ID S8BK08_DACHA Unreviewed; 1060 AA.
AC S8BK08;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=H072_11045 {ECO:0000313|EMBL:EPS35577.1};
OS Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS (Monacrosporium haptotylum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Dactylellina.
OX NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS35577.1, ECO:0000313|Proteomes:UP000015100};
RN [1] {ECO:0000313|EMBL:EPS35577.1, ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS35577.1,
RC ECO:0000313|Proteomes:UP000015100};
RX PubMed=24244185;
RA Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL PLoS Genet. 9:E1003909-E1003909(2013).
RN [2] {ECO:0000313|Proteomes:UP000015100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA Ahren D.G.;
RT "Genomic mechanisms accounting for the adaptation to parasitism in
RT nematode-trapping fungi.";
RL Submitted (APR-2013) 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:EPS35577.1}.
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DR EMBL; AQGS01001127; EPS35577.1; -; Genomic_DNA.
DR RefSeq; XP_011116415.1; XM_011118113.1.
DR AlphaFoldDB; S8BK08; -.
DR STRING; 1284197.S8BK08; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_0_1; -.
DR OMA; SARCICR; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000015100; 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; 1.
DR Gene3D; 3.30.70.100; -; 1.
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; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
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:UP000015100};
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 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 441..462
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 474..495
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 507..525
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 658..684
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 696..723
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1000..1023
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1029..1051
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 259..326
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1060 AA; 112746 MW; 6EAC8EB9D43BAF8C CRC64;
MAKSCIRKAA ALKCNATCGT EGKGKVVIPK KPDACKDGCC SNSAKLLPPE GVSPAKALHT
DTEVAKEVKE KCCTQKENGC CAPKKPTYIS PEPKGKAFGS SHKKESCCAP VRGNGSFTEK
ESCCKPKKEG CCSPPAAKDE KCCDVQQTAS LPIEQPAPSI KSIDSSTTLA EACATHLQQA
FNQYLSYLDE GRCICRNILN ASSNCRSQTS LPPPPKNGVK VQSTCDFDEI EIAPISPSST
KGIVARSKEV EPENSASRQH VVLKVSGMTC TGCSRKLMNV LKNFAGLSNI DVTFVTGVAE
FDLNLFVANL QQVVLRIEKE TGFKFSQIES NCQTLDLLIQ PDSVQTVRKQ LGDLVESIEQ
VGKAIYRINY DPAMIGARTI FSAVEGPGIS LAPPGNNAEL ANSKRRLLHL TYSTVAATVL
TIPILALNWS DNPVPYSRRS IVSLVLATLV QALAVPEFYV GAIKSLVFSR VLEMDMLVVI
SITAAYIYSL VAFSLTHAGV ALEIGEFFET SSLLITLVLL GRLIATIAKV KAVSAVSFRS
LQAEKAILVT GPASTIEIDA RLLQLGDCFV VPAHSRIVTD GIVIHGSGSV DESMVTGESI
PVSKVVGDNV IAGTINGPGS LTIRMTRLPG KNSITDIANL VENALAAKPH IQDVADRVAS
YFIPVVISIS LIVFGIWIAV ALRIRGNNGG SAFGTAITYA IAVLAISCPC ALGLAVPMVL
VIAGSTAARS GVIIKRADAI ERAYKVTDAV FDKTGTLTKG DLAIVHEQIL GEQEEFEIIS
LSKSLTKNNQ HPVSMAVAAH LESKPGDFVC VENVESIPGA GIQCEWRGSI VKAGNPYWLN
IDSDPEISNL IEQGMTLFCI TVDLKPIAVF GLKSNLRGEA KGVIQQLQKC NIKCHIVSGD
NSRVVEDVAA TVDIPLSNTA SRNSPAQKLQ YVKELMSQNR TVLFCGDGTN DAAAVAQANI
GVLIGTASDV TKGAADVVLL GGLDGVVTLL EISRRSSHRI FFNFIWSAVY NIFAILLAAG
AFVKARIPPT YAGLGEIVSV VPVIFVAMTL FRARNPARAS
//
