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Database: UniProt
Entry: H6C9H1_EXODN
LinkDB: H6C9H1_EXODN
Original site: H6C9H1_EXODN 
ID   H6C9H1_EXODN            Unreviewed;      1048 AA.
AC   H6C9H1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Ca2+-transporting ATPase {ECO:0000313|EMBL:EHY59880.1};
GN   ORFNames=HMPREF1120_07859 {ECO:0000313|EMBL:EHY59880.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY59880.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY59880.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY59880.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; JH226136; EHY59880.1; -; Genomic_DNA.
DR   RefSeq; XP_009160341.1; XM_009162093.1.
DR   AlphaFoldDB; H6C9H1; -.
DR   STRING; 858893.H6C9H1; -.
DR   GeneID; 20312498; -.
DR   VEuPathDB; FungiDB:HMPREF1120_07859; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   HOGENOM; CLU_002360_3_3_1; -.
DR   InParanoid; H6C9H1; -.
DR   OMA; KMHACET; -.
DR   OrthoDB; 203629at2759; -.
DR   Proteomes; UP000007304; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:UniProt.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
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; 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   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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304};
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        332..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        888..908
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        938..954
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        975..993
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1005..1023
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          37..111
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          463..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  113534 MW;  87ECF6DF5076733D CRC64;
     MSTLSVPALP FVKPDSSPKR ARSPAPYADT FTSITSSYAL LSPQQTADRL QTSLTHGLSQ
     SEAQARLARD GPNELPHEEE EPLWLRFLKQ FKETLILLLL ASAAISLFIG NKDDAVSIAL
     AVTIVVTVGF VQEYRSEKSL EALNRLVPYH AHVRRTGLRP WMQASRLPIP EDEIELEPLS
     NGLTSEDKTS ATIPASQLVV GDLVIFSTGD RIPADIRITR SSELTIDESN LTGENEPVEK
     HAAALDRAAP SFAHHGTPEP LNAAGTVGAD VRLNDQHNIA FMGTLVRSGH GEGVVIATGG
     NTEFGTISLS LQEIEAPRTP LQQSMDLLGK QLSYMSFVVI GIIMIIGLLQ GKKPLDLFTI
     GVSLAVAAIP EGLPIIVTVT LALGVLRMAK RGAIVRKLPS VETLGSVNVV CSDKTGTLTM
     NHMTVTEMWH FDMPKPFGVD TSAEPSAATR AILRIGNISN NGRLSHTTSG TPATAASAAV
     LSSTRDRSST NTRSRWLGQP TDIAMLDLLD AFGEDDIREQ IGHRTAETPF SSERKWMGVV
     IGNALGELAN DHGTSTETAY IKGSIEQVLS RSDTYLTRDG QEVILDETRR QQALAAAQTM
     AEEGLRVIAF ASGVVRNKQR QPSRSPTPSR ADKKPEETDI FQGLCFAGLV GMNDPPRKDV
     HRSIRRLMSG GVKVIMITGD AETTAVAIAK NLGMPINQGS SASRSVLRGD ELDRMSEQEL
     AEAIGKTTVF ARTSPDHKMK IIRALQARGD VVAMTGDGVN DAPALKKADI GIAMGMLGTD
     VAKEAADMIL TDDDFSTILR AIEQGKGIFY NIQNFITFQL STSVAALTLV LLSTMFGFKN
     PLNAMQILWI NILMDGPPAQ SLGVEPVDPR VMTQPPRPRN ANVLTKRLIR RVLTSAFIIM
     IGTLTVYIHE MAVVDDPSAG VTDDGAPLRT RMVTKRDTTM TFTTFVLFDM FNALTCRSEA
     KSVLFGEIKL FGNKMFNYAV AGSLAGQLCV IYLPFLQRVF QTEALGLGDL LALVCIASTV
     FWADEFRKWI ERRRAAGYLP SVGYSASV
//
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