ID D5GG65_TUBMM Unreviewed; 907 AA.
AC D5GG65;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ83508.1};
GN ORFNames=GSTUM_00007233001 {ECO:0000313|EMBL:CAZ83508.1};
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:CAZ83508.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ83508.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ83508.1,
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FN430242; CAZ83508.1; -; Genomic_DNA.
DR RefSeq; XP_002839317.1; XM_002839271.1.
DR AlphaFoldDB; D5GG65; -.
DR STRING; 656061.D5GG65; -.
DR EnsemblFungi; CAZ83508; CAZ83508; GSTUM_00007233001.
DR GeneID; 9184570; -.
DR KEGG; tml:GSTUM_00007233001; -.
DR eggNOG; KOG0498; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_006113_0_0_1; -.
DR InParanoid; D5GG65; -.
DR OMA; RMKSVWD; -.
DR OrthoDB; 1330350at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45638; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR PANTHER; PTHR45638:SF11; CYCLIC NUCLEOTIDE-GATED CATION CHANNEL SUBUNIT A; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF16643; cNMPbd_u2; 1.
DR Pfam; PF00646; F-box; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00367; LRR_CC; 8.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
DR PROSITE; PS50181; FBOX; 1.
PE 4: Predicted;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 70..187
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 268..391
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 530..577
FT /note="F-box"
FT /evidence="ECO:0000259|PROSITE:PS50181"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 100524 MW; DD9E3ED94094EBC6 CRC64;
MHHRRRAPPI VLSPAPPPGA DDSNGHVNTI EIVHHFESQT NPAKPARPSP LTTSNGMPLV
LLERLRSFPL FLSAPEEFLS AVATHLRPQP YSPRDYILTE GDEAKAMYWL VRGAVAVTSR
DGESTYAELR PGAFFGEIGI LMDIPRTATI IARSRCLLVV LTKEALQREL PKFPEVERAI
REEAEERLTL LNKKKKERES SPRTGGVKRA VDSDGDVEIG DNIYLKPDTP RAFGGPSPIP
KPGSQWVTNS ALGSGQVNIR QLLKELPLFA NLPQENLHFL GLSAAPRTYA PFQTIIQQYS
MGREIYFIVG GEVEVVDEMV MDPKQNKVKA RLRKGQHFGE VVALSLAPRR TATVRAITPV
ECLVIEGDVL EELWKKCPPE VQQQLEMTAR DRMDGDGENV LMRDAPATPT QSIDRLDISD
LPKASSMNLT VPESRFTGPN DSNLVEPFDP DPYLPADFES LRSKSRRGSL APPPPQSSAT
SSSSSPTEEN PSPLSRSTTP SPVKTKHVTT PPEHHATVKR ARILSRKPSR FNIGQFKDDI
LIQIFKHMEL HELMRVRQVS THWSRLLTNS PYLLTTLDLK PYNRVINDNV LIHAIAPFVG
HRPSLIDISN CFHIGDEGFM VLAQTCGANV KVWKMKSVWD ITGQAILEMS NRAKGLEEID
LSNCRKVSDT LLARVVGWVQ APPQPPPMYP APGTVIGCPN LSRLTLSYCK HVTDRTMSHL
AAHAARRLEH VDLTRCTTIT DQGFQSWSMT RFERLRSLCL ADCTYLTDSA VVFLTNAAKG
LRSLDLSFCC ALSDTATEVL SLGCPHLSVL KLSFCGSAVS DSSLRAIGLH LLELRELSVR
GCVRVTGVGV EAVVEGCHNL EVFDVSQCKN LARWIESGGV EKCTQTWKRN IRFETVAVDV
IAGDRRR
//
