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Conserved domains on  [gi|2130890012|ref|XP_044941764|]
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septin-9 isoform X3 [Mustela putorius furo]

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 ...
287-557 1.43e-173

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: 492.06  E-value: 1.43e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 287 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 366
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 367 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 446
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 447 VYFKQRITADLLSNGIDVYPQKEFDEDPEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 526
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2130890012 527 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 557
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKL 271
PHA03247 super family cl33720
large tegument protein UL36; Provisional
133-265 3.90e-07

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  133 KTPEPAPRRTEITIVKPQESAHRRMESPASKI----PEMPTAPAVDAAPKRVeiQVPKPAEGPASPLPPQtlensehALV 208
Cdd:PHA03247  2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAapapPAVPAGPATPGGPARP--ARPPTTAGPPAPAPPA-------APA 2776
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012  209 SQLQSRLEPKPQPPVVEALPKSQEAPEAAPGCVgdmAETPRDAGLKQAPAPRNEKAP 265
Cdd:PHA03247  2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPA---AVLAPAAALPPAASPAGPLPP 2830
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
287-557 1.43e-173

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: 492.06  E-value: 1.43e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 287 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 366
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 367 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 446
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 447 VYFKQRITADLLSNGIDVYPQKEFDEDPEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 526
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2130890012 527 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 557
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKL 271
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
288-557 2.31e-137

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: 399.75  E-value: 2.31e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 288 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 367
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 368 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 447
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 448 YFKQRITADLLSNGIDVYPQKEFDED-PEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 526
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2130890012 527 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 557
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
269-563 9.56e-128

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 379.36  E-value: 9.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 269 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 347
Cdd:COG5019     2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 348 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 427
Cdd:COG5019    82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 428 VVNIVPVIAKADTLTLEERVYFKQRITADLLSNGIDVYpqKEFD-EDPEDRLVNE--KFREMIPFAVVGSDHEYQVNGKR 504
Cdd:COG5019   162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF--DPYDpEDDEDESLEEnqDLRSLIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2130890012 505 ILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLHEGSNA 563
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNS 298
PHA03247 PHA03247
large tegument protein UL36; Provisional
133-265 3.90e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  133 KTPEPAPRRTEITIVKPQESAHRRMESPASKI----PEMPTAPAVDAAPKRVeiQVPKPAEGPASPLPPQtlensehALV 208
Cdd:PHA03247  2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAapapPAVPAGPATPGGPARP--ARPPTTAGPPAPAPPA-------APA 2776
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012  209 SQLQSRLEPKPQPPVVEALPKSQEAPEAAPGCVgdmAETPRDAGLKQAPAPRNEKAP 265
Cdd:PHA03247  2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPA---AVLAPAAALPPAASPAGPLPP 2830
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
290-357 1.43e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 48.52  E-value: 1.43e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 290 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 357
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
PLN03118 PLN03118
Rab family protein; Provisional
291-357 7.89e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.19  E-value: 7.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012 291 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 357
Cdd:PLN03118   15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
287-557 1.43e-173

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: 492.06  E-value: 1.43e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 287 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 366
Cdd:cd01850     1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 367 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 446
Cdd:cd01850    81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 447 VYFKQRITADLLSNGIDVYPQKEFDEDPEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 526
Cdd:cd01850   161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2130890012 527 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 557
Cdd:cd01850   241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKL 271
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
288-557 2.31e-137

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: 399.75  E-value: 2.31e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 288 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 367
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 368 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 447
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 448 YFKQRITADLLSNGIDVYPQKEFDED-PEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 526
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDeDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2130890012 527 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 557
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
269-563 9.56e-128

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 379.36  E-value: 9.56e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 269 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 347
Cdd:COG5019     2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 348 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 427
Cdd:COG5019    82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 428 VVNIVPVIAKADTLTLEERVYFKQRITADLLSNGIDVYpqKEFD-EDPEDRLVNE--KFREMIPFAVVGSDHEYQVNGKR 504
Cdd:COG5019   162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVF--DPYDpEDDEDESLEEnqDLRSLIPFAIIGSNTEIENGGEQ 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2130890012 505 ILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLHEGSNA 563
Cdd:COG5019   240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLSGLKNS 298
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
295-466 3.36e-09

