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Unreviewed, UniProtKB/TrEMBL Q9RMB8 (Q9RMB8_ARTSP)

Last modified June 16, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

Names and origin

Protein namesSubmitted name:
    Chitinase EMBL CAB62382.1
    EC=3.2.1.14
Gene names
Name: chitiA EMBL CAB62382.1
OrganismArthrobacter sp. EMBL CAB62382.1
Taxonomic identifier1667 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length880 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

Ontologies

Keywords
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological processchitin catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

cation binding

Inferred from electronic annotation. Source: InterPro

chitinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential EMBL CAB62382.1
Chain34 – 880847 Potential EMBL CAB62382.1
PRO_5000065724

Sequences

Sequence LengthMass (Da)Tools
Q9RMB8-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E90B03B95E86ECE9

FASTA88092,821
        10         20         30         40         50         60 
MQTPTLAQDG RSAAIVTGFA LVASIGITTQ VAYASPSGTT TTKACATVAP ASSYSSNAVV 

        70         80         90        100        110        120 
SHQSVNYSAK WWTQNNVPGS DPWGPWTSQG TCGTVTDPTP TPTPTPTPTP TAVPTTTPTA 

       130        140        150        160        170        180 
VPTATPTTPP PTTPAAGTPW TSNPDEKCRP DGLYQTPGVN VPYCSVYDEA GRELLPNGLE 

       190        200        210        220        230        240 
QRVIGYFTSW RTGENGAPRY LASDIPWKKL SHINYAFAHI DKNNKVSVGA ETPGNAATDL 

       250        260        270        280        290        300 
TWPGGCGAEM DPTLPYKGHL NQLKKFKKEN PGVKTLVSVG GWAETGGHFA ADGTRVGDGG 

       310        320        330        340        350        360 
FYTLTESQAK IDTFSDSAVE FIRKYGFSGV DIDYEYATSN SKAGNPDDFA ISEPRRAVLF 

       370        380        390        400        410        420 
ENYMKLMKTL REKLDKASVA DGTYYQLTVA APASGWLLRG MEAHQVVKYL DFVNMMSYDL 

       430        440        450        460        470        480 
HGAWNNFVGG NPALFDDGKD PELAAGGVYN AYKGIGYLNS DWAYHYFRGA MPAGRINLGV 

       490        500        510        520        530        540 
PFYTRGWTNV QGGTNGLYGS SVLADQNKCA PGTGPKAGGN SKCGDGAGGI DNLWHDSDPM 

       550        560        570        580        590        600 
GGELAAGANP IWHVLNLQKG VVGDYAASYG SPTGALKGTY TRHFDNVTKN EWWWNDTTKT 

       610        620        630        640        650        660 
FLSGDADQAI QAKADYVADK GLGGVMIWEL AGDYEYNASK GQYEMGSTLV NKIHSTLSAS 

       670        680        690        700        710        720 
KPYGATKANV KMPTKAIDLG VELKNFALGD NNYPINPEAH FTNNSKTTIP AGATITFDSA 

       730        740        750        760        770        780 
ASDTGEMKEQ SGWTITKDSS DHTGSNVGGL KGDFHTYTIK VPAGGIAPGA TVSTKLAWTL 

       790        800        810        820        830        840 
PTSMISNFRV SIGSEQYALL TDYPRGVSVV EPSAGTGGGN GAGPVESCNG AVTWSAAAVY 

       850        860        870        880 
TGGAVVAHAG SSYKAKWWTQ GEVPGSGAAN AWGSPILCGK 

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References

[1]"Cloning, sequences, and characterization of two chitinase genes from the Antarctic Arthrobacter sp. strain TAD20: isolation and partial characterization of the enzymes."
Lonhienne T., Mavromatis K., Vorgias C.E., Buchon L., Gerday C., Bouriotis V.
J. Bacteriol. 183:1773-1779(2001) [PubMed: 11160110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases

AJ250585 Genomic DNA. Translation: CAB62382.1.

3D structure databases

HSSPHSSP built from PDB template 1ITX based on UniProtKB P20533.
ModBaseSearch...

Protein family/group databases

CAZyCBM5. Carbohydrate-Binding Module Family 5.
GH18. Glycoside Hydrolase Family 18.

Family and domain databases

InterProIPR003610. CBM_5_12.
IPR009470. Chi_C.
IPR011583. Chitinase_II.
IPR001223. Glyco_hydro18cat.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]
Gene3DG3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PfamPF02839. CBM_5_12. 2 hits.
PF06483. ChiC. 1 hit.
PF00704. Glyco_hydro_18. 1 hit.
[Graphical view]
ProDomPD000471. Chitinase_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00495. ChtBD3. 2 hits.
SM00636. Glyco_18. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ9RMB8_ARTSP
AccessionPrimary (citable) accession number: Q9RMB8
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
Names and origin · Protein attributes · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information