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Conserved domains on  [gi|164698500|ref|NP_001106966|]
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septin-9 isoform e [Homo sapiens]

Protein Classification

septin family protein( domain architecture ID 10110922)

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924|GO:0061640|GO:0060090
PubMed:  14611653|12445407|12111093|17637674|18478031

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 ...
 131-405 1.90e-175

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: 490.91  E-value: 1.90e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 131 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 210
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 211 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 290
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 291 VHFKQRITADLLSNGIDVYPQKEFDEDSEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 370
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 164698500 371 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRLNEGS 405
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
PHA03269 super family cl29788
envelope glycoprotein C; Provisional
 2-114 2.52e-07

envelope glycoprotein C; Provisional


The actual alignment was detected with superfamily member PHA03269:

Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 52.81  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTApspaQTLENSEPAPVSQLQSRLEPKPQ--PPVAEA-TPRSQEAT 78
Cdd:PHA03269  41 DPAPAPHQAASRAPDPAVAPTSAASRKPDLAQAPTP----AASEKFDPAPAPHQAASRAPDPAvaPQLAAApKPDAAEAF 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 164698500  79 EAAPSCVGDMADTPRDAGLKQA-PASRNEKAPVDFGY 114
Cdd:PHA03269 117 TSAAQAHEAPADAGTSAASKKPdPAAHTQHSPPPFAY 153
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 131-405 1.90e-175

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: 490.91  E-value: 1.90e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 131 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 210
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 211 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 290
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 291 VHFKQRITADLLSNGIDVYPQKEFDEDSEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 370
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 164698500 371 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRLNEGS 405
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 132-401 7.40e-140

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: 400.52  E-value: 7.40e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  132 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 211
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  212 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 291
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  292 HFKQRITADLLSNGIDVYPQKEFDEDS-EDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 370
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDEdEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164698500  371 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 401
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 113-419 3.21e-130

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 379.75  E-value: 3.21e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 113 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 191
Cdd:COG5019    2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 192 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 271
Cdd:COG5019   82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 272 VVNIVPVIAKADTLTLEERVHFKQRITADLLSNGIDVYPQKEFDEDSEDRL-VNEKFREMIPFAVVGSDHEYQVNGKRIL 350
Cdd:COG5019  162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLeENQDLRSLIPFAIIGSNTEIENGGEQVR 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698500 351 GRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLnEGSSAMANGMEEKEPEA 419
Cdd:COG5019  242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL-SGLKNSGEPSLKEIHEA 309
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 2-114 2.52e-07

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 52.81  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTApspaQTLENSEPAPVSQLQSRLEPKPQ--PPVAEA-TPRSQEAT 78
Cdd:PHA03269  41 DPAPAPHQAASRAPDPAVAPTSAASRKPDLAQAPTP----AASEKFDPAPAPHQAASRAPDPAvaPQLAAApKPDAAEAF 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 164698500  79 EAAPSCVGDMADTPRDAGLKQA-PASRNEKAPVDFGY 114
Cdd:PHA03269 117 TSAAQAHEAPADAGTSAASKKPdPAAHTQHSPPPFAY 153
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 134-201 1.29e-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: 48.14  E-value: 1.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698500  134 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 201
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
PLN03118 PLN03118
Rab family protein; Provisional
 135-201 5.26e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.19  E-value: 5.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698500 135 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 201
Cdd:PLN03118  15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 4-72 1.02e-03

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 39.37  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698500   4 PASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQlqsrlePKPQPPVAEATP 72
Cdd:COG3147    1 PAEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAA------AAPAAKAAAPAG 63
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 1-79 8.02e-03

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 36.21  E-value: 8.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698500    1 MEPPAskvPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPvsqLQSRLEPKpqPPVAEATPRSQEATE 79
Cdd:pfam12526  38 DPPPP---VGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTGPAG---PPSPLAPP--APAQKPPLPPPRPQR 108
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 131-405 1.90e-175

