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Conserved domains on  [gi|410991922|ref|NP_001258606|]
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interferon gamma inducible protein 47 [Mus musculus]

Protein Classification

p47_IIGP_like domain-containing protein( domain architecture ID 12060281)

p47_IIGP_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 40-414 0e+00

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: 641.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922   40 SPETLTGIHKALQEGNLSDVMIQIQKAISAAENAILEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPY 119
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  120 QHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANYDFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQK 199
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  200 AKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPNISDASIELK 279
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  280 KHFLREKIWLEALKSAAVSFIPFMTFFKGFDLPEQEQCLKDYRSYFGLDDQSIKEIAEKLGAPLADIKGELKCLDFWSLV 359
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 410991922  360 KDNSIIAQATSAAEAFCAVKGGPESSAFQALKVYYRRTQFLNIVVDDAKHLLRKI 414
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 40-414 0e+00

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: 641.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922   40 SPETLTGIHKALQEGNLSDVMIQIQKAISAAENAILEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPY 119
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  120 QHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANYDFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQK 199
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  200 AKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPNISDASIELK 279
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  280 KHFLREKIWLEALKSAAVSFIPFMTFFKGFDLPEQEQCLKDYRSYFGLDDQSIKEIAEKLGAPLADIKGELKCLDFWSLV 359
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 410991922  360 KDNSIIAQATSAAEAFCAVKGGPESSAFQALKVYYRRTQFLNIVVDDAKHLLRKI 414
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 75-270 2.20e-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: 348.16  E-value: 2.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  75 LEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPYQHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANY 154
Cdd:cd04104    2 LNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 155 DFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQKAKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFL 234
Cdd:cd04104   82 DFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVFL 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 410991922 235 ISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPN 270
Cdd:cd04104  162 VSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
YeeP COG3596
Predicted GTPase [General function prediction only];
62-297 8.24e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 59.78  E-value: 8.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  62 QIQKAISAAENAI--LEVAVIGQSGTGKSSFINALrgLGHEAdesADVGTVE-TTMCKTPY--QHPKYPKVIFWDLPGTG 136
Cdd:COG3596   25 LLAEALERLLVELppPVIALVGKTGAGKSSLINAL--FGAEV---AEVGVGRpCTREIQRYrlESDGLPGLVLLDTPGLG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 137 TPNfHAD----AYLDQVGFAnyDFFI-IISSSRF---SLNDALLAQKIKDAGKKFYFVRTKVD-----------SDLYNE 197
Cdd:COG3596  100 EVN-ERDreyrELRELLPEA--DLILwVVKADDRalaTDEEFLQALRAQYPDPPVLVVLTQVDrleperewdppYNWPSP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 198 QKAKPIAFKKEKVLQQIRDYCvtnliktgvtEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLpnisDASIE 277
Cdd:COG3596  177 PKEQNIRRALEAIAEQLGVPI----------DRVIPVSAAEDRTGYGLEELVDALAEALPEAKRSRLARLL----RAKAI 242

                        250       260
                 ....*....|....*....|
gi 410991922 278 LKKHFLREKIWLEALKSAAV 297
Cdd:COG3596  243 DRYTLLAAAAALLAAALLAL 262
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 71-94 9.55e-03

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 37.07  E-value: 9.55e-03
                          10        20
                  ....*....|....*....|....
gi 410991922   71 ENAILEVAVIGQSGTGKSSFINAL 94
Cdd:TIGR03598  15 PDDGPEIAFAGRSNVGKSSLINAL 38
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 40-414 0e+00

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: 641.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922   40 SPETLTGIHKALQEGNLSDVMIQIQKAISAAENAILEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPY 119
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  120 QHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANYDFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQK 199
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  200 AKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPNISDASIELK 279
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  280 KHFLREKIWLEALKSAAVSFIPFMTFFKGFDLPEQEQCLKDYRSYFGLDDQSIKEIAEKLGAPLADIKGELKCLDFWSLV 359
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 410991922  360 KDNSIIAQATSAAEAFCAVKGGPESSAFQALKVYYRRTQFLNIVVDDAKHLLRKI 414
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 75-270 2.20e-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: 348.16  E-value: 2.20e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  75 LEVAVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPYQHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANY 154
Cdd:cd04104    2 LNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 155 DFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQKAKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFL 234
Cdd:cd04104   82 DFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVFL 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 410991922 235 ISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPN 270
Cdd:cd04104  162 VSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 78-209 6.56e-12

