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Conserved domains on  [gi|184186090|ref|NP_001019401|]
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uncharacterized protein LOC432555 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IIGP super family cl27085
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 169-541 1.20e-180

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.


The actual alignment was detected with superfamily member pfam05049:

Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 513.57  E-value: 1.20e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  169 SEETITLIESHLEDKNLQGALSEISHALSNIDKAPLNIAVTGETGTGKSSFINALRGVRGEEEGAAPTGVVETTMKRTPY 248
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  249 PHPKLPNVTIWDLPGIGSTNFQPQNYLTEMKFGEYDFFIIISATRFKEIDAHLAKAIAKMNTKFYFVRTKIDQDVSNEQR 328
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  329 SKPKSFNRDSVLKKIRDDCSGHLQKVLSSQPPVFLVSNFDVSDFDFPKLENTLLRELPAHKRHLFMMSLHSVTETAIDRK 408
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  409 RDFLRQRIWLEALKAGVWTTIPLGGLVR-DKMQKLEETLTLYRSYFGLDEASLENIAKDFNVSVNEIKAHLRSLQLLTKN 487
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGdSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 184186090  488 NDMSFKEKLLKYIEYISCVTGGPLASGLYFRKTYYWQSLFIDTVASDAKSLLNK 541
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
IIGP super family cl27085
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 2-119 3.68e-24

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.


The actual alignment was detected with superfamily member pfam05049:

Pssm-ID: 461536 [Multi-domain]  Cd Length: 375  Bit Score: 104.49  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090    2 LKQKIWKESIMPRAWATIPSRG-LTQKDMEMLQQTLNDYRSSFGLDEASLENIAEDLNVTLEELKANIKSPHLLSDEPDT 80
Cdd:pfam05049 244 LKQKIWLEALKAAAVSIIPSLTfLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLTKDD 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 184186090   81 SLTEKLLKYIG------------NPYFSKVFHLQNYFIDTVASDVKIILSK 119
Cdd:pfam05049 324 SILARLTRYINafcrvlggplcvNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 169-541 1.20e-180

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: 513.57  E-value: 1.20e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  169 SEETITLIESHLEDKNLQGALSEISHALSNIDKAPLNIAVTGETGTGKSSFINALRGVRGEEEGAAPTGVVETTMKRTPY 248
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  249 PHPKLPNVTIWDLPGIGSTNFQPQNYLTEMKFGEYDFFIIISATRFKEIDAHLAKAIAKMNTKFYFVRTKIDQDVSNEQR 328
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  329 SKPKSFNRDSVLKKIRDDCSGHLQKVLSSQPPVFLVSNFDVSDFDFPKLENTLLRELPAHKRHLFMMSLHSVTETAIDRK 408
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  409 RDFLRQRIWLEALKAGVWTTIPLGGLVR-DKMQKLEETLTLYRSYFGLDEASLENIAKDFNVSVNEIKAHLRSLQLLTKN 487
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGdSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 184186090  488 NDMSFKEKLLKYIEYISCVTGGPLASGLYFRKTYYWQSLFIDTVASDAKSLLNK 541
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 203-399 2.08e-131

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: 381.29  E-value: 2.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 203 PLNIAVTGETGTGKSSFINALRGVRGEEEGAAPTGVVETTMKRTPYPHPKLPNVTIWDLPGIGSTNFQPQNYLTEMKFGE 282
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 283 YDFFIIISATRFKEIDAHLAKAIAKMNTKFYFVRTKIDQDVSNEQRSKPKSFNRDSVLKKIRDDCSGHLQKVLSSQPPVF 362
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 184186090 363 LVSNFDVSDFDFPKLENTLLRELPAHKRHLFMMSLHS 399
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 2-119 3.68e-24

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: 104.49  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090    2 LKQKIWKESIMPRAWATIPSRG-LTQKDMEMLQQTLNDYRSSFGLDEASLENIAEDLNVTLEELKANIKSPHLLSDEPDT 80
Cdd:pfam05049 244 LKQKIWLEALKAAAVSIIPSLTfLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLTKDD 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 184186090   81 SLTEKLLKYIG------------NPYFSKVFHLQNYFIDTVASDVKIILSK 119
Cdd:pfam05049 324 SILARLTRYINafcrvlggplcvNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
YeeP COG3596
Predicted GTPase [General function prediction only];
171-268 8.27e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 69.41  E-value: 8.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 171 ETITLIESHLEDKnlqgALSEISHALSNidKAPLNIAVTGETGTGKSSFINALRGvrgeeEGAAPTGVVE-TTMKRTPY- 248
Cdd:COG3596   13 EALKRLPQVLREL----LAEALERLLVE--LPPPVIALVGKTGAGKSSLINALFG-----AEVAEVGVGRpCTREIQRYr 81

                         90       100
                 ....*....|....*....|.
gi 184186090 249 -PHPKLPNVTIWDLPGIGSTN 268
Cdd:COG3596   82 lESDGLPGLVLLDTPGLGEVN 102
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 169-541 1.20e-180

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: 513.57  E-value: 1.20e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  169 SEETITLIESHLEDKNLQGALSEISHALSNIDKAPLNIAVTGETGTGKSSFINALRGVRGEEEGAAPTGVVETTMKRTPY 248
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  249 PHPKLPNVTIWDLPGIGSTNFQPQNYLTEMKFGEYDFFIIISATRFKEIDAHLAKAIAKMNTKFYFVRTKIDQDVSNEQR 328
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  329 SKPKSFNRDSVLKKIRDDCSGHLQKVLSSQPPVFLVSNFDVSDFDFPKLENTLLRELPAHKRHLFMMSLHSVTETAIDRK 408
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  409 RDFLRQRIWLEALKAGVWTTIPLGGLVR-DKMQKLEETLTLYRSYFGLDEASLENIAKDFNVSVNEIKAHLRSLQLLTKN 487
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGdSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 184186090  488 NDMSFKEKLLKYIEYISCVTGGPLASGLYFRKTYYWQSLFIDTVASDAKSLLNK 541
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 203-399 2.08e-131

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: 381.29  E-value: 2.08e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 203 PLNIAVTGETGTGKSSFINALRGVRGEEEGAAPTGVVETTMKRTPYPHPKLPNVTIWDLPGIGSTNFQPQNYLTEMKFGE 282
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 283 YDFFIIISATRFKEIDAHLAKAIAKMNTKFYFVRTKIDQDVSNEQRSKPKSFNRDSVLKKIRDDCSGHLQKVLSSQPPVF 362
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 184186090 363 LVSNFDVSDFDFPKLENTLLRELPAHKRHLFMMSLHS 399
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 2-119 3.68e-24

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: 104.49  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090    2 LKQKIWKESIMPRAWATIPSRG-LTQKDMEMLQQTLNDYRSSFGLDEASLENIAEDLNVTLEELKANIKSPHLLSDEPDT 80
Cdd:pfam05049 244 LKQKIWLEALKAAAVSIIPSLTfLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLTKDD 323

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 184186090   81 SLTEKLLKYIG------------NPYFSKVFHLQNYFIDTVASDVKIILSK 119
Cdd:pfam05049 324 SILARLTRYINafcrvlggplcvNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 207-373 1.08e-15

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: 74.80  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 207 AVTGETGTGKSSFINALRGvrgeEEGAAPTGVVETTMKRTPYP---HPKLPNVTIWDLPGIGSTNFQPQNYLTEMKFGEY 283
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLG----GEVGEVSDVPGTTRDPDVYVkelDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 284 DFFII-ISATR---FKEIDAHLAKAIAKMNTKFYFVRTKIDQDVSNEQRSKPKSFnrdsvlkkirddcsghlQKVLSSQP 359
Cdd:cd00882   77 DLILLvVDSTDresEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLRLE-----------------ELAKILGV 139

                        170
                 ....*....|....
gi 184186090 360 PVFLVSNFDVSDFD 373
Cdd:cd00882  140 PVFEVSAKTGEGVD 153
YeeP COG3596
Predicted GTPase [General function prediction only];
171-268 8.27e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 69.41  E-value: 8.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 171 ETITLIESHLEDKnlqgALSEISHALSNidKAPLNIAVTGETGTGKSSFINALRGvrgeeEGAAPTGVVE-TTMKRTPY- 248
Cdd:COG3596   13 EALKRLPQVLREL----LAEALERLLVE--LPPPVIALVGKTGAGKSSLINALFG-----AEVAEVGVGRpCTREIQRYr 81

                         90       100
                 ....*....|....*....|.
gi 184186090 249 -PHPKLPNVTIWDLPGIGSTN 268
Cdd:COG3596   82 lESDGLPGLVLLDTPGLGEVN 102
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 204-385 1.62e-08

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: 54.47  E-value: 1.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 204 LNIAVTGETGTGKSSFINALRGvrgeeEGAAPTGVVETTMKRTPYPHPKLPNVTIWDLPGIGSTNfQPQNYLTEMKFGEY 283
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALLG-----EEVLPTGVTPTTAVITVLRYGLLKGVVLVDTPGLNSTI-EHHTEITESFLPRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 284 DFFI-IISATR-FKEIDAHLAKAIAK-MNTKFYFVRTKIDQDVSNEqrskpksfnRDSVLKKIRDdcSGHLQKVLSSQPP 360
Cdd:cd09912   75 DAVIfVLSADQpLTESEREFLKEILKwSGKKIFFVLNKIDLLSEEE---------LEEVLEYSRE--ELGVLELGGGEPR 143

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 184186090 361 VFLVS---------NFDVSDFD---FPKLENTLLREL 385
Cdd:cd09912  144 IFPVSakealearlQGDEELLEqsgFEELEEHLEEFL 180
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 207-267 3.92e-06

