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Conserved domains on  [gi|130507340|ref|NP_001076284|]
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uncharacterized protein LOC558037 [Danio rerio]

Protein Classification

septin family protein( domain architecture ID 11107662)

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
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
102-368 2.44e-147

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: 417.86  E-value: 2.44e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  102 GFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHIPVASEKIARTVSITKSTVDIVEEGVNLRLTVIDTPGFGDALDNRES 181
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  182 WKAALRYVNQQMVKYYKDEVGVNRQNIKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKVNIVPVLAKADSLTQKETRN 261
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  262 MKAKILSEIHKHKIKIFQVPECDpDDNHLHRQQDLELKRSIPFAVVGSNTVIESNGRRVRARVYPWGTVEVENPAHSDFV 341
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEE-SDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260
                  ....*....|....*....|....*..
gi 130507340  342 HLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYR 266
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
102-368 2.44e-147

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: 417.86  E-value: 2.44e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  102 GFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHIPVASEKIARTVSITKSTVDIVEEGVNLRLTVIDTPGFGDALDNRES 181
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  182 WKAALRYVNQQMVKYYKDEVGVNRQNIKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKVNIVPVLAKADSLTQKETRN 261
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  262 MKAKILSEIHKHKIKIFQVPECDpDDNHLHRQQDLELKRSIPFAVVGSNTVIESNGRRVRARVYPWGTVEVENPAHSDFV 341
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEE-SDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260
                  ....*....|....*....|....*..
gi 130507340  342 HLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYR 266
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
101-368 2.26e-141

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: 402.69  E-value: 2.26e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 101 RGFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHIPVASEKIARTVSITKSTVDIVEEGVNLRLTVIDTPGFGDALDNRE 180
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 181 SWKAALRYVNQQMVKYYKDEVGVNR-QNIKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKVNIVPVLAKADSLTQKET 259
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 260 RNMKAKILSEIHKHKIKIFQVPECDPDDNhlHRQQDLELKRSIPFAVVGSNTVIESNGRRVRARVYPWGTVEVENPAHSD 339
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEE--EIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                        250       260
                 ....*....|....*....|....*....
gi 130507340 340 FVHLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:cd01850  239 FVKLRNLLIRTHLQDLKETTHNVHYENYR 267
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
85-368 3.91e-113

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 334.68  E-value: 3.91e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  85 VGIVTLPNQVKYKAVKRGFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHI-PVASEKIARTVSITKSTVDIVEEGVNLR 163
Cdd:COG5019    4 VGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIdDIRAEGTSPTLEIKITKAELEEDGFHLN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 164 LTVIDTPGFGDALDNRESWKAALRYVNQQMVKYYKDEVGVNRQN-IKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKV 242
Cdd:COG5019   84 LTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 243 NIVPVLAKADSLTQKETRNMKAKILSEIHKHKIKIFQ--VPECDPDDNHLHRQQdleLKRSIPFAVVGSNTVIESNGRRV 320
Cdd:COG5019  164 NLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpyDPEDDEDESLEENQD---LRSLIPFAIIGSNTEIENGGEQV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 130507340 321 RARVYPWGTVEVENPAHSDFVHLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:COG5019  241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYR 288
 
Name Accession Description Interval E-value
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
102-368 2.44e-147

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: 417.86  E-value: 2.44e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  102 GFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHIPVASEKIARTVSITKSTVDIVEEGVNLRLTVIDTPGFGDALDNRES 181
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  182 WKAALRYVNQQMVKYYKDEVGVNRQNIKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKVNIVPVLAKADSLTQKETRN 261
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  262 MKAKILSEIHKHKIKIFQVPECDpDDNHLHRQQDLELKRSIPFAVVGSNTVIESNGRRVRARVYPWGTVEVENPAHSDFV 341
Cdd:pfam00735 161 FKKRIREEIERQNIPIYHFPDEE-SDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260
                  ....*....|....*....|....*..
gi 130507340  342 HLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYR 266
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
101-368 2.26e-141

