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Database: UniProt
Entry: A0A1L9RX25_ASPWE
LinkDB: A0A1L9RX25_ASPWE
Original site: A0A1L9RX25_ASPWE 
ID   A0A1L9RX25_ASPWE        Unreviewed;      1272 AA.
AC   A0A1L9RX25;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN   ORFNames=ASPWEDRAFT_37188 {ECO:0000313|EMBL:OJJ39407.1};
OS   Aspergillus wentii DTO 134E9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Cremei.
OX   NCBI_TaxID=1073089 {ECO:0000313|EMBL:OJJ39407.1, ECO:0000313|Proteomes:UP000184383};
RN   [1] {ECO:0000313|Proteomes:UP000184383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DTO 134E9 {ECO:0000313|Proteomes:UP000184383};
RX   PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA   de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA   Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA   Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA   Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA   Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA   Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA   Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA   Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA   Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA   Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA   Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA   Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA   Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA   Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA   Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA   Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA   van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA   Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA   Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA   Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA   Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT   "Comparative genomics reveals high biological diversity and specific
RT   adaptations in the industrially and medically important fungal genus
RT   Aspergillus.";
RL   Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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; KV878210; OJJ39407.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L9RX25; -.
DR   STRING; 1073089.A0A1L9RX25; -.
DR   VEuPathDB; FungiDB:ASPWEDRAFT_37188; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000184383; 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:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd00371; HMA; 4.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 4.
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; 2.
DR   NCBIfam; TIGR00003; copper ion binding protein; 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; 4.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
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; 4.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
DR   PROSITE; PS50846; HMA_2; 3.
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:UP000184383};
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        489..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        579..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        618..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        787..810
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        830..858
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1187..1209
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1233..1255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          25..90
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          228..294
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          311..376
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          191..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1272 AA;  137746 MW;  2084C1B8EC30BB4C CRC64;
     MPSHARLSGA SLSGLRTSEP DLDCPKSTFF VSNIHCSSCV AYITEVLFEI PSVKTVDVSI
     FTHEVHVRHG AETQASGLAA ALIQAAFEVH YVTTYDHKGT IISELDTTSW LSSDPVPFSP
     PRTVDHRSAP QNQLHIANCD ACRKEENERL SSLPYPSNVA SPRERRLRNY SRPISNVHLV
     NQNFDQLESD TESLVRPISS TSHISHKSHR SEQSSTQKEL QTGKNEEFKA RISIGGMSCA
     SCVNSITNEV KQLEFVKDIT VNLLTNSAAL VYTGPRSKID KIVEQIEDIG FEAAIDEVDV
     ITQPKQNLTA YVAEIAISGM TCGSCVGSVT RGLEELPFVT NVSVNLLSHS GKVEFEGQEN
     IGEIVEKIED LGYDASVNSI NPLAASNDGD LTISSRTVSI RVNGMFCHHC PEKVLKSLEG
     FSDVQVDQAL SFKTPILKVT YTPQPPSLTI RNILSAIDSA HDEFKPEVYH PPSVEDRSRA
     MHLHERRRLL SRLAFVLAAA IPTFLIGVVF MSLVSSKNRI RMYLEQPMWV GSVTRLEWAL
     FIMTTPVMFY GTDIFHVRAI KEIHALWRPG SRVPLLRRFY RFGSMNLLIS AGTTVAYLSS
     LAVLIMDAVM DSPASGHSSS YFDSVVFLTL FILAGRFMEA YSKAKTGNAV ASLGKLRPSE
     ALLFISPSTG TDQTGSDSIG TETIQRINVD LLDIGDTVSI PHGASPPADG IVVGTGSYQF
     DESSLTGESK PVKKSAGDQV FTGSVNVGQP VQIKISAVGG SSMLDQIISV VREGQSRRAP
     LERVADLLTS HFVPIITLIA ILTFAIWFAL GQSGALPPDY LDVSRGGWAF WSLEFAISVF
     VVACPCGLAL AAPTALFVGG GLAAKQGILV KGGGEAFQEA SRLDAIVFDK TGTLTEGGSL
     KVSDHEALIK DPEELQVAWA LAQKLEESSN HPIARAISDF CCDKTSRSIE SSDIQEISGQ
     GMKGTFTISS DQSTVQYEAA IGNERLLQEL ASPDIDTYYL TNLLTEYQSA GKSTAILSLR
     KIGSPDLKDS QFAPAIVFAT SDLIRPEAVQ VISKLRKRQV EVFMCTGDNQ TTAHAVADML
     GIPRSNVIAN VMPSGKADFV RQVQEGTNGS NSEGTNEPLS RSIVGFVGDG VNDSPALAAA
     DVSIAMASGS DVAMNSASFI LLNSDLDTIL QLVILSRRVF NRVKMNFCWA VVYNISLIPI
     AAGVLYPIVN GHRHEMVGGE LVTLDNHWRL SPVWAALAMA LSSFSVICSS LALGIEWEKI
     KKVLGLGKSE QS
//
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