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Conserved domains on  [gi|197382616|ref|NP_001094945|]
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interferon-inducible GTPase-like [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 ...
35-403 6.34e-145

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: 416.88  E-value: 6.34e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616   35 SQETIDLIKLYLNKGNIHGANSLISDALRNIDNAPINIAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETTMKRTSY 114
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  115 KHPKIETLTLWDLPGIGTQKFPPKTYLEEVKFKEYDFFIIVSATRFTKLELDLAKAITNMKKNYYFVRTKVDIDVENERK 194
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  195 SKPRTFEREKALKQIQSYSVKIFNDNNMAVPPIFLISNYDLSDYDFPFLVDTLIKELHVQKRHNFMLSLPNFTDQAIDRK 274
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  275 YKATQQFIWLEAFKIGVVAIFPVLGNLRNKDMKKIKNTLNYYQKIFGVDDESLELVAKDFQVPVEQVKKTMKTPHLLKKY 354
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197382616  355 REETFRNDFKKLVSTFGRLL----AVGLYFPAIYYLQLHILDTVTEDAKVLLR 403
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLggplCVNTYLREIYYLRYLFLDIVAEDAKTLLR 373
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
35-403 6.34e-145

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: 416.88  E-value: 6.34e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616   35 SQETIDLIKLYLNKGNIHGANSLISDALRNIDNAPINIAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETTMKRTSY 114
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  115 KHPKIETLTLWDLPGIGTQKFPPKTYLEEVKFKEYDFFIIVSATRFTKLELDLAKAITNMKKNYYFVRTKVDIDVENERK 194
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  195 SKPRTFEREKALKQIQSYSVKIFNDNNMAVPPIFLISNYDLSDYDFPFLVDTLIKELHVQKRHNFMLSLPNFTDQAIDRK 274
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  275 YKATQQFIWLEAFKIGVVAIFPVLGNLRNKDMKKIKNTLNYYQKIFGVDDESLELVAKDFQVPVEQVKKTMKTPHLLKKY 354
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197382616  355 REETFRNDFKKLVSTFGRLL----AVGLYFPAIYYLQLHILDTVTEDAKVLLR 403
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLggplCVNTYLREIYYLRYLFLDIVAEDAKTLLR 373
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
69-265 1.16e-109

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: 320.43  E-value: 1.16e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  69 PINIAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETTMKRTSYKHPKIETLTLWDLPGIGTQKFPPKTYLEEVKFKE 148
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616 149 YDFFIIVSATRFTKLELDLAKAITNMKKNYYFVRTKVDIDVENERKSKPRTFEREKALKQIQSYSVKIFNDNNMAVPPIF 228
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 197382616 229 LISNYDLSDYDFPFLVDTLIKELHVQKRHNFMLSLPN 265
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
YeeP COG3596
Predicted GTPase [General function prediction only];
57-142 1.76e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 70.95  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  57 LISDALRN--IDNAPINIAVTGESGAGKSSLINALIGigpeeEGAAEVGVIE-TTMKRTSY--KHPKIETLTLWDLPGIG 131
Cdd:COG3596   25 LLAEALERllVELPPPVIALVGKTGAGKSSLINALFG-----AEVAEVGVGRpCTREIQRYrlESDGLPGLVLLDTPGLG 99
                         90
                 ....*....|.
gi 197382616 132 TQKFPPKTYLE 142
Cdd:COG3596  100 EVNERDREYRE 110
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
72-108 6.63e-05

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 44.97  E-value: 6.63e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 197382616   72 IAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETT 108
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
71-91 1.20e-03

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 40.98  E-value: 1.20e-03
                         10        20
                 ....*....|....*....|.
gi 197382616  71 NIAVTGESGAGKSSLINALIG 91
Cdd:PRK11174 378 RIALVGPSGAGKTSLLNALLG 398
 
Name Accession Description Interval E-value
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
35-403 6.34e-145

