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Protein

Pheromone-processing carboxypeptidase KEX1

Gene

KEX1

Organism
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity).By similarity

Catalytic activityi

Preferential release of a C-terminal arginine or lysine residue.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791By similarity
Active sitei381 – 3811By similarity
Active sitei445 – 4451By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Keywords - Biological processi

Apoptosis

Protein family/group databases

ESTHERiashgo-q752m5. Carboxypeptidase_S10.
MEROPSiS10.007.

Names & Taxonomyi

Protein namesi
Recommended name:
Pheromone-processing carboxypeptidase KEX1 (EC:3.4.16.6)
Alternative name(s):
Carboxypeptidase D
Gene namesi
Name:KEX1
Ordered Locus Names:AFR549W
OrganismiAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
Taxonomic identifieri284811 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium
ProteomesiUP000000591 Componenti: Chromosome VI

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 512493LumenalSequence AnalysisAdd
BLAST
Transmembranei513 – 53321HelicalSequence AnalysisAdd
BLAST
Topological domaini534 – 59966CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 599580Pheromone-processing carboxypeptidase KEX1PRO_0000411901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi33169.AAS53920.

Structurei

3D structure databases

ProteinModelPortaliQ752M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000208879.
InParanoidiQ752M5.
KOiK01288.
OMAiWVECKSA.
OrthoDBiEOG7TJ3SJ.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q752M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVRKLTLIG AALARAALAL QQEDFVVNGE LLPGVREIDR AEVPEMHAGL
60 70 80 90 100
MPLEEDEDGR ALFFWRMGEQ CGKRCSNELI VWLNGGPGCS SMDGALMETG
110 120 130 140 150
AFRVAEDGKL YLNSGSWHTR GTMLFVDQPV GTGFSRPGRD GRLRTELSQL
160 170 180 190 200
ADDFLLFMER YYAVFPEDRR RTLVLAGESY AGQYLPYFAD AVVRRNAERA
210 220 230 240 250
PEERYKLQNV MIGNGWVDPD LQSLSYVPFV SSRGLFGPET RNFQDILRDQ
260 270 280 290 300
EACQNAINHG PAKGFSHPEC EGILPKLLSS IPGPDRPVQQ CINMYDIRLR
310 320 330 340 350
DVFPSCGMNW PADLPNVHKF FGTPGVLEAL HVDPQVAGPW VECKSAVSEA
360 370 380 390 400
LVNAHSRPSV HLIPGLIEAG VKFVFFNGDQ DVICNNMGVE MLIAELRWRG
410 420 430 440 450
HMGFSNATEN FDWYHSDADA KTLVAAGVVK RDGPVTFISV FNASHMVPFD
460 470 480 490 500
VPRISRGIID IERSATILGV KGDSRMLITV DTEEDVTLST NAERNQQIRH
510 520 530 540 550
NQLKRLNGDT RKFTIAVFGL TISSIIGVIV YFSMRLHYGA KIRAILTNPK
560 570 580 590
SGTSSADDFS MDDEYTGTVM GDFHHGTHKK GQYYAVPDTD ISSSELHSV
Length:599
Mass (Da):66,497
Last modified:July 5, 2004 - v1
Checksum:i64D09A52E115AF6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016819 Genomic DNA. Translation: AAS53920.1.
RefSeqiNP_986096.1. NM_212232.1.

Genome annotation databases

EnsemblFungiiAAS53920; AAS53920; AGOS_AFR549W.
GeneIDi4622376.
KEGGiago:AGOS_AFR549W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016819 Genomic DNA. Translation: AAS53920.1.
RefSeqiNP_986096.1. NM_212232.1.

3D structure databases

ProteinModelPortaliQ752M5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi33169.AAS53920.

Protein family/group databases

ESTHERiashgo-q752m5. Carboxypeptidase_S10.
MEROPSiS10.007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAS53920; AAS53920; AGOS_AFR549W.
GeneIDi4622376.
KEGGiago:AGOS_AFR549W.

Phylogenomic databases

HOGENOMiHOG000208879.
InParanoidiQ752M5.
KOiK01288.
OMAiWVECKSA.
OrthoDBiEOG7TJ3SJ.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00560. CARBOXYPEPT_SER_HIS. 1 hit.
PS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
    Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
    Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
  2. "Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
    Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
    G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Entry informationi

Entry nameiKEX1_ASHGO
AccessioniPrimary (citable) accession number: Q752M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 72 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.