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: 55.93  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 295 VVGQSGLGKSTLINTLFKSKISrksvqPTSEERIPkTIEIKSITHDIEEKGVrmKLTVIDTPGFGDhinnencwqpimkf 374
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVG-----EVSDVPGT-TRDPDVYVKELDKGKV--KLVLVDTPGLDE-------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 375 indqyEKYLQEEvninRKKRIPDTRVHCCLYFIPATGH-SLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEERVYFKQR 452
Cdd:cd00882    60 -----FGGLGRE----ELARLLLRGADLILLVVDSTDReSEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRL 130
                         170
                  ....*....|....
gi 2130890012 453 ITAdLLSNGIDVYP 466
Cdd:cd00882   131 EEL-AKILGVPVFE 143
YeeP COG3596
Predicted GTPase [General function prediction only];
276-360 5.28e-09

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 57.85  E-value: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 276 ILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVqptseeRIPKTIEIKSITHDIEEKGVrmkLTVIDT 355
Cdd:COG3596    25 LLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAEVGV------GRPCTREIQRYRLESDGLPG---LVLLDT 95

                  ....*
gi 2130890012 356 PGFGD 360
Cdd:COG3596    96 PGLGE 100
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
252-406 5.88e-08

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: 53.86  E-value: 5.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 252 GLKQAPAPRNEKApadfgyvgidsiLEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLF---KSKISRKSVQPTSEERI 328
Cdd:cd01853     5 GFQFFPDATQTKL------------HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFgerKVSVSAFQSETLRPREV 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 329 PKTIeiksithdieeKGVrmKLTVIDTPGFgdhinNENCWQPIMKFINDQYEKYLqeevninrKKRIPDtrvhCCLYF 406
Cdd:cd01853    73 SRTV-----------DGF--KLNIIDTPGL-----LESQDQRVNRKILSIIKRFL--------KKKTID----VVLYV 120
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
291-466 3.36e-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: 50.62  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 291 FNIMVVGQSGLGKSTLINTLFkskisRKSVQPTSEerIPKTIEIKSITHDIeEKGVrmklTVIDTPGFGDHINNencwqp 370
Cdd:cd09912     1 FLLAVVGEFSAGKSTLLNALL-----GEEVLPTGV--TPTTAVITVLRYGL-LKGV----VLVDTPGLNSTIEH------ 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 371 imkfindqyekyLQEEVninrKKRIPdtRVHCCLYFIPAtGHSLRPLDIEFMKRLSKVV--NIVPVIAKADTLT---LEE 445
Cdd:cd09912    63 ------------HTEIT----ESFLP--RADAVIFVLSA-DQPLTESEREFLKEILKWSgkKIFFVLNKIDLLSeeeLEE 123
                         170       180
                  ....*....|....*....|...
gi 2130890012 446 RVYFKQRITA--DLLSNGIDVYP 466
Cdd:cd09912   124 VLEYSREELGvlELGGGEPRIFP 146
PHA03247 PHA03247
large tegument protein UL36; Provisional
133-265 3.90e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.40  E-value: 3.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  133 KTPEPAPRRTEITIVKPQESAHRRMESPASKI----PEMPTAPAVDAAPKRVeiQVPKPAEGPASPLPPQtlensehALV 208
Cdd:PHA03247  2706 PTPEPAPHALVSATPLPPGPAAARQASPALPAapapPAVPAGPATPGGPARP--ARPPTTAGPPAPAPPA-------APA 2776
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012  209 SQLQSRLEPKPQPPVVEALPKSQEAPEAAPGCVgdmAETPRDAGLKQAPAPRNEKAP 265
Cdd:PHA03247  2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPA---AVLAPAAALPPAASPAGPLPP 2830
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
292-435 9.37e-07

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 47.61  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 292 NIMVVGQSGLGKSTLINTLF--KSKISRKSvqptseeriPKTIEIksITHDIEEKGVRMKLtvIDTPGFgdhinnencwq 369
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL----------- 56
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2130890012 370 pimkfindqYEKYLQEEVNINRKKRIpdTRVHCCLYFIPATgHSLRPLDIEFMKRLSKvvNIVPVI 435
Cdd:pfam01926  57 ---------IEGASEGEGLGRAFLAI--IEADLILFVVDSE-EGITPLDEELLELLRE--NKKPII 108
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
290-357 1.43e-06

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 48.52  E-value: 1.43e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 290 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 357
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
272-372 1.03e-05

ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of GTPases involved in ribosome biogenesis. Like YqlF, it shows a cyclical permutation relative to GTPases EngA (in which the GTPase domain is duplicated), Era, and others. Members of this protein family are found in a relatively small number of bacterial species, including Bacillus subtilis but not Escherichia coli. [Protein synthesis, Other]


Pssm-ID: 213834 [Multi-domain]  Cd Length: 360  Bit Score: 48.00  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 272 GIDSILEQMRRKAMKQgfefNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSeeRIPKTieiksiTHDIEEKGVRMKLT 351
Cdd:TIGR03597 140 GIDELLDKIKKARNKK----DVYVVGVTNVGKSSLINKLLKQNNGDKDVITTS--PFPGT------TLDLIEIPLDDGHS 207
                          90       100
                  ....*....|....*....|....*.
gi 2130890012 352 VIDTPGFGD-----HINNENCWQPIM 372
Cdd:TIGR03597 208 LYDTPGIINshqmaHYLDKKDLKYIT 233
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
272-358 1.30e-05

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: 46.10  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 272 GIDSILEQMRRKAMKQGfefNIMVVGQSGLGKSTLINTLFKSKisRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLT 351
Cdd:cd01855   110 GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSN--GGKVQAQALVQRLTVSPIPGTTLGLIKIPLGEGKK 184

                  ....*..
gi 2130890012 352 VIDTPGF 358
Cdd:cd01855   185 LYDTPGI 191
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
289-462 3.59e-05

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 44.59  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 289 FEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPtseeripkTIEIKSITHDIEEKGVRMKLTVIDTPGfgdhinnencw 368
Cdd:COG1100     2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--------TNGVTIDKKELKLDGLDVDLVIWDTPG----------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 369 QPIMKFINDQYEKYLQEevninrkkripdtrVHCCLYFI----PATGHSLrPLDIEFMKRLSKVVNIVPVIAKADtLTLE 444
Cdd:COG1100    63 QDEFRETRQFYARQLTG--------------ASLYLFVVdgtrEETLQSL-YELLESLRRLGKKSPIILVLNKID-LYDE 126
                         170
                  ....*....|....*...
gi 2130890012 445 ERVYFKQRITADLLSNGI 462
Cdd:COG1100   127 EEIEDEERLKEALSEDNI 144
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
292-357 4.94e-05

AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.


Pssm-ID: 398307 [Multi-domain]  Cd Length: 200  Bit Score: 44.52  E-value: 4.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130890012 292 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVQPTSEE--RIPKTIEIKsithdieekgvrmkltVIDTPG 357
Cdd:pfam04548   2 RIVLVGKTGNGKSATGNSIlgrkaFESKLRAQGVTKTCQLvsRTWDGRIIN----------------VIDTPG 58
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
296-359 5.73e-05

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: 43.10  E-value: 5.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130890012 296 VGQSGLGKSTLINTLFKSKISRKSVqptseeRIPKTIEIKSITHDIEEKGvrmkLTVIDTPGFG 359
Cdd:cd11383     3 MGKTGAGKSSLCNALFGTEVAAVGD------RRPTTRAAQAYVWQTGGDG----LVLLDLPGVG 56
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
272-358 1.09e-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: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 272 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSEERipktieiKSI-------TH----D 340
Cdd:cd01854    75 GLDELRELLKGK--------TSVLVGQSGVGKSTLLNALLP-----ELVLATGEIS-------EKLgrgrhttTHrelfP 134
                          90
                  ....*....|....*...
gi 2130890012 341 IEEKGVrmkltVIDTPGF 358
Cdd:cd01854   135 LPGGGL-----IIDTPGF 147
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
289-375 1.18e-04

chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K protein originally described is proposed to have three domains. The N-terminal A-domain is acidic, repetitive, weakly conserved, readily removed by proteolysis during chloroplast isolation, and not required for protein translocation. The other domains are designated G (GTPase) and M (membrane anchor); this family includes most of the G domain and all of M. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273381 [Multi-domain]  Cd Length: 763  Bit Score: 44.94  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 289 FEFNIMVVGQSGLGKSTLINTLF-KSKISRKSVQPTSeeripktieiKSIThDIEEKGVRMKLTVIDTPGF----GDHIN 363
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFgEVKFSTDAFGMGT----------TSVQ-EIEGLVQGVKIRVIDTPGLkssaSDQSK 185
                          90
                  ....*....|..
gi 2130890012 364 NENCWQPIMKFI 375
Cdd:TIGR00993 186 NEKILSSVKKFI 197
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
295-360 1.64e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 42.23  E-value: 1.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012 295 VVGQSGLGKSTLINTLFKSKISRKSVQP-TSEERIPKTIEIKSIThdieekgvrmKLTVIDTPGFGD 360
Cdd:cd00880     2 IFGRPNVGKSSLLNALLGQNVGIVSPIPgTTRDPVRKEWELLPLG----------PVVLIDTPGLDE 58
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
273-357 1.95e-04

Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. The YlqF subfamily is represented in all eukaryotes as well as a phylogenetically diverse array of bacteria (including gram-positive bacteria, proteobacteria, Synechocystis, Borrelia, and Thermotoga).


Pssm-ID: 206749 [Multi-domain]  Cd Length: 171  Bit Score: 42.13  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 273 IDSILEQMRRKAMKQGF--EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQP--TseeripKTIEIKSITHDIEekgvrm 348
Cdd:cd01856    96 AKKLLKENEKLKAKGLLprPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPgvT------RGQQWIRIGPNIE------ 163

                  ....*....
gi 2130890012 349 kltVIDTPG 357
Cdd:cd01856   164 ---LLDTPG 169
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
293-446 2.66e-04

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: 41.73  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 293 IMVVGQSGLGKSTLINTLFKskisRKSVQPTSeeRIP-KTIEIksITHDIEEkgvrmKLTVIDTPGFG----DHINNENc 367
Cdd:cd01876     2 VAFAGRSNVGKSSLINALTN----RKKLARTS--KTPgRTQLI--NFFNVGD-----KFRLVDLPGYGyakvSKEVREK- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 368 WQPIMkfindqyEKYLQEEVNINRkkripdtrvhccLYFIPATGHSLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEER 446
Cdd:cd01876    68 WGKLI-------EEYLENRENLKG------------VVLLIDARHGPTPIDLEMLEFLEELgIPFLIVLTKADKLKKSEL 128
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
293-487 3.14e-04

GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other bacteria. It plays a role in ribosome biogenesis. Few bacteria lack this protein. [Protein synthesis, Other]


Pssm-ID: 129528 [Multi-domain]  Cd Length: 270  Bit Score: 42.76  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 293 IMVVGQSGLGKSTLINTLFKSKISRKSvqptseeRIPKTIEIKSITHDIEEKGvrmKLTVIDTPGFGD--HINNENCWQP 370
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITS-------PKAQTTRNRISGIHTTGAS---QIIFIDTPGFHEkkHSLNRLMMKE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 371 IMK---------FINDQYEKYLQEE--VNINRKKRIPdtrVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIA--K 437
Cdd:TIGR00436  73 ARSaiggvdlilFVVDSDQWNGDGEfvLTKLQNLKRP---VVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPISAltG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2130890012 438 ADTLTLEERVYFKqritadlLSNGIDVYPQKEFDEDPEDRLVNEKFREMI 487
Cdd:TIGR00436 150 DNTSFLAAFIEVH-------LPEGPFRYPEDYVTDQPDRFKISEIIREKI 192
PHA03247 PHA03247
large tegument protein UL36; Provisional
131-266 4.13e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.77  E-value: 4.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  131 GHKTPEPAPRRTEITIVKPQESAHRRMESP-----ASKIPEMPTAPAV-----------DAAPKRVEIQVPKPAEGPASP 194
Cdd:PHA03247  2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRLgraaqASSPPQRPRRRAArptvgsltslaDPPPPPPTPEPAPHALVSATP 2720
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130890012  195 LPPQTlensehalvsqlQSRLEPKPQPPVVEALPKSQEAPeAAPGCVGDMAETPRDAGLKQAPAPRNEKAPA 266
Cdd:PHA03247  2721 LPPGP------------AAARQASPALPAAPAPPAVPAGP-ATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
285-466 5.23e-04

