Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P28296 (ORYZ_ASPFU)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Oryzin
    EC=3.4.21.63
Alternative name(s):
    Alkaline proteinase
      Short name=ALP
    Elastase
    Elastinolytic serine proteinase
Gene names
Name: alk1
Synonyms: alp
ORF Names: AFUA_4G11800
OrganismAspergillus fumigatus (Sartorya fumigata) [Complete proteome]
Taxonomic identifier5085 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Elastolytic enzyme probably acting as a virulence factor in invasive aspergillosis.

Catalytic activity

Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase S8 family.

Ontologies

Keywords
   Biological processVirulence
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMGlycoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processnegative regulation of catalytic activity

Inferred from electronic annotation. Source: InterPro

pathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionidentical protein binding

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Propeptide22 – 121100 By similarity
PRO_0000027082
Chain122 – 403282Oryzin
PRO_0000027083

Sites

Active site1621Charge relay system By similarity
Active site1931Charge relay system By similarity
Active site3491Charge relay system By similarity

Amino acid modifications

Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation3071N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict106 – 1072SA → RG in CAA77666. Ref.1
Sequence conflict2951A → R in AAB07672. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P28296-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 2D900D1AE22CDD4A

FASTA40342,190
        10         20         30         40         50         60 
MLSIKRTLLL LGAVLPAVFG APVQETRRAA QKIPGKYIVT FKPGTDTATI ESHTLWATDL 

        70         80         90        100        110        120 
HKRNLERRDT TSGEPPVGIE KSYKIKDFAA YAGSFDDATI EEIRKSADVA HVEEDQIWYL 

       130        140        150        160        170        180 
DALTTQKGAP WGLGSISHKG QASTDYIYDT SAGAGTYAYV VDSGINVNHV EFESRASLAY 

       190        200        210        220        230        240 
NAAGGSHVDS IGHGTHVAGT IGGKTYGVAK KTNLLSVKVF QGESSSTSII LDGFNWAVND 

       250        260        270        280        290        300 
IVSKGRTKKA AINMSLGGGY SYAFNNAVEN AFDEGVLSVV AAGNENSDAS NTSPASAPNA 

       310        320        330        340        350        360 
LTVAAINKSN ARASFSNYGS VVDIFAPGQD ILSAWIGSTT ATNTISGTSM ATPHIVGLSV 

       370        380        390        400 
YLMGLENLSG PAAVTARIKE LATNGVVTNV KGSPNKLAYN GNA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatus."
Jaton-Ogay K., Suter M., Crameri R., Falchetto R., Fatih A., Monod M.
FEMS Microbiol. Lett. 71:163-168(1992) [PubMed: 1601287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evidence for possible involvement of an elastolytic serine protease in aspergillosis."
Kolattukudy P.E., Lee J.D., Rogers L.M., Zimmerman P., Ceselski S., Fox B., Stein B., Copelan E.A.
Infect. Immun. 61:2357-2368(1993) [PubMed: 8500876] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed: 16372009] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

Z11580 Genomic DNA. Translation: CAA77666.1.
M99420 Genomic DNA. Translation: AAB07672.1.
AAHF01000005 Genomic DNA. Translation: EAL89613.1.
PIRS22184.
RefSeqXP_751651.1.

3D structure databases

HSSPHSSP built from PDB template 1IC6 based on UniProtKB P06873.
ModBaseSearch...

Protein family/group databases

MEROPSS08.053.

Genome annotation databases

GeneID3509271.
KEGGafm:AFUA_4G11800.

Phylogenomic databases

HOGENOMP28296.
OMAP28296. GVAKSVN.

Enzyme and pathway databases

BRENDA3.4.21.63. 18841.

Family and domain databases

InterProIPR000209. Pept_S8_S53.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR010259. Prot_inh_S8A.
[Graphical view]
Gene3DG3DSA:3.40.50.200. Pept_S8_S53. 1 hit.
PANTHERPTHR10795. SubtilSerProt. 1 hit.
PfamPF05922. Inhibitor_I9. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
PROSITEPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameORYZ_ASPFU
AccessionPrimary (citable) accession number: P28296
Secondary accession number(s): Q4WQ71
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 6, 2005
Last modified: June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents