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Conserved domains on  [gi|74208202|dbj|BAE26317|]
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unnamed protein product [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 ...
438-810 2.50e-177

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: 515.11  E-value: 2.50e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   438 SEETITLIESHLEDKNLQEALTVISHALRNIDKAPLNIAVTGETGTGKSSFINALRGISSEEKDAAPTGVIETTMKRTPY 517
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   518 PHPKLPNVTIWDLPGIGSTNFPPQNYLTEMKFGEYDFFIIISATRFKEIDAHLAKAIAKMNIKFYFVRTKIDQDISNEQR 597
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   598 SKPKSFNRDSVLKKIKDECLGLLQKVLSSQPPIFLVSNFDVSDFDFPKLETTLLKELPAHKRHLFMMSLHSVTETTIARK 677
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   678 RDFLRQKIWLEALKAGLWATIPLGGLVR-DKMQKLEETLTLYRSYFGLDEASLENIAKDFNVSVNEIKAHLRSLQLLTKN 756
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGdSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74208202   757 NDMSFKEKLLKYIEYISCVTGGPLASGLYFSKTYYWQSLFIDTVASDAKSLLNK 810
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
IIGP super family cl27085
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
27-388 1.93e-132

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: 399.55  E-value: 1.93e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202    27 SQELIASIESSLENGNLQETVSAISTALGDIEKAPLNIAVMGETGAGKSSLINALQGVGDDEDGAAaSTGVVHTTTERTP 106
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSA-PTGVVETTMKRTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   107 YTYTKFPSVTLWDLPGIGSTDFQPHDYLKKIEFEEYDFFIIVSAIRIKQSDIELAKAIVQMNRGLYFVKTKTDSDLLNEK 186
Cdd:pfam05049  80 YSHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   187 RCNPMRFNRENTLKSIRICLSSNLKERFQQEPPVFLVSNFDVSDFDFPKLESTLLSQLPAYKHQIFMSTLQVVINAIVDR 266
Cdd:pfam05049 160 KGKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   267 KRDMLKQKIWKESIMPRAWATIPSRG-LTQKDMEMLQQTLNDYRSSFGLDEASLENIAEDLNVTLEELKANIKSPHLLSD 345
Cdd:pfam05049 240 KRQSLKQKIWLEALKAAAVSIIPSLTfLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKL 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74208202   346 EPDTSLTEKLLKYIG------------NPYFSKVFHLQNYFIDTVASDVKIILSK 388
Cdd:pfam05049 320 TKDDSILARLTRYINafcrvlggplcvNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
438-810 2.50e-177

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: 515.11  E-value: 2.50e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   438 SEETITLIESHLEDKNLQEALTVISHALRNIDKAPLNIAVTGETGTGKSSFINALRGISSEEKDAAPTGVIETTMKRTPY 517
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   518 PHPKLPNVTIWDLPGIGSTNFPPQNYLTEMKFGEYDFFIIISATRFKEIDAHLAKAIAKMNIKFYFVRTKIDQDISNEQR 597
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   598 SKPKSFNRDSVLKKIKDECLGLLQKVLSSQPPIFLVSNFDVSDFDFPKLETTLLKELPAHKRHLFMMSLHSVTETTIARK 677
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   678 RDFLRQKIWLEALKAGLWATIPLGGLVR-DKMQKLEETLTLYRSYFGLDEASLENIAKDFNVSVNEIKAHLRSLQLLTKN 756
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGdSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74208202   757 NDMSFKEKLLKYIEYISCVTGGPLASGLYFSKTYYWQSLFIDTVASDAKSLLNK 810
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
27-388 1.93e-132

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: 399.55  E-value: 1.93e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202    27 SQELIASIESSLENGNLQETVSAISTALGDIEKAPLNIAVMGETGAGKSSLINALQGVGDDEDGAAaSTGVVHTTTERTP 106
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSA-PTGVVETTMKRTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   107 YTYTKFPSVTLWDLPGIGSTDFQPHDYLKKIEFEEYDFFIIVSAIRIKQSDIELAKAIVQMNRGLYFVKTKTDSDLLNEK 186
Cdd:pfam05049  80 YSHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   187 RCNPMRFNRENTLKSIRICLSSNLKERFQQEPPVFLVSNFDVSDFDFPKLESTLLSQLPAYKHQIFMSTLQVVINAIVDR 266
Cdd:pfam05049 160 KGKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   267 KRDMLKQKIWKESIMPRAWATIPSRG-LTQKDMEMLQQTLNDYRSSFGLDEASLENIAEDLNVTLEELKANIKSPHLLSD 345
Cdd:pfam05049 240 KRQSLKQKIWLEALKAAAVSIIPSLTfLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKL 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74208202   346 EPDTSLTEKLLKYIG------------NPYFSKVFHLQNYFIDTVASDVKIILSK 388
Cdd:pfam05049 320 TKDDSILARLTRYINafcrvlggplcvNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
472-668 9.59e-125

