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Conserved domains on  [gi|1954668690|ref|NP_001376600|]
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neuronal-specific septin-3 isoform G [Homo sapiens]

Protein Classification

septin family protein( domain architecture ID 10110922)

septin family protein, a filament-forming cytoskeletal GTPase, is involved in various cellular processes, including cytoskeleton organization, cytokinesis, and membrane dynamics

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
502-767 7.45e-163

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


:

Pssm-ID: 206649  Cd Length: 275  Bit Score: 472.03  E-value: 7.45e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYIN 581
Cdd:cd01850    11 GESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVDYID 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 EQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKE 661
Cdd:cd01850    91 DQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRIMED 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 662 LEVNGIEFYPQKEFDEDLEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRT 741
Cdd:cd01850   171 IEENNIKIYKFPEDEEDEEEIEENKKLK-SLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLIRT 249
                         250       260
                  ....*....|....*....|....*.
gi 1954668690 742 HLQDLKEVTHNIHYETYRAKRLNDNG 767
Cdd:cd01850   250 HLQDLKETTHNVHYENYRSEKLEALK 275
PHA03247 super family cl33720
large tegument protein UL36; Provisional
6-248 7.65e-03

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690    6 APAPPEMQSHGAPGPGTSFSHSHVLGRPIRPSRLPGGGSPLTPVLRKTIhldtfPQSHIPQTSSRLGLGARTRSVPPQET 85
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP-----ARPPTTAGPPAPAPPAAPAAGPPRRL 2783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690   86 GIALGASLSPLPTSSLVPRKLSSISL-TLHQNSQARSLDRPLSHWEELPTPGKKAAPHEGGRVSSPGSPPVTLVPGGRVH 164
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690  165 SEGPGNPGLTKSNrmlATEKPLVSSyLALPFQSRLAQSAPVLA-EPGSLGQGHLVSVTDHMPTRASPGKGKPRARGIPRP 243
Cdd:PHA03247  2864 RRPPSRSPAAKPA---APARPPVRR-LARPAVSRSTESFALPPdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939

                   ....*
gi 1954668690  244 RGRLQ 248
Cdd:PHA03247  2940 QPPLA 2944
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
502-767 7.45e-163

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 472.03  E-value: 7.45e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYIN 581
Cdd:cd01850    11 GESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVDYID 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 EQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKE 661
Cdd:cd01850    91 DQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRIMED 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 662 LEVNGIEFYPQKEFDEDLEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRT 741
Cdd:cd01850   171 IEENNIKIYKFPEDEEDEEEIEENKKLK-SLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLIRT 249
                         250       260
                  ....*....|....*....|....*.
gi 1954668690 742 HLQDLKEVTHNIHYETYRAKRLNDNG 767
Cdd:cd01850   250 HLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
502-763 2.23e-135

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 401.68  E-value: 2.23e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYIN 581
Cdd:pfam00735  10 GESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVEYID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 EQYEKFLKEEVNIARKKRIpDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKE 661
Cdd:pfam00735  90 EQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIREE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 662 LEVNGIEFY--PQKEFDEDlEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVI 739
Cdd:pfam00735 169 IERQNIPIYhfPDEESDED-EEKELNEQLK-SSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFLKLRNMLI 246
                         250       260
                  ....*....|....*....|....
gi 1954668690 740 RTHLQDLKEVTHNIHYETYRAKRL 763
Cdd:pfam00735 247 RTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
502-763 5.08e-122

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 371.27  E-value: 5.08e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLF-KSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYI 580
Cdd:COG5019    30 GESGLGKTTFINTLFgTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIVDYI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 581 NEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRK 660
Cdd:COG5019   110 DDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKERIRE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 661 ELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIR 740
Cdd:COG5019   190 DLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIR 269
                         250       260
                  ....*....|....*....|...
gi 1954668690 741 THLQDLKEVTHNIHYETYRAKRL 763
Cdd:COG5019   270 THLQELKETTENLLYENYRTEKL 292
PHA03247 PHA03247
large tegument protein UL36; Provisional
6-248 7.65e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690    6 APAPPEMQSHGAPGPGTSFSHSHVLGRPIRPSRLPGGGSPLTPVLRKTIhldtfPQSHIPQTSSRLGLGARTRSVPPQET 85
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP-----ARPPTTAGPPAPAPPAAPAAGPPRRL 2783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690   86 GIALGASLSPLPTSSLVPRKLSSISL-TLHQNSQARSLDRPLSHWEELPTPGKKAAPHEGGRVSSPGSPPVTLVPGGRVH 164
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690  165 SEGPGNPGLTKSNrmlATEKPLVSSyLALPFQSRLAQSAPVLA-EPGSLGQGHLVSVTDHMPTRASPGKGKPRARGIPRP 243
Cdd:PHA03247  2864 RRPPSRSPAAKPA---APARPPVRR-LARPAVSRSTESFALPPdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939

                   ....*
gi 1954668690  244 RGRLQ 248
Cdd:PHA03247  2940 QPPLA 2944
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
502-767 7.45e-163

CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.


