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 A1CYM1

Entry ID Method Resolution Chain Position Source
AF-A1CYM1-F1 Predicted AlphaFoldDB

No variants for A1CYM1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1CYM1

No associated diseases with A1CYM1

2 regional properties for A1CYM1

Type Name Position InterPro Accession
domain Peptidase M24 146 - 450 IPR000994
binding_site Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site 231 - 247 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
MGSKSPEGHW QAPHASNSNE LKPANPDPQT SQNGSGSADL DRGVIGDDDD DDEDAEENGV
70 80 90 100 110 120
NTETPNVEKK KKRKKSNKKK KKKTKSGTLS VTELKQTSPP RVLVSTLFPS EYPVGELVPY
130 140 150 160 170 180
DCTTRTTDEE SRYNSRLWDD DFLPDYRQAA EIHRQVRQYA QKELIKPGAT LLSIAEGIED
190 200 210 220 230 240
GVRALSGHQG LEPGDFFKAG MGFPTGLCLN HIAAHWTPNP REKDVILDKG DVLKVDFGVH
250 260 270 280 290 300
VNGRIVDSAF TVAFDDKYDN LLTAVREATN TGIKHAGVDA RMSDIGAAIQ EVMESYEVEI
310 320 330 340 350 360
DGKVFPVKAI RNITGHDILR YHIHGGKQIP FIKNNNQDKM EEGEVYAIET FGSTGRGFLD
370 380 390 400 410 420
DDVGVYGYGR NENMSGANLR LSSAKSLLKT IDANFGSIVF SRRYLERLGV KNYLLGMKNL
430 440 450 460
VDNGIVECYS PLVDVKGSYT AQFEHTILLH SGGKEVISRG DDY