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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)DescriptionActionsGraphical viewLength
Active sitei41Charge relay system1
Active sitei87Charge relay system1
Active sitei178Charge relay system1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000886641 – 226BrachyurinAdd BLAST226

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 42
Disulfide bondi151 ↔ 164
Disulfide bondi174 ↔ 200

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1226
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 20Combined sources6
Turni21 – 23Combined sources3
Beta strandi24 – 32Combined sources9
Beta strandi35 – 38Combined sources4
Helixi40 – 43Combined sources4
Beta strandi49 – 54Combined sources6
Beta strandi56 – 60Combined sources5
Beta strandi66 – 70Combined sources5
Beta strandi73 – 75Combined sources3
Turni81 – 84Combined sources4
Beta strandi89 – 92Combined sources4
Beta strandi101 – 103Combined sources3
Beta strandi118 – 125Combined sources8
Beta strandi132 – 134Combined sources3
Beta strandi143 – 146Combined sources4
Helixi148 – 155Combined sources8
Beta strandi162 – 165Combined sources4
Turni168 – 170Combined sources3
Beta strandi181 – 184Combined sources4
Beta strandi187 – 196Combined sources10
Beta strandi206 – 211Combined sources6
Helixi212 – 214Combined sources3
Helixi215 – 222Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP00771.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 223Peptidase S1PROSITE-ProRule annotationAdd BLAST223

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)DescriptionActionsGraphical viewLength
Sequence conflicti91I → V AA sequence (PubMed:6252953).Curated1
Sequence conflicti147 – 148SN → NS AA sequence (PubMed:6252953).Curated2
Sequence conflicti175N → D AA sequence (PubMed:6252953).Curated1
Sequence conflicti185N → D AA sequence (PubMed:6252953).Curated1

Sequence databases

PIRiA00958. KCUF.

Cross-referencesi

Sequence databases

PIRiA00958. KCUF.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AZZX-ray2.30A/B1-226[»]
ProteinModelPortaliP00771.
SMRiP00771.
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: November 2, 2016
This is version 94 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.