Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for B9JCD8

Entry ID Method Resolution Chain Position Source
AF-B9JCD8-F1 Predicted AlphaFoldDB

No variants for B9JCD8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B9JCD8

No associated diseases with B9JCD8

2 regional properties for B9JCD8

Type Name Position InterPro Accession
domain Peptidase M17, leucyl aminopeptidase, C-terminal 184 - 488 IPR000819
domain Peptidase M17, leucyl aminopeptidase, N-terminal 29 - 143 IPR008283

Functions

Description
EC Number 3.4.11.1 Aminopeptidases
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
manganese ion binding Binding to a manganese ion (Mn).
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
MSVKFEISFA KTVRLNGGLA ILLKDADSES PAGAAGADPA NVFAKAARIA RFTAKGLSSL
70 80 90 100 110 120
DIVAPEGSPV DRIIVIGTGR AKELNAHDWL KLGGAAAARI RNVEKAAIFI DLPGVQAGGK
130 140 150 160 170 180
AAADFALGML LRAYSFDTYK TKKGDDDDKN GAQKPVKVTI VTPDVAAAKK LFAASEAIAD
190 200 210 220 230 240
GVILARDLVN EPPNVLGPVE FAAKAKALEK LGVEVEILTE REMRRLGMGA LLGVAQGSVR
250 260 270 280 290 300
PPRLVIMQWK GGKAKEKPVA FIGKGVVFDT GGISIKPAAG MEDMKGDMGG AAAVTGLMHT
310 320 330 340 350 360
LAARGAKVNA IGVIGLVENM PDGNAQRPGD IVTSMSGQTI EIINTDAEGR LVLCDALWYT
370 380 390 400 410 420
NDRFKPQFMI NLATLTGAIL VALGNLQAGL FSNDDQLANQ LTAAGLVTNE RLWRMPLGKD
430 440 450 460 470 480
YDKMIDSKFA DMKNTGGRYA GSITAAQFLK RFVQETPWAH LDIAGTAMGS TLDEINQSWG
490
SGFGVRLLDE LVRENYES