ID   A0A165FRX2_EXIGL        Unreviewed;       773 AA.
AC   A0A165FRX2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Glycoside hydrolase family 55 protein {ECO:0000313|EMBL:KZV89437.1};
GN   ORFNames=EXIGLDRAFT_147374 {ECO:0000313|EMBL:KZV89437.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV89437.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV89437.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV89437.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV426073; KZV89437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165FRX2; -.
DR   STRING; 1314781.A0A165FRX2; -.
DR   InParanoid; A0A165FRX2; -.
DR   OrthoDB; 3714838at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR   PANTHER; PTHR31339:SF9; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 2.
DR   SUPFAM; SSF51126; Pectin lyase-like; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KZV89437.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..773
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007857893"
FT   DOMAIN          63..286
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
FT   DOMAIN          414..559
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
SQ   SEQUENCE   773 AA;  81215 MW;  6963005CB7A9ED1A CRC64;
     MVCTRLAAVA LAVLSAVDAS LALGTTCSTP LGGGTAASGS PYWLQSLAQR GTSPFNSGYQ
     VRRNVKDFGA KGDGTTDDTA AINAAMSAGG RCGNPTGCSQ STLFPAVVYF PSGRYKISTP
     IISYWYTAMI GDGRNPPTLL AAANFSGIAL IDADPYLGGD AQWYVNQNNF YRSLRNFVVD
     LTPLPVSSGV NGLHWQVSQA TSISNLRIEM SRDASTNQVG MFMENGSGGY MGDITVNGGK
     TGLNLGNQQF TVRNVTVNNA QTAIFVNWSW VWLFYRIAIN NCPVGFRLNT GSTTSAQTTG
     ASIIADATFT NVGTAIQTTT NQPSTYASGF VLDNIVFSGV TNGVADQSNN VALSGGSKTV
     AQWLQGSVYT GTNSAFNYTR NTVAAVTKPS VLLEGGRFVS RPRPQYETYD VSQFVSVKAL
     GAKGDGSTDD TAILKSIFSQ YAGCKIIFFD AGIYKVSSTI TIPAGTQVIG EAWSTIMGFG
     SAFSNSASPQ VVVKVGDAGS TGRTEITDML FTTQGPAAGA IVVEWNVHDP SGQQGVAGAW
     DTIIRIGGAR GTNLQNAQCP KGSNNPSACS AAFLGLHLTR QSSAYLEGLW VWTADHDIDG
     DPQITVFSGR GILSESQGPV WLIGTGSEHN VLVQYNIANA ANHFLGVIQT ESPYYQPVPA
     PPAPFSINAA YQDPTSFSTP GNAWGLQVKN SSNILIYGAG LYSFFNNYVA DTCVGPANCQ
     NAIANIDTAS SNVVILGLST VGVTNMLNVN NAAVIAQSAN RFGTQATAIK WTR
//