ID F8QCB4_SERL3 Unreviewed; 780 AA.
AC F8QCB4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glycoside hydrolase family 55 protein {ECO:0000313|EMBL:EGN94233.1};
GN ORFNames=SERLA73DRAFT_171697 {ECO:0000313|EMBL:EGN94233.1};
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).
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DR EMBL; GL945489; EGN94233.1; -; Genomic_DNA.
DR AlphaFoldDB; F8QCB4; -.
DR STRING; 936435.F8QCB4; -.
DR eggNOG; ENOG502QV54; Eukaryota.
DR HOGENOM; CLU_002540_2_2_1; -.
DR InParanoid; F8QCB4; -.
DR OMA; PDYNSIC; -.
DR OrthoDB; 3714838at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039279; QRT3-like.
DR PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EGN94233.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..780
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003377286"
FT DOMAIN 64..290
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 419..489
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
SQ SEQUENCE 780 AA; 81128 MW; D62A11EB958115DB CRC64;
MRSSILIVLS TILGSTTSVS ALGSSCSAPL GAGTAAATDP FWLENMTHQG TSAFNPTPST
YEVFRNVKTF GAKGDGVTDD TAAINAAMTS GNRCGSTSCG SSTLTPAIVY FPSGTYVVSS
AIDMYYYTQM IGDAKNPPTL LASAAFSGFA VIDSDPYIPG GSGAQWFVNQ DNFYRSIRNL
VIDLRQMPAS APAVGLHWQV SQATSLMNIV VEMSTAPGNT HEGMFMENGS GGFMGDLVFN
GGNYGINVGN QQFTVRNLTI NNAQTAVFGI WNWGWTWQGV TINDCQIGFD LTTGGVTEDT
QTVGSQAIVD AVINNTPIFL RSSNSSDGKL AGSLVLNNIQ LNNVTTAVGV VGGADVLAGG
TTTIASWGQG DVYTGTSGTS TFTQGTIASS TKPSALLDST GKVFGKTHPQ YAEYATSQFV
SVKSSGAKGD GKTDDTAAIQ AVFDQYAGCK IIFFDAGAYY VTDTISIPAG SQVVGEAWSV
ILAGGTGFAD QTTPKVVVQA GASGSSGVLE ITDMLLSTAG PSPGAIMLEW NVADPSGQQG
AAGLWDTHLR LGGAVGTNMQ SGQCLNGTVN AACQAAFMGI HLTNSSTAYF EGTWVWTADH
DLDATGSPQT SVFTGRGILS ESAGPVWFIG TASEHSSLYQ YNLAGAKNHW IGFAQTESPY
YQPSPAAPAP FSTDSAYSDP SFSSSQTSAW GMYVQSSSDI TLFGAGFYSF YENYVQDCLN
TTNCQDQIFN MDSASASSMN VYALSTVGVV TELSVADAGV IKAAQNPDGL QDTATSWSSS
//