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: 372.82  E-value: 9.59e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 472 PLNIAVTGETGTGKSSFINALRGISSEEKDAAPTGVIETTMKRTPYPHPKLPNVTIWDLPGIGSTNFPPQNYLTEMKFGE 551
Cdd:cd04104   1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 552 YDFFIIISATRFKEIDAHLAKAIAKMNIKFYFVRTKIDQDISNEQRSKPKSFNRDSVLKKIKDECLGLLQKVLSSQPPIF 631
Cdd:cd04104  81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 74208202 632 LVSNFDVSDFDFPKLETTLLKELPAHKRHLFMMSLHS 668
Cdd:cd04104 161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
61-257 8.08e-103

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: 315.81  E-value: 8.08e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202  61 PLNIAVMGETGAGKSSLINALQGVGDDEDGAAAsTGVVHTTTERTPYTYTKFPSVTLWDLPGIGSTDFQPHDYLKKIEFE 140
Cdd:cd04104   1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAP-TGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 141 EYDFFIIVSAIRIKQSDIELAKAIVQMNRGLYFVKTKTDSDLLNEKRCNPMRFNRENTLKSIRICLSSNLKERFQQEPPV 220
Cdd:cd04104  80 EYDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPV 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 74208202 221 FLVSNFDVSDFDFPKLESTLLSQLPAYKHQIFMSTLQ 257
Cdd:cd04104 160 FLVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLP 196
YeeP COG3596
Predicted GTPase [General function prediction only];
57-127 4.17e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 71.34  E-value: 4.17e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74208202  57 IEKAPLNIAVMGETGAGKSSLINALQGVGddedgaAASTGVVH-TTTERTPYTYTKF--PSVTLWDLPGIGSTD 127
Cdd:COG3596  35 VELPPPVIALVGKTGAGKSSLINALFGAE------VAEVGVGRpCTREIQRYRLESDglPGLVLLDTPGLGEVN 102
YeeP COG3596
Predicted GTPase [General function prediction only];
444-544 4.29e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 70.95  E-value: 4.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 444 LIESHLEDKNLQEALTVISHALRNI----------DKAPLNIAVTGETGTGKSSFINALRGisseeKDAAPTGVIE-TTM 512
Cdd:COG3596   1 MSTEVSSLTERLEALKRLPQVLRELlaealerllvELPPPVIALVGKTGAGKSSLINALFG-----AEVAEVGVGRpCTR 75
                        90       100       110
                ....*....|....*....|....*....|....
gi 74208202 513 KRTPY--PHPKLPNVTIWDLPGIGSTNFPPQNYL 544
Cdd:COG3596  76 EIQRYrlESDGLPGLVLLDTPGLGEVNERDREYR 109
PRK01889 PRK01889
GTPase RsgA; Reviewed
64-104 4.19e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 40.30  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 74208202   64 IAVMGETGAGKSSLINALQGvgddEDgaAASTGVV--------HTTTER 104
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLG----EE--VQKTGAVreddskgrHTTTHR 240
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
438-810 2.50e-177

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: 515.11  E-value: 2.50e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   438 SEETITLIESHLEDKNLQEALTVISHALRNIDKAPLNIAVTGETGTGKSSFINALRGISSEEKDAAPTGVIETTMKRTPY 517
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   518 PHPKLPNVTIWDLPGIGSTNFPPQNYLTEMKFGEYDFFIIISATRFKEIDAHLAKAIAKMNIKFYFVRTKIDQDISNEQR 597
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   598 SKPKSFNRDSVLKKIKDECLGLLQKVLSSQPPIFLVSNFDVSDFDFPKLETTLLKELPAHKRHLFMMSLHSVTETTIARK 677
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   678 RDFLRQKIWLEALKAGLWATIPLGGLVR-DKMQKLEETLTLYRSYFGLDEASLENIAKDFNVSVNEIKAHLRSLQLLTKN 756
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGdSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74208202   757 NDMSFKEKLLKYIEYISCVTGGPLASGLYFSKTYYWQSLFIDTVASDAKSLLNK 810
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
27-388 1.93e-132