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: 490.91  E-value: 1.90e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 131 QGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNEN 210
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 211 CWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEER 290
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 291 VHFKQRITADLLSNGIDVYPQKEFDEDSEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 370
Cdd:cd01850  161 TEFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFV 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 164698500 371 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRLNEGS 405
Cdd:cd01850  241 KLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 132-401 7.40e-140

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: 400.52  E-value: 7.40e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  132 GFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENC 211
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  212 WQPIMKFINDQYEKYLQEEVNINRKKRIpDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERV 291
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  292 HFKQRITADLLSNGIDVYPQKEFDEDS-EDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFA 370
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYHFPDEESDEdEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDFL 239

                         250       260       270
                  ....*....|....*....|....*....|.
gi 164698500  371 YLRDLLIRTHMQNIKDITSSIHFEAYRVKRL 401
Cdd:pfam00735 240 KLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 113-419 3.21e-130

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 379.75  E-value: 3.21e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 113 GYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISR-KSVQPTSEERIPKTIEIKSITHDIEEKGVR 191
Cdd:COG5019    2 GYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTSLVDeTEIDDIRAEGTSPTLEIKITKAELEEDGFH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 192 MKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSK 271
Cdd:COG5019   82 LNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLSK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 272 VVNIVPVIAKADTLTLEERVHFKQRITADLLSNGIDVYPQKEFDEDSEDRL-VNEKFREMIPFAVVGSDHEYQVNGKRIL 350
Cdd:COG5019  162 RVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLeENQDLRSLIPFAIIGSNTEIENGGEQVR 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698500 351 GRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLnEGSSAMANGMEEKEPEA 419
Cdd:COG5019  242 GRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL-SGLKNSGEPSLKEIHEA 309
YeeP COG3596
Predicted GTPase [General function prediction only];
85-204 7.19e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 59.78  E-value: 7.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  85 VGDMADTPRDAGLKQAPASRNEKapvdfgyvgIDSILEQMRRKAMkqgfEFNIMVVGQSGLGKSTLINTLFKSKISRKSV 164
Cdd:COG3596    3 TEVSSLTERLEALKRLPQVLREL---------LAEALERLLVELP----PPVIALVGKTGAGKSSLINALFGAEVAEVGV 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 164698500 165 qptseeRIPKTIEIKSITHDIEEKGVrmkLTVIDTPGFGD 204
Cdd:COG3596   70 ------GRPCTREIQRYRLESDGLPG---LVLLDTPGLGE 100
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 139-310 4.49e-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: 55.16  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 139 VVGQSGLGKSTLINTLFKSKISrksvqPTSEERIPkTIEIKSITHDIEEKGVrmKLTVIDTPGFGDhinnencwqpimkf 218
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVG-----EVSDVPGT-TRDPDVYVKELDKGKV--KLVLVDTPGLDE-------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 219 indqyEKYLQEEvninRKKRIPDTRVHCCLYFIPATGH-SLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEERVHFKQR 296
Cdd:cd00882   60 -----FGGLGRE----ELARLLLRGADLILLVVDSTDReSEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRL 130

                        170
                 ....*....|....
gi 164698500 297 ITAdLLSNGIDVYP 310
Cdd:cd00882  131 EEL-AKILGVPVFE 143
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 96-250 1.91e-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: 55.02  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  96 GLKQAPASRNEKApvdfgyvgidsiLEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLF---KSKISRKSVQPTSEERI 172
Cdd:cd01853    5 GFQFFPDATQTKL------------HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFgerKVSVSAFQSETLRPREV 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698500 173 PKTIeiksithdieeKGVrmKLTVIDTPGFgdhinNENCWQPIMKFINDQYEKYLqeevninrKKRIPDtrvhCCLYF 250
Cdd:cd01853   73 SRTV-----------DGF--KLNIIDTPGL-----LESQDQRVNRKILSIIKRFL--------KKKTID----VVLYV 120
PHA03269 PHA03269
envelope glycoprotein C; Provisional
 2-114 2.52e-07

