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Conserved domains on  [gi|1277529350|ref|NP_001344963|]
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interferon-inducible GTPase 5 [Mus musculus]

Protein Classification

ABC transporter ATP-binding protein; betaine/proline/choline family ABC transporter ATP-binding protein( domain architecture ID 13591049)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates| betaine/proline/choline family ABC transporter ATP-binding protein with two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 52-248 9.16e-116

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: 337.76  E-value: 9.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  52 RLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPHPQFPDVTLWDLPGAGSPGCSADKYLKQVDFGR 131
Cdd:cd04104     1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 132 YDFFLLVSPRRCGAVESRLASEILRQGKKFYFVRTKVDEDLAATRSQRPSGFSEAAVLQEIRDHCTERLRVAGVNDPRIF 211
Cdd:cd04104    81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1277529350 212 LVSNLSPTRYDFPMLVTTWEHDLPAHRRHAGLLSLPD 248
Cdd:cd04104   161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
RsgA_GTPase super family cl38114
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 9-74 4.65e-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.


The actual alignment was detected with superfamily member pfam03193:

Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 40.99  E-value: 4.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277529350   9 VPEETTILMAKEELEAL--RTAFESGDIPQAASRLRELLANSETTrlevgVTGESGAGKSSLINALRG 74
Cdd:pfam03193  66 LDEEEELEELLKIYRAIgyPVLFVSAKTGEGIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
 
Name Accession Description Interval E-value
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 52-248 9.16e-116

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: 337.76  E-value: 9.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  52 RLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPHPQFPDVTLWDLPGAGSPGCSADKYLKQVDFGR 131
Cdd:cd04104     1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 132 YDFFLLVSPRRCGAVESRLASEILRQGKKFYFVRTKVDEDLAATRSQRPSGFSEAAVLQEIRDHCTERLRVAGVNDPRIF 211
Cdd:cd04104    81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1277529350 212 LVSNLSPTRYDFPMLVTTWEHDLPAHRRHAGLLSLPD 248
Cdd:cd04104   161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 20-401 5.97e-108

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: 324.82  E-value: 5.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  20 EELEALRTAFESGDIPQAASRLRELLANSETTRLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPH 99
Cdd:pfam05049   3 EVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPYSH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 100 PQFPDVTLWDLPGAGSPGCSADKYLKQVDFGRYDFFLLVSPRRCGAVESRLASEILRQGKKFYFVRTKVDEDLAATRSQR 179
Cdd:pfam05049  83 PHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQKGK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 180 PSGFSEAAVLQEIRDHCTERLRVAGVNDPRIFLVSNLSPTRYDFPMLVTTWEHDLPAHRRHAGLLSLPDISLEALQKKKD 259
Cdd:pfam05049 163 PQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKKRQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 260 MLQEQVLKTALVSGVIQALPVPGLAAAYDDALLIRSLRGYHRSFGLDDDSLAKLAEQVGKQAGDLRSVIRSP-LANEVSP 338
Cdd:pfam05049 243 SLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPaFFKLTKD 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277529350 339 ETVLRLysqssdgAMRVARAFERgipVFGTLVAGGISFGTVYTMLQGCLNEMAEDAQRVRIKA 401
Cdd:pfam05049 323 DSILAR-------LTRYINAFCR---VLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
YeeP COG3596
Predicted GTPase [General function prediction only];
38-317 9.97e-16