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: 399.55  E-value: 1.93e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202    27 SQELIASIESSLENGNLQETVSAISTALGDIEKAPLNIAVMGETGAGKSSLINALQGVGDDEDGAAaSTGVVHTTTERTP 106
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSA-PTGVVETTMKRTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   107 YTYTKFPSVTLWDLPGIGSTDFQPHDYLKKIEFEEYDFFIIVSAIRIKQSDIELAKAIVQMNRGLYFVKTKTDSDLLNEK 186
Cdd:pfam05049  80 YSHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   187 RCNPMRFNRENTLKSIRICLSSNLKERFQQEPPVFLVSNFDVSDFDFPKLESTLLSQLPAYKHQIFMSTLQVVINAIVDR 266
Cdd:pfam05049 160 KGKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   267 KRDMLKQKIWKESIMPRAWATIPSRG-LTQKDMEMLQQTLNDYRSSFGLDEASLENIAEDLNVTLEELKANIKSPHLLSD 345
Cdd:pfam05049 240 KRQSLKQKIWLEALKAAAVSIIPSLTfLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKL 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 74208202   346 EPDTSLTEKLLKYIG------------NPYFSKVFHLQNYFIDTVASDVKIILSK 388
Cdd:pfam05049 320 TKDDSILARLTRYINafcrvlggplcvNTYLREIYYLRYLFLDIVAEDAKTLLRK 374
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
472-668 9.59e-125

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: 372.82  E-value: 9.59e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 472 PLNIAVTGETGTGKSSFINALRGISSEEKDAAPTGVIETTMKRTPYPHPKLPNVTIWDLPGIGSTNFPPQNYLTEMKFGE 551
Cdd:cd04104   1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 552 YDFFIIISATRFKEIDAHLAKAIAKMNIKFYFVRTKIDQDISNEQRSKPKSFNRDSVLKKIKDECLGLLQKVLSSQPPIF 631
Cdd:cd04104  81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 74208202 632 LVSNFDVSDFDFPKLETTLLKELPAHKRHLFMMSLHS 668
Cdd:cd04104 161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
61-257 8.08e-103

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: 315.81  E-value: 8.08e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202  61 PLNIAVMGETGAGKSSLINALQGVGDDEDGAAAsTGVVHTTTERTPYTYTKFPSVTLWDLPGIGSTDFQPHDYLKKIEFE 140
Cdd:cd04104   1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAP-TGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 141 EYDFFIIVSAIRIKQSDIELAKAIVQMNRGLYFVKTKTDSDLLNEKRCNPMRFNRENTLKSIRICLSSNLKERFQQEPPV 220
Cdd:cd04104  80 EYDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPV 159
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 74208202 221 FLVSNFDVSDFDFPKLESTLLSQLPAYKHQIFMSTLQ 257
Cdd:cd04104 160 FLVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLP 196
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
476-642 4.50e-16

