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Q9GK11

- Q9GK11_CAMDR

UniProt

Q9GK11 - Q9GK11_CAMDR

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Protein
Submitted name:

Chymosin

Gene

chymosin

Organism
Camelus dromedarius (Dromedary) (Arabian camel)
Status
Unreviewed - Annotation score: 1 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl proteaseUniRule annotation, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.006.

Names & Taxonomyi

Protein namesi
Submitted name:
ChymosinImported (EC:3.4.23.4Imported)
Gene namesi
Name:chymosinImported
OrganismiCamelus dromedarius (Dromedary) (Arabian camel)Imported
Taxonomic identifieri9838 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaTylopodaCamelidaeCamelus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi158 – 1581N-linked (GlcNAc...)Imported

Keywords - PTMi

Disulfide bondSAAS annotation

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AA9X-ray1.60A62-381[»]
ProteinModelPortaliQ9GK11.
SMRiQ9GK11. Positions 59-381.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.UniRule annotation

Phylogenomic databases

HOVERGENiHBG000482.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9GK11-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRCLVVLLAA LALSQASGIT RIPLHKGKTL RKALKERGLL EDFLQRQQYA
60 70 80 90 100
VSSKYSSLGK VAREPLTSYL DSQYFGKIYI GTPPQEFTVV FDTGSSDLWV
110 120 130 140 150
PSIYCKSNVC KNHHRFDPRK SSTFRNLGKP LSIHYGTGSM EGFLGYDTVT
160 170 180 190 200
VSNIVDPNQT VGLSTEQPGE VFTYSEFDGI LGLAYPSLAS EYSVPVFDNM
210 220 230 240 250
MDRHLVARDL FSVYMDRNGQ GSMLTLGAID PSYYTGSLHW VPVTLQQYWQ
260 270 280 290 300
FTVDSVTING VAVACVGGCQ AILDTGTSVL FGPSSDILKI QMAIGATENR
310 320 330 340 350
YGEFDVNCGN LRSMPTVVFE INGRDYPLSP SAYTSKDQGF CTSGFQGDNN
360 370 380
SELWILGDVF IREYYSVFDR ANNRVGLAKA I
Length:381
Mass (Da):42,083
Last modified:March 1, 2001 - v1
Checksum:i24BADB57B2E7FDD7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ131677 mRNA. Translation: CAC19554.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ131677 mRNA. Translation: CAC19554.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AA9 X-ray 1.60 A 62-381 [» ]
ProteinModelPortali Q9GK11.
SMRi Q9GK11. Positions 59-381.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi A01.006.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000482.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of recombinant camel chymosin reveals superior properties for the coagulation of bovine and camel milk."
    Kappeler S.R., van den Brink H.J., Rahbek-Nielsen H., Farah Z., Puhan Z., Hansen E.B., Johansen E.
    Biochem. Biophys. Res. Commun. 342:647-654(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Stomach mucosaImported.
  2. "Camel and bovine chymosin: the relationship between their structures and cheese-making properties."
    Langholm Jensen J., Molgaard A., Navarro Poulsen J.C., Harboe M.K., Simonsen J.B., Lorentzen A.M., Hjerno K., van den Brink J.M., Qvist K.B., Larsen S.
    Acta Crystallogr. D 69:901-913(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 62-381, GLYCOSYLATION AT ASN-158.

Entry informationi

Entry nameiQ9GK11_CAMDR
AccessioniPrimary (citable) accession number: Q9GK11
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3