UniProt: S8A5I6

Database: UniProt
Entry: S8A5I6_DACHA

LinkDB:  S8A5I6_DACHA 
Original site:  S8A5I6_DACHA

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (3)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   S8A5I6_DACHA            Unreviewed;       231 AA.
AC   S8A5I6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
DE            EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590, ECO:0000256|PROSITE-ProRule:PRU01097};
GN   ORFNames=H072_10125 {ECO:0000313|EMBL:EPS36346.1};
OS   Dactylellina haptotyla (strain CBS 200.50) (Nematode-trapping fungus)
OS   (Monacrosporium haptotylum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Dactylellina.
OX   NCBI_TaxID=1284197 {ECO:0000313|EMBL:EPS36346.1, ECO:0000313|Proteomes:UP000015100};
RN   [1] {ECO:0000313|EMBL:EPS36346.1, ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|EMBL:EPS36346.1,
RC   ECO:0000313|Proteomes:UP000015100};
RX   PubMed=24244185;
RA   Meerupati T., Andersson K.M., Friman E., Kumar D., Tunlid A., Ahren D.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   PLoS Genet. 9:E1003909-E1003909(2013).
RN   [2] {ECO:0000313|Proteomes:UP000015100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 200.50 {ECO:0000313|Proteomes:UP000015100};
RA   Ahren D.G.;
RT   "Genomic mechanisms accounting for the adaptation to parasitism in
RT   nematode-trapping fungi.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|ARBA:ARBA00000681,
CC         ECO:0000256|PROSITE-ProRule:PRU01097, ECO:0000256|RuleBase:RU362015};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851, ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC       {ECO:0000256|ARBA:ARBA00007792, ECO:0000256|PROSITE-ProRule:PRU01097,
CC       ECO:0000256|RuleBase:RU362015}.
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:EPS36346.1}.
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DR   EMBL; AQGS01000918; EPS36346.1; -; Genomic_DNA.
DR   RefSeq; XP_011115625.1; XM_011117323.1.
DR   AlphaFoldDB; S8A5I6; -.
DR   eggNOG; ENOG502RXA7; Eukaryota.
DR   HOGENOM; CLU_052631_0_0_1; -.
DR   OMA; NMQNHFN; -.
DR   OrthoDB; 1778490at2759; -.
DR   UniPathway; UPA00114; -.
DR   Proteomes; UP000015100; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.120.180; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013319; GH11/12.
DR   InterPro; IPR018208; GH11_AS_1.
DR   InterPro; IPR033119; GH11_AS_2.
DR   InterPro; IPR033123; GH11_dom.
DR   InterPro; IPR001137; Glyco_hydro_11.
DR   PANTHER; PTHR46828; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   PANTHER; PTHR46828:SF2; ENDO-1,4-BETA-XYLANASE A-RELATED; 1.
DR   Pfam; PF00457; Glyco_hydro_11; 1.
DR   PRINTS; PR00911; GLHYDRLASE11.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00776; GH11_1; 1.
DR   PROSITE; PS00777; GH11_2; 1.
DR   PROSITE; PS51761; GH11_3; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01097};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|PROSITE-ProRule:PRU01097};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015100};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651, ECO:0000256|PROSITE-
KW   ProRule:PRU01097}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..231
FT                   /note="Endo-1,4-beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004560330"
FT   DOMAIN          41..229
FT                   /note="GH11"
FT                   /evidence="ECO:0000259|PROSITE:PS51761"
FT   ACT_SITE        125
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
FT   ACT_SITE        216
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01097"
SQ   SEQUENCE   231 AA;  25312 MW;  3659D86F73F8D569 CRC64;
     MVSFKSLLLA LTAATGVLAA PFDFLHERDD GNSTAALVKR QTTANSVGTH NGYFYSWWSD
     GGGYAQYTMG AGSKYNVVWR NTGNFVGGKG WNPGTGRTIN YGGSFSPSGN GYLAIYGWTR
     NPLVEYYVIE SYGTYNPSSG GQYKGTVNTD GGTYNIYVST RVNQPSIDGT KTFQQYWSVR
     TSKRVGGSVN MQNHFNAWRN YGMNLGSHYY QIVATEGYQS SGSSEIYAQT K
//

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