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Conserved domains on  [gi|578834645|ref|XP_006723346|]
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interferon-inducible GTPase 5 isoform X2 [Homo sapiens]

Protein Classification

P-loop containing Nucleoside Triphosphate Hydrolases and p47_IIGP_like domain-containing protein( domain architecture ID 13591049)

P-loop containing Nucleoside Triphosphate Hydrolases and p47_IIGP_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 54-250 9.52e-120

p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment.


:

Pssm-ID: 206690  Cd Length: 197  Bit Score: 347.78  E-value: 9.52e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  54 RLEVGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPHPQFPDVTLWDLPGAGSPGCPADKYLKQVDFSR 133
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 134 YDFFLLVSPRRCGAVETRLAAEILCQGKKFYFVRTKVDEDLAATRTQRPSGFREAAVLQEIRDHCAERLREAGVADPRIF 213
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578834645 214 LVSNLSPARYDFPTLVSTWEHDLPSHRRHAGLLSLPD 250
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
RsgA_GTPase super family cl38114
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 12-76 1.24e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


The actual alignment was detected with superfamily member pfam03193:

Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578834645   12 EEENTILMAKERLEAL--RTAFESGDLPQAASHLQELLASTESIrlevgVTGESGAGKSSLINALRG 76
Cdd:pfam03193  67 DEEEELEELLKIYRAIgyPVLFVSAKTGEGIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
 
Name Accession Description Interval E-value
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 54-250 9.52e-120

p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment.


Pssm-ID: 206690  Cd Length: 197  Bit Score: 347.78  E-value: 9.52e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  54 RLEVGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPHPQFPDVTLWDLPGAGSPGCPADKYLKQVDFSR 133
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 134 YDFFLLVSPRRCGAVETRLAAEILCQGKKFYFVRTKVDEDLAATRTQRPSGFREAAVLQEIRDHCAERLREAGVADPRIF 213
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578834645 214 LVSNLSPARYDFPTLVSTWEHDLPSHRRHAGLLSLPD 250
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 22-403 4.09e-105

Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a role in in intracellular defence. IIGP is predominantly associated with the Golgi apparatus and also localizes to the endoplasmic reticulum and exerts a distinct role in IFN-induced intracellular membrane trafficking or processing.


Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 317.50  E-value: 4.09e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645   22 ERLEALRTAFESGDLPQAASHLQELLASTESIRLEVGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPH 101
Cdd:pfam05049   3 EVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPYSH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  102 PQFPDVTLWDLPGAGSPGCPADKYLKQVDFSRYDFFLLVSPRRCGAVETRLAAEILCQGKKFYFVRTKVDEDLAATRTQR 181
Cdd:pfam05049  83 PHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQKGK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  182 PSGFREAAVLQEIRDHCAERLREAGVADPRIFLVSNLSPARYDFPTLVSTWEHDLPSHRRHAGLLSLPDISLEALQKKKA 261
Cdd:pfam05049 163 PQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKKRQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  262 MLQEQVLKTALVLGVIQALPVPGLAAAYDDALLIHSLRGYHRSFGLDDDSLAKLAEQVGKQAGDLRSVIRSP-LANEVSP 340
Cdd:pfam05049 243 SLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPaFFKLTKD 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578834645  341 ETVLRLysqssdgAMRVARAFERgipVFGTLVAGGISFGAVYTMLQGCLNEMAEDAQRVRIKA 403
Cdd:pfam05049 323 DSILAR-------LTRYINAFCR---VLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
YeeP COG3596
Predicted GTPase [General function prediction only];
20-294 1.01e-14

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 74.80  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  20 AKERLEALrTAFESGDLPQAASHLQELLAstESIRLEVGVTGESGAGKSSLINALRGLEAEDPGAALTgvmeTTMQPSPY 99
Cdd:COG3596    8 LTERLEAL-KRLPQVLRELLAEALERLLV--ELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRP----CTREIQRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 100 --PHPQFPDVTLWDLPGAGSPGCPADKYLKQVDFS-RYDFFLLVSP--RRCGAVETRLAAEIL--CQGKKFYFVRTKVDE 172
Cdd:COG3596   81 rlESDGLPGLVLLDTPGLGEVNERDREYRELRELLpEADLILWVVKadDRALATDEEFLQALRaqYPDPPVLVVLTQVDR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 173 DLAATRTQRPSGFREAAVLQEIRDHCAERLREAGVADPRIFLVS-NLSPARYDFPTLVSTWEHDLPSHRRH--AGLLSLP 249
Cdd:COG3596  161 LEPEREWDPPYNWPSPPKEQNIRRALEAIAEQLGVPIDRVIPVSaAEDRTGYGLEELVDALAEALPEAKRSrlARLLRAK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578834645 250 DISLEALQKKKAMLQEQVLKTALVLGVIQALPVPGLAAAYDDALL 294
Cdd:COG3596  241 AIDRYTLLAAAAALLAAALLALLALLLAALAAAPVALAGLGPAAL 285
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 12-76 1.24e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578834645   12 EEENTILMAKERLEAL--RTAFESGDLPQAASHLQELLASTESIrlevgVTGESGAGKSSLINALRG 76
Cdd:pfam03193  67 DEEEELEELLKIYRAIgyPVLFVSAKTGEGIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
TIGR00157 TIGR00157
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ...
 19-74 1.53e-03

ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]


Pssm-ID: 272934 [Multi-domain]  Cd Length: 245  Bit Score: 40.09  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578834645   19 MAKERLEALR--------TAFESGDLPqaaSHLQELLASTESIrlevgVTGESGAGKSSLINAL 74
Cdd:TIGR00157  85 MEKEQLDIYRnigyqvlmTSSKNQDGL---KELIEALQNRISV-----FAGQSGVGKSSLINAL 140
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 29-74 1.54e-03

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 40.25  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578834645  29 TAFESGDlPQAASHLQELLAST-----ESIRleVGVTGESGAGKSSLINAL 74
Cdd:cd03114   19 TLVESGR-PDHRELAQELLDALlpqagRAFR--VGITGPPGAGKSTLIEAL 66
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
38-88 7.14e-03

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 38.26  E-value: 7.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578834645  38 QAASHLQELLAST-ESIRleVGVTGESGAGKSSLINAL------RGLE----AEDPGAALTG 88
Cdd:PRK09435  41 LAQELLDALLPHTgNALR--IGITGVPGVGKSTFIEALgmhlieQGHKvavlAVDPSSTRTG 100
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 57-82 8.31e-03

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 38.63  E-value: 8.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 578834645   57 VGVTGESGAGKSSLINALRGLEAEDP 82
Cdd:TIGR03269  29 LGILGRSGAGKSVLMHVLRGMDQYEP 54
 
Name Accession Description Interval E-value
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 54-250 9.52e-120

p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase family consists of several highly homologous proteins, including IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1. They are found in higher eukaryotes where they play a role in immune resistance against intracellular pathogens. p47 proteins exist at low resting levels in mouse cells, but are strongly induced by Type II interferon (IFN-gamma). ITGP is critical for resistance to Toxoplasma gondii infection and in involved in inhibition of Coxsackievirus-B3-induced apoptosis. TGTP was shown to limit vesicular stomatitis virus (VSV) infection of fibroblasts in vitro. IRG-47 is involved in resistance to T. gondii infection. LRG-47 has been implicated in resistance to T. gondii, Listeria monocytogenes, Leishmania, and mycobacterial infections. IIGP1 has been shown to localize to the ER and to the Golgi membranes in IFN-induced cells and inflamed tissues. In macrophages, IIGP1 interacts with hook3, a microtubule binding protein that participates in the organization of the cis-Golgi compartment.


Pssm-ID: 206690  Cd Length: 197  Bit Score: 347.78  E-value: 9.52e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  54 RLEVGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPHPQFPDVTLWDLPGAGSPGCPADKYLKQVDFSR 133
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 134 YDFFLLVSPRRCGAVETRLAAEILCQGKKFYFVRTKVDEDLAATRTQRPSGFREAAVLQEIRDHCAERLREAGVADPRIF 213
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 578834645 214 LVSNLSPARYDFPTLVSTWEHDLPSHRRHAGLLSLPD 250
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 22-403 4.09e-105

Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a role in in intracellular defence. IIGP is predominantly associated with the Golgi apparatus and also localizes to the endoplasmic reticulum and exerts a distinct role in IFN-induced intracellular membrane trafficking or processing.


Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 317.50  E-value: 4.09e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645   22 ERLEALRTAFESGDLPQAASHLQELLASTESIRLEVGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPH 101
Cdd:pfam05049   3 EVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPYSH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  102 PQFPDVTLWDLPGAGSPGCPADKYLKQVDFSRYDFFLLVSPRRCGAVETRLAAEILCQGKKFYFVRTKVDEDLAATRTQR 181
Cdd:pfam05049  83 PHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQKGK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  182 PSGFREAAVLQEIRDHCAERLREAGVADPRIFLVSNLSPARYDFPTLVSTWEHDLPSHRRHAGLLSLPDISLEALQKKKA 261
Cdd:pfam05049 163 PQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKKRQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  262 MLQEQVLKTALVLGVIQALPVPGLAAAYDDALLIHSLRGYHRSFGLDDDSLAKLAEQVGKQAGDLRSVIRSP-LANEVSP 340
Cdd:pfam05049 243 SLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPaFFKLTKD 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578834645  341 ETVLRLysqssdgAMRVARAFERgipVFGTLVAGGISFGAVYTMLQGCLNEMAEDAQRVRIKA 403
Cdd:pfam05049 323 DSILAR-------LTRYINAFCR---VLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
YeeP COG3596
Predicted GTPase [General function prediction only];
20-294 1.01e-14

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 74.80  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  20 AKERLEALrTAFESGDLPQAASHLQELLAstESIRLEVGVTGESGAGKSSLINALRGLEAEDPGAALTgvmeTTMQPSPY 99
Cdd:COG3596    8 LTERLEAL-KRLPQVLRELLAEALERLLV--ELPPPVIALVGKTGAGKSSLINALFGAEVAEVGVGRP----CTREIQRY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 100 --PHPQFPDVTLWDLPGAGSPGCPADKYLKQVDFS-RYDFFLLVSP--RRCGAVETRLAAEIL--CQGKKFYFVRTKVDE 172
Cdd:COG3596   81 rlESDGLPGLVLLDTPGLGEVNERDREYRELRELLpEADLILWVVKadDRALATDEEFLQALRaqYPDPPVLVVLTQVDR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 173 DLAATRTQRPSGFREAAVLQEIRDHCAERLREAGVADPRIFLVS-NLSPARYDFPTLVSTWEHDLPSHRRH--AGLLSLP 249
Cdd:COG3596  161 LEPEREWDPPYNWPSPPKEQNIRRALEAIAEQLGVPIDRVIPVSaAEDRTGYGLEELVDALAEALPEAKRSrlARLLRAK 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578834645 250 DISLEALQKKKAMLQEQVLKTALVLGVIQALPVPGLAAAYDDALL 294
Cdd:COG3596  241 AIDRYTLLAAAAALLAAALLALLALLLAALAAAPVALAGLGPAAL 285
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 58-219 1.13e-10

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 59.78  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  58 GVTGESGAGKSSLINALRGleaeDPGAALTGVMETTMQPSPYP---HPQFPDVTLWDLPGAGSPGCPADKYLKQVDFSRY 134
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLG----GEVGEVSDVPGTTRDPDVYVkelDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645 135 DFFLLV----SPRRCGAVETRLAAEILCQGKKFYFVRTKVDEdlaatrtqrpsgfreaaVLQEIRDHCAERLREAGVADP 210
Cdd:cd00882   77 DLILLVvdstDRESEEDAKLLILRRLRKEGIPIILVGNKIDL-----------------LEEREVEELLRLEELAKILGV 139


                 ....*....
gi 578834645 211 RIFLVSNLS 219
Cdd:cd00882  140 PVFEVSAKT 148
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 58-175 4.67e-08

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.


Pssm-ID: 206743 [Multi-domain]  Cd Length: 140  Bit Score: 51.96  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  58 GVTGESGAGKSSLINALRGLEaedpGAALTGVMETTMQPSPYP-HPQFPDVTLWDLPGAGSPGCPADKYLKQVD--FSRY 134
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTE----VAAVGDRRPTTRAAQAYVwQTGGDGLVLLDLPGVGERGRRDREYEELYRrlLPEA 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 578834645 135 DFFLLVSP---RRCGAVETRLAAEILCQGKKFYFVRTKVDEDLA 175
Cdd:cd11383   77 DLVLWLLDaddRALAADHDFYLLPLAGHDAPLLFVLNQVDPVLA 120
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 56-114 2.11e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 40.68  E-value: 2.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578834645   56 EVGVTGESGAGKSSLINALRGLEAE---DPGaaltgvmeTTMQPSPYP-HPQFPDVTLWDLPG 114
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIvsdYPG--------TTRDPNEGRlELKGKQIILVDTPG 55
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 57-111 5.02e-04

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 40.32  E-value: 5.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578834645   57 VGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPH------PQ----FPDVTLWD 111
Cdd:pfam00005  14 LALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRkeigyvFQdpqlFPRLTVRE 78
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
 35-117 5.15e-04

Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, recombination and repair];


