P35049 (TRYP_FUSOX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Trypsin EC=3.4.21.4
Organism	Fusarium oxysporum (Panama disease fungus)
Taxonomic identifier	5507 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › sordariomyceta › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › mitosporic Nectriaceae › Fusarium › Fusarium oxysporum species complex

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Subcellular location	Secreted.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Zymogen
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

17

Potential

Propeptide

18 – 25

8

Activation peptide

PRO_0000028301

Chain

26 – 248

223

Trypsin

PRO_0000028302

Regions

Domain

25 – 248

224

Peptidase S1

Sites

Active site

65

1

Charge relay system

Active site

108

1

Charge relay system

Active site

204

1

Charge relay system

Site

198

1

Required for specificity

Amino acid modifications

Disulfide bond

50 ↔ 66

Disulfide bond

174 ↔ 189

Disulfide bond

200 ↔ 225

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

39 – 44

6

Beta strand

47 – 56

10

Beta strand

59 – 62

4

Helix

64 – 67

4

Helix

72 – 74

3

Beta strand

75 – 80

6

Beta strand

82 – 91

10

Beta strand

93 – 98

6

Beta strand

110 – 116

7

Beta strand

141 – 147

7

Beta strand

162 – 169

8

Helix

171 – 178

8

Turn

180 – 182

3

Beta strand

187 – 190

4

Beta strand

207 – 209

3

Beta strand

215 – 221

7

Beta strand

223 – 226

4

Beta strand

232 – 236

5

Turn

237 – 239

3

Helix

241 – 247

7

Sequences

	Sequence		Length	Mass (Da)
	P35049 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: 1A0EBA88C3E70294	FASTA	248	24,576
	10 20 30 40 50 60 MVKFASVVAL VAPLAAAAPQ EIPNIVGGTS ASAGDFPFIV SISRNGGPWC GGSLLNANTV 70 80 90 100 110 120 LTAAHCVSGY AQSGFQIRAG SLSRTSGGIT SSLSSVRVHP SYSGNNNDLA ILKLSTSIPS 130 140 150 160 170 180 GGNIGYARLA ASGSDPVAGS SATVAGWGAT SEGGSSTPVN LLKVTVPIVS RATCRAQYGT 190 200 210 220 230 240 SAITNQMFCA GVSSGGKDSC QGDSGGPIVD SSNTLIGAVS WGNGCARPNY SGVYASVGAL RSFIDTYA

References

[1]	"The sequence and X-ray structure of the trypsin from Fusarium oxysporum." Rypniewski W.R., Hastrup S., Betzel C., Dauter M., Dauter Z., Papendorf G., Branner S., Wilson K.S. Protein Eng. 6:341-348(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[2]	"Structure of inhibited trypsin from Fusarium oxysporum at 1.55 A." Rypniewski W.R., Dambmann C., von der Osten C., Dauter M., Wilson K.S. Acta Crystallogr. D 51:73-84(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S63827 mRNA. Translation: AAB27568.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FN8	X-ray	0.81	A	25-248	[»]
1FY4	X-ray	0.81	A	25-248	[»]
1FY5	X-ray	0.81	A	25-248	[»]
1GDN	X-ray	0.81	A	25-248	[»]
1GDQ	X-ray	0.93	A	25-248	[»]
1GDU	X-ray	1.07	A	25-248	[»]
1PPZ	X-ray	1.23	A	25-248	[»]
1PQ5	X-ray	0.85	A	25-248	[»]
1PQ7	X-ray	0.80	A	25-248	[»]
1PQ8	X-ray	1.00	A	25-248	[»]
1PQA	X-ray	1.23	A	25-248	[»]
1TRY	X-ray	1.55	A	25-248	[»]
1XVM	X-ray	1.10	A	25-248	[»]
1XVO	X-ray	0.84	A	25-248	[»]
2G51	X-ray	1.84	A	25-248	[»]
2G52	X-ray	1.84	A	25-248	[»]
2VU8	X-ray	1.80	E	25-248	[»]

ProteinModelPortal

P35049.

SMR

P35049. Positions 25-248.

ModBase

Search...

Protein family/group databases

MEROPS

S01.103.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00089. Trypsin. 1 hit.
[Graphical view]

PRINTS

PR00722. CHYMOTRYPSIN.

SMART

SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.

PROSITE

PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35049.

Entry information

Entry name

TRYP_FUSOX

Accession

Primary (citable) accession number: P35049

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program