UniProt: A0A3N2FNZ1

Database: UniProt
Entry: A0A3N2FNZ1_9CELL

LinkDB:  A0A3N2FNZ1_9CELL 
Original site:  A0A3N2FNZ1_9CELL

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (25)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (4)   
   SMART (2)   
All databases (31)   

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ID   A0A3N2FNZ1_9CELL        Unreviewed;      1509 AA.
AC   A0A3N2FNZ1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Beta-xylanase {ECO:0000256|RuleBase:RU361174};
DE            EC=3.2.1.8 {ECO:0000256|RuleBase:RU361174};
GN   ORFNames=EDF34_2338 {ECO:0000313|EMBL:ROS26012.1};
OS   Cellulomonas sp. PhB150.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=2485188 {ECO:0000313|EMBL:ROS26012.1, ECO:0000313|Proteomes:UP000273256};
RN   [1] {ECO:0000313|EMBL:ROS26012.1, ECO:0000313|Proteomes:UP000273256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PhB150 {ECO:0000313|EMBL:ROS26012.1,
RC   ECO:0000313|Proteomes:UP000273256};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (NOV-2018) 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|RuleBase:RU361174};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family.
CC       {ECO:0000256|ARBA:ARBA00007495, ECO:0000256|RuleBase:RU361174}.
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:ROS26012.1}.
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DR   EMBL; RKHX01000003; ROS26012.1; -; Genomic_DNA.
DR   OrthoDB; 9815836at2; -.
DR   Proteomes; UP000273256; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
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-KW.
DR   CDD; cd00005; CBM9_like_1; 1.
DR   CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR   Gene3D; 2.60.40.1190; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR010502; Carb-bd_dom_fam9.
DR   InterPro; IPR003305; CenC_carb-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR31490:SF88; BETA-XYLANASE; 1.
DR   PANTHER; PTHR31490; GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF06452; CBM9_1; 1.
DR   Pfam; PF02018; CBM_4_9; 2.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00633; Glyco_10; 1.
DR   SMART; SM00409; IG; 3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   PROSITE; PS51760; GH10_2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS51677; NODB; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU361174};
KW   Glycosidase {ECO:0000256|RuleBase:RU361174, ECO:0000313|EMBL:ROS26012.1};
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:UP000273256};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000313|EMBL:ROS26012.1}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..1509
FT                   /note="Beta-xylanase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017988956"
FT   DOMAIN          221..405
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   DOMAIN          572..902
FT                   /note="GH10"
FT                   /evidence="ECO:0000259|PROSITE:PS51760"
FT   DOMAIN          1240..1323
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1329..1413
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1419..1505
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          186..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1509 AA;  157088 MW;  023BE61AD592A589 CRC64;
     MRSVRSLRRI GTAAVVLAVA VGTGGLTAVT AAADDGPTTL VSNDFESGTT APWDPRGPVT
     LATVDTDAHG GARSLLVSGR TGDWNGPATD AIAFPAGSPV TVSAWVKLAP GTAGSSAMHF
     TVQQSPADNE YTWVGSPVTA TADGWVELTG TYTRAASVTA ATLYLEAAPI AGANPSFLVD
     DVLVTTPGAG DPDPDPDPDV VPGGAVDPTT TPVSAARGTG DVAALTFDDG PNGATTGALL
     DFLQEQGIHA TFCVIGQNIQ APGGAEVLRR IVADGHTLCN HSTSYADMGS WTPAQVRADL
     VENLAIIRTA LGDPQAKVPF FRAPNGSWGQ TAAVAVSLGM QPLAVTNTIS DWETQDVPTL
     TTNLRAAMKP GQVVLTHDGG GDRSGTLAAV RTVVTERLAA GWSFTLPAGG AADDGPAPTS
     LSTGFEDGLG VWAARGNGTA PVVAISEVAH GGVQSASVTG RTDGWHGLGT SVTDAFVSGR
     TYQISAWVRL AAGETAPADV RVSVQRDTGG TSSYDTVTTA AGVTADGWVQ LTGSYTMTSA
     DSALLYFETA SGTASFLVDD VVVTGSTAPP VQQDIPSLKD ELPWPVGVAI DERETAGPGK
     ELVTKHFDQF TPENVMKPEA IQPTEGNFTF EAADQLVDFA IANGLRVYGH TLVWHSQTPA
     WFFQHEDGTP LTDSADDQAV LLARMTTHIE TVADHFRTKY GEYGTAGNPI VGFDVVNEVI
     AESESDGLRR SEWYRTLGPD YIKDAFEIAS QAFNGGDVDG PVKLFINDYN TELPAKRQAM
     FDVVDGLLKA GVPINGVGHQ FHVSLAQPVD QMRTTLEKFA TLGVLQDVSE LDVQIDGTVT
     QEKLVAQGYY FANVFSMLRD FPDLFSVTVW GPYDSRSWRT GAPLVFDDDL QAKPAYWGIV
     DPTELPTLTR AANAQQSSGA ADWRLLPDVE ISGGTGFQLR WSGDHLTARV HVVDATDDAD
     DSVTLFSSGD PVVVSRAAGT ATDDGYEVTA TLPLAAAGSV GTTVPFDVRV ADGSGSTTSW
     NDLSNHQETG GALGVVTLVE PIAFVSVPRA ATTPTIDGVI DAAWASAPSV RTDVQVEGSG
     GATAKVRLLW HGDSVDVLAE VTDPHLDATS SNAWEQDSVE IFLDPANAKS GAYHPVDGQY
     RINYLGAQSV SGDLSVIGDR LTSAAKVVDG GYVVEASLKL GHTVTPGDLA GLDFQVNDAT
     AGVRDAVRTW SDPTGRSYQD TSRWGVGELV EPVGPQPTAP AVTKQPASVT GALGATVTLT
     AAASGIPAPT VRWQRLGSTW TDVPGATSTS LAVKLSATTD GARYRAVFTN ATGVATTSTA
     TVTVKAQAPR VTTQPGSTQA RTGKSVTLKA VASGYPTPTV RWQQRASGSS TWRTVSGATR
     TSLTVKVGAK PVAYRAVFTN RGGTATTRTA TVTPTPVKPR ITAQPRSATV AAGKSVRFSV
     SVTGTPAPTI RWYQRVAGSS KWKAVTGATG RTLVVKATTG KSGNAYRVVV KNKAGSVTSH
     SAVLKVKRR
//

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