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 40.91  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 285 MKQGFefnIMVVGQSGLGKSTLINTLFKSKISrksvqPTSeeRIPKTieiksiT-HDIeeKGVRMK----LTVIDTPGfg 359
Cdd:cd04163     1 FKSGF---VAIIGRPNVGKSTLLNALVGQKIS-----IVS--PKPQT------TrNRI--RGIYTDddaqIIFVDTPG-- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 360 dhinnencwqpIMKfindqYEKYLQEEVNINRKKRIPDtrVHCCLYFIPATgHSLRPLDIEFMKRLSKV-VNIVPVIAKA 438
Cdd:cd04163    61 -----------IHK-----PKKKLGERMVKAAWSALKD--VDLVLFVVDAS-EWIGEGDEFILELLKKSkTPVILVLNKI 121
                         170       180
                  ....*....|....*....|....*...
gi 2130890012 439 DTLTLEERVyFKQRITADLLSNGIDVYP 466
Cdd:cd04163   122 DLVKDKEDL-LPLLEKLKELHPFAEIFP 148
PHA03269 PHA03269
envelope glycoprotein C; Provisional
142-270 5.38e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 42.79  E-value: 5.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 142 TEITIVKPQESAHRRMESPA-------SKIPEmptaPAVdaAPKRVEIQVPKPAEGPAsplpPQTLENSEHALVSQLQSR 214
Cdd:PHA03269   24 TNIPIPELHTSAATQKPDPApaphqaaSRAPD----PAV--APTSAASRKPDLAQAPT----PAASEKFDPAPAPHQAAS 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 215 LEPKPQP-PVVEALPKSQ--EAPEAAPGCVGDMAETPRDAGLKQA-PAPRNEKAPADFGY 270
Cdd:PHA03269   94 RAPDPAVaPQLAAAPKPDaaEAFTSAAQAHEAPADAGTSAASKKPdPAAHTQHSPPPFAY 153
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
272-357 6.27e-04

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: 40.76  E-value: 6.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 272 GIDSILEQMRRKAMKqGFEFNIMVVGQSGLGKSTLINTLfkskiSRKSVQPTSeeRIPKtieIKSITHDIEEKGVRMKLT 351
Cdd:cd01859    82 GTRILRRTIKELAID-GKPVIVGVVGYPKVGKSSIINAL-----KGRHSASTS--PIPG---SPGYTKGIQLVRIDSKIY 150

                  ....*.
gi 2130890012 352 VIDTPG 357
Cdd:cd01859   151 LIDTPG 156
PLN03118 PLN03118
Rab family protein; Provisional
291-357 7.89e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.19  E-value: 7.89e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012 291 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 357
Cdd:PLN03118   15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
91-286 9.12e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  91 PKAEPVSR-RTEISIDISSKQVESAGAAGPSRFGLKRAEALGHKTPEPAPRRTEiTIVKPQESAHRRMESPASKIPEMPT 169
Cdd:PRK07003  377 AGAVPAPGaRAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAP-APPATADRGDDAADGDAPVPAKANA 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 170 APAVDAAPKRVEIQ---VPKPAEGPASPLPPQTLENSEHALVSQLQSRLEPKPQPPVVEALPKSQEAPEAAPgcvgdmaE 246
Cdd:PRK07003  456 RASADSRCDERDAQppaDSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAP-------P 528
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2130890012 247 TPRDAglkqAPAPRNEKAPADFGyvGIDSILEQMRRKAMK 286
Cdd:PRK07003  529 APEAR----PPTPAAAAPAARAG--GAAAALDVLRNAGMR 562
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
292-360 1.50e-03

AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 (avrRpt2-induced gene 1) that appears to be involved in plant resistance to bacteria. The Arabidopsis disease resistance gene RPS2 is involved in recognition of bacterial pathogens carrying the avirulence gene avrRpt2. AIG1 exhibits RPS2- and avrRpt1-dependent induction early after infection with Pseudomonas syringae carrying avrRpt2. This subfamily also includes IAN-4 protein, which has GTP-binding activity and shares sequence homology with a novel family of putative GTP-binding proteins: the immuno-associated nucleotide (IAN) family. The evolutionary conservation of the IAN family provides a unique example of a plant pathogen response gene conserved in animals. The IAN/IMAP subfamily has been proposed to regulate apoptosis in vertebrates and angiosperm plants, particularly in relation to cancer, diabetes, and infections. The human IAN genes were renamed GIMAP (GTPase of the immunity associated proteins).