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: 416.88  E-value: 6.34e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616   35 SQETIDLIKLYLNKGNIHGANSLISDALRNIDNAPINIAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETTMKRTSY 114
Cdd:pfam05049   1 SPEVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  115 KHPKIETLTLWDLPGIGTQKFPPKTYLEEVKFKEYDFFIIVSATRFTKLELDLAKAITNMKKNYYFVRTKVDIDVENERK 194
Cdd:pfam05049  81 SHPHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  195 SKPRTFEREKALKQIQSYSVKIFNDNNMAVPPIFLISNYDLSDYDFPFLVDTLIKELHVQKRHNFMLSLPNFTDQAIDRK 274
Cdd:pfam05049 161 GKPQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  275 YKATQQFIWLEAFKIGVVAIFPVLGNLRNKDMKKIKNTLNYYQKIFGVDDESLELVAKDFQVPVEQVKKTMKTPHLLKKY 354
Cdd:pfam05049 241 RQSLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPAFFKLT 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 197382616  355 REETFRNDFKKLVSTFGRLL----AVGLYFPAIYYLQLHILDTVTEDAKVLLR 403
Cdd:pfam05049 321 KDDSILARLTRYINAFCRVLggplCVNTYLREIYYLRYLFLDIVAEDAKTLLR 373
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
69-265 1.16e-109

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: 320.43  E-value: 1.16e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  69 PINIAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETTMKRTSYKHPKIETLTLWDLPGIGTQKFPPKTYLEEVKFKE 148
Cdd:cd04104    1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616 149 YDFFIIVSATRFTKLELDLAKAITNMKKNYYFVRTKVDIDVENERKSKPRTFEREKALKQIQSYSVKIFNDNNMAVPPIF 228
Cdd:cd04104   81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 197382616 229 LISNYDLSDYDFPFLVDTLIKELHVQKRHNFMLSLPN 265
Cdd:cd04104  161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
73-204 5.51e-14

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: 69.41  E-value: 5.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  73 AVTGESGAGKSSLINALIGigpeEEGAAEVGVIETTMKRTSYK---HPKIETLTLWDLPGIGTQKFPPKTYLEEVKFKEY 149
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLG----GEVGEVSDVPGTTRDPDVYVkelDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGA 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 197382616 150 DFFIIVSATRFTKLELDLAKAITN----MKKNYYFVRTKVDIDVENERKSKPRTFEREK 204
Cdd:cd00882   77 DLILLVVDSTDRESEEDAKLLILRrlrkEGIPIILVGNKIDLLEEREVEELLRLEELAK 135
YeeP COG3596
Predicted GTPase [General function prediction only];
57-142 1.76e-13

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 70.95  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  57 LISDALRN--IDNAPINIAVTGESGAGKSSLINALIGigpeeEGAAEVGVIE-TTMKRTSY--KHPKIETLTLWDLPGIG 131
Cdd:COG3596   25 LLAEALERllVELPPPVIALVGKTGAGKSSLINALFG-----AEVAEVGVGRpCTREIQRYrlESDGLPGLVLLDTPGLG 99
                         90
                 ....*....|.
gi 197382616 132 TQKFPPKTYLE 142
Cdd:COG3596  100 EVNERDREYRE 110
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
71-217 5.91e-07

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: 49.47  E-value: 5.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  71 NIAVTGESGAGKSSLINALIGigpeeegaAEV---GVIETTMKRTSYKHPKIETLTLWDLPGIG---------TQKFPPK 138
Cdd:cd09912    2 LLAVVGEFSAGKSTLLNALLG--------EEVlptGVTPTTAVITVLRYGLLKGVVLVDTPGLNstiehhteiTESFLPR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616 139 TyleevkfkeyDFFIIV-SATR-FTKLELD-LAKAITNMKKNYYFVRTKVDIDVENERKSKPRTFEREKALKQIQSYSVK 215
Cdd:cd09912   74 A----------DAVIFVlSADQpLTESEREfLKEILKWSGKKIFFVLNKIDLLSEEELEEVLEYSREELGVLELGGGEPR 143

                 ..
gi 197382616 216 IF 217
Cdd:cd09912  144 IF 145
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
73-131 8.83e-07

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: 48.11  E-value: 8.83e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  73 AVTGESGAGKSSLINALIGIgpeeEGAAEVGVIETTMKRTSYK-HPKIETLTLWDLPGIG 131
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGT----EVAAVGDRRPTTRAAQAYVwQTGGDGLVLLDLPGVG 56
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
71-184 9.99e-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: 47.23  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616   71 NIAVTGESGAGKSSLINALIGigpeeeGAAEVGVIE-TTMKRTSYK-HPKIETLTLWDLPG-IGTQKFPPKTYLEEVKFK 147
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTG------AKAIVSDYPgTTRDPNEGRlELKGKQIILVDTPGlIEGASEGEGLGRAFLAII 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 197382616  148 EYD--FFIIVSATRFTKLELDLAKAITNMKKNYYFVRTK 184
Cdd:pfam01926  75 EADliLFVVDSEEGITPLDEELLELLRENKKPIILVLNK 113
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
73-203 1.02e-06

