ID A0A165JJS7_XYLHT Unreviewed; 1415 AA.
AC A0A165JJS7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=L228DRAFT_10174 {ECO:0000313|EMBL:KZF26326.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF26326.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF26326.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF26326.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the transport of
CC calcium. {ECO:0000256|RuleBase:RU361146}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=7.2.2.10;
CC Evidence={ECO:0000256|RuleBase:RU361146};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361146}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. {ECO:0000256|RuleBase:RU361146}.
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DR EMBL; KV407454; KZF26326.1; -; Genomic_DNA.
DR RefSeq; XP_018191881.1; XM_018328857.1.
DR STRING; 1328760.A0A165JJS7; -.
DR GeneID; 28893994; -.
DR InParanoid; A0A165JJS7; -.
DR OMA; QWGYSIV; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02081; P-type_ATPase_Ca_PMCA-like; 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; IPR006408; P-type_ATPase_IIB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01517; ATPase-IIB_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR24093:SF369; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR24093; CATION TRANSPORTING ATPASE; 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 PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU361146};
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU361146};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU361146};
KW Ion transport {ECO:0000256|RuleBase:RU361146};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU361146};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361146};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361146}; Transport {ECO:0000256|RuleBase:RU361146}.
FT TRANSMEM 284..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 321..339
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 488..509
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 529..556
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 998..1019
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1025..1047
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1068..1093
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1146..1167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1179..1200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1318..1336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 230..300
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1415 AA; 153991 MW; 705661E98624A221 CRC64;
MSQSDRPEIS RTSSGARRRR APTITIDTSA GDHHNSLHSE NNVAPELRPA QSFDSKQSRP
VSSHNVSSPT SKSNDGNFLS VPGSRSRQNS FDSDDGNRSP SSYGGETFYS PPSSSAQGDR
LAKSVSLQQD NSHITRDEEA LKPDPGTEAD FDIEDNKFAF SPGQLTKLFN PKSLGAFYAL
GGLSGLEKGL RTNCRAGLSM DEGALDGSVS FEDATMSQAA VAAPKGTEVP GFERTTTETT
TRTAVSGNED SFIDRRRVFG DNRIPERKAK NIFQLAWMAY NDKILILLTV AAVISLALGL
YETFGQKHDA SHPPVEWVEG VAIIVAILIV VVVGAANDWQ KERQFVKLNK KKEDRMIKLV
RSGKTQEVSI YDVLAGDVLL LEPGDMVPVD GILIEGHNVK CDESSATGES DLIKKSNADD
VYRAIEDNES TRKMDPFIIS GAKVTEGVGR FLVTGTGIHS SYGKTMMSLR EESEPTPLQS
KLNVLAEYIA KLGGAAALLL FVVLFIKFLV QLRGNHSSPS EKGQQFLQIF IVAVTIVVVA
VPEGLPLAVT LALAFATTRM LKDNNLVRVL RACETMGNAT AICSDKTGTL TQNKMTVVAG
TLGTASRFGD KSMPERDASA SLGTTDEAVS PTSSPKGKKP TPAAKTDGDD VSVGEFVSTL
HDDVKELVKK SVAINSTAFE GEEDGSSTFI GSKTETALLH FARDHLGMGP LSVERSNVDT
VQVFPFDSGR KCMASVIKLD NGRFRMYVKG ASEIMLSHCT KIIADPTAGI SETSISKDNV
EALEHIIQSY ASRSLRTLGL LYRDFQQWPP SSARTQEGNS REAIFDDVFK EMIFLGVIGI
QDPLRDGVAD AVFTCQKAGV FVRMVTGDNI LTARAIAQQC GIFTEGGLIM EGPKFRKLSK
TQLDQIIPRL QVLARSSPED KRILVRRLKE LGETVAVTGD GTNDAPALKS ADVGFSMGIA
GTEVAKEASA IILMDDNFTS IVKAMMWGRA VNDSVKKFLQ FQLTVNITAV LLAFVSAVAS
KDESSVLTAV QLLWVNLIMD TFAALALATD PPSSSVLDRK PDPKSAPLIS VTMWKMIIGQ
AIYQLVVTFI LYFGGVKILS YQTAREQHQL NTLVFNTFVW MQIFNELNNR RLDNHFNIFE
GVFRNYFFIV ITLIMIAGQV MIVFVGGRAF SVTRLNGAQW AYSIILGALS IPVGIVLRLI
PDELILKAVP RSWRRKPAPQ LVVSDDDRRY EFSQALEGIR EDLVFLKKIR GGRLNALKFK
LQHPREALLY RSRSVSRSGS SDLPRTPTAE GGASDFGSLS ATPDSRNRRR GRSRSNSAFG
PAAAMAGIIA GSVAGWSPIE RSAASDDGIP KFTRSRARSD LESQEGVEVH PSTKPDDPII
SEDIHARTTP PSQRPEETPN FHEESRCSAP QTSPR
//
