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
//