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Database: UniProt
Entry: D5G7D1_TUBMM
LinkDB: D5G7D1_TUBMM
Original site: D5G7D1_TUBMM 
ID   D5G7D1_TUBMM            Unreviewed;       578 AA.
AC   D5G7D1;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ80424.1};
GN   ORFNames=GSTUM_00002555001 {ECO:0000313|EMBL:CAZ80424.1};
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:CAZ80424.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ80424.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ80424.1,
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; FN430024; CAZ80424.1; -; Genomic_DNA.
DR   RefSeq; XP_002836233.1; XM_002836187.1.
DR   AlphaFoldDB; D5G7D1; -.
DR   STRING; 656061.D5G7D1; -.
DR   EnsemblFungi; CAZ80424; CAZ80424; GSTUM_00002555001.
DR   GeneID; 9185322; -.
DR   KEGG; tml:GSTUM_00002555001; -.
DR   eggNOG; KOG4628; Eukaryota.
DR   HOGENOM; CLU_007230_0_0_1; -.
DR   InParanoid; D5G7D1; -.
DR   OMA; LSGQLWV; -.
DR   OrthoDB; 206729at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22765:SF406; PA AND RING FINGER DOMAIN PROTEIN (AFU_ORTHOLOGUE AFUA_2G02470); 1.
DR   PANTHER; PTHR22765; RING FINGER AND PROTEASE ASSOCIATED DOMAIN-CONTAINING; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          495..538
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          237..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        250..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..445
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..578
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  61696 MW;  D70DDEB332E6AF3A CRC64;
     MPLTLTRTLV LLLSLLSLFC LFLYVSLTNL SSASSSGRNR QSATNFLFPS TAIISLSDDN
     STFFLSRPAA FGPPLPKSGL KGELFVLEEG QLACDDTPGW DPSSSPPVPM VGEDGTDDFD
     YAPKSLVATI TKPGGAHADI ESLQQSAEIE GKIVLVARGG CGFLEKVLWT QRRGGVALIV
     GDYKRSGGTI GGGALVTMYA KGDTSNITIP STFTTYTTAK LLTTLLPKHV SLPLTRPNTL
     GPVAGPEPKG GEGKRIEGGE KAGLRLKRPL EERNRAPPEL QPAGAPAKSE KTTITTFIGK
     TATPTSPPAG PDIHVDSSHR PPMSGELGGI VFVVDPDEGK PGDENSDRGG DKDGDIEKDG
     LWITLTPTSM SSSPFFDTLL VLVISPLVTL TIVYALLLAR SVIRRRRWRA PKSVVERLPV
     RTYQSTPSTS TPRTPPPPPT RRPLSLPPRS NRERNVGNVS SGRVLSTPSA PENQNKEFIH
     QSPPCSGYQG GSVECVVCLE EYVDGVSRVM RLPCGHEFHA GCITPWLTTR RRTCPICKGD
     VVRGAAAGGP GPSWGRHSDV GEASERTPLV IRDGEEEV
//
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