LeishMANIAdb
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Putative G-actin binding protein

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

Quick info

Protein:
Putative G-actin binding protein
Gene product:
twinfilin
Species:
Leishmania major
UniProt:
Q4Q2X1_LEIMA
TriTrypDb:
LmjF.34.2290 , LMJLV39_340027600 , LMJSD75_340028500
Length:
331

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
Term Name Level Count
GO:0005737 cytoplasm 2 2
GO:0005884 actin filament 6 2
GO:0032838 plasma membrane bounded cell projection cytoplasm 4 2
GO:0097014 ciliary plasm 5 2
GO:0099080 supramolecular complex 2 2
GO:0099081 supramolecular polymer 3 2
GO:0099512 supramolecular fiber 4 2
GO:0099513 polymeric cytoskeletal fiber 5 2
GO:0099568 cytoplasmic region 3 2
GO:0110165 cellular anatomical entity 1 12
GO:0005856 cytoskeleton 5 10
GO:0043226 organelle 2 10
GO:0043228 non-membrane-bounded organelle 3 10
GO:0043229 intracellular organelle 3 10
GO:0043232 intracellular non-membrane-bounded organelle 4 10

Expansion

Sequence features

Q4Q2X1
Sequence
MSA
Disorder
Secondary
Topology
Domains
SignalP
GPI
Phosphorylations
ELMs

Structure

Predicted structure by AlphaFold2

Related structures:

AlphaFold database: Q4Q2X1

Function

Biological processes
Term Name Level Count
GO:0007015 actin filament organization 5 2
GO:0008064 regulation of actin polymerization or depolymerization 6 12
GO:0008154 actin polymerization or depolymerization 6 2
GO:0009987 cellular process 1 12
GO:0010639 negative regulation of organelle organization 6 12
GO:0016043 cellular component organization 3 12
GO:0022411 cellular component disassembly 4 2
GO:0030042 actin filament depolymerization 7 2
GO:0030832 regulation of actin filament length 5 12
GO:0030833 regulation of actin filament polymerization 7 12
GO:0030834 regulation of actin filament depolymerization 7 2
GO:0030835 negative regulation of actin filament depolymerization 7 2
GO:0030837 negative regulation of actin filament polymerization 7 12
GO:0031333 negative regulation of protein-containing complex assembly 6 12
GO:0032271 regulation of protein polymerization 6 12
GO:0032272 negative regulation of protein polymerization 7 12
GO:0032507 maintenance of protein location in cell 3 2
GO:0032535 regulation of cellular component size 4 12
GO:0032956 regulation of actin cytoskeleton organization 5 12
GO:0032970 regulation of actin filament-based process 4 12
GO:0032984 protein-containing complex disassembly 5 2
GO:0033043 regulation of organelle organization 5 12
GO:0042989 sequestering of actin monomers 4 2
GO:0043242 negative regulation of protein-containing complex disassembly 6 2
GO:0043244 regulation of protein-containing complex disassembly 5 2
GO:0043254 regulation of protein-containing complex assembly 5 12
GO:0043933 protein-containing complex organization 4 2
GO:0044087 regulation of cellular component biogenesis 4 12
GO:0045185 maintenance of protein location 3 2
GO:0048519 negative regulation of biological process 3 12
GO:0048523 negative regulation of cellular process 4 12
GO:0050789 regulation of biological process 2 12
GO:0050794 regulation of cellular process 3 12
GO:0051016 barbed-end actin filament capping 9 2
GO:0051128 regulation of cellular component organization 4 12
GO:0051129 negative regulation of cellular component organization 5 12
GO:0051179 localization 1 2
GO:0051235 maintenance of location 2 2
GO:0051261 protein depolymerization 6 2
GO:0051493 regulation of cytoskeleton organization 6 12
GO:0051494 negative regulation of cytoskeleton organization 7 12
GO:0051651 maintenance of location in cell 2 2
GO:0051693 actin filament capping 8 2
GO:0065007 biological regulation 1 12
GO:0065008 regulation of biological quality 2 12
GO:0071840 cellular component organization or biogenesis 2 12
GO:0090066 regulation of anatomical structure size 3 12
GO:0097435 supramolecular fiber organization 4 2
GO:0110053 regulation of actin filament organization 6 12
GO:1901879 regulation of protein depolymerization 6 2
GO:1901880 negative regulation of protein depolymerization 7 2
GO:1902903 regulation of supramolecular fiber organization 5 12
GO:1902904 negative regulation of supramolecular fiber organization 6 12
Molecular functions
Term Name Level Count
GO:0003779 actin binding 4 12
GO:0003785 actin monomer binding 5 2
GO:0005488 binding 1 12
GO:0005515 protein binding 2 12
GO:0008092 cytoskeletal protein binding 3 12
GO:0044877 protein-containing complex binding 2 2
GO:0051015 actin filament binding 3 2

