Q6FTM0

PR
Gene name
CAGL0G01430g
Protein name
Leucine aminopeptidase 2
Names
Epoxide hydrolase, Leukotriene A-4 hydrolase homolog, LTA-4 hydrolase
Species
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
KEGG Pathway
cgr:CAGL0G01430g
EC number
3.3.2.10: Ether hydrolases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-151 (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 Q6FTM0

Entry ID Method Resolution Chain Position Source
AF-Q6FTM0-F1 Predicted AlphaFoldDB

No variants for Q6FTM0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6FTM0

No associated diseases with Q6FTM0

3 regional properties for Q6FTM0

Type Name Position InterPro Accession
domain Peptidase M1, membrane alanine aminopeptidase 258 - 475 IPR014782
domain Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal 490 - 650 IPR015211
domain Aminopeptidase N-like, N-terminal domain 54 - 227 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

4 GO annotations of cellular component

Name Definition
fungal-type vacuole lumen The volume enclosed within the vacuolar membrane of a vacuole, the shape of which correlates with cell cycle phase. An example of this structure is found in Saccharomyces cerevisiae.
multivesicular body A type of endosome in which regions of the limiting endosomal membrane invaginate to form internal vesicles; membrane proteins that enter the internal vesicles are sequestered from the cytoplasm.
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.
NVT complex A protein complex that is capable of contributing to protein localization by the NVT pathway. In fission yeast, the Nvt complex consists of Ape2, Lap2 and Nbr1.

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).

5 GO annotations of biological process

Name Definition
cellular lipid metabolic process The chemical reactions and pathways involving lipids, as carried out by individual cells.
cytoplasm to vacuole transport by the NVT pathway A pathway targeting soluble cytosolic proteins to the vacuole lumen. It uses a selective autophagy receptor protein Nbr1, which is an ortholog of mammalian NBR1, and is remotely related to S. cerevisiae Cvt pathway receptor protein Atg19. Similar to the Cvt pathway, the cargos transported by this pathway are hydrolases, which presumably contribute to the hydrolytic activities in the vacuole lumen. Different from the Cvt pathway, this pathway does not require the macroautophagy machinery, but instead relies on the ESCRT machinery for cargo sequestration. This pathway is observed in the fission yeast S. pombe.
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
MINRLIQRIV PFSRPLSTVK KTMLTPFLES KRPQQSPEYD YSTLSNYKSF QIKHTTLNFL
70 80 90 100 110 120
LSFEKSTVSG DVVFDLTTLK EAVKHIDLDT SYLDVNEVLV DDKPVEFKIE ERKQPLGSKL
130 140 150 160 170 180
VIAAELEAER QFKLRVKFST TKDCTALQWL TPQQTSGDKP YMFSQLEAIH ARALFPCFDT
190 200 210 220 230 240
PSYKSTFTAN IESTLPVVFS GIATGSTPNG ESTVYHFKQD IPIPAYLVGI ASGDLVSASI
250 260 270 280 290 300
GPRSKVYTEP HRLDDCVWEF SNDVEKFIKT AENLIFDYEW GTYDILVNVD SYPYGGMESP
310 320 330 340 350 360
NMTFATPTLI AHDKTNIDVI AHELAHSWSG NLVTNCSWNH FWLNEGWTVY IERRIVGALH
370 380 390 400 410 420
GEPTRHFSAL IGWSDLENSI NSMRNPEKFS TLVQNLNDGT DPDDAFSTVP YEKGFNLLFH
430 440 450 460 470 480
LETVLGGPQE FDPFIRHYFK KFARQSLDTF QFLDTLFEFF ENKREILENV DWETWLFKPG
490 500 510 520 530 540
MPPKPQFITT MADNVFSLVN KWIVKAQELK TTEEFSKEFS ESDLSEFNSN QVVLFLEELV
550 560 570 580 590 600
AQNCVPVESK IEWSKYSVAS ESLLSIYKKQ VTESQNAEVV FKNYKFQTTA RIQPSYQQLA
610 620 630 640 650
NWLGTVGRMK FVRPGYRLLN AVDRDLAIAT FEKLKDTYHP ICKQLVKQDL EL