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Database: UniProt
Entry: F8Q0G9_SERL3
LinkDB: F8Q0G9_SERL3
Original site: F8Q0G9_SERL3 
ID   F8Q0G9_SERL3            Unreviewed;       628 AA.
AC   F8Q0G9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN97798.1};
GN   ORFNames=SERLA73DRAFT_109025 {ECO:0000313|EMBL:EGN97798.1};
OS   Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN   [1] {ECO:0000313|Proteomes:UP000008063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX   PubMed=21764756; DOI=10.1126/science.1205411;
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA   Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA   Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA   Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA   Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA   Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "The plant cell wall-decomposing machinery underlies the functional
RT   diversity of forest fungi.";
RL   Science 333:762-765(2011).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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DR   EMBL; GL945481; EGN97798.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8Q0G9; -.
DR   STRING; 936435.F8Q0G9; -.
DR   eggNOG; KOG1185; Eukaryota.
DR   HOGENOM; CLU_013748_4_0_1; -.
DR   InParanoid; F8Q0G9; -.
DR   OMA; DMCFPGD; -.
DR   OrthoDB; 2291769at2759; -.
DR   Proteomes; UP000008063; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT   DOMAIN          3..134
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          459..622
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   628 AA;  67272 MW;  28A989873212D338 CRC64;
     MYTTSSLFLN TLAQVGITHA FVNWGSDHPA LLEDLERQRV EKGETEPKIV TCPNEMVALS
     AAQGYTQVTG KPAAVIVHVD VGTQALAGAV HNVNRGRAPV LIYAGSSPFS AEGELKGSRN
     EWIHWMQDVH DQPAILRQYM RYTAQINSPA NLPHLVRRAL QIATSDPKGP VYLWGRREVM
     EQEIDEGLLK VPAPMLKWPS VEPCALSHSA AAIIAAALRQ AVNPLLITSH AGRNTNVFTS
     LSALCSLIGM PVFVPCPAVL NTPFSYALYV GVGHLAPGTQ TTLLKDADVI LVLDVELPWI
     PMNKDSNGDH ERPKEDARVF VIDGGDPLKE NIGMYHVDAE MVCRADAEVA LGQIVEAIQH
     SDSTEGVIIA ESAIVQARTR EMEKMHSEWV AKLDKAESFP TSLTSSIPAY TVPQVISALR
     RAVISGTPSG GAHTLMLNES ISNYPLVWSH MRPEVLGGMI GSGGSSLGWA LGASVGAFLG
     GKVAEKGPGK QGYELVASIV GDGTFLFGVP ASAFWMARKY QTPFLTVILN NGGWKSPKLS
     MLGVYPSGHG SKVLGQQLTV GFGPDMPDYA QIAVAASGGW AWGRKVDAST ISEGKNPKDA
     LEEVIAEAVR VVVQEGRCAV IDCVLESI
//
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