ID C6HCA9_AJECH Unreviewed; 1260 AA.
AC C6HCA9;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Copper-transporting P-type ATPase {ECO:0000313|EMBL:EER42199.1};
GN ORFNames=HCDG_03658 {ECO:0000313|EMBL:EER42199.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER42199.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) 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; GG692422; EER42199.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HCA9; -.
DR STRING; 544712.C6HCA9; -.
DR VEuPathDB; FungiDB:HCDG_03658; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR OMA; QGMKGTF; -.
DR Proteomes; UP000002624; 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; 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; 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; 4.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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; PS01047; HMA_1; 2.
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 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:UP000002624};
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 482..506
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 531..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 580..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 613..630
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 779..798
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 818..846
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1176..1199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1219..1239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 29..94
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 216..282
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 299..364
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 386..458
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 170..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1260 AA; 136511 MW; 9B64522E2AF6C977 CRC64;
MADNQPIPKP AAVAKRTSLP LLSAGPKTTT TVLLVNNIHC ASCVAYAKEV LFHIPHIISV
DVTILAHKVH IRHGPEVSTT HLVNALINAA FEVYHASSRD ESGAEISNID VSLPASPFIE
RHLFRTGDQG DKNAQARNRT HIDNCDACRA EELARTQAEE KKDLSSFPQL HAVGDKTPMG
NDLSKKPEKV ADESWMIKRS DVPDLEKGLA LTDEEYNVSI SISGMSCSSC AGTVTSAIEQ
LSFVKSVDVA FLTHSASLTI RGPKENIDEV LSVIDGLGYE GELQDISLKS SPSSRRDIYA
ATASIGGMTC GSCVGTITRG IQELPFVTNV VVDLLGSSAK FEFEGRERLD EIKQVVEGLG
YEFVVSQCVP LKRSGTGPDD SGPLKRTVEI QVDGMFCHHC PEKILSALEA MDGGESVSVV
ESLTFKKNVV KITYQPNPPS MTIRKIIAVI ESANDAFKAS IYHPPTIEDR SRAMQLLERR
RILLRLLFVF IAAIPTFLIG VVWMSLVPST NRLRTYFYEP IWAGQVTRLE WALFIITTPV
MCYGADVFHV RAFKEIRALW RPRSKVPILR RFYRFGSMNL LISAGTSVAY FASIAMLAVA
AGMEEHQPHM SPYFDTVVFL TLFILAGRFL EAYSKAKAGD AVASLGKLRP SEALLVLDSP
STNPDDALSS NLQRVNVDLL EVGDIVNIPH GASPPADGIV TSSDTYRFDE SSLTGESKPI
TKVAGDKVYS GSVNVGQPVY IRVSDIGSTS MLDQIVAVVR EGLTKRAPVE GVADIMTSYF
VPVITLIAIL TFVIWLSLGL SGSLPTDYLD SAQGGWAFWS LKFAIAVFVV ACPCGLALAA
PTALFVGGGL AARRGILVRG GGEAFQEASK LEAIVFDKTG TLTEGGTLRV SDHEMLVADE
EQQQVAWKLA KILEQSSTHP IANAIADFCA EQSSVSVISS TLTEIPGQGM KGMFSLTVNG
IEVKYEAAIG SQRLLDSLVD ENGTDLYFLS NTLTKYQSEA KSTAILAIRQ ISDALSPFVP
AIVFATSDPI RPEAASVISS LQSKNIEVFM CSGDNQTTAH AVAATIGIPA SNVLANVLPS
QKAEYIRQIQ DNKLHTSSSS SINKEKPDKK RIIAFVGDGT NDSPALTAAN VSIAMASGSD
VAVNSAGFIL LNSDLTTILE LCTLSRRVFN RVKWNFGWAA IYNMILVPVA AGVLFPIVTG
KKVKEDGTVV NEHWRLDPVW ASLAMALSSI SVVVSSLALR FEWRRARPWI VRKVRFWTKA
//
