P52718

PR
Gene name
pepF
Protein name
Serine-type carboxypeptidase F
Names
Proteinase F, CPD-II
Species
Aspergillus niger
KEGG Pathway
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

3-81 (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 P52718

Entry ID Method Resolution Chain Position Source
AF-P52718-F1 Predicted AlphaFoldDB

No variants for P52718

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P52718

No associated diseases with P52718

2 regional properties for P52718

Type Name Position InterPro Accession
active_site Serine carboxypeptidase, serine active site 207 - 214 IPR018202
active_site Serine carboxypeptidases, histidine active site 497 - 514 IPR033124

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

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
MLFRSLLSTA VLAVSLCTDN ASAAKHGRFG QKARDAMNIA KRSANAVKHS LKIPVEDYQF
70 80 90 100 110 120
LNNKTKPYRV ESLPDVHFDL GEMYSGLVPI EKGNVSRSLF FVFQPTIGEP VDEITIWLNG
130 140 150 160 170 180
GPGCSSLEAF LQENGRFVWQ PGTYQPVENP YSWVNLTNVL WVDQPVGTGF SLGVPTATSE
190 200 210 220 230 240
EEIAEDFVKF FKNWQQIFGI KNFKIYVTGE SYAGRYVPYI SAAFLDQNDT EHFNLKGALA
250 260 270 280 290 300
YDPCIGQFDY VQEEAPVVPF VQKNNALFNF NASFLAELES IHEQCGYKDF IDQYLVFPAS
310 320 330 340 350 360
GVQPPKAMNW SDPTCDVYDI VNNAVLDPNP CFNPYEINEM CPILWDVLGF PTEVDYLPAG
370 380 390 400 410 420
ASIYFDRADV KRAMHAPNIT WSECSVESVF VGGDGGPEQE GDYSANPIEH VLPQVIEGTN
430 440 450 460 470 480
RVLIGNGDYD MVILTNGTLL SIQNMTWNGK LGFDTAPSTP INIDIPDLMY NEVFIENGYD
490 500 510 520 530
PQGGQGVMGI QHYERGLMWA ETFQSGHMQP QFQPRVSYRH LEWLLGRRDT L