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 52.81  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTApspaQTLENSEPAPVSQLQSRLEPKPQ--PPVAEA-TPRSQEAT 78
Cdd:PHA03269  41 DPAPAPHQAASRAPDPAVAPTSAASRKPDLAQAPTP----AASEKFDPAPAPHQAASRAPDPAvaPQLAAApKPDAAEAF 116

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 164698500  79 EAAPSCVGDMADTPRDAGLKQA-PASRNEKAPVDFGY 114
Cdd:PHA03269 117 TSAAQAHEAPADAGTSAASKKPdPAAHTQHSPPPFAY 153
DLP_2 cd09912
Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The ...
 135-310 4.05e-07

Dynamin-like protein including dynamins, mitofusins, and guanylate-binding proteins; The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. This family also includes bacterial DLPs. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes mitofusins (MFN1 and MFN2 in mammals) that are involved in mitochondrial fusion. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.


Pssm-ID: 206739 [Multi-domain]  Cd Length: 180  Bit Score: 49.85  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 135 FNIMVVGQSGLGKSTLINTLFkskisRKSVQPTSEerIPKTIEIKSITHDIeEKGVrmklTVIDTPGFGDHINNencwqp 214
Cdd:cd09912    1 FLLAVVGEFSAGKSTLLNALL-----GEEVLPTGV--TPTTAVITVLRYGL-LKGV----VLVDTPGLNSTIEH------ 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 215 imkfindqyekyLQEEVninrKKRIPdtRVHCCLYFIPAtGHSLRPLDIEFMKRLSKVV--NIVPVIAKADTLT---LEE 289
Cdd:cd09912   63 ------------HTEIT----ESFLP--RADAVIFVLSA-DQPLTESEREFLKEILKWSgkKIFFVLNKIDLLSeeeLEE 123

                        170       180
                 ....*....|....*....|...
gi 164698500 290 RVHFKQRITA--DLLSNGIDVYP 310
Cdd:cd09912  124 VLEYSREELGvlELGGGEPRIFP 146
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 136-279 6.56e-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: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  136 NIMVVGQSGLGKSTLINTLF--KSKISRKSvqptseeriPKTIEIksITHDIEEKGVRMKLtvIDTPGFgdhinnencwq 213
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL----------- 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698500  214 pimkfindqYEKYLQEEVNINRKKRIpdTRVHCCLYFIPATgHSLRPLDIEFMKRLSKvvNIVPVI 279
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 ...
 134-201 1.29e-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: 48.14  E-value: 1.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698500  134 EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIpktieiksITHDIEEKGVRMKLTVIDTPG 201
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGSITEYYPGTTRNY--------VTTVIEEDGKTYKFNLLDTAG 60
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 116-202 8.66e-06

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: 8.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 116 GIDSILEQMRRKAMKQGfefNIMVVGQSGLGKSTLINTLFKSKisRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLT 195
Cdd:cd01855  110 GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSN--GGKVQAQALVQRLTVSPIPGTTLGLIKIPLGEGKK 184


                 ....*..
gi 164698500 196 VIDTPGF 202
Cdd:cd01855  185 LYDTPGI 191
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
133-306 9.52e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 45.74  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 133 FEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPtseeripkTIEIKSITHDIEEKGVRMKLTVIDTPGfgdhinnencw 212
Cdd:COG1100    2 GEKKIVVVGTGGVGKTSLVNRLVGDIFSLEKYLS--------TNGVTIDKKELKLDGLDVDLVIWDTPG----------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 213 QPIMKFINDQYEKYLQEevninrkkripdtrVHCCLYFI----PATGHSLrPLDIEFMKRLSKVVNIVPVIAKADtLTLE 288
Cdd:COG1100   63 QDEFRETRQFYARQLTG--------------ASLYLFVVdgtrEETLQSL-YELLESLRRLGKKSPIILVLNKID-LYDE 126

