E3QCU0

PR
Gene name
AMPP (GLRG_03822)
Protein name
Probable Xaa-Pro aminopeptidase P
Names
AMPP, Aminopeptidase P, Aminoacylproline aminopeptidase, Prolidase
Species
Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola)
KEGG Pathway
EC number
3.4.11.9: Aminopeptidases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

119-209 (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 E3QCU0

Entry ID Method Resolution Chain Position Source
AF-E3QCU0-F1 Predicted AlphaFoldDB

No variants for E3QCU0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for E3QCU0

No associated diseases with E3QCU0

5 regional properties for E3QCU0

Type Name Position InterPro Accession
domain Creatinase, N-terminal 9 - 144 IPR000587
domain Peptidase M24 326 - 544 IPR000994
conserved_site Peptidase M24B, X-Pro dipeptidase/aminopeptidase P, conserved site 484 - 496 IPR001131
domain Peptidase M24, C-terminal domain 555 - 617 IPR032416
domain Aminopeptidase P 326 - 552 IPR033740

Functions

Description
EC Number 3.4.11.9 Aminopeptidases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cellular anatomical entity A part of a cellular organism that is either an immaterial entity or a material entity with granularity above the level of a protein complex but below that of an anatomical system. Or, a substance produced by a cellular organism with granularity above the level of a protein complex.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
metalloaminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.

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
MERIDTTGRL SRLRELMKER NVDVYVIPSE DSHASEYIAG CDARREFISG FSGSAGCAVV
70 80 90 100 110 120
TLDKAALATD GRYFNQASKQ LDQNWLLLKQ GLQDVPTWQE WSAEQSAGGK VVGVDPELIT
130 140 150 160 170 180
GSIAKKLTEK VKRSGGSDLV PLDENLVDLV WAEARPARPK NPIKVLPEKF SGKDVKTKLK
190 200 210 220 230 240
ELRQELDRKN SRAFVVSMLD EIAWLFNLRG DDIPYNPVFF SYAIITSDSA TLYVDASKLG
250 260 270 280 290 300
EETRAYLADN DVCVKPYDIV FDSINTLRSS DTSCQTTSGV SSKRFMISTK ASWALKRSLG
310 320 330 340 350 360
GDSQVDEVRS PIGDSKAVKN KSEMAGMRAC HIRDGAALIE YFAWLEDQLV AKKVKLDEVQ
370 380 390 400 410 420
AADKLEQLRS KQKDYVGLSF DTISSTGANA AVIHYKPERG ACSIIDPTAI YLCDSGAQYL
430 440 450 460 470 480
DGTTDTTRTL HFGQPTEAEK LAYTLVLKGN IALDTAIFPK GTTGFAIDCL ARQHLWKEGL
490 500 510 520 530 540
DYRHGTGHGV GSYLNVHEGP IGIGTRVQFA EVALAPGNVL SIEPGFYEDG SYGIRIENVA
550 560 570 580 590 600
MVTEVKTKHS FGDKPYLGFE HVTMVPYCRN LIEPNLLTAE EKAWLNAHHA DILQKTKGYF
610
QDDPLTMTWL ARETQPL