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Database: UniProt
Entry: A0A0D8JUI6_COCIM
LinkDB: A0A0D8JUI6_COCIM
Original site: A0A0D8JUI6_COCIM 
ID   A0A0D8JUI6_COCIM        Unreviewed;       858 AA.
AC   A0A0D8JUI6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Magnesium-transporting ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00013555};
DE            EC=7.2.2.14 {ECO:0000256|ARBA:ARBA00012786};
DE   AltName: Full=Mg(2+) transport ATPase, P-type 1 {ECO:0000256|ARBA:ARBA00029806};
GN   ORFNames=CIMG_04662 {ECO:0000313|EMBL:KJF61015.1};
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410 {ECO:0000313|EMBL:KJF61015.1, ECO:0000313|Proteomes:UP000001261};
RN   [1] {ECO:0000313|Proteomes:UP000001261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2] {ECO:0000313|Proteomes:UP000001261}
RP   GENOME REANNOTATION.
RC   STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
CC   -!- FUNCTION: Mediates magnesium influx to the cytosol.
CC       {ECO:0000256|ARBA:ARBA00003954}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mg(2+)(out) = ADP + H(+) + Mg(2+)(in) + phosphate;
CC         Xref=Rhea:RHEA:10260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00001857};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIB subfamily. {ECO:0000256|ARBA:ARBA00008746}.
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DR   EMBL; GG704914; KJF61015.1; -; Genomic_DNA.
DR   RefSeq; XP_004446078.1; XM_004446021.1.
DR   AlphaFoldDB; A0A0D8JUI6; -.
DR   GeneID; 4563081; -.
DR   VEuPathDB; FungiDB:CIMG_04662; -.
DR   OMA; WTQEMVI; -.
DR   OrthoDB; 1381139at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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:0015444; F:P-type magnesium transporter activity; IEA:UniProtKB-EC.
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; 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; IPR006415; P-type_ATPase_IIIB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01524; ATPase-IIIB_Mg; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 1.
DR   Pfam; PF13246; Cation_ATPase; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001261};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          50..123
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   858 AA;  94468 MW;  2F40A573DCCFE65E CRC64;
     MRFLLRRLTK WPGGQKVEPE NRQNVNGTTH ANWWHMPLAK DSTSPSILRA FASIPPDSAL
     GYMQSCRQGL SQAEADARLK IAGPNVLSSK NPPPWWKLLL LILPNPFTIL LVFLAIISVA
     TPQPDWKTFV ILMVMILISS AVRFWQEYRS SIAVIKLQSS VSADTKVRRQ CPTSGKFLDG
     TQTSESTIHV KDIVPGDIVI IRPGLTVPAD CLILEASSLY ISQSTLTGEN EPLRKTPNLQ
     PAKFEKEDPR FFELENIAFM GTSVISGSGL GLVLRTGDDS FIATIMKQLN KKRPVNSFQR
     GIRNVTYMLI GFMLTMVPIV LGISGKTTGN WGNAALFSLS VAVGLVPEML PAIVNTNLAK
     GAFSLSKKKT IVKRLDSIQN LGGMSILCSD KTGTLTKDEI TLSDYLDCSG VRNRGVFQLA
     FINAKCQEIQ GTSIDSAIIN FQSREPMQTP PYEAVSEIAF TFERRRSSCI IRGPTKKLKL
     VCKGAYEEVL ALCTSVRDGA KTLSLCAEWH KKLAAQAERL SSDGFRVILV ATREVKDSEM
     GNEDFIEDDL ESSLTLEGFL TFLDPPKEDA AASIQRLQRL GVDVRILTGD NMPIALRLCQ
     LLNLVSYVSE GDAQAITGPE LARLEGTDQF HDVIRTCKVF AKLSPAQKGQ VILSLKANGD
     CVGMLGDGIN DCVALRFADV GISVDSGAGV AKDCADVILT EKGLNIIVDA VTMGRVTYGN
     TIKYIKMVAS SNFGNVFSIL IASAWLPFEP MTSLQLLIQN LLYDISQIAI PWDRMDEEYL
     QEPKKWDAIG GFRLNISLGS LCQLMCDVDL LRFIIVLGPT SSTIDVLTFC LGWFYYNIRT
     ADDPEAVKLF RTHWFLQG
//
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