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: 48.40  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  73 AVTGESGAGKSSLINALIGigpeeEGAAEVGVIE-TTMKRTSYKHPKIE--TLTLWDLPGIGTqKFPPKTYLEEVKFKEY 149
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLG-----QNVGIVSPIPgTTRDPVRKEWELLPlgPVVLIDTPGLDE-EGGLGRERVEEARQVA 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 197382616 150 D-----FFIIVSATRFTKLELDLAKAItNMKKNYYFVRTKVDIDVENERKSKPRTFERE 203
Cdd:cd00880   75 DradlvLLVVDSDLTPVEEEAKLGLLR-ERGKPVLLVLNKIDLVPESEEEELLRERKLE 132
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
70-198 1.35e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 48.44  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  70 INIAVTGESGAGKSSLINALIG--IGPEEEGaaevGVIETTMKRTSYKHPKIE-TLTLWDLPGIGTQKFPPKTYLEevKF 146
Cdd:COG1100    4 KKIVVVGTGGVGKTSLVNRLVGdiFSLEKYL----STNGVTIDKKELKLDGLDvDLVIWDTPGQDEFRETRQFYAR--QL 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 197382616 147 KEYDFFIIV-SATRFTKL--ELDLAKAITNMKKN--YYFVRTKVDIDVENERKSKPR 198
Cdd:COG1100   78 TGASLYLFVvDGTREETLqsLYELLESLRRLGKKspIILVLNKIDLYDEEEIEDEER 134
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
72-108 6.63e-05

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 44.97  E-value: 6.63e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 197382616   72 IAVTGESGAGKSSLINALIGIGPEEEGAAEVGVIETT 108
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
61-103 1.77e-04

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 43.59  E-value: 1.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 197382616  61 ALRNID---NAPINIAVTGESGAGKSSLINALIGIGPEEEGAAEVG 103
Cdd:COG4988  352 ALDGLSltiPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN 397
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
72-91 4.90e-04

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: 41.23  E-value: 4.90e-04
                         10        20
                 ....*....|....*....|
gi 197382616  72 IAVTGESGAGKSSLINALIG 91
Cdd:cd01854   88 SVLVGQSGVGKSTLLNALLP 107
VirB11-like_ATPase cd01130
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...
58-108 5.84e-04

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: 40.60  E-value: 5.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 197382616  58 ISDALRNIDNAPINIAVTGESGAGKSSLINALIGIGPEEEgaaEVGVIETT 108
Cdd:cd01130    1 MAAFLRLAVRARKNILISGGTGSGKTTLLNALLSFIPPDE---RIVTIEDT 48
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
72-105 1.05e-03

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 40.87  E-value: 1.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 197382616  72 IAVTGESGAGKSSLINALIgigPEEEgaAEVGVI 105
Cdd:COG1162  169 SVLVGQSGVGKSTLINALL---PDAD--LATGEI 197
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
61-102 1.07e-03

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 40.14  E-value: 1.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 197382616  61 ALRNIdNAPIN----IAVTGESGAGKSSLINALIGIGPEEEGAAEV 102
Cdd:cd03225   16 ALDDI-SLTIKkgefVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV 60
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
71-91 1.20e-03

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 40.98  E-value: 1.20e-03
                         10        20
                 ....*....|....*....|.
gi 197382616  71 NIAVTGESGAGKSSLINALIG 91
Cdd:PRK11174 378 RIALVGPSGAGKTSLLNALLG 398
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
59-91 1.27e-03

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 39.76  E-value: 1.27e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 197382616  59 SDALRNID-NAPIN--IAVTGESGAGKSSLINALIG 91
Cdd:cd03250   18 SFTLKDINlEVPKGelVAIVGPVGSGKSSLLSALLG 53
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
61-132 1.32e-03

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


Pssm-ID: 440463 [Multi-domain]  Cd Length: 582  Bit Score: 40.77  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  61 ALRNIDNAPINIAVTGESGAGKSSLINALIG--IGPEEEGaaevgviETTMKRTSYKHPKIETLTL-------WDLPGIG 131
Cdd:COG0699   24 ARLDLADPSLRIVMAGTTSQGKSQLVNALLGrrLLPSGAG-------ETTGVPTEIKHAEGSSARLlptagsvADTKRWP 96

