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Database: UniProt
Entry: G4TMB5_SERID
LinkDB: G4TMB5_SERID
Original site: G4TMB5_SERID 
ID   G4TMB5_SERID            Unreviewed;       925 AA.
AC   G4TMB5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Related to Cu-transporting P1-type ATPase {ECO:0000313|EMBL:CCA72456.1};
GN   ORFNames=PIIN_06392 {ECO:0000313|EMBL:CCA72456.1};
OS   Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS   (Piriformospora indica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Sebacinales; Serendipitaceae; Serendipita.
OX   NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA72456.1, ECO:0000313|Proteomes:UP000007148};
RN   [1] {ECO:0000313|EMBL:CCA72456.1, ECO:0000313|Proteomes:UP000007148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA72456.1,
RC   ECO:0000313|Proteomes:UP000007148};
RX   PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA   Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA   Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA   Kogel K.H.;
RT   "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT   the Mutualistic Root Symbiont Piriformospora indica.";
RL   PLoS Pathog. 7:e1002290-e1002290(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCA72456.1}.
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DR   EMBL; CAFZ01000165; CCA72456.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4TMB5; -.
DR   STRING; 1109443.G4TMB5; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   HOGENOM; CLU_001771_0_2_1; -.
DR   InParanoid; G4TMB5; -.
DR   OMA; QGMKGTF; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000007148; 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   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; 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:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 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   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 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|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007148};
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        188..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        230..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        313..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        474..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        519..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        872..893
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        899..921
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          14..80
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   925 AA;  101161 MW;  ED58DEED4ADFD4C4 CRC64;
     MDTVTVTSPQ PRIKRASFGI QGMTCSACTN AIQDAFKDLP TVQTVNVSLL NNSMTITFDE
     NGLNTAQIME MIEDLGYEPS QWDMAGQEEL SSAPDERQVQ IIFHGLESKG DIEEVNRYLS
     GLGLISFTPI TESRGITTLR YIPSSILNIR YILSRPPHPI TASIYQQPSL HSRSREIQRK
     EAKRMLRLFL ASAVFAIPTF VIGIVGMLLL PRDNRFRQWC QRTGWWGGAS HAVILLWIFA
     TIVQFGIARI FFIHAWGSLR FRRHWSTLFR FGNMNLLVAL STGVAYIASV VMLVIDIRTE
     PHMTEMSGEM RSYFDSCVFL TFFILAGKAL ETRARLKTGD AIAMLGQLRP ERALLLGNEP
     QSPVDLKSQQ TEDVSVDMLE LGDHILVRPG SIPPADGTVL EGTTTVDESS LTGESVPVLK
     SPGDPLLSGT VVVSSAVVMR IDHLGEETML QQIVRAVGES QNTKAPIEEL ADRITAVFVP
     VIIYIAIIVS VLWLSLALTP GGLPVGYIPK DKTQTADRVF FALEFAIAVL AVACPCGIGL
     AAPAAQAVGS GMAAKAGILA QGGGTAFQLA TEVDVVVFDK TGTLTQGQPT VVQSIVTQTP
     SWILDAVVAI EQTSTHPLAA ALVRYVEGKR SAVEKPAIEG IDIREIEEIA GKGARGQLHI
     QDKKFEFRLG NRAIIDDATF TAETQEQRHQ DVETWKRQGY SVVYFAISHN FSPFDIVAVF
     AIADPPRPEA KSVIASLKRM GKEVYMLSGD NEVTARTVGR ELGIDTNHVV AGVLPHEKSK
     FIQELRQPNR VEKDSKIGGQ KERSRVVMFA GDGLNDSAAV ATADVGVAFA HGSQVTLTSA
     SFVLLQTQAP LEGVLNILRL SRRVYRRQKF NFAWAMIYNI ILIPLSAGAF YPLNHTRIPP
     VWSALAMALS SVSVVLSSLA LRWGL
//
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