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Protein

Beta-xylanase

Gene

xynA

Organism
Thermoanaerobacterium
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationImported

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:xynAImported
OrganismiThermoanaerobacteriumImported
Taxonomic identifieri28895 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae Sedis

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 13481316Beta-xylanaseSequence analysisPRO_5004265466Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ60043.
SMRiQ60043. Positions 857-1041.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini351 – 673323GH10 (glycosyl hydrolase family 10)InterPro annotationAdd
BLAST
Domaini1164 – 122360SLH (S-layer homology)InterPro annotationAdd
BLAST
Domaini1224 – 128663SLH (S-layer homology)InterPro annotationAdd
BLAST
Domaini1289 – 134860SLH (S-layer homology)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 10 (cellulase F) family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. SLH_dom.
[Graphical view]
PfamiPF06452. CBM9_1. 2 hits.
PF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSIVNRVVS IVTALIMIFG TSLFSQHIRA FADDTNTNLV SNGDFETGTI
60 70 80 90 100
DGWIKQGNPT LEVTTEQAIG QYSMRVTGRT QTYEGPAYSF LGKMQKGESY
110 120 130 140 150
NVSLKVRLVS EQNSSNPFIT VTMFREDDDG KHYDTIVCQK QVSEDSWTTV
160 170 180 190 200
SGTYTLDYTG TLKTLYMYVE SPDPTLEYYI DDVVVTPQNP IQVGNVITNG
210 220 230 240 250
TFENGNTSGW VGTGSSVVKA VYGVSHIGGY SLLTTGRTAN WNGPSYDLTA
260 270 280 290 300
KIVPGQQHNV DFWVKFVNGN DTEQIKATVK STSDKGNYIR VNDFANVNRG
310 320 330 340 350
EWTEIKGSFT LPVADYSGVS IYVESRNPTL EKNNDDFSVK GEISNKQITI
360 370 380 390 400
QNDIPDLYSV LKDYFPIGVA VDPSRLNDAE AHAQLTARHF NMLAAANAMK
410 420 430 440 450
PESLQPTEGN FAFDNADKIV DYAIAHNMKM RGHTLLWHNQ VPDWVFQEPS
460 470 480 490 500
DPSKPSSRDL LRQRLSTHIT AVLEHIQTKC GSLDPIGGWD VVNEVLDESG
510 520 530 540 550
NLRNPTWLQI IGPDYIDKAS EYAHEGDPSM TSFITYHNIE NGVKTQAMYD
560 570 580 590 600
LVKKLKNEGV PINGIGMQMH ISINSNIDNI KASIEKLASL GVEIQVTELD
610 620 630 640 650
MNMNGDVSND ALLKQARLYK QLFDLFKAEK HYITDVVFRG VSDDVSWLSK
660 670 680 690 700
PNAPLLFDSK LQAKPAYWAI VDPGKAIPDI QSAKALEGSP TIGANVDSSW
710 720 730 740 750
KLVKPLDANT YVKGTIGATA AVKSMWDTKN LYLLVQISDN TPSNNDGIEI
760 770 780 790 800
SVDKNDNKST TYESDDEHYI AKRDGTGSSN ITKYVMSNAD GYVAQIAIPI
810 820 830 840 850
EDISPVLNDK LGFDIRINDD QGSGNVTAIT AWNDYTNSQD TNTAYFGDLV
860 870 880 890 900
LSKPAQIATA IYGTPVIDGK VDGVWNNPEA ISTNTWVLGS NGATATAKMM
910 920 930 940 950
WDDKYLYILA DVTDNNLNKS SVNPYEQDSV EVFVDQNNDK TTYYENDDGQ
960 970 980 990 1000
LRVNYDNEQS FGGSTNSNGF KSATSLTQNG YIVEEAIPWT SITPLNGTII
1010 1020 1030 1040 1050
GFDLQVNDAD ENGKRTGIVT WCDPSGNSWQ ATSGFGNLML TGKPSVIKSD
1060 1070 1080 1090 1100
NASIALTEDA LNRNQIQCGV DVSIKDTWKA NVTNYVTLAN VVDMTISGSS
1110 1120 1130 1140 1150
GNVALPKPVE VTLNISIAND PRRVAVYYYN PATNQWEYVG GKVDASSGTM
1160 1170 1180 1190 1200
TFDATHFSQY AAFEYDETFN DIKDNWPKDV IEVLASRHIV EGMTDTQYEP
1210 1220 1230 1240 1250
NKTVARAEFT AMILRLLNIE EEAYSGEFSD VKSGDWYADA IEAAYKAGII
1260 1270 1280 1290 1300
EGDGKNARPY DSITREEMTA IPMRAYEMLT QYREENIGAT TFSDDKSISD
1310 1320 1330 1340
WARNVVANAA KLGIVNGEPN NVFAPKGNAT RAEAAAIICG LLEKTNNL
Length:1,348
Mass (Da):148,376
Last modified:November 1, 1996 - v1
Checksum:iD0C55E9E539F8E50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27183 Genomic DNA. Translation: AAC43719.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U27183 Genomic DNA. Translation: AAC43719.1.

3D structure databases

ProteinModelPortaliQ60043.
SMRiQ60043. Positions 857-1041.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. SLH_dom.
[Graphical view]
PfamiPF06452. CBM9_1. 2 hits.
PF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and expression of the gene encoding a large S-layer-associated endoxylanase from Thermoanaerobacterium sp. strain JW/SL-YS 485 in Escherichia coli."
    Liu S.Y., Gherardini F.C., Matuschek M., Bahl H., Wiegel J.
    J. Bacteriol. 178:1539-1547(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JW/SL-YS 485Imported.

Entry informationi

Entry nameiQ60043_9FIRM
AccessioniPrimary (citable) accession number: Q60043
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.