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Protein
Submitted name:

Xylanase

Gene

XynD

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradationImported

Protein family/group databases

CAZyiGH39. Glycoside Hydrolase Family 39.

Names & Taxonomyi

Protein namesi
Submitted name:
XylanaseImported
Gene namesi
Name:XynDImported
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)Imported
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Interactioni

Protein-protein interaction databases

STRINGi351627.Csac_2409.

Structurei

3D structure databases

ProteinModelPortaliO30428.
SMRiO30428. Positions 20-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG4105F2F. Bacteria.
COG3664. LUCA.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSiPR00745. GLHYDRLASE39.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O30428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEGIVTNIK IEKGKQIGIF PDKWKFCVGS GRIGLALQKE YIDALLYVKK
60 70 80 90 100
HIDFKYIRAH GLLHDDVGIY REDIIDGNEV SFYNFTYIDR IYDSFLELGI
110 120 130 140 150
RPFVEIGFMP SKLASGTQTV FYWRGNVTPP KDYGKWERLI KSVVKHFIDR
160 170 180 190 200
YGEKEVVQWP FEIWNEPNLN VFWKDANQAE YFKLYEVTAK AIKEVNENIK
210 220 230 240 250
VGGPAICGGS DYWIDDFLHF CYKNKVPVDF LTRHAYTGKP PQYTPHFVYQ
260 270 280 290 300
DVHPIEYMLN EFKSVREKVR NSPFPDLPIH ITEFNSSYHP LCPIHDTPFN
310 320 330 340 350
AAYLARVLSE AGDYVDSFSY WTFSDVFEEA DVPRAIFHGG FGLVAFNNIP
360 370 380 390 400
KPVFHMFTFF NAMGNKILYR DEHILITERE NGTIAIVAWN EVMKKEEATD
410 420 430
RKYKIEIPVD YNDVFIKQKL IDEENGNPWR TWIQMG
Length:436
Mass (Da):50,928
Last modified:January 1, 1998 - v1
Checksum:i6C2A948801D3277B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005383 Genomic DNA. Translation: AAB87373.1.
PIRiT30911.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005383 Genomic DNA. Translation: AAB87373.1.
PIRiT30911.

3D structure databases

ProteinModelPortaliO30428.
SMRiO30428. Positions 20-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351627.Csac_2409.

Protein family/group databases

CAZyiGH39. Glycoside Hydrolase Family 39.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105F2F. Bacteria.
COG3664. LUCA.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000514. Glyco_hydro_39.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01229. Glyco_hydro_39. 1 hit.
[Graphical view]
PRINTSiPR00745. GLHYDRLASE39.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS01027. GLYCOSYL_HYDROL_F39. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile 'Caldocellum saccharolyticum'."
    Luthi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D., Bergquist P.L.
    Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "A cluster of genes involved in xylan degradation cloned from the extreme thermophile Caldicellulosiruptor saccharolyticus."
    Te'o V.S.Jr., Gibbs M.D., Saul D.J., Bergquist P.L.
    Appl. Environ. Microbiol. 0:0-0(1997)
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiO30428_CALSA
AccessioniPrimary (citable) accession number: O30428
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: March 16, 2016
This is version 61 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.