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Database: UniProt
Entry: A0A0D1EBR9_USTMA
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ID   A0A0D1EBR9_USTMA        Unreviewed;      1056 AA.
AC   A0A0D1EBR9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative P-type ATPase, Cu(2+)-transporting ATPase {ECO:0000313|EMBL:KIS71795.1};
GN   ORFNames=UMAG_00227 {ECO:0000313|EMBL:KIS71795.1};
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS71795.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS71795.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA   de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA   Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA   Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA   Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA   Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA   Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA   Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA   Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA   Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2] {ECO:0000313|Proteomes:UP000000561}
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003140; KIS71795.1; -; Genomic_DNA.
DR   RefSeq; XP_011386160.1; XM_011387858.1.
DR   AlphaFoldDB; A0A0D1EBR9; -.
DR   STRING; 237631.A0A0D1EBR9; -.
DR   EnsemblFungi; KIS71795; KIS71795; UMAG_00227.
DR   GeneID; 23561593; -.
DR   KEGG; uma:UMAG_00227; -.
DR   VEuPathDB; FungiDB:UMAG_00227; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   InParanoid; A0A0D1EBR9; -.
DR   OMA; GGKFMVC; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000000561; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR   GO; GO:0043682; F:P-type divalent copper transporter activity; IBA:GO_Central.
DR   GO; GO:0055070; P:copper ion homeostasis; IBA:GO_Central.
DR   CDD; cd00371; HMA; 2.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR00003; copper ion binding protein; 2.
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; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00942; CUATPASEI.
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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000000561};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        210..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        248..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        281..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        342..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        499..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        541..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        922..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        951..970
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          25..91
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          119..185
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1035..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  113013 MW;  6B51318EE85296C8 CRC64;
     MSPTAPLLEE PQASGSTSPP MGAKVTATFQ IGGMTCGACV ETIERMIRSQ PGIESISVAL
     LAEKATITFD DSIWSLDKVA EEIEDTGFDA TFLEVLRTER PDAGFASKEA SSDPVPRLDT
     VQLSVYGMTC ASCSSTIERE TAKIDGIRSI SVSLSTEKAA IVYDPSKLGI RDLIEHIEDL
     GFDAVVSDDR NSTQLASLGR IKEIAEWRSA FLFSLSMGLP VFFLSMVLPK FSVTHAILWW
     QPISGFYLQD LICLALTIPV QFGIGLRFYR TSWKAIKHGS ATMDVLIVIG TTASWTFSVF
     SMIARLFCVD ELATATKEAA SIVARSSGMI DMMVPGQCTK PATFFDTTTM LFTFVSFGRF
     LENTAKGKTS EALSRLIGLT PTSATIYTDG AEGKIEKKVA SELVQRGDYV KVVPGERIVA
     DGVIVRGEST VDESMVTGEA VPIHKLRGSS VIGGTVNGTG TFDFLVQRAG KDTSLAQIVK
     LVDEAQTSKA PIQAFADRVA GYFVPTVVGL GALTFVAWMV IAHLLSGHML PSIFNQQGVT
     KFMVCLKLCI SVIVVACPCA LGLSTPTAVM VGTGVGAQNG ILIKGGGPLE ASTTIRRMLF
     DKTGTLTVGK LTLSQVIWPN GEEGGLDNIA VGGLSRRQVI RIIGAAETRS EHPLARAIAS
     WAASQLETGI TAVDEQADIV MSGTSIEAFQ SFTGKGVVCR VQLEETMTLH EVRIGTPEFI
     LSDEKHALDH TEFGSQATEV LSQQQSQGRT AVLASVDGTL AAVLSLSDRL KPEAKQTLGA
     LRRMGIQCSM VTGDAYATAR ALARELGMDE QNDVYAEMSP IDKQEIILQL RRESRVADLE
     SGETFSPFRA NGRSKSGGIA MVGDGINDSP ALASADLGIA LGTGSDVAIE AASIVLMRSS
     LLDVAASIHL SRRIFRQIKL NFIWATVYNM IGIPLAMGIF LPWGLSLHPM MAGAAMAFSS
     VSVVASSLTL KWYKRPAELT LPTEVETPDS IQLQEMLARS DAGALDRVVA NLKDVGYQVL
     GKFESILSKS RLSLGRGSSR RPAQTEGYQQ VASDDV
//
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