ID F9XLV7_ZYMTI Unreviewed; 1093 AA.
AC F9XLV7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Calcium-transporting ATPase {ECO:0000256|RuleBase:RU361146};
DE EC=7.2.2.10 {ECO:0000256|RuleBase:RU361146};
GN ORFNames=MYCGRDRAFT_49054 {ECO:0000313|EMBL:EGP83932.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP83932.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP83932.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001205; EGP83932.1; -; Genomic_DNA.
DR RefSeq; XP_003848956.1; XM_003848908.1.
DR AlphaFoldDB; F9XLV7; -.
DR STRING; 336722.F9XLV7; -.
DR EnsemblFungi; Mycgr3T49054; Mycgr3P49054; Mycgr3G49054.
DR GeneID; 13398201; -.
DR KEGG; ztr:MYCGRDRAFT_49054; -.
DR eggNOG; KOG0204; Eukaryota.
DR HOGENOM; CLU_002360_9_3_1; -.
DR InParanoid; F9XLV7; -.
DR OMA; RRSVVFN; -.
DR OrthoDB; 847at2759; -.
DR Proteomes; UP000008062; Chromosome 10.
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:SF346; 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 Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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:UP000008062};
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 152..169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 189..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 399..426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 823..844
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 850..872
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 893..919
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 931..948
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 969..988
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT TRANSMEM 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361146"
FT DOMAIN 90..168
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 31..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1063..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 117852 MW; 3A7FE5C1C8ED18ED CRC64;
MTQKPHLEGR DRSLSALSGS TQFSTLKVPK ASYDATSSAS SMFSEGGRED ALRPDPGSEA
DFVVKDSPFA FSPGQLNKLL NPKSLPAYVA LGGIRGIEKG LRTNLETGLS ADEASLHGSF
ADRLRIYSNN ALPEKKATSL WKLMWIAYND KVLILLTVAA AISLALGLYE TFGVEHQPGE
PMPVDWIEGL AICIAIVVVV LVGSLNDYQK ERAFVKLNAK KEDRMVKVLR SGKSSMVNVV
DIMAGDILHL EPGDMIPVDG IFISGHGVKC DESSATGESD ALKKVGGEQV MRMLEEGHQD
LKDMDCFIIS GSKVLEGIGT YMATSVGVNS SYGKILMSMR VDMAPTPLQV KLDGLATAIA
KLGSSAALLL FFVLLFRFVA TLSSNTGSPN QKASQFMDIL IVAVTVIVVA VPEGLPLAVT
LALAFATTRL VKLNNLVRIL KSCETMGNAT TVCSDKTGTL TTNVMTVVTG QFGERSFDDK
NHTGSEVRST EFASQLSSEE RRRLVQAIAI NSTAFEGEDG FIGSKTETAL LSFARTLGMG
SLAEERANCP AHAFFPFDSG RKCMGAVQTL PDGTFRLVVK GASEILLGHS TSIATTSGPK
PLDGTTRETL EANIDSYAKQ SLRTIALISR EFPSWPPAGC TVENDPTEAD FGAVLSNMTF
DGLVGIQDPV RPGVPEAVAK CAHAGVSVRM VTGDNVITAK AIATECGIYT GGVVMEGPVF
RTLSESQMNE VLPKLQVLAR SSPEDKRILV TSLRALGEIV AVTGDGTNDG PALKAADIGF
SMGIAGTEVA KEASAIILMD DNFASILTAL MWGRAVNDAV RKFLQFQLTV NITAVIITFV
SAVANEGMRS VLVAVQLLWI NLIMDSMAAL TLASDAPTEE ILNRKPTLRS APLISTTMWK
MIIGQAILQM AVIFTLYYAG PSILNYPFDG TEIRSVVFNA FVWLQIFNMF NSRRLDNKFN
VFAGVTRNWY FMIITLVMVG CQVMIMYVGG RAFQISRISG KDWGISIVIG LLSMPAAVFI
RLFPDHIFEK IARICGKPVV LVYRPLSRGM HAVGRKIRGL RRSKKESGEV AEIAEGQERE
EKRVGDVERG RAN
//