                        170
                 ....*....|....*...
gi 164698500 289 ERVHFKQRITADLLSNGI 306
Cdd:COG1100  127 EEIEDEERLKEALSEDNI 144
GTPase_YqeH TIGR03597
ribosome biogenesis GTPase YqeH; This family describes YqeH, a member of a larger family of ...
 116-216 1.21e-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: 47.23  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  116 GIDSILEQMRRKAMKQgfefNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSeeRIPKTieiksiTHDIEEKGVRMKLT 195
Cdd:TIGR03597 140 GIDELLDKIKKARNKK----DVYVVGVTNVGKSSLINKLLKQNNGDKDVITTS--PFPGT------TLDLIEIPLDDGHS 207

                          90       100
                  ....*....|....*....|....*.
gi 164698500  196 VIDTPGFGD-----HINNENCWQPIM 216
Cdd:TIGR03597 208 LYDTPGIINshqmaHYLDKKDLKYIT 233
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
5-109 1.50e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.15  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   5 ASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTA-PSPAQTLENSE-----PAPVSQLQS-RLEPKPQPPVAEATPRSQEA 77
Cdd:PRK07003 396 VPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAaPAPPATADRGDdaadgDAPVPAKANaRASADSRCDERDAQPPADSG 475

                         90       100       110
                 ....*....|....*....|....*....|..
gi 164698500  78 TEAAPScvgdmADTPrdaglkqaPASRNEKAP 109
Cdd:PRK07003 476 SASAPA-----SDAP--------PDAAFEPAP 494
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
3-120 1.87e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.79  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPA-------QTLENSEPAPVSQLQSRLEPKPQP--PVAEATPR 73
Cdd:PRK12323 391 APAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPApealaaaRQASARGPGGAPAPAPAPAAAPAAaaRPAAAGPR 470

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 164698500  74 SQEATEAAPSCVGDMADTPRDAGLKQAPAsrnEKAPVDFGYVGIDSI 120
Cdd:PRK12323 471 PVAAAAAAAPARAAPAAAPAPADDDPPPW---EELPPEFASPAPAQP 514
AIG1 pfam04548
AIG1 family; Arabidopsis protein AIG1 appears to be involved in plant resistance to bacteria.
 136-201 3.17e-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: 3.17e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164698500  136 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVQPTSEE--RIPKTIEIKsithdieekgvrmkltVIDTPG 201
Cdd:pfam04548   2 RIVLVGKTGNGKSATGNSIlgrkaFESKLRAQGVTKTCQLvsRTWDGRIIN----------------VIDTPG 58
YfjP cd11383
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ...
 140-203 3.95e-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: 3.95e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698500 140 VGQSGLGKSTLINTLFKSKISRKSVqptseeRIPKTIEIKSITHDIEEKGvrmkLTVIDTPGFG 203
Cdd:cd11383    3 MGKTGAGKSSLCNALFGTEVAAVGD------RRPTTRAAQAYVWQTGGDG----LVLLDLPGVG 56
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-83 4.67e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    3 PPASKVPEVPTAPATDAAPKRVEIQMPKPaeAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAeatPRSQEATEAAP 82
Cdd:PHA03247 2881 PPVRRLARPAVSRSTESFALPPDQPERPP--QPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLA---PTTDPAGAGEP 2955


                  .
gi 164698500   83 S 83
Cdd:PHA03247 2956 S 2956
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 133-219 4.76e-05

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: 45.71  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  133 FEFNIMVVGQSGLGKSTLINTLF-KSKISRKSVQPTSeeripktieiKSIThDIEEKGVRMKLTVIDTPGF----GDHIN 207
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFgEVKFSTDAFGMGT----------TSVQ-EIEGLVQGVKIRVIDTPGLkssaSDQSK 185