                 .
gi 197382616 132 T 132
Cdd:COG0699   97 G 97
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
72-98 2.21e-03

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 38.40  E-value: 2.21e-03
                          10        20
                  ....*....|....*....|....*..
gi 197382616   72 IAVTGESGAGKSSLINALIGIGPEEEG 98
Cdd:pfam00005  14 LALVGPNGAGKSTLLKLIAGLLSPTEG 40
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
72-103 4.05e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 37.61  E-value: 4.05e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 197382616  72 IAVTGESGAGKSSLINALIGIGPEEEGAAEVG 103
Cdd:cd00267   28 VALVGPNGSGKSTLLRAIAGLLKPTSGEILID 59
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
62-87 4.48e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 39.24  E-value: 4.48e-03
                         10        20
                 ....*....|....*....|....*....
gi 197382616  62 LRNID-NAPIN--IAVTGESGAGKSSLIN 87
Cdd:COG0178  621 LKNVDvEIPLGvlTCVTGVSGSGKSTLVN 649
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
72-231 5.20e-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: 37.84  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616   72 IAVTGESGAGKSSLINALIGIGpeeeGAAevgviettmkRTSyKHP---------KI-ETLTLWDLPGIGTQKFPPK--- 138
Cdd:TIGR03598  21 IAFAGRSNVGKSSLINALTNRK----KLA----------RTS-KTPgrtqlinffEVnDGFRLVDLPGYGYAKVSKEeke 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616  139 -------TYLEE------VkfkeydfFIIVSATR-FTKLELDLAKAITNMKKNYYFVRTKVDidvenerKSKPRtfEREK 204
Cdd:TIGR03598  86 kwqklieEYLEKrenlkgV-------VLLMDIRHpLKELDLEMIEWLRERGIPVLIVLTKAD-------KLKKS--ELNK 149
                         170       180
                  ....*....|....*....|....*..
gi 197382616  205 ALKQIQSYSVKIFNDnnmavPPIFLIS 231
Cdd:TIGR03598 150 QLKKIKKALKKDADD-----PSVQLFS 171
Dynamin_N pfam00350
Dynamin family;
72-126 6.34e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 37.21  E-value: 6.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 197382616   72 IAVTGESGAGKSSLINALIG--IGPEEEGAAEVGVIETTMKRTSYKHPKIETLTLWD 126
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNALLGrdILPRGPGPTTRRPTVLRLGESPGASEGAVKVEYKD 57
PRK13721 PRK13721
conjugal transfer ATP-binding protein TraC; Provisional
63-90 6.46e-03

conjugal transfer ATP-binding protein TraC; Provisional


Pssm-ID: 237480 [Multi-domain]  Cd Length: 844  Bit Score: 38.94  E-value: 6.46e-03
                         10        20
                 ....*....|....*....|....*...
gi 197382616  63 RNIDNAPINIAVTGESGAGKSSLINALI 90
Cdd:PRK13721 443 RGMNNTNYNMAVCGTSGAGKTGLIQPLI 470
CpaF COG4962
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ...
58-108 6.73e-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: 38.61  E-value: 6.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 197382616  58 ISDALRNIDNAPINIAVTGESGAGKSSLINALIG-IGPEEegaaEVGVIETT 108
Cdd:COG4962  171 MAEFLRAAVRARLNILVSGGTGSGKTTLLNALSGfIPPDE----RIVTIEDA 218
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
6-130 8.71e-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: 36.74  E-value: 8.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197382616   6 SDTSKTEDNEDLVSSFNE-----YFKNIKTEKIISQETIDLIKLYlnkgnihgaNSLISDALRNIDNAPINIAVTGESGA 80
Cdd:cd01856   56 ADLADPAKTKKWLKYFKSqgepvLFVNAKNGKGVKKLLKKAKKLL---------KENEKLKAKGLLPRPLRAMVVGIPNV 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 197382616  81 GKSSLINALIGIgpeeeGAAEV----GVieTTMKRTSYKHPKIEtltLWDLPGI 130
Cdd:cd01856  127 GKSTLINRLRGK-----KVAKVgnkpGV--TRGQQWIRIGPNIE---LLDTPGI 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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