Pssm-ID: 206651 [Multi-domain]  Cd Length: 201  Bit Score: 40.21  E-value: 1.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130890012 292 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVqptseeripkTIEIKSITHDIEEKgvrmKLTVIDTPGFGD 360
Cdd:cd01852     2 RLVLVGKTGNGKSATGNTIlgrkvFESKLSASGV----------TKTCQKESAVWDGR----RVNVIDTPGLFD 61
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
292-360 1.50e-03

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: 40.65  E-value: 1.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 292 NIMVVGQSGLGKSTLINT-LFKSK-ISRK-------SVQPTSEERIPKTIEIKSITHDIEEKGVrmKLTVIDTPGFGD 360
Cdd:cd04170     1 NIALVGHSGSGKTTLAEAlLYATGaIDRLgrvedgnTVSDYDPEEKKRKMSIETSVAPLEWNGH--KINLIDTPGYAD 76
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
272-358 1.56e-03

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 40.87  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 272 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSE--ERIPK----TieiksiTH----DI 341
Cdd:COG1162   156 GLDELRELLKGK--------TSVLVGQSGVGKSTLINALLP-----DADLATGEisEKLGRgrhtT------THaelyPL 216
                          90
                  ....*....|....*..
gi 2130890012 342 EEKGVrmkltVIDTPGF 358
Cdd:COG1162   217 PGGGW-----LIDTPGF 228
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
295-358 1.59e-03