Putative motif mimicry

Leishmania From To Domain/Motif Score
CLV_NRD_NRD_1 307 309 PF00675 0.642
CLV_PCSK_KEX2_1 116 118 PF00082 0.556
CLV_PCSK_PC1ET2_1 116 118 PF00082 0.544
CLV_PCSK_SKI1_1 137 141 PF00082 0.546
CLV_PCSK_SKI1_1 218 222 PF00082 0.319
CLV_PCSK_SKI1_1 227 231 PF00082 0.322
CLV_PCSK_SKI1_1 296 300 PF00082 0.548
CLV_PCSK_SKI1_1 35 39 PF00082 0.497
CLV_PCSK_SKI1_1 60 64 PF00082 0.554
CLV_PCSK_SKI1_1 66 70 PF00082 0.534
DEG_Nend_Nbox_1 1 3 PF02207 0.525
DOC_MAPK_DCC_7 156 166 PF00069 0.607
DOC_PP2B_LxvP_1 40 43 PF13499 0.510
DOC_PP2B_PxIxI_1 254 260 PF00149 0.581
DOC_USP7_MATH_1 301 305 PF00917 0.570
DOC_USP7_MATH_1 44 48 PF00917 0.474
DOC_USP7_UBL2_3 35 39 PF12436 0.508
DOC_WW_Pin1_4 108 113 PF00397 0.553
DOC_WW_Pin1_4 232 237 PF00397 0.572
DOC_WW_Pin1_4 251 256 PF00397 0.374
LIG_14-3-3_CanoR_1 120 125 PF00244 0.492
LIG_14-3-3_CanoR_1 308 314 PF00244 0.664
LIG_14-3-3_CanoR_1 97 107 PF00244 0.501
LIG_BIR_III_2 223 227 PF00653 0.525
LIG_DCNL_PONY_1 1 4 PF03556 0.591
LIG_FHA_1 116 122 PF00498 0.508
LIG_FHA_1 191 197 PF00498 0.490
LIG_FHA_1 22 28 PF00498 0.491
LIG_FHA_1 286 292 PF00498 0.575
LIG_FHA_1 57 63 PF00498 0.453
LIG_FHA_1 79 85 PF00498 0.530
LIG_FHA_2 143 149 PF00498 0.449
LIG_FHA_2 173 179 PF00498 0.578
LIG_FHA_2 220 226 PF00498 0.581
LIG_FHA_2 288 294 PF00498 0.525
LIG_LIR_Gen_1 225 236 PF02991 0.549
LIG_LIR_Gen_1 69 79 PF02991 0.375
LIG_LIR_Gen_1 80 88 PF02991 0.354
LIG_LIR_Nem_3 225 231 PF02991 0.549
LIG_LIR_Nem_3 297 302 PF02991 0.586
LIG_LIR_Nem_3 69 75 PF02991 0.362
LIG_LIR_Nem_3 80 86 PF02991 0.355
LIG_SH2_PTP2 247 250 PF00017 0.501
LIG_SH2_PTP2 72 75 PF00017 0.502
LIG_SH2_PTP2 83 86 PF00017 0.516
LIG_SH2_STAP1 261 265 PF00017 0.562
LIG_SH2_STAP1 54 58 PF00017 0.434
LIG_SH2_STAT5 247 250 PF00017 0.487
LIG_SH2_STAT5 72 75 PF00017 0.497
LIG_SH2_STAT5 83 86 PF00017 0.403
LIG_SH2_STAT5 87 90 PF00017 0.351
LIG_SH3_3 161 167 PF00018 0.515
LIG_SH3_3 24 30 PF00018 0.542
LIG_SH3_3 245 251 PF00018 0.544
LIG_SUMO_SIM_par_1 29 34 PF11976 0.426
LIG_TRAF2_1 15 18 PF00917 0.462
LIG_TYR_ITSM 79 86 PF00017 0.452
