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Database: UniProt
Entry: M1W368_CLAP2
LinkDB: M1W368_CLAP2
Original site: M1W368_CLAP2 
ID   M1W368_CLAP2            Unreviewed;       511 AA.
AC   M1W368;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Probable endo-1,4-beta-xylanase {ECO:0000313|EMBL:CCE28250.1};
GN   ORFNames=CPUR_01724 {ECO:0000313|EMBL:CCE28250.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE28250.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE28250.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE28250.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCE28250.1}.
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DR   EMBL; CAGA01000007; CCE28250.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W368; -.
DR   STRING; 1111077.M1W368; -.
DR   VEuPathDB; FungiDB:CPUR_01724; -.
DR   eggNOG; ENOG502SI39; Eukaryota.
DR   HOGENOM; CLU_009397_6_0_1; -.
DR   OrthoDB; 5470935at2759; -.
DR   PhylomeDB; M1W368; -.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd08990; GH43_AXH_like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Polysaccharide degradation {ECO:0000313|EMBL:CCE28250.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:CCE28250.1}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..511
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004019317"
FT   REGION          324..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            180
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ   SEQUENCE   511 AA;  56112 MW;  BA14E8F37A9D4697 CRC64;
     MAVTRLSFGR LFNIFLLLSV ADCQIPFVSD GNPILSNGTY YTADPGPIVV NGSLYIIAGH
     DSAPKDDNNF IINHWHLLAS DDPNPAGGNW KMYPDFVAPH TVFRWADTAA AYASQIVLGP
     DGGYYLYSPV SQSKTSSSDP FGIGVARADK IEGPYVDHHP RGPIVSQSYP APGNDIENID
     PTVLVDNDRV FMYWGTFGEL RGVELDKKDM STFVGDIVTV TSLNGFFEAA WLMKRGETYY
     MIYAANNVGK ECTPTLYHAC LAYGTSSGPL GPWTYRGVIL GIVSSTTSHS GAVAIKDQWY
     LVYHTADAHS GGNFRRSVAF DKMDFDDSTS PPRIRPVQQT HRPEPAPKPT YQRQQLAVAS
     SSPPCIDRYW IEAVHDQKIP NNPLPPEYWS TYSDEGTIPV QSTVTYSWET EQELNGVGMS
     FFADSPAGSV EGVAPPTEWF VEYKSSNGSW TAVRNSTGYS TQVTTHPKTT NFDVIKTKGL
     RATLRAPTNG TWTAGVGIKE WLVYSTTKAV V
//
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