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 B0XTJ7

Entry ID Method Resolution Chain Position Source
AF-B0XTJ7-F1 Predicted AlphaFoldDB

No variants for B0XTJ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0XTJ7

No associated diseases with B0XTJ7

2 regional properties for B0XTJ7

Type Name Position InterPro Accession
domain Peptidase M24 169 - 473 IPR000994
binding_site Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site 254 - 270 IPR018349

Functions

Description
EC Number 3.4.11.18 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
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.

2 GO annotations of biological process

Name Definition
protein initiator methionine removal The protein modification process in which the translation-initiating methionine or formylmethionine residue is removed from a protein.
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
MGSKSPEGHR QAPHASNCNE LKPANPDPQI SQNGSGSADL DRGVIGDDDD DEDAEENGVN
70 80 90 100 110 120
TETPNVGKLN QPPFPNLDQV HVTTTDGLCI TEKKKKRKKS NKKKKKTKSG ALPATELKQT
130 140 150 160 170 180
SPPRVLVSTL FPSEYPVGEL VPYDCTARTT DEELRYNSRL WDDDFLPDYR QAAEIHRQVR
190 200 210 220 230 240
QYAQKELIKP GATLLSIAEG IEDGVRALSG HQGLEPGDFF KAGMGFPTGL CLNHIAAHWT
250 260 270 280 290 300
PNPREKDVIL DKGDVLKVDF GVHVNGRIVD SAFTVAFDDK YDNLLTAVRE ATNTGIKHAG
310 320 330 340 350 360
VDARMSDIGA AIQEVMESYE VEIDGKVFPV KAIRNITGHD ILRYHIHGGK QIPFIKNNNQ
370 380 390 400 410 420
DKMEEGEVYA IETFGSTGRG FLDDDVGVYG YGRNENMSGA NLRLSSAKSL LKTIDASFGS
430 440 450 460 470 480
IVFSRRYLER LGVKNYLLGM KNLIDNGIVE CYSPLVDVKG SYTAQFEHTI LLHSGGKEVI
SRGDDY