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Database: UniProt
Entry: D5G5D4_TUBMM
LinkDB: D5G5D4_TUBMM
Original site: D5G5D4_TUBMM 
ID   D5G5D4_TUBMM            Unreviewed;       642 AA.
AC   D5G5D4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ79727.1};
GN   ORFNames=GSTUM_00004279001 {ECO:0000313|EMBL:CAZ79727.1};
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:CAZ79727.1, ECO:0000313|Proteomes:UP000006911};
RN   [1] {ECO:0000313|EMBL:CAZ79727.1, ECO:0000313|Proteomes:UP000006911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mel28 {ECO:0000313|EMBL:CAZ79727.1,
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; FN429998; CAZ79727.1; -; Genomic_DNA.
DR   RefSeq; XP_002835570.1; XM_002835524.1.
DR   AlphaFoldDB; D5G5D4; -.
DR   STRING; 656061.D5G5D4; -.
DR   EnsemblFungi; CAZ79727; CAZ79727; GSTUM_00004279001.
DR   GeneID; 9188146; -.
DR   KEGG; tml:GSTUM_00004279001; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   HOGENOM; CLU_009958_6_1_1; -.
DR   InParanoid; D5G5D4; -.
DR   OMA; MGRCTSR; -.
DR   OrthoDB; 1377857at2759; -.
DR   Proteomes; UP000006911; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10229; HSPA12_like_NBD; 1.
DR   Gene3D; 3.30.420.40; -; 3.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR14187; ALPHA KINASE/ELONGATION FACTOR 2 KINASE; 1.
DR   PANTHER; PTHR14187:SF79; HSP70 FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G15200); 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006911}.
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  71057 MW;  5F0DF3CDB2D03BB2 CRC64;
     MPPPGPYGPG QIGPIPPQGG PPMGMQGPPP GPYGAHPPVY PPAPQMGGHR DSHPGMHQMQ
     NRPHAAEVEG TNKSKAQLIV GIDFGTTFSG VAFAFATDQE AKEDIITEWP GAGNQTKNKI
     PTVLYYDQYQ KVVGWGPDIA DALAPTGYPK PGVQKVEWFK LQLMLSGNTY IDPINLPPLP
     PGKSEVDVAA DYLFKLRQAM RAQLQKTLGE VFNREERNIR YFLTVPAIWN DAGKAATRAA
     AIQAGFLRDE NDNRLTLITE PEAAAMFCSK TGLLNLKIHD AVLIVDCGGG TVDLIAYEVE
     EEVPFSVAEC TAGSGDSCGS TALNRNFSNI LRAKIRKMKL PDGSRTAGKV YAKCIMDFEN
     RIKADFRNNG QKWAVDVGIE AEFPDAGIEE GYMTFTNEEI LQCFEPVVNR ILELVRNQII
     AIQAQNRQLQ NVLVVGGFGA SEYLFQQIKL HVPPQFQSKV VRPMDSVAAI VKGAVTAGIT
     EKVVTSRVAR RHYLMATLQP FKEGHHPEQY RVPSLDGKDR CKYTRQIFVT KGQRVKIGEP
     VKVSFFRQVA PGATLMYEDI LYACDDDVCP EYTKDPRIKE VVTLTSDLSR KNLEKDFERM
     DTPQGTFYRV YFDIFLTLDG SEFNAELVCQ GEVMGRCVAK FR
//
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