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Protein

Brachyurin

Gene
N/A
Organism
Uca pugilator (Atlantic sand fiddler crab) (Ocypoda pugilator)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme is a serine protease capable of degrading the native triple helix of collagen.

Catalytic activityi

Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei41 – 411Charge relay system
Active sitei87 – 871Charge relay system
Active sitei178 – 1781Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Collagen degradation

Protein family/group databases

MEROPSiS01.122.

Names & Taxonomyi

Protein namesi
Recommended name:
Brachyurin (EC:3.4.21.32)
Alternative name(s):
Collagenolytic protease
OrganismiUca pugilator (Atlantic sand fiddler crab) (Ocypoda pugilator)
Taxonomic identifieri6772 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataBrachyuraEubrachyuraOcypodoideaOcypodidaeUcinaeUcaLeptuca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226BrachyurinPRO_0000088664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 42
Disulfide bondi151 ↔ 164
Disulfide bondi174 ↔ 200

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 206Combined sources
Turni21 – 233Combined sources
Beta strandi24 – 329Combined sources
Beta strandi35 – 384Combined sources
Helixi40 – 434Combined sources
Beta strandi49 – 546Combined sources
Beta strandi56 – 605Combined sources
Beta strandi66 – 705Combined sources
Beta strandi73 – 753Combined sources
Turni81 – 844Combined sources
Beta strandi89 – 924Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi118 – 1258Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi143 – 1464Combined sources
Helixi148 – 1558Combined sources
Beta strandi162 – 1654Combined sources
Turni168 – 1703Combined sources
Beta strandi181 – 1844Combined sources
Beta strandi187 – 19610Combined sources
Beta strandi206 – 2116Combined sources
Helixi212 – 2143Combined sources
Helixi215 – 2228Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZZX-ray2.30A/B1-226[»]
ProteinModelPortaliP00771.
SMRiP00771. Positions 1-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00771.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 223223Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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: Complete.

P00771-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IVGGVEAVPN SWPHQAALFI DDMYFCGGSL ISPEWILTAA HCMDGAGFVD
60 70 80 90 100
VVLGAHNIRE DEATQVTIQS TDFTVHENYN SFVISNDIAV IRLPVPVTLT
110 120 130 140 150
AAIATVGLPS TDVGVGTVVT PTGWGLPSDS ALGISDVLRQ VDVPIMSNAD
160 170 180 190 200
CDAVYGIVTD GNICIDSTGG KGTCNGDSGG PLNYNGLTYG ITSFGAAAGC
210 220
EAGYPDAFTR VTYFLDWIQT QTGITP
Length:226
Mass (Da):23,511
Last modified:July 15, 1998 - v2
Checksum:iE45591CAF332CE8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911I → V AA sequence (PubMed:6252953).Curated
Sequence conflicti147 – 1482SN → NS AA sequence (PubMed:6252953).Curated
Sequence conflicti175 – 1751N → D AA sequence (PubMed:6252953).Curated
Sequence conflicti185 – 1851N → D AA sequence (PubMed:6252953).Curated

Sequence databases

PIRiA00958. KCUF.

Cross-referencesi

Sequence databases

PIRiA00958. KCUF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZZX-ray2.30A/B1-226[»]
ProteinModelPortaliP00771.
SMRiP00771. Positions 1-226.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.122.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP00771.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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...

Entry informationi

Entry nameiCOGS_UCAPU
AccessioniPrimary (citable) accession number: P00771
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 15, 1998
Last modified: September 7, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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.