ID A0A094E209_9PEZI Unreviewed; 1061 AA.
AC A0A094E209;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
DE Flags: Fragment;
GN ORFNames=V499_09110 {ECO:0000313|EMBL:KFY70513.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY70513.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY70513.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY70513.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY70513.1}.
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DR EMBL; JPKB01001673; KFY70513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094E209; -.
DR HOGENOM; CLU_001771_0_1_1; -.
DR Proteomes; UP000029295; 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; 3.
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; 2.
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; 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; 3.
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; 4.
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; 4.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS50846; HMA_2; 4.
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|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
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 383..401
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 413..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 459..478
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 490..508
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 667..688
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 708..731
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 25..91
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 121..187
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 210..276
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 291..357
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT NON_TER 1061
FT /evidence="ECO:0000313|EMBL:KFY70513.1"
SQ SEQUENCE 1061 AA; 111512 MW; 824A82540ACC8641 CRC64;
MAPTYTPVAS DDTVETLLAA PPQLAVTTLR CGGMTCGACT SAVEAGVEGL PGVQSVSVSL
IMERVVVNHD PSKTSAEKIA EAIEDRGFDA EVLTTDVRTP TYDKAPPYDS IEESEVGAQT
TTTTIAVEGM TCGACTSAVE GGFTDVPGVK HFSISLLAER AVIEHDATIL SAAQIAETIE
DRGFGATIID SQLSTPKHAV AHSANETQVA TTTVEVQGMT CGACTSAVEG GFQDLEGLVQ
FNISLLAERA VIVHDPAKLS PEKIAEIIED RGFDARILST TIGTSEQSNG ISSQFKVFGL
RDAAAANGLE SALRAIPGVT SASISISTSR LIVNHKPRIV GLRALVEKIE SLGFNALIAD
NDDNNAQLES LAKTKEIAEW RSAFRTSLCF AIPVFLISMI IPMFLKPIDF GKILLYFPGL
YLGDVVCLIL TVPVQFGVGK RFYISAYKGL KHRAPTMDLL VVMGTSAAFF FSVASMLVSI
LCPPHTRPSI LFDTSTMLFT FVSLGRFLEN RAKGQTSKAL STLMSLAPSM ATIYADPIAA
EKAAENWNKD KNEESASDST ASEEKVIPTE LLEMGDVVIL RPGDKIPADG VVTNGETYVD
ESMVTGEAMP IQKSKGSMLS AGTVNGAGRV DFRVTKAGRD TQLSQIVKLV QSAQTSRAPI
QRLADTIAGY FVPCILVLGI STFSVWMILS HVMHDPPKVF VDEASGGRLM VCVKLCISVI
VFACPCALGL ATPTAVMVGT GVGAERGILV KGGAALETAT TITQVVLDKT GTLTMGKMSV
AEAKLEPEWE NSDAKKKLWW SAIGLAEMGS EHPIGKAIVA AARTSLQLGP SDAVDGSIGD
FQPVVGLGIN ALVEPASASR TRYRVLIGSV RFLRSHSVDV PKSAITASED INALATTSSK
PTGSSGTTNI FTAIDGIYTG HICLADTLKP SAAAAVAALH RMRIKTAIVT GDQRSTALAV
ARAVGIPAEH VYAGVSPDQK QELIKKFQAA GEVVAMVGDG INDSPALATA DIGIAMASGT
DVAMEAADIV LMRPNDLMDV PGAIALAKGI FGRIKLNLAW A
//
