ID A0A093YEN1_9PEZI Unreviewed; 1102 AA.
AC A0A093YEN1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
DE Flags: Fragment;
GN ORFNames=V490_00207 {ECO:0000313|EMBL:KFY03349.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFY03349.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFY03349.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFY03349.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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}.
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:KFY03349.1}.
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DR EMBL; JPJS01000076; KFY03349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093YEN1; -.
DR STRING; 1437433.A0A093YEN1; -.
DR HOGENOM; CLU_001771_0_2_1; -.
DR Proteomes; UP000029320; 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; 2.
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; 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 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; 2.
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; 2.
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; 2.
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:UP000029320};
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 345..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 443..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 632..653
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 673..703
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1032..1054
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1066..1087
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 82..147
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 162..228
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 47..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFY03349.1"
SQ SEQUENCE 1102 AA; 119480 MW; 3A9DF06A8782B8A4 CRC64;
HVALFDNHGR QVEEHDLAGI NYSEASRSQQ KHIDNCNACQ KEWGRDGASP VLPTRSTAMG
SNDNPTVIDI DDPSEYDSST TYTASLSIEG MSCGSCIGKI TAGLEELPFV TKVNIDLLTN
SGAVEFRGKI NVDPILEKVG DLGYSATLVE LVEPRPKSNP TYTASLSIEG MSCGSCIGKI
TTGLEGLPFV ATANIDLLTS SGSVEFRGEM RNLDLILDKV GDMGYRATVV ELVEPKSSLA
CQERVVDVQI DGMHCIRCPE RVVLVLEELR SEKGVASSLS ISRPPSFKDP RVQITYKPSL
SEGLTIRCFI STIQSVDSAF SVYVYHPPTI EERSRRIQHQ ESRSILWRLV FAGLVAIPSL
IIGVVYMALV PGDNPTRIWF EEPMWAGNAT RTEWALLILT TPVMFFGTDL FHRRAFKEIW
AMWKPNSAVP MLRRFYRFGS MNMLISVGTM VAYFSSLAVL IMNATQKTER DHSMRMSSSY
FDVITFLTFF ILMGRYLEAY SKAKTGDAVA MLSKLRPNQA LLVGKDREVQ KVPVDQLEVG
DVVQIPRGNS PPADGTVEHD GSFSFDESSL TGESRPVRKT KGDTVFTGTV NVADPVEIKV
TELGGASMLD QIIEVVRGGQ AKRAPIERFA DVLTGYFVPV VTLLAIVTWV TWLGLGLSGR
LPGAWLDSSQ GGWAFWSLEF AIAVFVVACP CGIGLAAPTA LFVGGGLAAK QGILVQGGGQ
AFQEASNLNV MVFDKTGTLT QGQMKVTDYE QLHPDISKDR LFSMARAMEG ISSHPIAQAI
TTFCAPSSEE LTMSDIREIP GHGMTARFTF GSESGEHAVE AAIGNGKLLD LLNGTETEKA
EASVRSGNSI DNKIATTSST NLQQALYRHQ IQGHSVAVVA IRHSNRYKAV GIFVLSDPLR
PEAPEVIASL RSLGLAIHLC TGDNATTAHA IALQLNIPPE NVRAGVLPQG KAEYIHELQH
PTEGGRKLVA FAGDGLNDTP ALTAADVSIS LSSGSDIAIN ASSFILLNSD LAAIRTLFTL
SKRVFLRVKM NFFWAGIYNV TLIPVAAGVL YTIGATEQHA GWRMSPVWAA IAMAGSSISV
VLSSLALKLP ELRWPFKSQK PN
//