                          90
                  ....*....|..
gi 164698500  208 NENCWQPIMKFI 219
Cdd:TIGR00993 186 NEKILSSVKKFI 197
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 1-109 5.70e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.44  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASKVPEVpTAPATDAAPKRVEIQMPKPAEAPtapSPAQTLENSEPAPVsqlQSRLEPKPQPPVAEATPrsqeaTEA 80
Cdd:PRK14959 397 IPTPGTQGPQG-TAPAAGMTPSSAAPATPAPSAAP---SPRVPWDDAPPAPP---RSGIPPRPAPRMPEASP-----VPG 464

                         90       100
                 ....*....|....*....|....*....
gi 164698500  81 APSCVGDMADTPRDAGLKQAPASRNEKAP 109
Cdd:PRK14959 465 APDSVASASDAPPTLGDPSDTAEHTPSGP 493
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
3-109 5.74e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 45.61  E-value: 5.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQtlenSEPAPVSQLQSRLEP---KPQPPVAEATPRSQEATE 79
Cdd:PRK07003 426 PPAAPAPPATADRGDDAADGDAPVPAKANARASADSRCDE----RDAQPPADSGSASAPasdAPPDAAFEPAPRAAAPSA 501

                         90       100       110
                 ....*....|....*....|....*....|
gi 164698500  80 AAPSCVGDmADTPRDAGLKQAPASRNEKAP 109
Cdd:PRK07003 502 ATPAAVPD-ARAPAAASREDAPAAAAPPAP 530
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 3-88 6.04e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.19  E-value: 6.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAA-PKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAA 81
Cdd:PRK14950 362 PVPAPQPAKPTAAAPSPVrPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEK 441


                 ....*..
gi 164698500  82 PSCVGDM 88
Cdd:PRK14950 442 PKYTPPA 448
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 116-202 7.20e-05

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: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 116 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSEERipktieiKSI-------TH----D 184
Cdd:cd01854   75 GLDELRELLKGK--------TSVLVGQSGVGKSTLLNALLP-----ELVLATGEIS-------EKLgrgrhttTHrelfP 134

                         90
                 ....*....|....*...
gi 164698500 185 IEEKGVrmkltVIDTPGF 202
Cdd:cd01854  135 LPGGGL-----IIDTPGF 147
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 1-105 7.45e-05

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 44.92  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASKVPEVPTAPAtdAAPKRVE-IQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSR----------LEPKPQP-PVA 68
Cdd:PLN03209 380 LKPPTSPIPTPPSSSP--ASSKSVDaVAKPAEPDVVPSPGSASNVPEVEPAQVEAKKTRplspyaryedLKPPTSPsPTA 457

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 164698500  69 EATPRSQEATEAAPSCVGDMAdTPRDAGLKQAPASRN 105
Cdd:PLN03209 458 PTGVSPSVSSTSSVPAVPDTA-PATAATDAAAPPPAN 493
kgd PRK12270
multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine ...
 1-87 9.76e-05

multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit;


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 44.88  E-value: 9.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    1 MEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSqlqsrlePKPQPPVAEATPRSQEATEA 80
Cdd:PRK12270   36 YGPGSTAAPTAAAAAAAAAASAPAAAPAAKAPAAPAPAPPAAAAPAAPPKPAA-------AAAAAAAPAAPPAAAAAAAP 108


                  ....*..
gi 164698500   81 APSCVGD 87
Cdd:PRK12270  109 AAAAVED 115
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 139-204 9.81e-05

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: 42.62  E-value: 9.81e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698500 139 VVGQSGLGKSTLINTLFKSKISRKSVQP-TSEERIPKTIEIKSIThdieekgvrmKLTVIDTPGFGD 204
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVGIVSPIPgTTRDPVRKEWELLPLG----------PVVLIDTPGLDE 58
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 2-95 1.03e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAA 81
Cdd:PRK07764 424 APAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAP 503

