LeishMANIAdb
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Chaperonin HSP60, mitochondrial

Quick info Annotations Function or PPIs Localization Abundance Expansion Sequence features Structure Function Putative motif mimicry Homologs Download

Quick info

Protein:
Chaperonin HSP60, mitochondrial
Gene product:
chaperonin HSP60 - mitochondrial precursor
Species:
Leishmania infantum
UniProt:
A4IDH4_LEIIN
TriTrypDb:
LINF_360027100
Length:
566

Annotations

Annotations by Jardim et al.

Chaperone/Protein Folding, Chaperonin HSP60, mitochondrial

Localization

Secreted promastigote
Source Evidence on protein Close homologs
Cuervo et al. no yes: 1
Hassani et al. no yes: 1
Forrest at al. (metacyclic) no yes: 1
Forrest at al. (procyclic) no yes: 1
Silverman et al. no yes: 2
Pissara et al. yes yes: 8
Secreted amastigote
Source Evidence on protein Close homologs
Pires et al. no yes: 0
Exosome
Source Evidence on protein Close homologs
Silverman et al. no yes: 3
Glycosome
Source Evidence on protein Close homologs
Jamdhade et al. no yes: 6
Predictions
Source Evidence on protein Close homologs
DeepLoc
SignalP6 no yes: 0, no: 14
NetGPI no yes: 0, no: 14
Cellular components
TermNameLevelCount
GO:0005737 cytoplasm 2 2
GO:0005739 mitochondrion 5 2
GO:0005929 cilium 4 2
GO:0042995 cell projection 2 2
GO:0043226 organelle 2 2
GO:0043227 membrane-bounded organelle 3 2
GO:0043229 intracellular organelle 3 2
GO:0043231 intracellular membrane-bounded organelle 4 2
GO:0110165 cellular anatomical entity 1 2
GO:0120025 plasma membrane bounded cell projection 3 2
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Abundance

Amastigote (protein)
Source Evidence on protein Close homologs
Pescher et al. (upgregulation) no yes: 0
Promastigote and amastigote
Source Evidence on protein Close homologs
Lahav et al.
- mRNA
- Protein

Expansion

Sequence features

A4IDH4
Sequence
MSA
Disorder
Secondary
Topology
Domains
SignalP
GPI
Phosphorylations
ELMs

Structure

Predicted structure by AlphaFold2

Related structures:

AlphaFold database: A4IDH4

Function

Biological processes
TermNameLevelCount
GO:0006457 protein folding 2 15
GO:0009987 cellular process 1 15
GO:0042026 protein refolding 3 15
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Molecular functions
TermNameLevelCount
GO:0000166 nucleotide binding 3 15
GO:0005488 binding 1 15
GO:0005524 ATP binding 5 15
GO:0017076 purine nucleotide binding 4 15
GO:0030554 adenyl nucleotide binding 5 15
GO:0032553 ribonucleotide binding 3 15
GO:0032555 purine ribonucleotide binding 4 15
GO:0032559 adenyl ribonucleotide binding 5 15
GO:0035639 purine ribonucleoside triphosphate binding 4 15
GO:0036094 small molecule binding 2 15
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Putative motif mimicry

LeishmaniaFromToDomain/MotifScore
CLV_C14_Caspase3-7 183 187 PF00656 0.263
CLV_NRD_NRD_1 20 22 PF00675 0.470
CLV_PCSK_KEX2_1 124 126 PF00082 0.279
CLV_PCSK_KEX2_1 20 22 PF00082 0.470
CLV_PCSK_PC1ET2_1 124 126 PF00082 0.263
CLV_PCSK_SKI1_1 143 147 PF00082 0.283
CLV_PCSK_SKI1_1 153 157 PF00082 0.305
CLV_PCSK_SKI1_1 204 208 PF00082 0.406
CLV_PCSK_SKI1_1 25 29 PF00082 0.479
CLV_PCSK_SKI1_1 252 256 PF00082 0.288
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Homologs

ProteinTaxonomySequence identityCoverage
A0A0N1HUI9 Leptomonas seymouri 47% 100%
A0A0N1I104 Leptomonas seymouri 23% 99%
A0A0N1PDS3 Leptomonas seymouri 58% 95%
A0A0S4IN05 Bodo saltans 57% 96%
A0A0S4ITK5 Bodo saltans 46% 82%
A0A0S4J048 Bodo saltans 22% 99%
A0A0S4J2A3 Bodo saltans 22% 98%
A0A0S4J618 Bodo saltans 76% 100%
A0A1X0NUX8 Trypanosomatidae 57% 95%
A0A1X0P1I2 Trypanosomatidae 45% 100%
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LeishMANIAdb - Server version: v0.0.2. - Database version: v0.0.1. - ChangeLog - © 2022-2025 Protein Bioinformatics Research Group, Institute of Enzymology, RCNS