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: 76.34  E-value: 4.50e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 476 AVTGETGTGKSSFINALRGISSEEKDAAPtgviETTMKRTPYP---HPKLPNVTIWDLPGIGSTNFPPQNYLTEMKFGEY 552
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLGGEVGEVSDVP----GTTRDPDVYVkelDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 553 DFFII-ISATR---FKEIDAHLAKAIAKMNIKFYFVRTKIDQDISNEQRskpksfnrdsvlkkikdECLGLLQKVLSSQP 628
Cdd:cd00882  77 DLILLvVDSTDresEEDAKLLILRRLRKEGIPIILVGNKIDLLEEREVE-----------------ELLRLEELAKILGV 139
                       170
                ....*....|....
gi 74208202 629 PIFLVSNFDVSDFD 642
Cdd:cd00882 140 PVFEVSAKTGEGVD 153
YeeP COG3596
Predicted GTPase [General function prediction only];
57-127 4.17e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 71.34  E-value: 4.17e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74208202  57 IEKAPLNIAVMGETGAGKSSLINALQGVGddedgaAASTGVVH-TTTERTPYTYTKF--PSVTLWDLPGIGSTD 127
Cdd:COG3596  35 VELPPPVIALVGKTGAGKSSLINALFGAE------VAEVGVGRpCTREIQRYRLESDglPGLVLLDTPGLGEVN 102
YeeP COG3596
Predicted GTPase [General function prediction only];
444-544 4.29e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 70.95  E-value: 4.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 444 LIESHLEDKNLQEALTVISHALRNI----------DKAPLNIAVTGETGTGKSSFINALRGisseeKDAAPTGVIE-TTM 512
Cdd:COG3596   1 MSTEVSSLTERLEALKRLPQVLRELlaealerllvELPPPVIALVGKTGAGKSSLINALFG-----AEVAEVGVGRpCTR 75
                        90       100       110
                ....*....|....*....|....*....|....
gi 74208202 513 KRTPY--PHPKLPNVTIWDLPGIGSTNFPPQNYL 544
Cdd:COG3596  76 EIQRYrlESDGLPGLVLLDTPGLGEVNERDREYR 109
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
65-232 5.75e-13

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: 67.48  E-value: 5.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202  65 AVMGETGAGKSSLINALQGvgddeDGAAASTGVVHTTTERTPYTY---TKFPSVTLWDLPGIGSTDFQPHDYLKKIEFEE 141
Cdd:cd00882   1 VVVGRGGVGKSSLLNALLG-----GEVGEVSDVPGTTRDPDVYVKeldKGKVKLVLVDTPGLDEFGGLGREELARLLLRG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 142 YDFFIIVSAIRIKQSDIELAKAIVQMNRG----LYFVKTKtdSDLLNEKRCNPmrfnrentlksiricLSSNLKERFQQE 217
Cdd:cd00882  76 ADLILLVVDSTDRESEEDAKLLILRRLRKegipIILVGNK--IDLLEEREVEE---------------LLRLEELAKILG 138
                       170
                ....*....|....*
gi 74208202 218 PPVFLVSNFDVSDFD 232
Cdd:cd00882 139 VPVFEVSAKTGEGVD 153
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
65-126 7.28e-10

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: 57.74  E-value: 7.28e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74208202  65 AVMGETGAGKSSLINALQGvgddedGAAASTGVVH-TTTERTPYTY-TKFPSVTLWDLPGIGST 126
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFG------TEVAAVGDRRpTTRAAQAYVWqTGGDGLVLLDLPGVGER 58
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
62-244 1.50e-09

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: 57.94  E-value: 1.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202  62 LNIAVMGETGAGKSSLINALqgVGDDedgaAASTGVVHTTTERTPYTYTKFPSVTLWDLPGIGSTDfQPHDYLKKIEFEE 141
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNAL--LGEE----VLPTGVTPTTAVITVLRYGLLKGVVLVDTPGLNSTI-EHHTEITESFLPR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 142 YDFFIIVSAIR--IKQSDIELAKAIVQ-MNRGLYFVKTKtdSDLLNEKrcnpmrfNRENTLKSIRIclSSNLKERFQQEP 218
Cdd:cd09912  74 ADAVIFVLSADqpLTESEREFLKEILKwSGKKIFFVLNK--IDLLSEE-------ELEEVLEYSRE--ELGVLELGGGEP 142
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 74208202 219 PVFLVS---------NFDVSDFD---FPKLESTLLSQL 244
Cdd:cd09912 143 RIFPVSakealearlQGDEELLEqsgFEELEEHLEEFL 180
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
473-634 5.53e-09

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: 56.40  E-value: 5.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 473 LNIAVTGETGTGKSSFINALRGisseeKDAAPTGVIETTMKRTPYPHPKLPNVTIWDLPGIGSTNfPPQNYLTEMKFGEY 552
Cdd:cd09912   1 FLLAVVGEFSAGKSTLLNALLG-----EEVLPTGVTPTTAVITVLRYGLLKGVVLVDTPGLNSTI-EHHTEITESFLPRA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 553 DFFI-IISATR-FKEIDAHLAKAIAK-MNIKFYFVRTKIDQdISNEQrskpksfnRDSVLKKIKDEClgLLQKVLSSQPP 629
Cdd:cd09912  75 DAVIfVLSADQpLTESEREFLKEILKwSGKKIFFVLNKIDL-LSEEE--------LEEVLEYSREEL--GVLELGGGEPR 143