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: 402.69  E-value: 2.26e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 101 RGFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHIPVASEKIARTVSITKSTVDIVEEGVNLRLTVIDTPGFGDALDNRE 180
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 181 SWKAALRYVNQQMVKYYKDEVGVNR-QNIKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKVNIVPVLAKADSLTQKET 259
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRnRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 260 RNMKAKILSEIHKHKIKIFQVPECDPDDNhlHRQQDLELKRSIPFAVVGSNTVIESNGRRVRARVYPWGTVEVENPAHSD 339
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEE--EIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCD 238
                        250       260
                 ....*....|....*....|....*....
gi 130507340 340 FVHLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:cd01850  239 FVKLRNLLIRTHLQDLKETTHNVHYENYR 267
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
85-368 3.91e-113

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 334.68  E-value: 3.91e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  85 VGIVTLPNQVKYKAVKRGFVFNLMVVGESGLGKSTLVDTLFLTNLYMDRHI-PVASEKIARTVSITKSTVDIVEEGVNLR 163
Cdd:COG5019    4 VGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDETEIdDIRAEGTSPTLEIKITKAELEEDGFHLN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 164 LTVIDTPGFGDALDNRESWKAALRYVNQQMVKYYKDEVGVNRQN-IKDNRVHCCLYFISPHGHGLRPIDVKFMKALEQKV 242
Cdd:COG5019   84 LTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPkFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSKRV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 243 NIVPVLAKADSLTQKETRNMKAKILSEIHKHKIKIFQ--VPECDPDDNHLHRQQdleLKRSIPFAVVGSNTVIESNGRRV 320
Cdd:COG5019  164 NLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpyDPEDDEDESLEENQD---LRSLIPFAIIGSNTEIENGGEQV 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 130507340 321 RARVYPWGTVEVENPAHSDFVHLRNMLICTHMQDLKHTTHHMLYENYR 368
Cdd:COG5019  241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYR 288
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
109-275 4.02e-08

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: 52.07  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 109 VVGESGLGKSTLVdtlfltNLYMDRHIPVASEKIARTVSITKSTVDIVEEGVNLRLtvIDTPGFGDALDNRESWKAALRY 188
Cdd:cd00882    2 VVGRGGVGKSSLL------NALLGGEVGEVSDVPGTTRDPDVYVKELDKGKVKLVL--VDTPGLDEFGGLGREELARLLL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 189 vnqqmvkyykdevgvnrqnikdNRVHCCLYFISPHGHGL--RPIDVKFMKALEQKVNIVPVLAKADSLTQKETRNMK-AK 265
Cdd:cd00882   74 ----------------------RGADLILLVVDSTDRESeeDAKLLILRRLRKEGIPIILVGNKIDLLEEREVEELLrLE 131
                        170
                 ....*....|
gi 130507340 266 ILSEIHKHKI 275
Cdd:cd00882  132 ELAKILGVPV 141
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
110-281 1.66e-06

YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli YihA, an essential protein involved in cell division control. YihA and its orthologs are small proteins that typically contain less than 200 amino acid residues and consists of the GTPase domain only (some of the eukaryotic homologs contain an N-terminal extension of about 120 residues that might be involved in organellar targeting). Homologs of yihA are found in most Gram-positive and Gram-negative pathogenic bacteria, with the exception of Mycobacterium tuberculosis. The broad-spectrum nature of YihA and its essentiality for cell viability in bacteria make it an attractive antibacterial target.


