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Protein

Penicillolysin

Gene

plnC

Organism
Penicillium citrinum
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi302 – 3021Zinc; catalyticPROSITE-ProRule annotation
Active sitei303 – 3031PROSITE-ProRule annotation
Metal bindingi306 – 3061Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi317 – 3171Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM35.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Penicillolysin (EC:3.4.24.39)
Alternative name(s):
Deuterolysin
Gene namesi
Name:plnC
OrganismiPenicillium citrinum
Taxonomic identifieri5077 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 174155PRO_0000029234Add
BLAST
Chaini175 – 351177PenicillolysinPRO_0000029235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliP47189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M35 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001384. Peptidase_M35.
[Graphical view]
PfamiPF02102. Peptidase_M35. 1 hit.
[Graphical view]
PRINTSiPR00768. DEUTEROLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P47189-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFTTLSTAF LALAQNVYAF PIESDLSALD VTLSQVSDTR IKAVVKNTGA
60 70 80 90 100
ENVTFVHLNF FRDSAPVKKV SVYRENNEVV FDGIKRRFQL QGLASESLTT
110 120 130 140 150
LEAGEVLEDE FDIATTTDLS SGGAITLRSN GLVPVVKDGA VTGYLPYSSN
160 170 180 190 200
DLKLNIDGAK ASTVTKALKP LDRRTKETCS NASRKSALEK ALSNTVKLAN
210 220 230 240 250
AAATAARSGS ASKFSEYFKT TSSSTRSVVA ARLEAVAKEA QSASSGSTTY
260 270 280 290 300
YCSDTLGYCE TNVLAYTLPA RNIIANCDIY YSYLPALAGT CHQQDQATTT
310 320 330 340 350
LHEFTHAPGV YSPGTDDLGY GYSAATSLSS SQAVLNADSY ALYANAINLG

C
Length:351
Mass (Da):37,387
Last modified:November 1, 1995 - v1
Checksum:i5FA83F285F2E2F16
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25535 mRNA. Translation: BAA05018.1.
PIRiS47635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D25535 mRNA. Translation: BAA05018.1.
PIRiS47635.

3D structure databases

ProteinModelPortaliP47189.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM35.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR024079. MetalloPept_cat_dom.
IPR001384. Peptidase_M35.
[Graphical view]
PfamiPF02102. Peptidase_M35. 1 hit.
[Graphical view]
PRINTSiPR00768. DEUTEROLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of the complementary DNA for penicillolysin gene, plnC, and 18 kDa metalloendopeptidase gene from Penicillium citrinum."
    Matsumoto K., Yamaguchi M., Ichishima E.
    Biochim. Biophys. Acta 1218:469-472(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: NBRC 6026 / FAT 1131.

Entry informationi

Entry nameiPLNC_PENCI
AccessioniPrimary (citable) accession number: P47189
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.