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P91818 (P91818_TACTR) Unreviewed, UniProtKB/TrEMBL

Last modified March 8, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
OrganismTachypleus tridentatus (Japanese horseshoe crab) EMBL BAA12864.1
Taxonomic identifier6853 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaChelicerataMerostomataXiphosuraLimulidaeTachypleus

Protein attributes

Sequence length98 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Ontologies

Keywords
   Technical term3D-structure PDB 1DQC
Gene Ontology (GO)
   Biological processchitin metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functionchitin binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
P91818 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 6A9F6957F1D45815

FASTA9811,031
        10         20         30         40         50         60 
MASSFMFAVV VLFISLAANV ESYLAFRCGR YSPCLDDGPN VNLYSCCSFY NCHKCLARLE 

        70         80         90 
NCPKGLHYNA YLKVCDWPSK AGCTSVNKEC HLWKTGRK 

« Hide

References

[1]"Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity."
Kawabata S., Nagayama R., Hirata M., Shigenaga T., Agarwala K.L., Saito T., Cho J., Nakajima H., Takagi T., Iwanaga S.
J. Biochem. 120:1253-1260(1996) [PubMed: 9010778] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"Tachycitin, a Small Granular Component in Horseshoe Crab Hemocytes, is an Antimicrobial Protein with Chitin-binding Activity."
Kawabata S., Nagayama R., Hirata M., Shigenaga T., Saito T., Agarwala L., Cho J., Nakajima H., Takagi T., Iwanaga S.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Chitin-binding proteins in invertebrates and plants comprise a common chitin-binding structural motif."
Suetake T., Tsuda S., Kawabata S., Miura K., Iwanaga S., Hikichi K., Nitta K., Kawano K.
J. Biol. Chem. 275:17929-17932(2000) [PubMed: 10770921] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-95.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85756 mRNA. Translation: BAA12864.1.
PIRJC5147.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQCNMR-A23-95[»]
ProteinModelPortalP91818.
SMRP91818. Positions 23-95.
ModBaseSearch...

Protein family/group databases

CAZyCBM14. Carbohydrate-Binding Module Family 14.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002557. Chitin-bd_dom.
[Graphical view]
Gene3DG3DSA:2.170.140.10. Chitin-bd_dom. 1 hit.
PfamPF01607. CBM_14. 1 hit.
[Graphical view]
SMARTSM00494. ChtBD2. 1 hit.
[Graphical view]
SUPFAMSSF57625. Chitin_bind_PerA. 1 hit.
PROSITEPS50940. CHIT_BIND_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP91818_TACTR
AccessionPrimary (citable) accession number: P91818
Entry history
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: March 8, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)