LIG_WRC_WIRS_1 191 196 PF05994 0.581
MOD_CDK_SPK_2 232 237 PF00069 0.593
MOD_CDK_SPK_2 251 256 PF00069 0.407
MOD_CDK_SPxxK_3 251 258 PF00069 0.562
MOD_CK1_1 122 128 PF00069 0.496
MOD_CK1_1 219 225 PF00069 0.559
MOD_CK1_1 235 241 PF00069 0.471
MOD_CK1_1 89 95 PF00069 0.515
MOD_CK2_1 120 126 PF00069 0.474
MOD_CK2_1 127 133 PF00069 0.441
MOD_CK2_1 142 148 PF00069 0.383
MOD_CK2_1 294 300 PF00069 0.510
MOD_GlcNHglycan 17 21 PF01048 0.514
MOD_GlcNHglycan 263 266 PF01048 0.342
MOD_GlcNHglycan 296 299 PF01048 0.488
MOD_GlcNHglycan 303 306 PF01048 0.598
MOD_GlcNHglycan 92 95 PF01048 0.446
MOD_GSK3_1 115 122 PF00069 0.453
MOD_GSK3_1 313 320 PF00069 0.705
MOD_GSK3_1 74 81 PF00069 0.481
MOD_GSK3_1 86 93 PF00069 0.515
MOD_GSK3_1 98 105 PF00069 0.546
MOD_LATS_1 311 317 PF00433 0.518
MOD_N-GLC_1 56 61 PF02516 0.441
MOD_NEK2_1 16 21 PF00069 0.486
MOD_NEK2_1 203 208 PF00069 0.581
MOD_NEK2_1 56 61 PF00069 0.525
MOD_NEK2_1 98 103 PF00069 0.444
MOD_PIKK_1 179 185 PF00454 0.509
MOD_PIKK_1 235 241 PF00454 0.498
MOD_PIKK_1 78 84 PF00454 0.509
MOD_PK_1 120 126 PF00069 0.327
MOD_PKA_2 119 125 PF00069 0.486
MOD_PKA_2 307 313 PF00069 0.657
MOD_Plk_1 203 209 PF00069 0.502
MOD_Plk_4 127 133 PF00069 0.411
MOD_Plk_4 216 222 PF00069 0.526
MOD_Plk_4 325 331 PF00069 0.648
MOD_ProDKin_1 108 114 PF00069 0.556
MOD_ProDKin_1 232 238 PF00069 0.572
MOD_ProDKin_1 251 257 PF00069 0.374
MOD_SUMO_for_1 194 197 PF00179 0.539
MOD_SUMO_rev_2 130 139 PF00179 0.553
TRG_DiLeu_BaEn_1 36 41 PF01217 0.504
TRG_ENDOCYTIC_2 72 75 PF00928 0.457
TRG_ENDOCYTIC_2 83 86 PF00928 0.421

Homologs

Protein Taxonomy Sequence identity Coverage
A0A0N0P8Y3 Leptomonas seymouri 63% 100%
A0A0S4JJ86 Bodo saltans 26% 100%
A0A1X0P9W3 Trypanosomatidae 33% 97%
A0A3R7M8Y8 Trypanosoma rangeli 30% 100%
A0A3S7X7X8 Leishmania donovani 92% 100%
A4HAU1 Leishmania braziliensis 74% 100%
A4IA09 Leishmania infantum 92% 100%
C9ZMM6 Trypanosoma brucei gambiense (strain MHOM/CI/86/DAL972) 29% 100%
E9B515 Leishmania mexicana (strain MHOM/GT/2001/U1103) 88% 100%
V5BPY6 Trypanosoma cruzi 30% 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