Pssm-ID: 206649  Cd Length: 275  Bit Score: 472.03  E-value: 7.45e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYIN 581
Cdd:cd01850    11 GESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDCWKPIVDYID 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 EQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKE 661
Cdd:cd01850    91 DQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELTEFKKRIMED 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 662 LEVNGIEFYPQKEFDEDLEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIRT 741
Cdd:cd01850   171 IEENNIKIYKFPEDEEDEEEIEENKKLK-SLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVKLRNLLIRT 249
                         250       260
                  ....*....|....*....|....*.
gi 1954668690 742 HLQDLKEVTHNIHYETYRAKRLNDNG 767
Cdd:cd01850   250 HLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
502-763 2.23e-135

Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.


Pssm-ID: 395596  Cd Length: 272  Bit Score: 401.68  E-value: 2.23e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYIN 581
Cdd:pfam00735  10 GESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNCWRPIVEYID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 EQYEKFLKEEVNIARKKRIpDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRKE 661
Cdd:pfam00735  90 EQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQRFKKRIREE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 662 LEVNGIEFY--PQKEFDEDlEDKTENDKIRqESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVI 739
Cdd:pfam00735 169 IERQNIPIYhfPDEESDED-EEKELNEQLK-SSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFLKLRNMLI 246
                         250       260
                  ....*....|....*....|....
gi 1954668690 740 RTHLQDLKEVTHNIHYETYRAKRL 763
Cdd:pfam00735 247 RTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
502-763 5.08e-122

Septin family protein [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 371.27  E-value: 5.08e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLF-KSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENCWEPIEKYI 580
Cdd:COG5019    30 GESGLGKTTFINTLFgTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGFHLNLTVIDTPGFGDFIDNSKCWEPIVDYI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 581 NEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKSEFKQRVRK 660
Cdd:COG5019   110 DDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRVNLIPVIAKADTLTDDELAEFKERIRE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 661 ELEVNGIEFYPQKEFDEDLEDKTENDKIRQESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFALLRDFVIR 740
Cdd:COG5019   190 DLEQYNIPVFDPYDPEDDEDESLEENQDLRSLIPFAIIGSNTEIENGGEQVRGRKYPWGVVEIDDEEHSDFKKLRNLLIR 269
                         250       260
                  ....*....|....*....|...
gi 1954668690 741 THLQDLKEVTHNIHYETYRAKRL 763
Cdd:COG5019   270 THLQELKETTENLLYENYRTEKL 292
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
502-671 3.27e-07

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: 50.53  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRKasswnrEEKIPKTVEIKAIGHVIEEGGVkmKLTVIDTPGFGDqINNENCWEPIEKYIN 581
Cdd:cd00882     4 GRGGVGKSSLLNALLGGEVGEV------SDVPGTTRDPDVYVKELDKGKV--KLVLVDTPGLDE-FGGLGREELARLLLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 eqyekflkeevniarkkripdtRVHCCLYFISPTGH-SLRPLDLEFMKHLSKV-VNIIPVIAKADTMTLEEKSEFKQRVR 659
Cdd:cd00882    75 ----------------------GADLILLVVDSTDReSEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRLEE 132
                         170
                  ....*....|..
gi 1954668690 660 KELEvNGIEFYP 671
Cdd:cd00882   133 LAKI-LGVPVFE 143
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
502-563 1.54e-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: 43.54  E-value: 1.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668690 502 GQSGLGKSTLVNTLFKsqvsrkasswnrEEKIpKTVEI-KAIG-----------HVIEEGGVkmkltVIDTPGF 563
Cdd:cd01854    92 GQSGVGKSTLLNALLP------------ELVL-ATGEIsEKLGrgrhttthrelFPLPGGGL-----IIDTPGF 147
YeeP COG3596
Predicted GTPase [General function prediction only];
502-641 1.88e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 44.37  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSRkasswnREEKIPKTVEIKAigHVIEEGGVKMkLTVIDTPGFGDQINNEncwepiEKYIn 581
Cdd:COG3596    46 GKTGAGKSSLINALFGAEVAE------VGVGRPCTREIQR--YRLESDGLPG-LVLLDTPGLGEVNERD------REYR- 109
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 582 eQYEKFLKEevniarkkripdtrVHCCLYFISPTGHSLRpLDLEFMKHLSKVVNIIPVIA 641
Cdd:COG3596   110 -ELRELLPE--------------ADLILWVVKADDRALA-TDEEFLQALRAQYPDPPVLV 153
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
502-611 4.07e-04

Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like (Translocon at the Outer-envelope membrane of Chloroplasts) family contains several Toc proteins, including Toc34, Toc33, Toc120, Toc159, Toc86, Toc125, and Toc90. The Toc complex at the outer envelope membrane of chloroplasts is a molecular machine of ~500 kDa that contains a single Toc159 protein, four Toc75 molecules, and four or five copies of Toc34. Toc64 and Toc12 are associated with the translocon, but do not appear to be part of the core complex. The Toc translocon initiates the import of nuclear-encoded preproteins from the cytosol into the organelle. Toc34 and Toc159 are both GTPases, while Toc75 is a beta-barrel integral membrane protein. Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, suggesting that assembly of the Toc complex is dynamic. Toc34 and Toc75 act sequentially to mediate docking and insertion of Toc159 resulting in assembly of the functional translocon.


Pssm-ID: 206652  Cd Length: 248  Bit Score: 42.69  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLF---KSQVSRKASSWNREEKIPKTVeikaighvieeGGVKmkLTVIDTPGF---GDQINNENCWEP 575
Cdd:cd01853    38 GKTGVGKSSTINSIFgerKVSVSAFQSETLRPREVSRTV-----------DGFK--LNIIDTPGLlesQDQRVNRKILSI 104
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1954668690 576 IEKYIneqyekflkeevniarKKRIPDtrvhCCLYF 611
Cdd:cd01853   105 IKRFL----------------KKKTID----VVLYV 120
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
502-640 6.54e-04

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: 39.91  E-value: 6.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690 502 GQSGLGKSTLVNTLF--KSQVSRKAsswnreekiPKTVEIkaIGHVIEEGGVKMKLtvIDTPGFgdqinnencwepieky 579
Cdd:pfam01926   6 GRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL---------------- 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954668690 580 ineqYEKFLKEEVNIARKKRIPDTRVhccLYFISPTGHSLRPLDLEFMKHLSKvvNIIPVI 640
Cdd:pfam01926  57 ----IEGASEGEGLGRAFLAIIEADL---ILFVVDSEEGITPLDEELLELLRE--NKKPII 108
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
502-565 3.31e-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: 39.15  E-value: 3.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668690 502 GQSGLGKSTLVNTLFKSQVSrKASSWNREEKIPKTVEIKaighVIEEGGVkmklTVIDTPGFGD 565
Cdd:cd00880     4 GRPNVGKSSLLNALLGQNVG-IVSPIPGTTRDPVRKEWE----LLPLGPV----VLIDTPGLDE 58
PHA03247 PHA03247
large tegument protein UL36; Provisional
6-248 7.65e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 7.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690    6 APAPPEMQSHGAPGPGTSFSHSHVLGRPIRPSRLPGGGSPLTPVLRKTIhldtfPQSHIPQTSSRLGLGARTRSVPPQET 85
Cdd:PHA03247  2709 EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARP-----ARPPTTAGPPAPAPPAAPAAGPPRRL 2783
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690   86 GIALGASLSPLPTSSLVPRKLSSISL-TLHQNSQARSLDRPLSHWEELPTPGKKAAPHEGGRVSSPGSPPVTLVPGGRVH 164
Cdd:PHA03247  2784 TRPAVASLSESRESLPSPWDPADPPAaVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVR 2863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668690  165 SEGPGNPGLTKSNrmlATEKPLVSSyLALPFQSRLAQSAPVLA-EPGSLGQGHLVSVTDHMPTRASPGKGKPRARGIPRP 243
Cdd:PHA03247  2864 RRPPSRSPAAKPA---APARPPVRR-LARPAVSRSTESFALPPdQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939

                   ....*
gi 1954668690  244 RGRLQ 248
Cdd:PHA03247  2940 QPPLA 2944
 
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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