LeishMANIAdb
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Co-chaperonin CPN10

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

Quick info

Protein:
Co-chaperonin CPN10
Gene product:
10 kDa heat shock protein, putative
Species:
Leishmania donovani
UniProt:
Q963A7_LEIDO
TriTrypDb:
LdBPK_260610.1 , LdCL_260011600 , LDHU3_26.0790 , LDHU3_26.0810
Length:
100

Annotations

Annotations by Jardim et al.

Chaperone/Protein Folding, 10 kDa heat shock

Localization

Secreted promastigote
Source Evidence on protein Close homologs
Cuervo et al. no yes: 0
Hassani et al. yes yes: 2
Forrest at al. (metacyclic) yes yes: 2
Forrest at al. (procyclic) no yes: 0
Silverman et al. no yes: 0
Pissara et al. yes yes: 18
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: 5
Glycosome
Source Evidence on protein Close homologs
Jamdhade et al. yes yes: 15
Predictions
Source Evidence on protein Close homologs
DeepLoc
SignalP6 no yes: 0, no: 14
NetGPI no yes: 0, no: 14
Cellular components
TermNameLevelCount
GO:0005759 mitochondrial matrix 5 2
GO:0031974 membrane-enclosed lumen 2 2
GO:0043233 organelle lumen 3 2
GO:0070013 intracellular organelle lumen 4 2
GO:0110165 cellular anatomical entity 1 2
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Expansion

Sequence features

Q963A7
Sequence
MSA
Disorder
Secondary
Topology
Domains
SignalP
GPI
Phosphorylations
ELMs

Structure

No structure information available for this entry

Related structures:

Function

Biological processes
TermNameLevelCount
GO:0006457 protein folding 2 2
GO:0006458 'de novo' protein folding 3 2
GO:0009987 cellular process 1 2
GO:0051084 'de novo' post-translational protein folding 4 2
GO:0051085 chaperone cofactor-dependent protein refolding 4 2
GO:0061077 chaperone-mediated protein folding 3 2
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Molecular functions
TermNameLevelCount
GO:0000166 nucleotide binding 3 15
GO:0005488 binding 1 15
GO:0005515 protein binding 2 2
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
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Putative motif mimicry

LeishmaniaFromToDomain/MotifScore
CLV_PCSK_KEX2_1 22 24 PF00082 0.327
CLV_PCSK_PC1ET2_1 22 24 PF00082 0.427
CLV_PCSK_PC7_1 18 24 PF00082 0.327
DEG_Nend_Nbox_1 1 3 PF02207 0.378
DOC_MAPK_gen_1 28 36 PF00069 0.527
DOC_MAPK_MEF2A_6 57 65 PF00069 0.551
DOC_MAPK_RevD_3 7 23 PF00069 0.402
DOC_PP4_FxxP_1 4 7 PF00568 0.483
DOC_SPAK_OSR1_1 3 7 PF12202 0.347
DOC_USP7_MATH_1 53 57 PF00917 0.570
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Homologs

ProteinTaxonomySequence identityCoverage
A0A0S4JFG4 Bodo saltans 81% 100%
A0A1X0NSW2 Trypanosomatidae 83% 100%
A0A1X0NU48 Trypanosomatidae 84% 100%
A0A3R7NAS6 Trypanosoma rangeli 80% 100%
A0A3R7NCP0 Trypanosoma rangeli 81% 100%
A0A3S7WZQ9 Leishmania donovani 99% 100%
A0AKH6 Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8) 33% 100%
A0PME8 Mycobacterium ulcerans (strain Agy99) 34% 100%
A0Q2T2 Clostridium novyi (strain NT) 37% 100%
A0Q839 Francisella tularensis subsp. novicida (strain U112) 38% 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