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: 39.83  E-value: 1.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 295 VVGQSGLGKSTLINTLfkskisrksvQPTSEERipktieiksiTHDIEEKGVRMKLT--------------VIDTPGF 358
Cdd:pfam03193 111 LAGQSGVGKSTLLNAL----------LPELDLR----------TGEISEKLGRGRHTtthvelfplpggglLIDTPGF 168
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
133-243 2.11e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 133 KTPEPAPRRTEITIVKPQESAHRRMESPASKIPEMPTAPAVDAAPKRV-----EIQVPKPAEGPASPLPPQTLENSEHAL 207
Cdd:PRK14951  379 KTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVaapaaAAPAAAPAAAPAAVALAPAPPAQAAPE 458
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2130890012 208 VSQLQSRLEPKPQPPVVEALPKSQEAPEA-APGCVGD 243
Cdd:PRK14951  459 TVAIPVRVAPEPAVASAAPAPAAAPAAARlTPTEEGD 495
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
114-265 2.33e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  114 AGAAGPSRFGLKRAEALGHKTPEPAPRRTEITIVKPQESAHRRMESPASKIPEMPTAPAVdaapkrveiqvPKPAEGPAS 193
Cdd:PHA03307    57 AGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDP-----------PPPTPPPAS 125
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130890012  194 PLPPQTLENSEhalvsqlqsrlEPKPQPPVVEALPKSQEAPEAAPGCVGDMAETPRDAGLKQAPAPRNEKAP 265
Cdd:PHA03307   126 PPPSPAPDLSE-----------MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAP 186
PRK00098 PRK00098
GTPase RsgA; Reviewed
275-365 2.56e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.19  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 275 SILEQMRRKAMKQGFEFNI-MVVGQSGLGKSTLINTLfkskisrksvqptseerIPKtIEIKsiTHDIEEKGVRMKLT-- 351
Cdd:PRK00098  148 SAKEGEGLDELKPLLAGKVtVLAGQSGVGKSTLLNAL-----------------APD-LELK--TGEISEALGRGKHTtt 207
                          90       100       110
                  ....*....|....*....|....*....|
gi 2130890012 352 ------------VIDTPGFG----DHINNE 365
Cdd:PRK00098  208 hvelydlpggglLIDTPGFSsfglHDLEAE 237
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
33-246 2.76e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.63  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  33 NSTPHRRVQTPVLRATVASStqkfqdlgvknSEPAARHVDSLSQRSPKAALRRVELSGPKAEPVSRRTEISIDISSKQVE 112
Cdd:PRK12323  371 GAGPATAAAAPVAQPAPAAA-----------APAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQA 439
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 113 SAGAAGPSRFGLKRAEAlghkTPEPAPRRTeitIVKPQESAHRRMESPASKIPEMPTAPAVDAAPK----RVEIQVPKPA 188
Cdd:PRK12323  440 SARGPGGAPAPAPAPAA----APAAAARPA---AAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweelPPEFASPAPA 512
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 189 EGPASPLPPQTLENSEHALVSQLQSRLEPKPQPPVVEALPKSQEAPEAAPGCVGDMAE 246
Cdd:PRK12323  513 QPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASA 570
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
75-211 2.90e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.47  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  75 SQRSPKAALRRVELSGPKAEPVSRRteisidisskQVESAGAAGPSrfGLKRAEALGHKTPEPAPRRTEITIVKPQESAH 154
Cdd:PRK14951  373 AAPAEKKTPARPEAAAPAAAPVAQA----------AAAPAPAAAPA--AAASAPAAPPAAAPPAPVAAPAAAAPAAAPAA 440
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2130890012 155 RRMESPASKIPEMPTAPAVDAAPKRVEIQVPKPAEGPASPLPPQ--TLENSE-----HALVSQL 211
Cdd:PRK14951  441 APAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAaaRLTPTEegdvwHATVQQL 504
PRK12727 PRK12727
flagellar biosynthesis protein FlhF;
67-255 3.75e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 237182 [Multi-domain]  Cd Length: 559  Bit Score: 39.97  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  67 AARHVDSLSQRSPKAALRRVELSG-----------PKAEPVSRRTEISIDISSKQ---VESAGAAGPSRFGLKRAEALGH 132
Cdd:PRK12727   43 ASNYDEELVQRALETARSDTPATAaapapapqaptKPAAPVHAPLKLSANANMSQrqrVASAAEDMIAAMALRQPVSVPR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 133 KTPEPAPRRTEITIV-KPQESAH-------RRMESPASKIPE-----MPTAPAVDA---APKRVEIQVPKPAEGPASPLP 196
Cdd:PRK12727  123 QAPAAAPVRAASIPSpAAQALAHaaavrtaPRQEHALSAVPEqlfadFLTTAPVPRapvQAPVVAAPAPVPAIAAALAAH 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2130890012 197 PQTLENSEHALVSQLQSRLEPKPQPPVVEALPKSQEAPEAAPGCVGDMAETP---RDAGLKQ 255
Cdd:PRK12727  203 AAYAQDDDEQLDDDGFDLDDALPQILPPAALPPIVVAPAAPAALAAVAAAAPapqNDEELKQ 264
PHA03378 PHA03378
EBNA-3B; Provisional
116-249 4.46e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 116 AAGPSRFGLKRAEALGHKTPEPAPRRteitiVKPQESAHRRMESPASKIPEMP---TAPAVDAAPKRVEIQVPKPAEGPA 192
Cdd:PHA03378  698 PRAPTPMRPPAAPPGRAQRPAAATGR-----ARPPAAAPGRARPPAAAPGRARppaAAPGRARPPAAAPGRARPPAAAPG 772
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 193 SPLPPQTLENSEhalVSQLQSRLEPKPQPPvVEALPKS-QEAPEAAPGCVGDMAETPR 249
Cdd:PHA03378  773 APTPQPPPQAPP---APQQRPRGAPTPQPP-PQAGPTSmQLMPRAAPGQQGPTKQILR 826
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
89-266 5.20e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  89 SGPKAEPV-SRRTEISIDISSKQVESAGAAGPSRFGLKRAEALGHKTPEPAPrrtEITIVKPQESAHRRMESPASKipem 167
Cdd:PRK12323  379 AAPVAQPApAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAP---EALAAARQASARGPGGAPAPA---- 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 168 PTAPAVDAAPKRVEIQVPKPAEGPASPLPPQTLENSEHAlvsqlqsrlePKPQ-PPVVEALPKSQEAP---EAAPGCVGD 243
Cdd:PRK12323  452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPA----------PADDdPPPWEELPPEFASPapaQPDAAPAGW 521
                         170       180
                  ....*....|....*....|...
gi 2130890012 244 MAETPRDAGLKQAPAPRNEKAPA 266
Cdd:PRK12323  522 VAESIPDPATADPDDAFETLAPA 544
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
131-268 5.97e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 39.70  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 131 GHKTPEPAPRRTEITIVKPQESAHRRMESPASKIPEmPTAPAVDAAPKRVEIQVPKPAEGPASPLPPQTLEnsEHALVSQ 210
Cdd:PRK14951  369 AAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPA-AAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAP--AAAPAAV 445
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2130890012 211 LQSRLEPKPQPPVVEALPKsQEAPEAAPgcvgdmAETPRDAGLKQAPAPRNEKAPADF 268
Cdd:PRK14951  446 ALAPAPPAQAAPETVAIPV-RVAPEPAV------ASAAPAPAAAPAAARLTPTEEGDV 496
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
296-446 7.73e-03

ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase associated with ribosome biogenesis, typified by YsxC from Bacillus subutilis. The family is widely but not universally distributed among bacteria. Members commonly are called EngB based on homology to EngA, one of several other GTPases of ribosome biogenesis. Cutoffs as set find essentially all bacterial members, but also identify large numbers of eukaryotic (probably organellar) sequences. This protein is found in about 80 percent of bacterial genomes. [Protein synthesis, Other]


Pssm-ID: 274670 [Multi-domain]  Cd Length: 179  Bit Score: 37.84  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 296 VGQSGLGKSTLINTLFKSK-ISRKSVQPTseeripKTIEIksITHDIEEkgvrmKLTVIDTPGFG-------DHINnenc 367
Cdd:TIGR03598  24 AGRSNVGKSSLINALTNRKkLARTSKTPG------RTQLI--NFFEVND-----GFRLVDLPGYGyakvskeEKEK---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 368 WQPIMkfindqyEKYLQEEVNInrkkripdtrvhCCLYFIPATGHSLRPLDIEFMKRL-SKVVNIVPVIAKADTLTLEER 446
Cdd:TIGR03598  87 WQKLI-------EEYLEKRENL------------KGVVLLMDIRHPLKELDLEMIEWLrERGIPVLIVLTKADKLKKSEL 147
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
148-266 8.00e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.93  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 148 KPQeSAHRRMESPASKIPEMPTAPAVDA--APKRVEIQVPKPAEGPASPLPPQTLENSEHALVSQLQSRLEPKPQPPVVE 225
Cdd:PRK14951  365 KPA-AAAEAAAPAEKKTPARPEAAAPAAapVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPA 443
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2130890012 226 ALP--KSQEAPEAAPGCVGDMAETPRDAGLKQAPAPRNEKAPA 266
Cdd:PRK14951  444 AVAlaPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAA 486
PHA03247 PHA03247
large tegument protein UL36; Provisional
134-286 8.04e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 8.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  134 TPEPAPRRTEITIvkpQESAHRRMESPASKIPEMPTAPAVDAapkrveiqvpkPAEGPASPLPPQTlensehalvsqlqs 213
Cdd:PHA03247  2570 PPRPAPRPSEPAV---TSRARRPDAPPQSARPRAPVDDRGDP-----------RGPAPPSPLPPDT-------------- 2621
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2130890012  214 rlePKPQPPVVEALPKSQEAPEAAPGCVGDMAETPRDAGLKQAPAPRNEKAPADfgYVGIDSILEQMRRKAMK 286
Cdd:PHA03247  2622 ---HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGR--AAQASSPPQRPRRRAAR 2689
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
115-259 8.67e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.20  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012 115 GAAGPSRFGLKRAEALGHKTPEPAPRRTeitivkPQESAHRRMESPASKIPEmPTAPAVDAAPKRVEIQVPKPAEGPAS- 193
Cdd:PRK07764  366 SASDDERGLLARLERLERRLGVAGGAGA------PAAAAPSAAAAAPAAAPA-PAAAAPAAAAAPAPAAAPQPAPAPAPa 438
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2130890012 194 PLPPQTLENSEHALVSQLQSRLEPKPQP-PVVEALPKSQEAPEAAPGCVGDMAETPRDAglkQAPAP 259
Cdd:PRK07764  439 PAPPSPAGNAPAGGAPSPPPAAAPSAQPaPAPAAAPEPTAAPAPAPPAAPAPAAAPAAP---AAPAA 502
PHA03247 PHA03247
large tegument protein UL36; Provisional
137-266 8.68e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 8.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2130890012  137 PAPRRTEITIVKPQESAHRRMESPASKIPEMPTAPAVDAapkrveiqvPKPAEGPASPLPPQTLENSEHALVSQLQSRLE 216
Cdd:PHA03247  2866 PPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQ---------PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2130890012  217 PKPQPPvVEALPKSQEAPEAAPGC----VGDMAETPRDAGLKQAPAPRNEK-APA 266
Cdd:PHA03247  2937 PRPQPP-LAPTTDPAGAGEPSGAVpqpwLGALVPGRVAVPRFRVPQPAPSReAPA 2990
 
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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