C0SGX7

PR
Gene name
CPYA (PABG_06849)
Protein name
Carboxypeptidase Y homolog A
Names
Species
Paracoccidioides brasiliensis (strain Pb03)
KEGG Pathway
EC number
3.4.16.5: Serine-type carboxypeptidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-121 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for C0SGX7

Entry ID Method Resolution Chain Position Source
AF-C0SGX7-F1 Predicted AlphaFoldDB

No variants for C0SGX7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C0SGX7

No associated diseases with C0SGX7

2 regional properties for C0SGX7

Type Name Position InterPro Accession
domain Propeptide, carboxypeptidase Y 1 - 101 IPR008442
active_site Serine carboxypeptidase, serine active site 265 - 272 IPR018202

Functions

Description
EC Number 3.4.16.5 Serine-type carboxypeptidases
Subcellular Localization
  • Vacuole
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
vacuole A closed structure, found only in eukaryotic cells, that is completely surrounded by unit membrane and contains liquid material. Cells contain one or several vacuoles, that may have different functions from each other. Vacuoles have a diverse array of functions. They can act as a storage organelle for nutrients or waste products, as a degradative compartment, as a cost-effective way of increasing cell size, and as a homeostatic regulator controlling both turgor pressure and pH of the cytosol.

1 GO annotations of molecular function

Name Definition
serine-type carboxypeptidase activity Catalysis of the hydrolysis of a single C-terminal amino acid residue from the C-terminus of a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).

1 GO annotations of biological process

Name Definition
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKSLVLGLLV GSAIASGPLQ HVLHAPPDPE PKPEPEPQVV KDPFEELRDT FDRLRNKAGD
70 80 90 100 110 120
IWDDVMDNIP NIMSNMRPLT IPAKKFTRRP DSEWTHIVRG ADLEALWVDD ESGYKHRKID
130 140 150 160 170 180
GKLAQYDLRI KAVDPSDLGI DKVKQYSGYL DDNANDKHLF FWFFESRNDP FGDPVVLWLN
190 200 210 220 230 240
GGPGCSSLTG MFFELGPASI DENITANYNP YSWNSNSSII FLDQPVNVGY SYSSQAVSDT
250 260 270 280 290 300
VTAAKDVYAL LTLFFTQFRQ YSAQDFHIAG ESYAGHYIPV FASEILHHNN TNINLQSVLI
310 320 330 340 350 360
GNGLTDPLSQ YPFYRPMACG DGGYPSVLDS QSCQSMDNAL PRCLSMIKSC YDIESTFTCL
370 380 390 400 410 420
PASIYCNNAL IGPYQKTGRN PYDVRTNCTG NDLCYPQLNY ITEYLNKPHV MRSLGVEVDS
430 440 450 460 470 480
YESCNMDINR NFLFHGDWMK PYHRLVPSLL ARIPVLIYAG DADFICNWLG NKAWTEALEY
490 500 510 520 530 540
PGHAKFAEAP MENLTMINSQ GKNEVFGEVK SHSNLTFMRI FKAGHMTPFD SPQASLEFAN
SWLSGEWSEV