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: 63.24  E-value: 6.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  78 AVIGQSGTGKSSFINALRGLGHEADESADVGTVETTMCKTPYQHPKYpKVIFWDLPGTGTPNFHADAYLDQVGFANYDFF 157
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEVSDVPGTTRDPDVYVKELDKGKV-KLVLVDTPGLDEFGGLGREELARLLLRGADLI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 410991922 158 III--SSSRFSLNDA--LLAQKIKDAGKKFYFVRTKVDSDLYNEQKAKPIAFKKEK 209
Cdd:cd00882   80 LLVvdSTDRESEEDAklLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLEELAK 135
YeeP COG3596
Predicted GTPase [General function prediction only];
62-297 8.24e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 59.78  E-value: 8.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  62 QIQKAISAAENAI--LEVAVIGQSGTGKSSFINALrgLGHEAdesADVGTVE-TTMCKTPY--QHPKYPKVIFWDLPGTG 136
Cdd:COG3596   25 LLAEALERLLVELppPVIALVGKTGAGKSSLINAL--FGAEV---AEVGVGRpCTREIQRYrlESDGLPGLVLLDTPGLG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 137 TPNfHAD----AYLDQVGFAnyDFFI-IISSSRF---SLNDALLAQKIKDAGKKFYFVRTKVD-----------SDLYNE 197
Cdd:COG3596  100 EVN-ERDreyrELRELLPEA--DLILwVVKADDRalaTDEEFLQALRAQYPDPPVLVVLTQVDrleperewdppYNWPSP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 198 QKAKPIAFKKEKVLQQIRDYCvtnliktgvtEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLpnisDASIE 277
Cdd:COG3596  177 PKEQNIRRALEAIAEQLGVPI----------DRVIPVSAAEDRTGYGLEELVDALAEALPEAKRSRLARLL----RAKAI 242

                        250       260
                 ....*....|....*....|
gi 410991922 278 LKKHFLREKIWLEALKSAAV 297
Cdd:COG3596  243 DRYTLLAAAAALLAAALLAL 262
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 76-189 1.26e-05

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: 44.15  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922   76 EVAVIGQSGTGKSSFINALrgLGHEADESADVGtveTTMCKTPYQ-HPKYPKVIFWDLPGT-GTPNFHADAYLDQVGFAN 153
Cdd:pfam01926   1 RVALVGRPNVGKSTLINAL--TGAKAIVSDYPG---TTRDPNEGRlELKGKQIILVDTPGLiEGASEGEGLGRAFLAIIE 75

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 410991922  154 YD--FFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTK 189
Cdd:pfam01926  76 ADliLFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
 55-127 1.16e-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: 44.24  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410991922  55 NLSDVMIQIQKAISAAENAILEVAVIGQSGTGKSSFINALRGLgheadESADVGTVETTMCKTPYQHPKYPKV 127
Cdd:COG0699   13 DRADLRRRLDQARLDLADPSLRIVMAGTTSQGKSQLVNALLGR-----RLLPSGAGETTGVPTEIKHAEGSSA 80
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
77-225 2.69e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.51  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  77 VAVIGQSGTGKSSFINALrgLGHEADESADVGTVETTMCKTPYQHPKY-PKVIFWDLPGT----GTPNFHADAYLDQVGF 151
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRL--VGDIFSLEKYLSTNGVTIDKKELKLDGLdVDLVIWDTPGQdefrETRQFYARQLTGASLY 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 410991922 152 AnydfFII---ISSSRFSLNdaLLAQKIKDAGKK--FYFVRTKvdSDLYNEQKAKPiafkKEKVLQQIRDYCVTNLIKT 225
Cdd:COG1100   84 L----FVVdgtREETLQSLY--ELLESLRRLGKKspIILVLNK--IDLYDEEEIED----EERLKEALSEDNIVEVVAT 150
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 77-256 6.87e-04

