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Database: UniProt
Entry: K1WYP4_MARBU
LinkDB: K1WYP4_MARBU
Original site: K1WYP4_MARBU 
ID   K1WYP4_MARBU            Unreviewed;       735 AA.
AC   K1WYP4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=MBM_04071 {ECO:0000313|EMBL:EKD17702.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD17702.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD17702.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD17702.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.;
CC         EC=3.2.1.8; Evidence={ECO:0000256|RuleBase:RU361174};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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DR   EMBL; JH921435; EKD17702.1; -; Genomic_DNA.
DR   RefSeq; XP_007291960.1; XM_007291898.1.
DR   AlphaFoldDB; K1WYP4; -.
DR   GeneID; 18760006; -.
DR   KEGG; mbe:MBM_04071; -.
DR   eggNOG; ENOG502QR4K; Eukaryota.
DR   HOGENOM; CLU_377251_0_0_1; -.
DR   InParanoid; K1WYP4; -.
DR   OrthoDB; 548101at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490:SF35; ENDO-1,4-BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361174};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326,
KW   ECO:0000256|RuleBase:RU361174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..735
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003853171"
FT   DOMAIN          22..333
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   REGION          457..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  78648 MW;  70BF32620F3BD05A CRC64;
     MHFPILLPIL ALPAAFGQLN KLAKAKGLKY FGSATDNHEL TDTQYVAILS DTNEFGQITA
     GNAQKWSYTE PTQGSFSWTQ GDVISNLAKS NGQLLRCHTL VWHSQLPGWV TSGTWTNATL
     IAAMKNHIAN EVTHYKGQCY AWDVVNEAFN EDGTWRRSVF YNIIGPEFIP IAFQTAALYD
     PDAKLYYNDY NIESAGSKVT STLSLVRSLK ARGIKIDGVG MQAHFIVGST PSLSAQTSNL
     RSFTALGVEV AYSELDVRFT SLPPTTTGLA QQSTDYVNTV SACLATVGCV GITLWDFTDK
     YSWIPATFSG QGQACLWYAD FTKHPAYNAV VSVLGGTASS TAAATKMSTA TSAPASTATS
     GIIPKPSAAP PIIQQHACFL NYAADTAKDL RGTCSSPGRL GDDLEENLKI CQSGQVAWSG
     LLVEFTPDFS HHGPATIDPH GSLARTPSDR RGILQDGDRF VRHGAGETPQ RPRVPQRDRH
     PPPRRSVRAE VDCHPAEGGR RGGGGAEPAG SDRRLRGHDG YAGHPVHGGA DAPLPGCRRD
     LLDEGPGQLV AERAGADAEH RAVVAGSRVL AGAHAEAGEG VPNEQRQHER SSLYSSGGAA
     GTAVFLQRQG RMGAALQNLE LSGTRRAVPE SKRCEGHAGV FREDAESRAG EMDADFCYLG
     GVHRDGFLGL DNSERDEDTK VFSSRNGSVD CSLNIGPAGY GPLSWIAQAD RPGASNFDRR
     MLVMNSGINC AKIQT
//
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