ID A0A2T9Z083_9FUNG Unreviewed; 1457 AA.
AC A0A2T9Z083;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=BB559_001812 {ECO:0000313|EMBL:PVU97977.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU97977.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU97977.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU97977.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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:PVU97977.1}.
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DR EMBL; MBFT01000092; PVU97977.1; -; Genomic_DNA.
DR STRING; 61424.A0A2T9Z083; -.
DR Proteomes; UP000245699; 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; -; 5.
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; 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; 3.
DR NCBIfam; TIGR00003; copper ion binding protein; 3.
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; 5.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR PRINTS; PR00942; CUATPASEI.
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; 5.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 4.
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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000245699};
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 480..498
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 518..539
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 551..576
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 747..766
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 786..810
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1156..1179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1185..1204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..69
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 98..164
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 299..365
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 389..455
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1358..1377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1457 AA; 159383 MW; AA849CEE76A0D3FD CRC64;
MKTVSLSIQG MTCKSCVNAV NKALDNINDV ISCSVDLQKG FALVKVSDSN EFVVSSILSS
IEDCGFDVQI LSTDFDSHNT SNEKQTSQPL ASQNTAESEA WIDIVGMTCN SCVRSIENTL
KSTPGISYVK VYLENNNANV KYIPSQYSID KIITSIEDCG FDAKVSSNTL ENLQTTKFWS
CKVQDLHSKE LAKIVSRNIK TLEGVTLVDI DILTGIVNIT YNPNTDEVVD IVAKIEECGV
AVLSENTDNL ATEFSTDQSI SGDEKDFKSS TRHPISMWKN IQKTNKESCS TVTLQKEERI
ALIDIKGMTC ASCVNAIETG LKKLQFISEV NVNLLAQQAK IKYESSISMS NIFVEEIENL
GFDATENSDE QVSKTEYATN GENISDNMTK AYLQIYGMTC SSCVNSIENG LNRLQGVESA
LVNLAMQNAV VRYDKTILGI RDITTKIEEL GFDVVVGSKV GSAQVQSLQR TEEILMWKKS
AIISLWLGIP VLIIAKLLPN FQWTKGIVMT RIVKGMPLGT TLELILTTIL MFTSGTQFFK
RSYKALKGGH ATMDVLVATG AGLSYVFSLF MFSWSVIRKQ HAKAHCFFEA AAMLITFVSG
GRYLENMAKG SASTALAKLM TLTPSRAMLV ERDENGQVTN ERYIATELIQ IGDELRVFPG
ERIAADGIII EGSTEVDEST VTGEAVPVSK RIGSQLVAGT VNTTGSITMK CNQVGSDTTL
AQIVRLVEDA QVGKTPIQLF ADKVSHYFVP TVLLLALLTF ICWMLISRLP DSYKPKLFMD
HVEKTGSYFV VSLQIAVAVV IVSCPCALGL STPTAVMVGT GVGAQMGILI KGGDALETTQ
KVSTVIFDKT GTLTKGELDI SDIVIDRSWK KEMFLAVVGA AESRSEHSLG KSIHKHCESV
LGNNVIQSTT ETLDFRALTG MGIRCKVGIM PRASFFDPKL PKQLSILVGN LRLMEISNVE
IPKYALKAIE KYETVGCTVL LVSIENIFAG LLALADVLRP ESLPTVHTLK SMGIHVVMVT
GDQPRTARYI AKKCGIDTVY AGISPSGKQE IVSYLQTQPP RYTNRSWFSS IFNKIFRKRS
AGQYQALGGT SCVAMVGDGI NDSPALAAAD VGIAICSGTH VAMEAASMVL MRKDISDVVA
ALDLSRTIFR RIKYNYFWAC LYNFMGIPVA MGFLIPYGIE LPPVFASAAM MLSSLSVMSS
SLLLKLYRKP FCRAPPSMSD CEPKVMDIND ININHQSLIL NGVPCSPTLT DMTRISSYGS
PLSDITFTTP SETPKSQSLY LDTHGSRYSR FQNGTFDKSR SHLEFVMQEA VLESSPQPVL
FSPSNTPKYE NMTYINNDMY LNSTYGLNVD GSKLSKSRSL VHNSKSGSVS PGSSFTSNLR
QQALHNSLLE SGLANSFDTR DNLSSNFTRG HDSTQRSGTH GSTSPLLQQE NYDLQRESSV
ELLPTKFSSM SKTFNYQ
//