                ....*
gi 74208202 630 IFLVS 634
Cdd:cd09912 144 IFPVS 148
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
63-177 8.28e-07

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: 48.38  E-value: 8.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202    63 NIAVMGETGAGKSSLINALqgVGDDedgaAASTGVVHTTTERTPYTYTKF-PSVTLWDLPGI---GSTDFQPHDYLKKIe 138
Cdd:pfam01926   1 RVALVGRPNVGKSTLINAL--TGAK----AIVSDYPGTTRDPNEGRLELKgKQIILVDTPGLiegASEGEGLGRAFLAI- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 74208202   139 fEEYD--FFIIVSAIRIKQSDIELAKAIVQMNRGLYFVKTK 177
Cdd:pfam01926  74 -IEADliLFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
475-533 9.22e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.90  E-value: 9.22e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74208202 475 IAVTGETGTGKSSFINAL-RGISSEEKDAAPTGVietTMKRTPYPHPKL-PNVTIWDLPGI 533
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLvGDIFSLEKYLSTNGV---TIDKKELKLDGLdVDLVIWDTPGQ 63
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
474-587 1.03e-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: 45.30  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202   474 NIAVTGETGTGKSSFINALRGISSEEKDAAPtgvieTTMKRTPYP-HPKLPNVTIWDLPG-IGSTNFPPQNYLTEMKFGE 551
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIVSDYPG-----TTRDPNEGRlELKGKQIILVDTPGlIEGASEGEGLGRAFLAIIE 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 74208202   552 YD--FFIIISATRFKEIDAHLAKAIAKMNIKFYFVRTK 587
Cdd:pfam01926  76 ADliLFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
64-224 1.85e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 46.13  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202  64 IAVMGETGAGKSSLINALQGVGDDEDGAAASTGVVHTTTERTPYTYTkfPSVTLWDLPGIgsTDFQP-HDYLKKiEFEEY 142
Cdd:COG1100   6 IVVVGTGGVGKTSLVNRLVGDIFSLEKYLSTNGVTIDKKELKLDGLD--VDLVIWDTPGQ--DEFREtRQFYAR-QLTGA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 143 DFFIIVSAIRIKQSD---IELAKAIVQMNRG--LYFVKTKtdSDLLNEKrcnpmrfnrentlksiRICLSSNLKERFQQE 217
Cdd:COG1100  81 SLYLFVVDGTREETLqslYELLESLRRLGKKspIILVLNK--IDLYDEE----------------EIEDEERLKEALSED 142

                ....*....
gi 74208202 218 --PPVFLVS 224
Cdd:COG1100 143 niVEVVATS 151
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
64-105 2.50e-05

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: 46.24  E-value: 2.50e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 74208202  64 IAVMGETGAGKSSLINALQGvgddedGAAASTGVV--------HTTTERT 105
Cdd:cd01854  88 SVLVGQSGVGKSTLLNALLP------ELVLATGEIseklgrgrHTTTHRE 131
Dynamin_N pfam00350
Dynamin family;
475-529 2.77e-05

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 45.30  E-value: 2.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74208202   475 IAVTGETGTGKSSFINALRGisseeKDAAPTGVIETT-------MKRTPYPHPKLPNVTIWD 529
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLG-----RDILPRGPGPTTrrptvlrLGESPGASEGAVKVEYKD 57
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
64-122 5.59e-05

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 45.88  E-value: 5.59e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74208202  64 IAVMGETGAGKSSLINALQGvgddedGAAASTGVV--------HTTTertpytytkfpSVTLWDLPG 122
Cdd:COG1162 169 SVLVGQSGVGKSTLINALLP------DADLATGEIseklgrgrHTTT-----------HAELYPLPG 218
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
476-536 1.45e-04

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: 42.71  E-value: 1.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74208202 476 AVTGETGTGKSSFINALRGISSeekdAAPTGVIETTMKRTPYP-HPKLPNVTIWDLPGIGST 536
Cdd:cd11383   1 GLMGKTGAGKSSLCNALFGTEV----AAVGDRRPTTRAAQAYVwQTGGDGLVLLDLPGVGER 58
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
64-128 2.49e-04

