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 Q6CLD3

Entry ID Method Resolution Chain Position Source
AF-Q6CLD3-F1 Predicted AlphaFoldDB

No variants for Q6CLD3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6CLD3

No associated diseases with Q6CLD3

3 regional properties for Q6CLD3

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 269 - 486 IPR014782
domain Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal 501 - 660 IPR015211
domain Aminopeptidase N-like, N-terminal domain 67 - 238 IPR045357

Functions

Description
EC Number 3.3.2.10 Ether hydrolases
Subcellular Localization
  • Cytoplasm
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

4 GO annotations of molecular function

Name Definition
aminopeptidase activity Catalysis of the hydrolysis of a single N-terminal amino acid residue from a polypeptide chain.
epoxide hydrolase activity Catalysis of the reaction: an epoxide + H2O = a glycol.
metallopeptidase activity Catalysis of the hydrolysis of peptide bonds 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.
zinc ion binding Binding to a zinc ion (Zn).

4 GO annotations of biological process

Name Definition
cellular lipid metabolic process The chemical reactions and pathways involving lipids, as carried out by individual cells.
peptide catabolic process The chemical reactions and pathways resulting in the breakdown of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
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
MLFNFYNKTS AACKSLPAKA LSNVRYFQTS PISRKMPLPP VLESRRPKES PEFDYSTLSN
70 80 90 100 110 120
YKSFKVKHSQ LDVSVDFKKK TISGSVSYEI EKVKKDENTI KLDTSYLKIS KVKVDDEDDV
130 140 150 160 170 180
KFKLLERKHP LGAQLIVSPS SLPEIFHLCL QFSTTADCTA LQWLDEHQTS GKPYVFSQLE
190 200 210 220 230 240
AIHARSLFTC FDTPSVKSTY LANIKSELPV VFSGIQTGYD DSTKVYSFKQ EVPIPAYLIG
250 260 270 280 290 300
IASGDLASAD IGPRSKVYVE PYRLKDAQWE FDGDVEKFIT TAEDIIFKYE WGTYDILVNP
310 320 330 340 350 360
NSYPYGGMES PNMTFATPTL IAHDKSNIDV IAHELAHSWS GNLVTNCSWD HFWLNEGWTV
370 380 390 400 410 420
YLERRITGAI HGEATRHFSS LIGWNDLEGS ISAMQNPERF SCLVQNLKDG TDPDNAFSTV
430 440 450 460 470 480
PYEKGSNLLF YLENLLGGKE VFDPFIKHYF TKFARQSLDT WQFLDALFEF FHDKREILES
490 500 510 520 530 540
VDWQTWLFTP GMPPKPKLIT DLADDVYALA NKWIASAQKF TEREQFEKEF SIKDISEFSS
550 560 570 580 590 600
NQIVLLLDTL VQGGMPEKDT FKWSNYPEAS EIFTDIYEDK ISKSQNAEVI FRNYRLQVKS
610 620 630 640 650 660
HITSSYPELA EWLGTVGRMK FVRPGYRLLN EVDRELAIKT FHRFRDSYHP ICKSLVKQDL
GI