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Protein
Submitted name:

Xylanase

Gene
N/A
Organism
Rhodothermus marinus (Rhodothermus obamensis)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi219 – 2191Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi221 – 2211Calcium 1Combined sources
Metal bindingi232 – 2321Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi238 – 2381Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi239 – 2391Calcium 2Combined sources
Metal bindingi262 – 2621Calcium 1Combined sources
Metal bindingi265 – 2651Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi370 – 3701Calcium 1Combined sources

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationImported

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Protein family/group databases

CAZyiCBM4. Carbohydrate-Binding Module Family 4.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Submitted name:
XylanaseImported
OrganismiRhodothermus marinus (Rhodothermus obamensis)Imported
Taxonomic identifieri29549 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeRhodothermus

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y64X-ray1.40A212-376[»]
2Y6GX-ray1.30A212-376[»]
2Y6HX-ray1.08A212-376[»]
2Y6JX-ray1.70A212-376[»]
2Y6KX-ray1.36A212-376[»]
2Y6LX-ray1.28A212-376[»]
3JXSX-ray1.60A/B/C212-376[»]
ProteinModelPortaliQ7WTN6.
SMRiQ7WTN6. Positions 40-200, 212-374.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7WTN6.

Family & Domainsi

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR026444. Secre_tail.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR04183. Por_Secre_tail. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7WTN6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTATDLRFL RNAVGNASRS AIFLFLVFSL VGQAWGQTPA NVNGSFESTP
60 70 80 90 100
AGVVTDLAGG VEGWVLNVGS LVTNPPVFEV VEATDAPHGS KVLAVTVNGA
110 120 130 140 150
GNNPWDIEAT AFPVNVEPGV TYTYTIWARA EQDGAVVSFT VGNQSYQEYG
160 170 180 190 200
RLHEQQITTE WQPYTFEFTV SDQETVIRAP IHFGYAANAG NTIYIDALVI
210 220 230 240 250
MGPEPEPAGP ELVANINGGF ESTPAGVVTD LAEGVEGWDL NVGSSVTNPP
260 270 280 290 300
VFEVLETSDA PEGNKVLAVT VNGVGNNPWD IEATAFPVNV RPGVTYTYTI
310 320 330 340 350
WARAEQDGAV VSFTVGNQSF QEYGRLHEQQ ITTEWQPFTF EFTVSDQETV
360 370 380 390 400
IRAPIHFGYA ANVGNTIYID GLAIVDSVGA WRPVIVEAED GELGSEWAVE
410 420 430 440 450
TEGNVTYITI TTDYNETTGD ADHPGENRTA TYQVTFPAPG WYDLYARVYV
460 470 480 490 500
GPETFNDDSF FYADSFGVKD PESPDDWIIA NQLRAAGYTE PDEYVTGLGA
510 520 530 540 550
AGSEVWKWIN LSENSFNDVP SDSFYVSPES LTVTFMIGAR ENGLRIDKLA
560 570 580 590 600
FGRSDLLYTV ADLDTGGPGS PEPEEPPVVL PERPLAADVD KFLGNIYSPS
610 620 630 640 650
QVENFEYYWN CVTPENAGKW GSVEGTRDQM NWSSLDAAYA LARDNGFCFN
660 670 680 690 700
FHVLLWGAQQ PAWISELSPE EQLEEIQEWF QAVAERYSFT ASPFDVVQVV
710 720 730 740 750
NEPLHQPPDG QEGRANYIEA LGGAGETGWD WVITAFELAR QIFPEGTRLM
760 770 780 790 800
INDYGILSSL ETAQQYLELI QLLKERNLID VIGVQGHAFS TRSGAPIQEV
810 820 830 840 850
LDLLATTGLP IQVTEMDIDG NPNQSPFVTR EQSEQNQLRD MQRIFPTVWY
860 870 880 890 900
HPAVEGVTFW GWRPGLWRND YEAYLVYSNG AERPAMVWLR EFMEAYRESY
910 920 930 940 950
LSANEPEGTL PEELSVVSWP NPSRGQVRFR YALPFEAEVR LQVFDVLGRE
960 970 980 990
VMTLASGRHR AGVYEVAFDG RHLPSGLYLY RLEANGRVRS GRLVLMR
Length:997
Mass (Da):110,343
Last modified:October 1, 2003 - v1
Checksum:iCE6ABF99CC4AC1A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11564 Genomic DNA. Translation: CAA72323.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11564 Genomic DNA. Translation: CAA72323.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Y64X-ray1.40A212-376[»]
2Y6GX-ray1.30A212-376[»]
2Y6HX-ray1.08A212-376[»]
2Y6JX-ray1.70A212-376[»]
2Y6KX-ray1.36A212-376[»]
2Y6LX-ray1.28A212-376[»]
3JXSX-ray1.60A/B/C212-376[»]
ProteinModelPortaliQ7WTN6.
SMRiQ7WTN6. Positions 40-200, 212-374.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM4. Carbohydrate-Binding Module Family 4.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ7WTN6.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR026444. Secre_tail.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR04183. Por_Secre_tail. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence of a thermostable multidomain xylanase from the bacterium Rhodothermus marinus."
    Nordberg Karlsson E., Bartonek-Roxa E., Holst O.
    Biochim. Biophys. Acta 1353:118-124(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Nordberg Karlsson E.M.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "The crystal structure of XG-34, an evolved xyloglucan-specific carbohydrate-binding module."
    Gullfot F., Tan T.C., von Schantz L., Karlsson E.N., Ohlin M., Brumer H., Divne C.
    Proteins 78:785-789(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 212-376 IN COMPLEX WITH CALCIUM.
  4. "Structural basis for carbohydrate-binding specificity--a comparative assessment of two engineered carbohydrate-binding modules."
    von Schantz L., Hakansson M., Logan D.T., Walse B., Osterlin J., Nordberg-Karlsson E., Ohlin M.
    Glycobiology 22:948-961(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 212-376 IN COMPLEX WITH CALCIUM.

Entry informationi

Entry nameiQ7WTN6_RHOMR
AccessioniPrimary (citable) accession number: Q7WTN6
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: April 29, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.