
SKEYGRSMST VFGASEKRYA VLDEEDDDPV LEDLRILDYR YMRFSFHPVK DRFVLSNSWK
DPAWTDVKSI RAGIDGDEKE IRELVFGKNL IDIKQKTIPQ LLIDEAFHPF YVFQIASLIL
WSFDEYYYYA ACIFLISATM RRLREISRFE CDVRVLRNSF WRYVPSSELV PGDVYEVTDP
ALTQFPCDSI LLTGDCIVNE SMLTGESVPV SKVPATDQSL RLLNLTASSI AADLARHFLF
CGTKIIRARR PQDDKDDEAV ALAMAVRTGF NTTKGALVRS MLFPKPSGFK FYRDSFRYIS
VMGGIALLGF IASFINFVRL KLAWHLIIVR ALDLITIVVP PALPATLSIG TNFALSRLRK
KQIFCISPQR VNVGGKLDIV CFDKTGTLTE DGLDVLGIRV AQKPLNRFSD ILADALSLLP
VAAYERDPTV EYDLHKAVLH TMATCHSLRV VEGELVGDPL DVKMFEFTGW SFEEGQQRGG
DTEDEEQGGL SPSIARPPAG MEYDIDDNDN PQSTSRSPIE LGVLKSFEFV YQLRRASVIV
RNFGSPGCDV YVKGAPECMK DVCRAESFPS DYEELLAYYT HRGFRVIACA TKHIAKLNWV
KVQKMKRAEA ESGLDFIGFI IFENKLKPST AGVLDELSKA GIRKVMCTGD NILTAISVAR
ECNLIDKTAH CFVPHFGEGD FQDPKARLSW ESIDNNIFTL DEHTLTPLPP PAEGDASLPY
DISNLRNYSL AVSGDVFRWI IDFAQPVVLQ RMLVCGQVFA RMSPDEKHEL VEKLQSIDYC
CGFCGDGAND CGALKAADVG ISLSEAEASV AAPFTSRVFD ITCVPEVIRE GRAALVTSFS
CFKYMSLYSA IQFTSVSFLY ASASNLGDFQ FLFIDLVLIL PIAIFMGWTG PFPVLCMKRP
TANLVSRKVL TPLLGQIAIC ILIQAVGFRM VRRQPWFIPP HLDREKSNVE NSENTTLFLV
SCYEYILSGI VLSVGPPFRQ SMAHNLPFVV TIVVALLFCS YMLFDPSESV AKFMQLTKMS
WDFRSFNWIL DGGYLPHAVI RIGIRRQLRD RIELIKSTSL EEAYKSKMSY VELLRSRPIA
IETATANEQH YEVGTGVLTA CLGPRMKYSS CLYPKGGETL AQAEIAMLET YVEKAQLKDG
MSILDLGCGW GSGALYFAEV LPNSRVTAFS NSRTQKIYID QKAKEKGLKN LTVVTGNVVD
YEFENEAFDR VVSIELFEHM KNYELLMAKI SRTLKPSGKL FVHIFSHNTT PYDFEEGWMS
THFFSGGTMP SADLLLYFQR DLKLETQWWV NGKHYAKTCE DWLSKMTASK KEIWPHLTET
YGEKDTAMWY HRWQIFYMAC AELFAYEGGD TWGVSHYLFE KPRSS
//
