LeishMANIAdb
  • Home
  • Browse
  • Manual
  • FAQ
  • Download

Heat shock protein DNAJ, putative

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

Quick info

Protein:
Heat shock protein DNAJ, putative
Gene product:
heat shock protein DNAJ, putative
Species:
Leishmania donovani
UniProt:
A0A3Q8IC51_LEIDO
TriTrypDb:
LdBPK_220009.1 , LdCL_220005800 , LDHU3_22.0130
Length:
331

Annotations

LeishMANIAdb annotations

An extensive family in kinetoplastids, these chaperone proteins are likely also involved in the folding of secreted proteins as well.. This group contains both cytoplasmic and secreted (likely ER) proteins.. Localization: Cytoplasmic (by homology) / ER (by feature)

Localization

Secreted promastigote
Source Evidence on protein Close homologs
Cuervo et al. no yes: 0
Hassani et al. no yes: 0
Forrest at al. (metacyclic) no yes: 0
Forrest at al. (procyclic) no yes: 0
Silverman et al. no yes: 0
Pissara et al. no yes: 0
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: 0
Glycosome
Source Evidence on protein Close homologs
Jamdhade et al. no yes: 0
Predictions
Source Evidence on protein Close homologs
DeepLoc
SignalP6 no yes: 0, no: 11
NetGPI no yes: 0, no: 11
Cellular components
TermNameLevelCount
GO:0005654 nucleoplasm 2 1
GO:0005730 nucleolus 5 1
GO:0005737 cytoplasm 2 1
GO:0005829 cytosol 2 1
GO:0043226 organelle 2 1
GO:0043228 non-membrane-bounded organelle 3 1
GO:0043229 intracellular organelle 3 1
GO:0043232 intracellular non-membrane-bounded organelle 4 1
GO:0110165 cellular anatomical entity 1 1
Previous1Next

Expansion

Sequence features

A0A3Q8IC51
Sequence
MSA
Disorder
Secondary
Topology
Domains
SignalP
GPI
Phosphorylations
ELMs

Structure

Predicted structure by AlphaFold2

Related structures:

AlphaFold database: A0A3Q8IC51

Function

Biological processes
TermNameLevelCount
GO:0006457 protein folding 2 12
GO:0009987 cellular process 1 12
GO:0042026 protein refolding 3 1
Previous1Next
Molecular functions
TermNameLevelCount
GO:0005488 binding 1 12
GO:0005515 protein binding 2 12
GO:0030544 Hsp70 protein binding 4 12
GO:0031072 heat shock protein binding 3 12
GO:0043167 ion binding 2 11
GO:0043169 cation binding 3 11
GO:0046872 metal ion binding 4 11
GO:0051082 unfolded protein binding 3 12
GO:0051087 protein-folding chaperone binding 3 1
Previous1Next

Putative motif mimicry

LeishmaniaFromToDomain/MotifScore
CLV_C14_Caspase3-7 213 217 PF00656 0.313
CLV_NRD_NRD_1 33 35 PF00675 0.413
CLV_NRD_NRD_1 58 60 PF00675 0.401
CLV_NRD_NRD_1 75 77 PF00675 0.237
CLV_PCSK_FUR_1 31 35 PF00082 0.487
CLV_PCSK_KEX2_1 33 35 PF00082 0.417
CLV_PCSK_KEX2_1 60 62 PF00082 0.369
CLV_PCSK_KEX2_1 74 76 PF00082 0.214
CLV_PCSK_PC1ET2_1 60 62 PF00082 0.380
CLV_PCSK_PC1ET2_1 74 76 PF00082 0.284
Previous1234567Next

Homologs

ProteinTaxonomySequence identityCoverage
A0A0N1I0E7 Leptomonas seymouri 70% 93%
A0A0N1I257 Leptomonas seymouri 29% 71%
A0A0N1I2U4 Leptomonas seymouri 34% 83%
A0A0N1IMD5 Leptomonas seymouri 32% 74%
A0A0N1P953 Leptomonas seymouri 26% 70%
A0A0N1PCG8 Leptomonas seymouri 32% 83%
A0A0N1PCJ3 Leptomonas seymouri 29% 68%
A0A0S4IL02 Bodo saltans 33% 80%
A0A0S4IM72 Bodo saltans 30% 72%
A0A0S4J3S5 Bodo saltans 35% 83%
Previous12345…56Next

Download

Download
LeishMANIAdb - Server version: v0.0.2. - Database version: v0.0.1. - ChangeLog - © 2022-2025 Protein Bioinformatics Research Group, Institute of Enzymology, RCNS