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Protein

Cysteine proteinase EP-B 2

Gene

EPB2

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei158 – 1581By similarity
Active sitei297 – 2971By similarity
Active sitei318 – 3181By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Germination

Protein family/group databases

MEROPSiI29.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine proteinase EP-B 2 (EC:3.4.22.-)
Gene namesi
Name:EPB2
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Propeptidei29 – 133105Activation peptideSequence analysisPRO_0000026422Add
BLAST
Chaini134 – 373240Cysteine proteinase EP-B 2PRO_0000026423Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi155 ↔ 197By similarity
Disulfide bondi189 ↔ 230By similarity
Disulfide bondi291 ↔ 343By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Inductioni

Synthesized by the aleurone cells stimulated by gibberellic acid.

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni140 – 1445Combined sources
Helixi158 – 17518Combined sources
Helixi183 – 1897Combined sources
Helixi196 – 1983Combined sources
Helixi202 – 21110Combined sources
Beta strandi215 – 2173Combined sources
Turni218 – 2203Combined sources
Helixi232 – 2387Combined sources
Beta strandi247 – 2504Combined sources
Helixi256 – 26510Combined sources
Beta strandi268 – 2725Combined sources
Helixi277 – 2804Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi297 – 30610Combined sources
Beta strandi312 – 3176Combined sources
Beta strandi329 – 3357Combined sources
Helixi342 – 3443Combined sources
Turni345 – 3473Combined sources
Beta strandi350 – 3534Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FO5X-ray2.20A/B/C/D131-373[»]
ProteinModelPortaliP25250.
SMRiP25250. Positions 133-356.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25250.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25250-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLSKKLLV ASMVAAVLAV AAVELCSAIP MEDKDLESEE ALWDLYERWQ
60 70 80 90 100
SAHRVRRHHA EKHRRFGTFK SNAHFIHSHN KRGDHPYRLH LNRFGDMDQA
110 120 130 140 150
EFRATFVGDL RRDTPSKPPS VPGFMYAALN VSDLPPSVDW RQKGAVTGVK
160 170 180 190 200
DQGKCGSCWA FSTVVSVEGI NAIRTGSLVS LSEQELIDCD TADNDGCQGG
210 220 230 240 250
LMDNAFEYIK NNGGLITEAA YPYRAARGTC NVARAAQNSP VVVHIDGHQD
260 270 280 290 300
VPANSEEDLA RAVANQPVSV AVEASGKAFM FYSEGVFTGE CGTELDHGVA
310 320 330 340 350
VVGYGVAEDG KAYWTVKNSW GPSWGEQGYI RVEKDSGASG GLCGIAMEAS
360 370
YPVKTYSKPK PTPRRALGAR ESL
Length:373
Mass (Da):40,511
Last modified:May 1, 1992 - v1
Checksum:i439C56A3EF2851DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19384 Genomic DNA. Translation: AAA85036.1.
PIRiJQ1110.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19384 Genomic DNA. Translation: AAA85036.1.
PIRiJQ1110.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FO5X-ray2.20A/B/C/D131-373[»]
ProteinModelPortaliP25250.
SMRiP25250. Positions 133-356.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiI29.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
COG4870. LUCA.

Miscellaneous databases

EvolutionaryTraceiP25250.

Family and domain databases

InterProiIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYSP2_HORVU
AccessioniPrimary (citable) accession number: P25250
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 17, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.