ID A0A165IAB7_EXIGL Unreviewed; 1283 AA.
AC A0A165IAB7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Heavy metal translocatin {ECO:0000313|EMBL:KZV93124.1};
GN ORFNames=EXIGLDRAFT_646465 {ECO:0000313|EMBL:KZV93124.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV93124.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV93124.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV93124.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425995; KZV93124.1; -; Genomic_DNA.
DR STRING; 1314781.A0A165IAB7; -.
DR InParanoid; A0A165IAB7; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000077266; 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; 2.
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; 1.
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; 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:UP000077266};
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 634..654
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 660..679
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 700..721
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 882..904
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 924..951
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1228..1253
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1259..1278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 474..541
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 285..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1283 AA; 135149 MW; C9DE6C5E052FE2EB CRC64;
MLPPGDTGVD AEDPHSQPCC ASDHCEDGPA RSLGIAGDRF VVGDCLPDGA GGCQRSLAHG
ASCCKTGDGL ANDACCGGTD ADSCSEGCCA KDDAAAPIHA AHDDCCPGHG EANVIGQGTC
CPNVTDACCS DDASVDSCDA SCCGGRKDIA AQLWPSADAA APSKTGGCCS DCATPVPQAS
SGAANVEPAV SKGCCDDCAS DFESVVADAP AAAEPQGICC AAPSAPAADD GPANKGCCDD
CGSDSASLGA LAHSAPSASA NAKSGSSSKC CDDCGPAPEA VIAHSHTHSH AHAHEHSHEH
EHPHSHEHEH PHSHEHGHSH EHSHAHASSH GHSKDNCCEG HGPSAAQTVR RRAAPHAHGS
GDAHSPVAGH DHVHKHASGS NRKARHKHKH HKHHKHSHSS GDSSSCAAET TMGRFYEVAC
CCLIDWARAR KRNKAKDDCC GHDHSHDDKS VYSEKASGSH DKAADVERGG GKRLTMLMSV
EGMDCPSCAS KVTRALLSIP SVRDVKVNVF AAQATLGYSE GLAFPFDIAK RTAELTGFAC
GVMEESIPQG EVSVLRIRVP PTLDISWEKA SLPPGVSIKS QHPSVEGTML EVEFNTLSIL
PRDVVAAFSR WDGVFVPTPR VRVSEQADKE LRSLFRRSFI SVLLCVPVLI FSWAPLPSHP
VAYGGACLAL ATIIQVYVGS PIYSASLRSL FLQRILDMDL LVVLSTSIAY VFSIVAYSLL
VSGHFFSDPF FETSSLLITL ITLGRLLSAY ARRFATSTLD ELYMLQVDVV ELLDSKGVQH
TISTELIHKG DILVISPDSL VPTDGIVQAG TSLVDESTIT GESIPVEKLV GSRLTAGTLN
THGTMHMRVE RMPSDNTVAE IGHLMLEVQN QRLPIQDLAD KVASYLAPVI LAISIITFSI
WIAIELKVRH EDSGSAGVAA LRYSIAVMVV SCPCALVLCV PMVVVITTAV ASKLGILFKS
AEAVQYAKDT QVAVFDKTGT LTTGVLSVAD SHIQNEDAIP IILGLVSGSR HPVSQAIFNH
LSMRYPGVQP TKLSDIISLP GQGLECLFNA ISIRGGNATW LNMTAHPDIE SLQAKALTIF
AVTIESNLVA AFGLSDTLRL DAHSTVEMLG RRGIDVYIVS GDSQRVVDAL AAQIHIPAER
AFGGCLPQDK LARVRALQRT ENGEMRRVMF VGDGTNDALA LAQSDLGVSF SSGTSVAASA
ASVLLLNPSL CAELDAILTL SLGASRRIYI NFAWSFVYNL LAVLAAAGAF VKIRIAPEYA
GLGEIVSVLP VVIIAWSIRI FKK
//
