Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Hepatopancreas trypsin

Gene
N/A
Organism
Astacus leptodactylus (Turkish narrow-clawed crayfish) (Pontastacus leptodactylus)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Calcium 1Combined sources
Metal bindingi66 – 661Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi69 – 691Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi71 – 711Calcium 1Combined sources
Metal bindingi74 – 741Calcium 1Combined sources
Metal bindingi156 – 1561Calcium 2Combined sources
Metal bindingi170 – 1701Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi172 – 1721Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi224 – 2241Calcium 2Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine proteaseUniRule annotation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Protein family/group databases

MEROPSiS01.035.

Names & Taxonomyi

Protein namesi
Submitted name:
Hepatopancreas trypsinImported
OrganismiAstacus leptodactylus (Turkish narrow-clawed crayfish) (Pontastacus leptodactylus)Imported
Taxonomic identifieri6717 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataAstacideaAstacoideaAstacidaeAstacus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 46Combined sources
Disulfide bondi159 ↔ 174Combined sources
Disulfide bondi185 ↔ 213Combined sources

Keywords - PTMi

Disulfide bondSAAS annotation

Interactioni

Protein-protein interaction databases

IntActiQ52V24. 1 interaction.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F91X-ray1.20A1-237[»]
4BNRX-ray2.00A/B1-237[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ52V24.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 237237Peptidase S1InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.SAAS annotation
Contains 1 peptidase S1 domain.UniRule annotation

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q52V24-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IVGGTDATLG EFPYQLSFQE TFIGFSFHFC GASIYNENYA ITAGHCAYGD
60 70 80 90 100
DYENPSGLQI VAGELDMSVN EGSEQIITVS KIILHENFDY NLLDNDISLL
110 120 130 140 150
KLSGSLTFND NVAPIALPEQ GHTATGDVIV TGWGTTSEGG NTPDVLQKVT
160 170 180 190 200
VPLVSDEDCR ADYGADEILD SMICAGVPEG GKDSCQGDSG GPLAASDTGS
210 220 230
TYLAGIVSWG YGCARPGYPG VYTEVSYHVD WIKANAV
Length:237
Mass (Da):25,033
Last modified:May 24, 2005 - v1
Checksum:iE9C74D1EA3847025
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY906961 mRNA. Translation: AAX98287.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY906961 mRNA. Translation: AAX98287.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F91X-ray1.20A1-237[»]
4BNRX-ray2.00A/B1-237[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ52V24. 1 interaction.

Protein family/group databases

MEROPSiS01.035.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ52V24.

Family and domain databases

InterProiIPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition."
    Fodor K., Harmat V., Hetenyi C., Kardos J., Antal J., Perczel A., Patthy A., Katona G., Graf L.
    J. Mol. Biol. 350:156-169(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis."
    Fodor K., Harmat V., Neutze R., Szilagyi L., Graf L., Katona G.
    Biochemistry 45:2114-2121(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS), DISULFIDE BONDS.
  3. "Comparison of complexes formed by a crustacean and a vertebrate trypsin with bovine pancreatic trypsin inhibitor - the key to achieving extreme stability?"
    Molnar T., Voros J., Szeder B., Takats K., Kardos J., Katona G., Graf L.
    FEBS J. 280:5750-5763(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH CALCIUM, DISULFIDE BONDS.

Entry informationi

Entry nameiQ52V24_ASTLP
AccessioniPrimary (citable) accession number: Q52V24
Entry historyi
Integrated into UniProtKB/TrEMBL: May 24, 2005
Last sequence update: May 24, 2005
Last modified: May 11, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.