ID D5GIQ7_TUBMM Unreviewed; 397 AA.
AC D5GIQ7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 22-FEB-2023, entry version 66.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ84400.1};
GN ORFNames=GSTUM_00008611001 {ECO:0000313|EMBL:CAZ84400.1};
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:CAZ84400.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ84400.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ84400.1,
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 -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|PIRSR:PIRSR000355-2};
CC Note=Binds 2 iron ions per subunit. {ECO:0000256|PIRSR:PIRSR000355-2};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000256|ARBA:ARBA00009303}.
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DR EMBL; FN430328; CAZ84400.1; -; Genomic_DNA.
DR RefSeq; XP_002840209.1; XM_002840163.1.
DR AlphaFoldDB; D5GIQ7; -.
DR STRING; 656061.D5GIQ7; -.
DR EnsemblFungi; CAZ84400; CAZ84400; GSTUM_00008611001.
DR GeneID; 9184765; -.
DR KEGG; tml:GSTUM_00008611001; -.
DR eggNOG; KOG1567; Eukaryota.
DR HOGENOM; CLU_035339_2_1_1; -.
DR InParanoid; D5GIQ7; -.
DR OMA; KVGEYQR; -.
DR OrthoDB; 5487627at2759; -.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SMALL CHAIN; 1.
DR PANTHER; PTHR23409:SF18; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR PIRSF; PIRSF000355; NrdB; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|PIRSR:PIRSR000355-2}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000355-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 223..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 38..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-1"
FT BINDING 136
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 264
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000355-2"
SQ SEQUENCE 397 AA; 45349 MW; 185E923DB4B69CD3 CRC64;
MSTVHMTPSK QAANALSNMT VDDAAAVKKN LNSAFENVKS PGKGGVKIDP EFKKPSEEDT
KSEEMDEPIL TENKHRFVLF PIKYHEIWQM YKKAEASFWV AEEIDLSKDM HDWSDRLNDD
ERYFISHVLA FFAASDGIVN ENLVQRFSNE VQIPEARCFY GFQIMMENVH SETYSLLIDT
YIKDPKQRTY LFDAIDTIPC IKKKADWAIR WIEDRNSTFA QRLVAFAAVE GIFFSGSFAS
IFWLKKRGLM PGLSFSNELI SRDEGLHTDF ACLLFNHLNN RPSQQAVQDI IVEAVGIEQE
FLTEALPCAL LGMNSKLMKQ YIEFVADRLL LSLGNPKFYN ATNPFDFMES ISLAGKTNFF
EKRVGDYQKA GVMASTQKKT EEPTNNGEGV IRFDEDF
//