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 77.88  E-value: 9.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  38 ASRLRELLANSETTRleVGVTGESGAGKSSLINALrgLGAEdpgAALTGVVE-TTMQPSPY--PHPQFPDVTLWDLPGAG 114
Cdd:COG3596    27 AEALERLLVELPPPV--IALVGKTGAGKSSLINAL--FGAE---VAEVGVGRpCTREIQRYrlESDGLPGLVLLDTPGLG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 115 SPGCSADKYLKQVDF-GRYDFFLLVSP--RRCGAVESRLASEILRQ--GKKFYFVRTKVDEDLAATRSQRPSGFSEAAVL 189
Cdd:COG3596   100 EVNERDREYRELRELlPEADLILWVVKadDRALATDEEFLQALRAQypDPPVLVVLTQVDRLEPEREWDPPYNWPSPPKE 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 190 QEIRDHCTERLRVAGVNDPRIFLVS-NLSPTRYDFPMLVTTWEHDLPAHRRH--AGLLSLPDISLEALQKKKDMLQEQ-- 264
Cdd:COG3596   180 QNIRRALEAIAEQLGVPIDRVIPVSaAEDRTGYGLEELVDALAEALPEAKRSrlARLLRAKAIDRYTLLAAAAALLAAal 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277529350 265 ------VLKTALVSGVIQALPVPGLAAAYDDALLIRSLRGYHRSFGLDDDSLAKLAEQV 317
Cdd:COG3596   260 lallalLLAALAAAPVALAGLGPAALKTALVASLAELALRAAAGAAAAAAELSATASAS 318
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 9-74 4.65e-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: 40.99  E-value: 4.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277529350   9 VPEETTILMAKEELEAL--RTAFESGDIPQAASRLRELLANSETTrlevgVTGESGAGKSSLINALRG 74
Cdd:pfam03193  66 LDEEEELEELLKIYRAIgyPVLFVSAKTGEGIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 16-74 1.25e-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: 39.22  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277529350  16 LMAKEELEALRTAFESGDIP----QAASRL---------RELLANSETTRleVGVTGESGAGKSSLINALRG 74
Cdd:cd01859    52 LVPREVLEKWKEVFESEGLPvvyvSARERLgtrilrrtiKELAIDGKPVI--VGVVGYPKVGKSSIINALKG 121
 
Name Accession Description Interval E-value
p47_IIGP_like cd04104
p47 GTPase family includes IGTP, TGTP/Mg21, IRG-47, GTPI, LRG-47, and IIGP1; The p47 GTPase ...
 52-248 9.16e-116

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: 337.76  E-value: 9.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  52 RLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPHPQFPDVTLWDLPGAGSPGCSADKYLKQVDFGR 131
Cdd:cd04104     1 PLNIAVTGESGAGKSSFINALRGIGHEEEGAAPTGVVETTMKRTPYPHPKFPNVTLWDLPGIGSTAFPPDDYLEEMKFSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 132 YDFFLLVSPRRCGAVESRLASEILRQGKKFYFVRTKVDEDLAATRSQRPSGFSEAAVLQEIRDHCTERLRVAGVNDPRIF 211
Cdd:cd04104    81 YDFFIIISSTRFSSNDVKLAKAIQMMGKKFYFVRTKVDSDLSNEQRSKPRSFNKEQVLQQIRDNCLENLQEAGVSEPPVF 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1277529350 212 LVSNLSPTRYDFPMLVTTWEHDLPAHRRHAGLLSLPD 248
Cdd:cd04104   161 LVSNFDPSDYDFPKLRDTLLKDLPAHKRHNFLLSLPN 197
IIGP pfam05049
Interferon-inducible GTPase (IIGP); Interferon-inducible GTPase (IIGP) is thought to play a ...
 20-401 5.97e-108

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: 324.82  E-value: 5.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  20 EELEALRTAFESGDIPQAASRLRELLANSETTRLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPH 99
Cdd:pfam05049   3 EVITLIEKALREGNLQKVVSIIKKAIQEISSAPLKIAVTGDSGNGKSSFINALRGIGHEEDGSAPTGVVETTMKRTPYSH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 100 PQFPDVTLWDLPGAGSPGCSADKYLKQVDFGRYDFFLLVSPRRCGAVESRLASEILRQGKKFYFVRTKVDEDLAATRSQR 179
Cdd:pfam05049  83 PHFPNVVLWDLPGLGATNFTVESYLEEMKFSEYDFFIIISSERFSLNDVKLAKAIQRMGKRFYFVRTKLDSDLSNEQKGK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 180 PSGFSEAAVLQEIRDHCTERLRVAGVNDPRIFLVSNLSPTRYDFPMLVTTWEHDLPAHRRHAGLLSLPDISLEALQKKKD 259
Cdd:pfam05049 163 PQTFPKEKVLQNIQDNCRNNLQKEGVKEPPIFLVSNLDPSHYDFPKLRDTLLKDLPIIKRHNFLLSLPNITDKTIEKKRQ 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 260 MLQEQVLKTALVSGVIQALPVPGLAAAYDDALLIRSLRGYHRSFGLDDDSLAKLAEQVGKQAGDLRSVIRSP-LANEVSP 338
Cdd:pfam05049 243 SLKQKIWLEALKAAAVSIIPSLTFLGDSDLENLEECLKFYRSYFGLDDTSLQQVARDLGIEVDDFKAMLKSPaFFKLTKD 322

