ID D5G711_TUBMM Unreviewed; 1141 AA.
AC D5G711;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ80304.1};
GN ORFNames=GSTUM_00004542001 {ECO:0000313|EMBL:CAZ80304.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ80304.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ80304.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ80304.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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DR EMBL; FN430020; CAZ80304.1; -; Genomic_DNA.
DR RefSeq; XP_002836113.1; XM_002836067.1.
DR AlphaFoldDB; D5G711; -.
DR STRING; 656061.D5G711; -.
DR EnsemblFungi; CAZ80304; CAZ80304; GSTUM_00004542001.
DR GeneID; 9182495; -.
DR KEGG; tml:GSTUM_00004542001; -.
DR eggNOG; KOG0207; Eukaryota.
DR HOGENOM; CLU_001771_0_2_1; -.
DR InParanoid; D5G711; -.
DR OMA; AMHRRHQ; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 2.
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; 2.
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; IPR001757; P_typ_ATPase.
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; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 421..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 519..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 579..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 783..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1072..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1103..1123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..302
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 123448 MW; 5B1E56D1018B8F47 CRC64;
MSSRADTTPQ QTTLPSPANP SLPLSENMPV VNEVISRLPG SLGENVITTL LIPNLHCFTC
SSAIEELLSG LAPPPLDISI SILDHSVIVT HTQLLSPRDI IRVLLEAGFK LDTVSSASGA
EESMIGPSLS GHIISFQGDT YDWLEDMQMR IREVVGKKNA EGERHLENCE LCRNEALQEK
GLSSSRSSIG AGWKGGATAQ VAISKENEVS VGQRGVRDMQ TPGFVPADTM HEAVMSIGGM
TCASCTGRVT EVLEALPEVK SVSVNLMGNS ATVVFNAEEM GGAETGAQKL VFEVEETGFE
CSLETLNALG GEPDTVVKGR VGVERAVTLK VEGMFCDHCP GKVIDALESS FPDELLSIVA
PITRQSGLVH IKYVPQPPGF ALRHITAAIS SISPGFMVSV HHPPTMEERS RQLQLRERNR
LLTRLIVCFI IAIPTFMIGI VWMTLVSKED RVRKYLQEPM WAGSVTRIGW ALLFLSTPVM
FFVADVFHKR AIHEIRAQWR KGSNVPILRR FYRFGSMNLL VSLGVSISYF ASVVLLALDA
VTMPMMKAEG INGRAGAHMG MEGMGDRGES KYETHTTTYF DSTVFLTMFL LIGRFLEAYS
KSKTADAVNL LRELRPSEAL LVNDPSNSEY ADSRTWGTRS ISTDLLEVGD IVCIVRGSSP
PADGTVISGH SQFDESSLTG EARLVPKSEG DFVYAGTINQ GQVVNVRVDC IGGYSMLDQI
VKVVREGQTR RAPIERLADV LTGYFVPVVT LLAVTTWVVW LGLGISGRLP DYYLDVDHGG
WAVWSLGFAI AVFVIACPCG IGLAAPTALF VGSGLAAKFG ILAKGGGEAF QEASWLDCIV
FDKTGTLTQG GEPKVTDERI LVEGSEAREI AYAIAHKLEG GSAHPLAIAT PGKGLNGVFK
LPDSWKLAGK SVVLLAIKKH GAADKDIFGS EYRLAAFFGA TDPLRPEAPN VVSSIRESGI
SIWMISGDNE KTAIAVASMV GIPTENRPRT GWRRFFHRKN SPKSKRAIVA MVGDGINDAP
ALSVADVGIA IGSGSDVAIS SAKFILVSSD LRSLLTLTEL ARAVFRRVKF NFLWACIYNL
IALPVAAGVL YPVAHRRIRL DPVWAALAMA FSSVSVVCSS LMLKTRWWGV GFRPSQERYR
Q
//
