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Protein

Rhizopuspepsin

Gene
N/A
Organism
Rhizopus chinensis (Bread mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of insulin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei103PROSITE-ProRule annotation1
Active sitei286PROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Rhizopuspepsin (EC:3.4.23.21)
OrganismiRhizopus chinensis (Bread mold)
Taxonomic identifieri4843 [NCBI]
Taxonomic lineageiEukaryotaFungiFungi incertae sedisMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4253.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000002588122 – 68Activation peptide1 PublicationAdd BLAST47
ChainiPRO_000002588269 – 393RhizopuspepsinAdd BLAST325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi116 ↔ 119
Disulfide bondi320 ↔ 353

Keywords - PTMi

Disulfide bond, Zymogen

Interactioni

Chemistry databases

BindingDBiP06026.

Structurei

Secondary structure

1393
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi73 – 79Combined sources7
Turni80 – 83Combined sources4
Beta strandi84 – 91Combined sources8
Turni92 – 95Combined sources4
Beta strandi96 – 103Combined sources8
Beta strandi110 – 113Combined sources4
Beta strandi121 – 123Combined sources3
Helixi128 – 130Combined sources3
Beta strandi135 – 144Combined sources10
Beta strandi150 – 162Combined sources13
Beta strandi165 – 178Combined sources14
Helixi180 – 183Combined sources4
Beta strandi188 – 192Combined sources5
Helixi196 – 198Combined sources3
Helixi207 – 213Combined sources7
Beta strandi218 – 226Combined sources9
Helixi229 – 231Combined sources3
Beta strandi235 – 239Combined sources5
Helixi244 – 246Combined sources3
Beta strandi252 – 255Combined sources4
Beta strandi264 – 267Combined sources4
Beta strandi269 – 272Combined sources4
Beta strandi275 – 278Combined sources4
Beta strandi281 – 285Combined sources5
Beta strandi290 – 295Combined sources6
Helixi296 – 305Combined sources10
Beta strandi312 – 314Combined sources3
Beta strandi316 – 318Combined sources3
Helixi322 – 324Combined sources3
Beta strandi328 – 332Combined sources5
Beta strandi335 – 339Combined sources5
Helixi341 – 344Combined sources4
Beta strandi345 – 349Combined sources5
Beta strandi352 – 367Combined sources16
Helixi369 – 372Combined sources4
Beta strandi375 – 380Combined sources6
Turni381 – 384Combined sources4
Beta strandi385 – 391Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UH7X-ray2.10A69-392[»]
1UH8X-ray2.30A69-392[»]
1UH9X-ray2.00A69-392[»]
2APRX-ray1.80A69-392[»]
3APRX-ray1.80E69-392[»]
4APRX-ray2.50E69-392[»]
5APRX-ray2.10E69-392[»]
6APRX-ray2.50E69-392[»]
ProteinModelPortaliP06026.
SMRiP06026.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06026.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini85 – 389Peptidase A1PROSITE-ProRule annotationAdd BLAST305

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 2 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P06026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFTLISSCI AIAALAVAVD AAPGEKKISI PLAKNPNYKP SAKNAIQKAI
60 70 80 90 100
AKYNKHKINT STGGIVPDAG VGTVPMTDYG NDVEYYGQVT IGTPGKKFNL
110 120 130 140 150
DFDTGSSDLW IASTLCTNCG SRQTKYDPKQ SSTYQADGRT WSISYGDGSS
160 170 180 190 200
ASGILAKDNV NLGGLLIKGQ TIELAKREAA SFANGPNDGL LGLGFDTITT
210 220 230 240 250
VRGVKTPMDN LISQGLISRP IFGVYLGKAS NGGGGEYIFG GYDSTKFKGS
260 270 280 290 300
LTTVPIDNSR GWWGITVDRA TVGTSTVASS FDGILDTGTT LLILPNNVAA
310 320 330 340 350
SVARAYGASD NGDGTYTISC DTSRFKPLVF SINGASFQVS PDSLVFEEYQ
360 370 380 390
GQCIAGFGYG NFDFAIIGDT FLKNNYVVFN QGVPEVQIAP VAQ
Length:393
Mass (Da):41,327
Last modified:October 1, 1996 - v2
Checksum:i479BBDB3D001D25C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti83V → I.1
Natural varianti129K → N.1
Natural varianti184N → S.1
Natural varianti230S → K.1
Natural varianti298V → I.1
Natural varianti309S → Y.1
Natural varianti361N → D.1
Natural varianti393Q → E.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33859 Genomic DNA. Translation: AAB59306.1.
L33858 Genomic DNA. Translation: AAB59305.1.
J02651 mRNA. Translation: AAA33879.1.
PIRiA26681.
A41415.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33859 Genomic DNA. Translation: AAB59306.1.
L33858 Genomic DNA. Translation: AAB59305.1.
J02651 mRNA. Translation: AAA33879.1.
PIRiA26681.
A41415.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UH7X-ray2.10A69-392[»]
1UH8X-ray2.30A69-392[»]
1UH9X-ray2.00A69-392[»]
2APRX-ray1.80A69-392[»]
3APRX-ray1.80E69-392[»]
4APRX-ray2.50E69-392[»]
5APRX-ray2.10E69-392[»]
6APRX-ray2.50E69-392[»]
ProteinModelPortaliP06026.
SMRiP06026.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP06026.
ChEMBLiCHEMBL4253.

Protein family/group databases

MEROPSiA01.012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP06026.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 2 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARP_RHICH
AccessioniPrimary (citable) accession number: P06026
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.