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Protein

Penicillolysin

Gene

plnC

Organism
Penicillium citrinum
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi302Zinc; catalyticPROSITE-ProRule annotation1
Active sitei303PROSITE-ProRule annotation1
Metal bindingi306Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi317Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandMetal-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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
PropeptideiPRO_000002923420 – 174Add BLAST155
ChainiPRO_0000029235175 – 351PenicillolysinAdd BLAST177

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi181N-linked (GlcNAc...) asparagineSequence analysis1

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
InterProiView protein in InterPro
IPR024079 MetalloPept_cat_dom_sf
IPR001384 Peptidase_M35
PfamiView protein in Pfam
PF02102 Peptidase_M35, 1 hit
PRINTSiPR00768 DEUTEROLYSIN
PROSITEiView protein in PROSITE
PS00142 ZINC_PROTEASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPLNC_PENCI
AccessioniPrimary (citable) accession number: P47189
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 25, 2018
This is version 77 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing
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Main funding by: National Institutes of Health