Pssm-ID: 440463 [Multi-domain]  Cd Length: 582  Bit Score: 42.31  E-value: 5.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834645  35 DLPQAASHLQELLASTESIRLEVGVTGESGAGKSSLINALRGLEAEDPGAAltgvmETTMQPSPYPHPQFPDVTLwdLPG 114
Cdd:COG0699   13 DRADLRRRLDQARLDLADPSLRIVMAGTTSQGKSQLVNALLGRRLLPSGAG-----ETTGVPTEIKHAEGSSARL--LPT 85


                 ...
gi 578834645 115 AGS 117
Cdd:COG0699   86 AGS 88
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 12-76 1.24e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578834645   12 EEENTILMAKERLEAL--RTAFESGDLPQAASHLQELLASTESIrlevgVTGESGAGKSSLINALRG 76
Cdd:pfam03193  67 DEEEELEELLKIYRAIgyPVLFVSAKTGEGIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
TIGR00157 TIGR00157
ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and ...
 19-74 1.53e-03

ribosome small subunit-dependent GTPase A; Members of this protein were designated YjeQ and are now designated RsgA (ribosome small subunit-dependent GTPase A). The strongest motif in the alignment of these proteins is GXSGVGKS[ST], a classic P-loop for nucleotide binding. This protein has been shown to cleave GTP and remain bound to GDP. A role as a regulator of translation has been suggested. The Aquifex aeolicus ortholog is split into consecutive open reading frames. Consequently, this model was build in fragment mode (-f option). [Protein synthesis, Translation factors]


Pssm-ID: 272934 [Multi-domain]  Cd Length: 245  Bit Score: 40.09  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578834645   19 MAKERLEALR--------TAFESGDLPqaaSHLQELLASTESIrlevgVTGESGAGKSSLINAL 74
Cdd:TIGR00157  85 MEKEQLDIYRnigyqvlmTSSKNQDGL---KELIEALQNRISV-----FAGQSGVGKSSLINAL 140
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 29-74 1.54e-03

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 40.25  E-value: 1.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578834645  29 TAFESGDlPQAASHLQELLAST-----ESIRleVGVTGESGAGKSSLINAL 74
Cdd:cd03114   19 TLVESGR-PDHRELAQELLDALlpqagRAFR--VGITGPPGAGKSTLIEAL 66
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
53-114 4.10e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 38.04  E-value: 4.10e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578834645  53 IRLEVGVTGESGAGKSSLINALRGLE-AEDPGAALTGV--METTMQPSPYPhpqfPDVTLWDLPG 114
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRLVGDIfSLEKYLSTNGVtiDKKELKLDGLD----VDLVIWDTPG 62
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 57-83 4.52e-03

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 38.63  E-value: 4.52e-03
                         10        20
                 ....*....|....*....|....*..
gi 578834645  57 VGVTGESGAGKSSLINALRGLEAEDPG 83
Cdd:COG1124   34 FGLVGESGSGKSTLLRALAGLERPWSG 60
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 57-100 5.23e-03

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 38.24  E-value: 5.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 578834645  57 VGVTGESGAGKSSLINALRGLEAEDPGA-ALTGVMETTMQPSPYP 100
Cdd:cd03298   27 TAIVGPSGSGKSTLLNLIAGFETPQSGRvLINGVDVTAAPPADRP 71
PRK09435 PRK09435
methylmalonyl Co-A mutase-associated GTPase MeaB;
38-88 7.14e-03

methylmalonyl Co-A mutase-associated GTPase MeaB;


Pssm-ID: 236515  Cd Length: 332  Bit Score: 38.26  E-value: 7.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578834645  38 QAASHLQELLAST-ESIRleVGVTGESGAGKSSLINAL------RGLE----AEDPGAALTG 88
Cdd:PRK09435  41 LAQELLDALLPHTgNALR--IGITGVPGVGKSTFIEALgmhlieQGHKvavlAVDPSSTRTG 100
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 57-82 8.31e-03

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 38.63  E-value: 8.31e-03
                          10        20
                  ....*....|....*....|....*.
gi 578834645   57 VGVTGESGAGKSSLINALRGLEAEDP 82
Cdd:TIGR03269  29 LGILGRSGAGKSVLMHVLRGMDQYEP 54
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 59-76 8.75e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 37.38  E-value: 8.75e-03
                         10
                 ....*....|....*...
gi 578834645  59 VTGESGAGKSSLINALRG 76
Cdd:cd01854   90 LVGQSGVGKSTLLNALLP 107
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 57-83 9.62e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 37.49  E-value: 9.62e-03
                         10        20
                 ....*....|....*....|....*..
gi 578834645  57 VGVTGESGAGKSSLINALRGLEAEDPG 83
Cdd:cd03257   34 LGLVGESGSGKSTLARAILGLLKPTSG 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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