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: 42.53  E-value: 2.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74208202    64 IAVMGETGAGKSSLINALQGvgddedGAAASTGVV--------HTTTERTPYtytKFPSVT-LWDLPGIGSTDF 128
Cdd:pfam03193 109 TVLAGQSGVGKSTLLNALLP------ELDLRTGEIseklgrgrHTTTHVELF---PLPGGGlLIDTPGFRELGL 173
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
65-123 3.45e-04

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: 41.85  E-value: 3.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74208202  65 AVMGETGAGKSSLINALqgVGDDedgaAASTGVVH-TTTERTPYTYTKFP--SVTLWDLPGI 123
Cdd:cd00880   1 AIFGRPNVGKSSLLNAL--LGQN----VGIVSPIPgTTRDPVRKEWELLPlgPVVLIDTPGL 56
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
476-603 1.44e-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: 40.31  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202 476 AVTGETGTGKSSFINALRGisseeKDAAPTGVI--ETTM-KRTPYPHPKLPNVTIWDLPGIGSTNF--PPQNYLTEMKFG 550
Cdd:cd00880   1 AIFGRPNVGKSSLLNALLG-----QNVGIVSPIpgTTRDpVRKEWELLPLGPVVLIDTPGLDEEGGlgRERVEEARQVAD 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74208202 551 EYD--FFIIISATRFKEIDAHLAKAIaKMNIKFYFVRTKIDQDISNEQRSKPKSF 603
Cdd:cd00880  76 RADlvLLVVDSDLTPVEEEAKLGLLR-ERGKPVLLVLNKIDLVPESEEEELLRER 129
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
461-500 1.85e-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: 40.22  E-value: 1.85e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 74208202 461 ISHALRNIDKAPLNIAVTGETGTGKSSFINAL-RGISSEEK 500
Cdd:cd01130   1 MAAFLRLAVRARKNILISGGTGSGKTTLLNALlSFIPPDER 41
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
465-511 2.68e-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: 40.92  E-value: 2.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 74208202 465 LRNIDKAPLNIAVTGETGTGKSSFINAL-RGISSEEKdaapTGVIETT 511
Cdd:COG4962 175 LRAAVRARLNILVSGGTGSGKTTLLNALsGFIPPDER----IVTIEDA 218
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
468-533 3.79e-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: 38.84  E-value: 3.79e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74208202 468 IDKAPLNIAVTGETGTGKSSFINALRGisseeKDAAPTGviettmkrtpyPHPKLP-------------NVTIWDLPGI 533
Cdd:cd01859  95 IDGKPVIVGVVGYPKVGKSSIINALKG-----RHSASTS-----------PIPGSPgytkgiqlvridsKIYLIDTPGV 157
PRK01889 PRK01889
GTPase RsgA; Reviewed
64-104 4.19e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 40.30  E-value: 4.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 74208202   64 IAVMGETGAGKSSLINALQGvgddEDgaAASTGVV--------HTTTER 104
Cdd:PRK01889 198 VALLGSSGVGKSTLVNALLG----EE--VQKTGAVreddskgrHTTTHR 240
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
36-123 4.65e-03

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH 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.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 39.17  E-value: 4.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74208202  36 SSLENGNLQETVSAISTALGDiekaPLNIAVMGETGAGKSSLINAL--QGVGDDEDGAAASTGVV--HTTTERTPYTYTK 111
Cdd:cd01855 104 SAKKGWGVEELIEEIKKLAKY----RGDVYVVGATNVGKSTLINALlkSNGGKVQAQALVQRLTVspIPGTTLGLIKIPL 179
                        90
                ....*....|..
gi 74208202 112 FPSVTLWDLPGI 123
Cdd:cd01855 180 GEGKKLYDTPGI 191
PRK00098 PRK00098
GTPase RsgA; Reviewed
66-102 6.91e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 39.42  E-value: 6.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 74208202   66 VMGETGAGKSSLINALQGvgddedGAAASTGVV--------HTTT 102
Cdd:PRK00098 169 LAGQSGVGKSTLLNALAP------DLELKTGEIsealgrgkHTTT 207
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
442-492 9.92e-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: 38.71  E-value: 9.92e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 74208202 442 ITLIESHLEDKnlQEALTVISHALRNIDKAPLNIAVTGETGTGKSSFINAL 492
Cdd:cd03114  18 ITLVESGRPDH--RELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEAL 66
 
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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