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277529350 339 ETVLRLysqssdgAMRVARAFERgipVFGTLVAGGISFGTVYTMLQGCLNEMAEDAQRVRIKA 401
Cdd:pfam05049 323 DSILAR-------LTRYINAFCR---VLGGPLCVNTYLREIYYLRYLFLDIVAEDAKTLLRKI 375
YeeP COG3596
Predicted GTPase [General function prediction only];
38-317 9.97e-16

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 77.88  E-value: 9.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  38 ASRLRELLANSETTRleVGVTGESGAGKSSLINALrgLGAEdpgAALTGVVE-TTMQPSPY--PHPQFPDVTLWDLPGAG 114
Cdd:COG3596    27 AEALERLLVELPPPV--IALVGKTGAGKSSLINAL--FGAE---VAEVGVGRpCTREIQRYrlESDGLPGLVLLDTPGLG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 115 SPGCSADKYLKQVDF-GRYDFFLLVSP--RRCGAVESRLASEILRQ--GKKFYFVRTKVDEDLAATRSQRPSGFSEAAVL 189
Cdd:COG3596   100 EVNERDREYRELRELlPEADLILWVVKadDRALATDEEFLQALRAQypDPPVLVVLTQVDRLEPEREWDPPYNWPSPPKE 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 190 QEIRDHCTERLRVAGVNDPRIFLVS-NLSPTRYDFPMLVTTWEHDLPAHRRH--AGLLSLPDISLEALQKKKDMLQEQ-- 264
Cdd:COG3596   180 QNIRRALEAIAEQLGVPIDRVIPVSaAEDRTGYGLEELVDALAEALPEAKRSrlARLLRAKAIDRYTLLAAAAALLAAal 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277529350 265 ------VLKTALVSGVIQALPVPGLAAAYDDALLIRSLRGYHRSFGLDDDSLAKLAEQV 317
Cdd:COG3596   260 lallalLLAALAAAPVALAGLGPAALKTALVASLAELALRAAAGAAAAAAELSATASAS 318
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 56-219 6.63e-10

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 57.85  E-value: 6.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  56 GVTGESGAGKSSLINALRGlgaeDPGAALTGVVETTMQPSPYP---HPQFPDVTLWDLPGAGSPGCSADKYLKQVDFGRY 132
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLG----GEVGEVSDVPGTTRDPDVYVkelDKGKVKLVLVDTPGLDEFGGLGREELARLLLRGA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 133 DFFLLV----SPRRCGAVESRLASEILRQGKKFYFVRTKVDEdlaatrsqrpsgfseaaVLQEIRDHCTERLRVAGVNDP 208
Cdd:cd00882    77 DLILLVvdstDRESEEDAKLLILRRLRKEGIPIILVGNKIDL-----------------LEEREVEELLRLEELAKILGV 139

                         170
                  ....*....|.
gi 1277529350 209 RIFLVSNLSPT 219
Cdd:cd00882   140 PVFEVSAKTGE 150
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 56-173 1.41e-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: 50.42  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  56 GVTGESGAGKSSLINALRGLgaedPGAALTGVVETTMQPSPYP-HPQFPDVTLWDLPGAGSPGCSADKYLKQVD--FGRY 132
Cdd:cd11383     1 GLMGKTGAGKSSLCNALFGT----EVAAVGDRRPTTRAAQAYVwQTGGDGLVLLDLPGVGERGRRDREYEELYRrlLPEA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1277529350 133 DFFLLVSP---RRCGAVESRLASEILRQGKKFYFVRTKVDEDLA 173
Cdd:cd11383    77 DLVLWLLDaddRALAADHDFYLLPLAGHDAPLLFVLNQVDPVLA 120
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 55-214 3.86e-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: 50.24  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  55 VGVTGESGAGKSSLINALrgLGAEdpgaAL-TGVVETTMQPSpypHPQF---PDVTLWDLPGAGSPGCS----ADKYLKQ 126
Cdd:cd09912     3 LAVVGEFSAGKSTLLNAL--LGEE----VLpTGVTPTTAVIT---VLRYgllKGVVLVDTPGLNSTIEHhteiTESFLPR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350 127 VDFGrydFFLLVSPRRCGAVESRLASEIL-RQGKKFYFVRTKVDedlAATRSQrpsgfsEAAVLQEIRDHCTERLRvaGV 205
Cdd:cd09912    74 ADAV---IFVLSADQPLTESEREFLKEILkWSGKKIFFVLNKID---LLSEEE------LEEVLEYSREELGVLEL--GG 139