Pssm-ID: 206665 [Multi-domain]  Cd Length: 170  Bit Score: 47.51  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 110 VGESGLGKSTLVDTLFLTNlymdrhipvaseKIARTVSITKSTVDIVEEGVNLRLTVIDTPGFGDA---LDNRESWKAAL 186
Cdd:cd01876    5 AGRSNVGKSSLINALTNRK------------KLARTSKTPGRTQLINFFNVGDKFRLVDLPGYGYAkvsKEVREKWGKLI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 187 -RYVNqqmvkyykdevgvNRQNIK------DNRvhcclyfisphgHGLRPIDVKFMKALEQ-KVNIVPVLAKADSLTQKE 258
Cdd:cd01876   73 eEYLE-------------NRENLKgvvlliDAR------------HGPTPIDLEMLEFLEElGIPFLIVLTKADKLKKSE 127
                        170       180
                 ....*....|....*....|...
gi 130507340 259 TRNMKAKILSEIHKHKIKIFQVP 281
Cdd:cd01876  128 LAKVLKKIKEELNLFNILPPVIL 150
YeeP COG3596
Predicted GTPase [General function prediction only];
105-191 5.30e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 47.84  E-value: 5.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 105 FNLMVVGESGLGKSTLVDTLFLtnlymdrhipvasEKIARTVSITKSTVDI----VEEGVNLRLTVIDTPGFGDALDNRE 180
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFG-------------AEVAEVGVGRPCTREIqryrLESDGLPGLVLLDTPGLGEVNERDR 106
                         90
                 ....*....|.
gi 130507340 181 SWKAALRYVNQ 191
Cdd:COG3596  107 EYRELRELLPE 117
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
98-219 2.92e-05

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: 45.00  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  98 AVKRGFVF--NLMVVGESGLGKSTLVDTLFltnlymdrhipvaSEKIARTVSITKSTVDIVE-EGVN--LRLTVIDTPGF 172
Cdd:cd01853   23 KLKKELDFslTILVLGKTGVGKSSTINSIF-------------GERKVSVSAFQSETLRPREvSRTVdgFKLNIIDTPGL 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 130507340 173 GDALDNreswkaalrYVNQQM---VKYYkdevgvnrqnIKDNRVHCCLYF 219
Cdd:cd01853   90 LESQDQ---------RVNRKIlsiIKRF----------LKKKTIDVVLYV 120
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
106-189 1.80e-04

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 42.58  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340 106 NLMVVGESGLGKSTLVDTLFLTNLYMDRHIPV---------ASEKIARTVSITKSTVDIVEEGVnlRLTVIDTPGFGDAL 176
Cdd:cd04170    1 NIALVGHSGSGKTTLAEALLYATGAIDRLGRVedgntvsdyDPEEKKRKMSIETSVAPLEWNGH--KINLIDTPGYADFV 78
                         90
                 ....*....|...
gi 130507340 177 dnRESWkAALRYV 189
Cdd:cd04170   79 --GETL-SALRAV 88
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
86-172 4.31e-04

Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH induces an excess initiation of DNA replication, suggesting that it negatively controls initiation of chromosome replication. The YqeH subfamily is common in eukaryotes and sporadically present in bacteria with probable acquisition by plants from chloroplasts. Proteins of the YqeH family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases.


Pssm-ID: 206748 [Multi-domain]  Cd Length: 191  Bit Score: 41.10  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 130507340  86 GIVTLPNQVKYKAVKRGFVFnlmVVGESGLGKSTLVDTLfltnLYMDRHIPVASEKIAR-TVS-ITKSTVDIVEEGVNLR 163
Cdd:cd01855  110 GVEELIEEIKKLAKYRGDVY---VVGATNVGKSTLINAL----LKSNGGKVQAQALVQRlTVSpIPGTTLGLIKIPLGEG 182

                 ....*....
gi 130507340 164 LTVIDTPGF 172
Cdd:cd01855  183 KKLYDTPGI 191
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
109-171 1.81e-03

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 38.81  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 130507340 109 VVGESGLGKSTLVdtlfltNLYMDRHIPVasEKIARTVSITKSTVDIVEEGVNLRLTVIDTPG 171
Cdd:COG1100    8 VVGTGGVGKTSLV------NRLVGDIFSL--EKYLSTNGVTIDKKELKLDGLDVDLVIWDTPG 62
 
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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