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Database: UniProt
Entry: G3APQ9_SPAPN
LinkDB: G3APQ9_SPAPN
Original site: G3APQ9_SPAPN 
ID   G3APQ9_SPAPN            Unreviewed;      1049 AA.
AC   G3APQ9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN   ORFNames=SPAPADRAFT_55732 {ECO:0000313|EMBL:EGW32230.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW32230.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; GL996502; EGW32230.1; -; Genomic_DNA.
DR   RefSeq; XP_007375506.1; XM_007375444.1.
DR   AlphaFoldDB; G3APQ9; -.
DR   STRING; 619300.G3APQ9; -.
DR   GeneID; 18871964; -.
DR   KEGG; spaa:SPAPADRAFT_55732; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   HOGENOM; CLU_001771_0_1_1; -.
DR   InParanoid; G3APQ9; -.
DR   OMA; GGKFMVC; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 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; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 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; SSF55008; HMA, heavy metal-associated domain; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        292..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        326..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        365..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        543..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        586..605
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        925..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        952..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          51..117
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   1049 AA;  114389 MW;  5A3443CD1ED0BC92 CRC64;
     MPSMPQPKTV KYAPVLHNDS SIDITVQEME HSSSVFSPLP SPYSPTLSSA SSTTLTIQGM
     TCGACSASIT ESLKSTPGVI DASISLITEN GLITHDSSII TAQQIKQTIE DCGFDAQIQS
     STNIMKEQPS SRSDIQDEED TNLQIVGISS AVDVSALRYN IEAYLHSCPG VIEFVLVLRN
     NSNDITQEDQ LEQSEDSTVL TDEISIKFQP SAVGIRDLVD GLNVIEPGVE FVVMNSLDQS
     SAAQLKLLSK VKDIEYWRNN CIKCVIFGLP CVVLEHVEQM EFWRSKLVFP GLFWVTLIQF
     VLASYIQFIL GAVFIKKFIA FVRNGFKGAS MDVLICISTV VSYLFSLTTI TLSVWYGEKE
     HPPKVLFDTM VMIILFISLG KLLENKAKGA TSTALSKLLS LTPSTCVIVK DVADYQLFMQ
     QQSEKTSAGA IQDFATRTIS IDLVQPNDIA IVLPGGKIPA DGTIVFGETE IDESLITGES
     LPVHKLRGDP VIGGSVNGPH LIHIQVSKTG KKSQLQQIIN LVKDSQVNKA PVQRYSDYLA
     ARFIPAVILL SIVTFILWSI VCYTIHPDKL PKIFVKDANG KLFVCLKLAI SVIVVACPCA
     LGLAAPTAVM VGTGVGASNG VLIKGGDILE KATGINVILF DKTGTLTTGE MSLVSATPKI
     ENLKLTVKDW WNLIGSVECN SEHPTGRALT KIAKNQLNMN FDEDQFDTII DEVKVVTGAG
     IHANVQLPSG DKYNVQIGNH KLIETLCPQF LPDVQKLNLD NSNNTLSHVI INNQYCGYIE
     LKDTLKDGSW DVVHYLQRQG YIVGMVTGDK RGAAWKIGRE VGIPESNIFY EVSPIHKDAV
     ITDLKNRLGG NDNVKVAFIG DGINDAPALA NADIGMAISS GTDIAIESAD VVLLGSSKKQ
     QTDLHGVINA LQISNATFTR IKVNFVWAAG YNFLMLPFAM GCFLPLNVML PPIAASAAMM
     LSSVSVVLSS LFLKNWKSPV ISSGARGKED LEAGTSTFNL KTGTLEEFNE VKRTRGFRIG
     RLFSMFKFHK RETKFVNHEY ELVPTQSRN
//
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