                  ....*....
gi 1277529350 206 NDPRIFLVS 214
Cdd:cd09912   140 GEPRIFPVS 148
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 54-167 7.18e-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: 41.84  E-value: 7.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  54 EVGVTGESGAGKSSLINALRGLGAE---DPGaaltgvveTTMQPSPYP-HPQFPDVTLWDLPGAgsPGCSADKYLKQVDF 129
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIvsdYPG--------TTRDPNEGRlELKGKQIILVDTPGL--IEGASEGEGLGRAF 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1277529350 130 ---GRYDFFLLV--SPRRCGAVESRLASEILRQGKKFYFVRTK 167
Cdd:pfam01926  71 laiIEADLILFVvdSEEGITPLDEELLELLRENKKPIILVLNK 113
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
16-88 1.66e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 43.56  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  16 LMAKEELEALRTAFESGDIP---------QAASRLRELLANsETTRLevgvTGESGAGKSSLINALrglgaeDPGAAL-T 85
Cdd:COG1162   126 LADDEELEELLAIYEALGYPvlavsaktgEGLDELRELLKG-KTSVL----VGQSGVGKSTLINAL------LPDADLaT 194


                  ...
gi 1277529350  86 GVV 88
Cdd:COG1162   195 GEI 197
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 16-88 3.20e-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: 42.00  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277529350  16 LMAKEELEALRTAFESGDIP---------QAASRLRELLANsETTrlevGVTGESGAGKSSLINALrglgaeDPGAAL-T 85
Cdd:cd01854    45 LVDDEELEELLEIYEKLGYPvlavsaktgEGLDELRELLKG-KTS----VLVGQSGVGKSTLLNAL------LPELVLaT 113


                  ...
gi 1277529350  86 GVV 88
Cdd:cd01854   114 GEI 116
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 9-74 4.65e-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: 40.99  E-value: 4.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277529350   9 VPEETTILMAKEELEAL--RTAFESGDIPQAASRLRELLANSETTrlevgVTGESGAGKSSLINALRG 74
Cdd:pfam03193  66 LDEEEELEELLKIYRAIgyPVLFVSAKTGEGIEALKELLKGKTTV-----LAGQSGVGKSTLLNALLP 128
CrfC COG0699
Replication fork clamp-binding protein CrfC (dynamin-like GTPase family) [Replication, ...
 21-99 8.82e-04

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


Pssm-ID: 440463 [Multi-domain]  Cd Length: 582  Bit Score: 41.54  E-value: 8.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277529350  21 ELEALRTAFEsgDIPQAASRLRELLANSETTRLEVGVTGESGAGKSSLINALRGLGAEDPGAALTGVVETTMQPSPYPH 99
Cdd:COG0699     3 PVGVLDETIE--DRADLRRRLDQARLDLADPSLRIVMAGTTSQGKSQLVNALLGRRLLPSGAGETTGVPTEIKHAEGSS 79
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 16-74 1.25e-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: 39.22  E-value: 1.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277529350  16 LMAKEELEALRTAFESGDIP----QAASRL---------RELLANSETTRleVGVTGESGAGKSSLINALRG 74
Cdd:cd01859    52 LVPREVLEKWKEVFESEGLPvvyvSARERLgtrilrrtiKELAIDGKPVI--VGVVGYPKVGKSSIINALKG 121
Dynamin_N pfam00350
Dynamin family;
55-109 3.03e-03

Dynamin family;


Pssm-ID: 459775 [Multi-domain]  Cd Length: 168  Bit Score: 38.37  E-value: 3.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277529350  55 VGVTGESGAGKSSLINALrgLGAEDPGaalTGVVETT-------MQPSPYPHPQFPDVTLWD 109
Cdd:pfam00350   1 IAVVGDQSSGKSSVLNAL--LGRDILP---RGPGPTTrrptvlrLGESPGASEGAVKVEYKD 57
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 55-75 8.79e-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: 36.86  E-value: 8.79e-03
                          10        20
                  ....*....|....*....|.
gi 1277529350  55 VGVTGESGAGKSSLINALRGL 75
Cdd:pfam00005  14 LALVGPNGAGKSTLLKLIAGL 34
 
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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