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 40.22  E-value: 6.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922  77 VAVIGQSGTGKSSFINALrgLGheaDESADVGTVETTMCKTpyqHPKY---PKVIFWDLPGTG-TPNFHAD---AYLDQV 149
Cdd:cd09912    3 LAVVGEFSAGKSTLLNAL--LG---EEVLPTGVTPTTAVIT---VLRYgllKGVVLVDTPGLNsTIEHHTEiteSFLPRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410991922 150 gfanyDFFIIISSSR--FSLNDALLAQKIKDA-GKKFYFVRTKVDsdlyneqkakpiAFKKEKVLQQIRDYCVTNLIKT- 225
Cdd:cd09912   75 -----DAVIFVLSADqpLTESEREFLKEILKWsGKKIFFVLNKID------------LLSEEELEEVLEYSREELGVLEl 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 410991922 226 GVTEPCIFLIS------------NLDLGAFDFPKLEETLLKEL 256
Cdd:cd09912  138 GGGEPRIFPVSakealearlqgdEELLEQSGFEELEEHLEEFL 180
FeoB_N pfam02421
Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) ...
 77-135 1.73e-03

Ferrous iron transport protein B; Escherichia coli has an iron(II) transport system (feo) which may make an important contribution to the iron supply of the cell under anaerobic conditions. FeoB has been identified as part of this transport system. FeoB is a large 700-800 amino acid integral membrane protein. The N terminus contains a P-loop motif suggesting that iron transport may be ATP dependent.


Pssm-ID: 460552 [Multi-domain]  Cd Length: 156  Bit Score: 38.59  E-value: 1.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410991922   77 VAVIGQSGTGKSSFINALRGLGHEadesadVG-----TVETTMCKTPYQHPKYpKVIfwDLPGT 135
Cdd:pfam02421   3 IALVGNPNVGKTTLFNALTGANQH------VGnwpgvTVEKKEGKFKYKGYEI-EIV--DLPGI 57
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 66-96 1.75e-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: 39.30  E-value: 1.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 410991922  66 AISAAENAILE----------VAVIGQSGTGKSSFINALRG 96
Cdd:cd01854   67 AVSAKTGEGLDelrellkgktSVLVGQSGVGKSTLLNALLP 107
Dynamin_N pfam00350
Dynamin family;
77-131 3.56e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 37.98  E-value: 3.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 410991922   77 VAVIGQSGTGKSSFINALrgLGHEADESadvGTVETTMC-------KTPYQHPKYPKVIFWD 131
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNAL--LGRDILPR---GPGPTTRRptvlrlgESPGASEGAVKVEYKD 57
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
77-110 4.39e-03

Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 38.94  E-value: 4.39e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 410991922  77 VAVIGQSGTGKSSFINALRGlgheaDESADVGTV 110
Cdd:COG1162  169 SVLVGQSGVGKSTLINALLP-----DADLATGEI 197
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 76-136 4.46e-03

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 37.88  E-value: 4.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 410991922  76 EVAVIGQSGTGKSSFINALRGLGHEADESadvgtvettmcKTP--YQHPKY----PKVIFWDLPGTG 136
Cdd:cd01876    1 EVAFAGRSNVGKSSLINALTNRKKLARTS-----------KTPgrTQLINFfnvgDKFRLVDLPGYG 56
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 77-96 5.92e-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: 37.52  E-value: 5.92e-03
                          10        20
                  ....*....|....*....|
gi 410991922   77 VAVIGQSGTGKSSFINALRG 96
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLP 128
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 77-134 6.61e-03

An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents archaeal GTPase typified by the protein MJ1464 from Methanococcus jannaschii. The members of this family show a circular permutation of the GTPase signature motifs so that C-terminal strands 5, 6, and 7 (strands 6 contain the NKxD motif) are relocated to the N terminus.


Pssm-ID: 206752 [Multi-domain]  Cd Length: 157  Bit Score: 37.30  E-value: 6.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 410991922  77 VAVIGQSGTGKSSFINALRGlGHEADESADVGTVETTmcKTPyQHPKYPKVI-FWDLPG 134
Cdd:cd01859  102 VGVVGYPKVGKSSIINALKG-RHSASTSPIPGSPGYT--KGI-QLVRIDSKIyLIDTPG 156
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 71-94 9.55e-03

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 37.07  E-value: 9.55e-03
                          10        20
                  ....*....|....*....|....
gi 410991922   71 ENAILEVAVIGQSGTGKSSFINAL 94
Cdd:TIGR03598  15 PDDGPEIAFAGRSNVGKSSLINAL 38
 
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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