LeishMANIAdb
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Guanine nucleotide-binding protein subunit beta-like protein

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

Quick info

Protein:
Guanine nucleotide-binding protein subunit beta-like protein
Gene product:
WD domain - G-beta repeat/Utp13 specific WD40 associated domain containing protein - putative
Species:
Leishmania infantum
UniProt:
A4I186_LEIIN
TriTrypDb:
LINF_250009500
Length:
1017

Annotations

Annotations by Jardim et al.

RNA Processing, Uncharacterized

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:0005730 nucleolus 5 12
GO:0005840 ribosome 5 12
GO:0030684 preribosome 3 12
GO:0030686 90S preribosome 4 1
GO:0032040 small-subunit processome 4 12
GO:0032991 protein-containing complex 1 12
GO:0043226 organelle 2 12
GO:0043228 non-membrane-bounded organelle 3 12
GO:0043229 intracellular organelle 3 12
GO:0043232 intracellular non-membrane-bounded organelle 4 12
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Phosphorylation

Promastigote: 99

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

A4I186
Sequence
MSA
Disorder
Secondary
Topology
Domains
SignalP
GPI
Phosphorylations
ELMs

Structure

Predicted structure by AlphaFold2

Related structures:

AlphaFold database: A4I186

Function

Biological processes
TermNameLevelCount
GO:0000469 cleavage involved in rRNA processing 7 1
GO:0000472 endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) 10 1
GO:0000478 endonucleolytic cleavage involved in rRNA processing 8 1
GO:0000479 endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) 9 1
GO:0000480 endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) 10 1
GO:0000966 RNA 5'-end processing 7 1
GO:0000967 rRNA 5'-end processing 9 1
GO:0006139 nucleobase-containing compound metabolic process 3 12
GO:0006364 rRNA processing 8 12
GO:0006396 RNA processing 6 12
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Molecular functions
TermNameLevelCount
GO:0003676 nucleic acid binding 3 1
GO:0003723 RNA binding 4 1
GO:0005488 binding 1 1
GO:0030515 snoRNA binding 5 1
GO:0034511 U3 snoRNA binding 6 1
GO:0097159 organic cyclic compound binding 2 1
GO:1901363 heterocyclic compound binding 2 1
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Putative motif mimicry

LeishmaniaFromToDomain/MotifScore
CLV_C14_Caspase3-7 159 163 PF00656 0.592
CLV_MEL_PAP_1 641 647 PF00089 0.348
CLV_NRD_NRD_1 1004 1006 PF00675 0.635
CLV_NRD_NRD_1 367 369 PF00675 0.310
CLV_NRD_NRD_1 379 381 PF00675 0.478
CLV_NRD_NRD_1 432 434 PF00675 0.386
CLV_NRD_NRD_1 466 468 PF00675 0.650
CLV_NRD_NRD_1 712 714 PF00675 0.203
CLV_NRD_NRD_1 856 858 PF00675 0.271
CLV_NRD_NRD_1 962 964 PF00675 0.354
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Homologs

ProteinTaxonomySequence identityCoverage
A0A0N0P7W8 Leptomonas seymouri 71% 100%
A0A0S4IPM0 Bodo saltans 41% 100%
A0A1X0P4G2 Trypanosomatidae 53% 100%
A0A3Q8IN66 Leishmania donovani 100% 100%
A0A3S5IS62 Trypanosoma rangeli 50% 100%
A4HDY5 Leishmania braziliensis 84% 100%
D0A5H1 Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972) 52% 100%
E9AXC0 Leishmania mexicana (strain MHOM/GT/2001/U1103) 92% 100%
Q05946 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) 25% 100%
Q12788 Homo sapiens 28% 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