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: 46.56  E-value: 3.92e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 184186090 207 AVTGETGTGKSSFINALRGVrgeeEGAAPTGVVETTMKRTPYP-HPKLPNVTIWDLPGIGST 267
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGT----EVAAVGDRRPTTRAAQAYVwQTGGDGLVLLDLPGVGER 58
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 205-318 4.12e-06

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: 45.69  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090  205 NIAVTGETGTGKSSFINALRGVRGEeegAAPT-GvveTTMKRTPYP-HPKLPNVTIWDLPG-IGSTNFQPQNYLTEMKFG 281
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAI---VSDYpG---TTRDPNEGRlELKGKQIILVDTPGlIEGASEGEGLGRAFLAII 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 184186090  282 EYD--FFIIISATRFKEIDAHLAKAIAKMNTKFYFVRTK 318
Cdd:pfam01926  75 EADliLFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
206-264 1.20e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.13  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 184186090 206 IAVTGETGTGKSSFINAL-RGVRGEEEGAAPTGVvetTMKRTPYPHPKL-PNVTIWDLPGI 264
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLvGDIFSLEKYLSTNGV---TIDKKELKLDGLdVDLVIWDTPGQ 63
Dynamin_N pfam00350
Dynamin family;
206-260 3.95e-05

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 44.14  E-value: 3.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 184186090  206 IAVTGETGTGKSSFINALRGVRgeeegAAPTGVVETT-------MKRTPYPHPKLPNVTIWD 260
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGRD-----ILPRGPGPTTrrptvlrLGESPGASEGAVKVEYKD 57
YlqF_related_GTPase cd01849
Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, ...
 171-264 6.46e-04

Circularly permuted YlqF-related GTPases; These proteins are found in bacteria, eukaryotes, and archaea. They all exhibit a circular permutation of the GTPase signature motifs so that the order of the conserved G box motifs is G4-G5-G1-G2-G3, with G4 and G5 being permuted from the C-terminal region of proteins in the Ras superfamily to the N-terminus of YlqF-related GTPases.


Pssm-ID: 206746 [Multi-domain]  Cd Length: 146  Bit Score: 40.45  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 171 ETITLIESHLEDKNLQGALSEISHALSNIDKAPLNIAVTGETGTGKSSFINALRGVRGEEEGAAPtgVVETTMKRTPYPH 250
Cdd:cd01849   59 TKTFFISATNGQGILKLKAEITKQKLKLKYKKGIRVGVVGLPNVGKSSFINALLNKFKLKVGSIP--GTTKLQQDVKLDK 136

                         90
                 ....*....|....
gi 184186090 251 pklpNVTIWDLPGI 264
Cdd:cd01849  137 ----EIYLYDTPGI 146
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
 201-223 1.93e-03

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.


Pssm-ID: 410874 [Multi-domain]  Cd Length: 177  Bit Score: 39.45  E-value: 1.93e-03
                         10        20
                 ....*....|....*....|...
gi 184186090 201 KAPLNIAVTGETGTGKSSFINAL 223
Cdd:cd01130   10 RARKNILISGGTGSGKTTLLNAL 32
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
 187-223 2.36e-03

Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443988 [Multi-domain]  Cd Length: 386  Bit Score: 40.53  E-value: 2.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 184186090 187 GALS-EISHALSNIDKAPLNIAVTGETGTGKSSFINAL 223
Cdd:COG4962  165 GSLTpEMAEFLRAAVRARLNILVSGGTGSGKTTLLNAL 202
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 199-264 5.27e-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: 37.68  E-value: 5.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 184186090 199 IDKAPLNIAVTGETGTGKSSFINALRGVRGeeegaAPTGvvettmkrtpyPHPKLP-------------NVTIWDLPGI 264
Cdd:cd01859   95 IDGKPVIVGVVGYPKVGKSSIINALKGRHS-----ASTS-----------PIPGSPgytkgiqlvridsKIYLIDTPGV 157
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 207-334 6.35e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that 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. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 37.61  E-value: 6.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 184186090 207 AVTGETGTGKSSFINALRGvrgeeEGAAPTGVV--ETTM-KRTPYPHPKLPNVTIWDLPGIGSTNFQ--PQNYLTEMKFG 281
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLG-----QNVGIVSPIpgTTRDpVRKEWELLPLGPVVLIDTPGLDEEGGLgrERVEEARQVAD 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 184186090 282 EYD--FFIIISATRFKEIDAHLAKAIaKMNTKFYFVRTKIDQDVSNEQRSKPKSF 334
Cdd:cd00880   76 RADlvLLVVDSDLTPVEEEAKLGLLR-ERGKPVLLVLNKIDLVPESEEEELLRER 129
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 203-264 6.98e-03

Circularly permuted YlqF GTPase; Proteins of the YlqF 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. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 37.51  E-value: 6.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 184186090 203 PLNIAVTGETGTGKSSFINALRGVRGEEEGAAPtGVveTTMKRTpyphPKL-PNVTIWDLPGI 264
Cdd:cd01856  115 PLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKP-GV--TRGQQW----IRIgPNIELLDTPGI 170
 
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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