ID A0A1Y1XHB9_9FUNG Unreviewed; 1122 AA.
AC A0A1Y1XHB9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 22-FEB-2023, entry version 15.
DE RecName: Full=endo-1,4-beta-xylanase {ECO:0000256|ARBA:ARBA00012590};
DE EC=3.2.1.8 {ECO:0000256|ARBA:ARBA00012590};
GN ORFNames=BCR32DRAFT_105274 {ECO:0000313|EMBL:ORX85092.1};
OS Anaeromyces robustus.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Anaeromyces.
OX NCBI_TaxID=1754192 {ECO:0000313|EMBL:ORX85092.1, ECO:0000313|Proteomes:UP000193944};
RN [1] {ECO:0000313|EMBL:ORX85092.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX85092.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX85092.1, ECO:0000313|Proteomes:UP000193944}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 {ECO:0000313|EMBL:ORX85092.1,
RC ECO:0000313|Proteomes:UP000193944};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) 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 -!- PATHWAY: Glycan degradation; xylan degradation.
CC {ECO:0000256|ARBA:ARBA00004851}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family.
CC {ECO:0000256|PROSITE-ProRule:PRU01097}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01097}.
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:ORX85092.1}.
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DR EMBL; MCFG01000041; ORX85092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1XHB9; -.
DR OrthoDB; 1778490at2759; -.
DR UniPathway; UPA00114; -.
DR Proteomes; UP000193944; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProtKB-EC.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.180; -; 3.
DR Gene3D; 3.90.1220.10; Cellulose docking domain, dockering; 2.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR002883; CBM10/Dockerin_dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR009034; Dockerin_dom_fun_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR018208; GH11_AS_1.
DR InterPro; IPR033123; GH11_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001137; Glyco_hydro_11.
DR InterPro; IPR002509; NODB_dom.
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; PF02013; CBM_10; 2.
DR Pfam; PF00457; Glyco_hydro_11; 3.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR PRINTS; PR00911; GLHYDRLASE11.
DR SUPFAM; SSF64571; Cellulose docking domain, dockering; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 3.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51763; CBM10; 2.
DR PROSITE; PS00776; GH11_1; 3.
DR PROSITE; PS51761; GH11_3; 3.
DR PROSITE; PS51677; NODB; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lectin {ECO:0000313|EMBL:ORX85092.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000193944};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1122
FT /note="endo-1,4-beta-xylanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013186327"
FT DOMAIN 21..60
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 68..107
FT /note="CBM10"
FT /evidence="ECO:0000259|PROSITE:PS51763"
FT DOMAIN 144..345
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT DOMAIN 405..606
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT DOMAIN 667..868
FT /note="GH11"
FT /evidence="ECO:0000259|PROSITE:PS51761"
FT DOMAIN 920..1110
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 362..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 122414 MW; 8E2E71F7D5DF5A92 CRC64;
MKIIQIILSV GAAYLVSAQS SCSSKITSQG YKCCASNCQV VYTDGDGDWG YENGDWCGCG
TNQPSTSKCS SKITAQGYSC CSKYCTIVYT DNDGTWGYEN GDWCGCGDNT PTITVTTTTT
SVKPTQTQKV DFCSSASHSG ESIKITNNNV GQIGDVGYEL WSDSGYNSAT FYSDGSFSCS
FSNAKDYLCR SGLSFDSTQT HDQIGHMYAD FKLVKQNIRN VDYSYIGVYG WSRDPLVEYY
VVDNWLSQYR PGDWVGNKKH GDFTIDGAKY TVYENTRYGP SIDGDTQFKQ YFSIRQQARD
CGTIDITAHF QQWEKLGMKL GKMHEAKVLG EAGSNGSGTS GTADFPYAKV YIGSGGNTGG
NSGGNSGGNT GGNSGGNTGG NSGGNSGSGN TNFCSSAKHS GQSVQETSNK VGQIGDVGYE
LWSDSGYNSA TFYSDGSFSC SFNNAKDYLC RSGLSFDSTK TYDQIGHMYA DFKLVKQNIR
NVDYSYVGVY GWTRNPLVEY YIVDNWLSQY RPGDWVGNKK HGDFTIDGAQ YTVYENTRYG
PSIDGDTQFK QYFSIRQQAR DCGTIDITAH FQQWEKLGMK LGNMHEAKVL GEAGSNGSGT
SGTADFPYAK VYIGSGGNTG GNSGGNSGGN TWDNPWGGYT GGNSGGNSGS SNTNFCSSAN
HSGQSVQETS NKVGQIGNIG YELWSDSGYN SATFYSDGSF SCSFNNAKDY LCRSGLSFDS
TKTHDQIGHM YADFKLVKQN IRNVDYSYVG VYGWTRNPLV EYYIVDNWLS QYRPGDWVGN
KKHGDFTIDG AQYTVYENTR YGPSIDGDTQ FKQYFSIRQQ ARDCGTIDIT AHFQQWEKLG
MRLGNMHEAK VLGEAGSNGS GTSGTADFPY AKVYIGNGGN SGGNSGGNSG GNTGGYSGGS
TTQYPKGSGF QFYTQCKNRN HWALTYDDGP TQYADDILDL LKKYDIKATF FLVGNMYIPS
YNSEWSRIVK RMYNEGHVIG SHTYSHNDLT QMSSQQIIQD MQQLEDAVYN AIGKRPAFMR
PPYGTGSGNQ NVMSTLQNFG MTAACTWYVD PMDWDNGGDI NYAKQVLGRL NGEGVISLNH
LQYNGASQQG IIALSTAEIE LMLSKGYKPV TMEECLGMSA YK
//
