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Database: UniProt
Entry: C0NPY7_AJECG
LinkDB: C0NPY7_AJECG
Original site: C0NPY7_AJECG 
ID   C0NPY7_AJECG            Unreviewed;      1388 AA.
AC   C0NPY7;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Cation-transporting ATPase {ECO:0000313|EMBL:EEH06997.1};
GN   ORFNames=HCBG_05217 {ECO:0000313|EMBL:EEH06997.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH06997.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR   EMBL; GG663368; EEH06997.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NPY7; -.
DR   STRING; 447093.C0NPY7; -.
DR   VEuPathDB; FungiDB:I7I50_04554; -.
DR   HOGENOM; CLU_001828_4_0_1; -.
DR   InParanoid; C0NPY7; -.
DR   OrthoDB; 6047at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd07543; 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   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; IPR047820; P5A-type_ATPase.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   NCBIfam; TIGR01657; P-ATPase-V; 1.
DR   PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR   PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001631};
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        138..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        520..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1388 AA;  155064 MW;  8D984EAAE3D5F141 CRC64;
     MWEDWTKEIG GLEAVRKNDC RRFPGESSGT LRRLRRKTIA SGSSEGLVRL NGTRILETSL
     RSINNCEPFI FSREILALTL PLALLPRCIL SWDLVYVYQL YLPDRASRAS SGIMPRLVDN
     SQIQSASLHN PLPLQLHAYV WPFLIIWPTF LAVYLSPERY DTYIQGSEWT FLWAGGIFTL
     QALVWLSTKW NVNVQALFTT STAKSVYSAK LIKVSPVVNA GSAEICPLLR EKYAGKDDIS
     FLFQKRRFLY YPDRNTFAPL SYAIDAEPKP LLKTFQHSQG LKTDKEIGEN QNHYGDNTFD
     IPVPTFTELF KEHAVAPFFV FQVFCVGLWL LDEYWYYSLF TLLMLVTFES TVVWQRQRTL
     NEFRGMSIKP YEVWVYRKNA WTEITSDKLL PGDVLSVNRT REDSGVACDI LMIEGSVIVN
     EAMLSGESTP LLKDSIQLRP EDDQLDPEGL DKNSFLYGGT KVLQITHPNS TASPPNGIPT
     PPDNGALGVV VKTGFETSQG SLVRTMIYST ERVSANNVEA LLFILFLLMF AIAASWYVWQ
     EGVAKDRKRS KLLLDCVLII TSVVPPELPM ELSLAVNTSL AALSKFAIFC TEPFRIPYAG
     RIDIACFDKT GTLTGEDLLV DGIAGLTLGH ASAKTDKHGA HTDITPVEKV ANETTLVLAT
     AHALVKLDEG EIVGDPMEKA TLNSLGWVLG RDDILTSKAT GASRQPGRAL DSVQIKRRFQ
     FSSALKRQSA IATVISTDRQ TSKKLRGTFV GVKGAPETIR TMLVSTPPYY EETFKYFTRN
     GARVLALGYK YLSTESELGQ GRINNLKRED VESELHFAGF LVLQCPLKDD AVKALRMLNE
     SNHRVVMITG DNPLTAAHVA RQVEIVDREV LILDAPENDN SGTKLVWRTI DDSFSVDVDP
     TQPLDREILE TKDLCVTGYA LTKFKNKKAL PDLLRHTWVY ARVSPKQKED ILLGMKDAGY
     TTLMCGDGTN DVGALKQAHV GVALLNGSQD DLNKIAEHWR NTKMKEIYEK QVSLMQRFNQ
     PAPPIPANIA HLYPPGPNNP HYEKALIREA QRKGITAPAA IGGNGIPTVT SPGAHAIQQS
     TMNLTPQQRQ QRHASLAAAG FADKLTATMM EQELDDNEPP TIKLGDASVA APFTSKLANV
     IAIPNIIRQG RCTLVATIQM YKILALNCLI SAYSLSVIYL DGIRFGDGQA TISGILMSVC
     FLSISRAKSV EGLSKERPQP NIFNMYIMGS VLGQFAVHVA TLIYLSNYVY TIEPAIYLLQ
     LIQQISTFSI NYQGRPFRES IRENRGMYWG LILTSGVAFS CATEFIPELN EKLRLVPFTT
     MFKVTLTALM LADYAGCWLI ENILKTYFSD YRPKDIAVRR PDQLAWEEER KRKEAVAEEN
     EKESKRKV
//
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