                         90
                 ....*....|....
gi 164698500  82 PScvGDMADTPRDA 95
Cdd:PRK07764 504 AG--ADDAATLRER 515
YlqF cd01856
Circularly permuted YlqF GTPase; Proteins of the YlqF family contain all sequence motifs ...
 117-201 1.63e-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: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 117 IDSILEQMRRKAMKQGF--EFNIMVVGQSGLGKSTLINTLFKSKISRKSVQP--TseeripKTIEIKSITHDIEekgvrm 192
Cdd:cd01856   96 AKKLLKENEKLKAKGLLprPLRAMVVGIPNVGKSTLINRLRGKKVAKVGNKPgvT------RGQQWIRIGPNIE------ 163


                 ....*....
gi 164698500 193 kltVIDTPG 201
Cdd:cd01856  164 ---LLDTPG 169
YihA_EngB cd01876
YihA (EngB) GTPase family; The YihA (EngB) subfamily of GTPases is typified by the E. coli ...
 137-290 1.86e-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: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 137 IMVVGQSGLGKSTLINTLFKskisRKSVQPTSeeRIP-KTIEIksITHDIEEkgvrmKLTVIDTPGFG----DHINNENc 211
Cdd:cd01876    2 VAFAGRSNVGKSSLINALTN----RKKLARTS--KTPgRTQLI--NFFNVGD-----KFRLVDLPGYGyakvSKEVREK- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 212 WQPIMkfindqyEKYLQEEVNINRkkripdtrvhccLYFIPATGHSLRPLDIEFMKRLSKV-VNIVPVIAKADTLTLEER 290
Cdd:cd01876   68 WGKLI-------EEYLENRENLKG------------VVLLIDARHGPTPIDLEMLEFLEELgIPFLIVLTKADKLKKSEL 128
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 3-112 2.30e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.55  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTA--PSPAQTLENSEPAPVSQLQSR----LEPKPQPPVA---EATPR 73
Cdd:PRK14951 375 PAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAaaSAPAAPPAAAPPAPVAAPAAAapaaAPAAAPAAVAlapAPPAQ 454

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 164698500  74 SQEATEAAPSCVG---DMADTPRDAGLKQAPASRNEKAPVDF 112
Cdd:PRK14951 455 AAPETVAIPVRVApepAVASAAPAPAAAPAAARLTPTEEGDV 496
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 1-87 2.53e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 43.16  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASKVPEVPTAPATDAAPKRV-----EIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQ 75
Cdd:PRK14951 403 PAAAPAAAASAPAAPPAAAPPAPVaapaaAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAA 482

                         90
                 ....*....|...
gi 164698500  76 EA-TEAAPSCVGD 87
Cdd:PRK14951 483 PAaARLTPTEEGD 495
MJ1464 cd01859
An uncharacterized, circularly permuted subfamily of the Ras GTPases; This family represents ...
 116-201 2.86e-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: 41.15  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 116 GIDSILEQMRRKAMKqGFEFNIMVVGQSGLGKSTLINTLfkskiSRKSVQPTSeeRIPKtieIKSITHDIEEKGVRMKLT 195
Cdd:cd01859   82 GTRILRRTIKELAID-GKPVIVGVVGYPKVGKSSIINAL-----KGRHSASTS--PIPG---SPGYTKGIQLVRIDSKIY 150


                 ....*.
gi 164698500 196 VIDTPG 201
Cdd:cd01859  151 LIDTPG 156
PHA03247 PHA03247
large tegument protein UL36; Provisional
 4-101 4.41e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.00  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    4 PASKVPEVPTAPATDAAPKRVEIQ-MPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEA---TPRSQEATE 79
Cdd:PHA03247 2861 DVRRRPPSRSPAAKPAAPARPPVRrLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpqpPPPPPPRPQ 2940

                          90       100
                  ....*....|....*....|..
gi 164698500   80 AAPSCVGDMADTPRDAGLKQAP 101
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAVPQP 2962
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 2-110 4.49e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    2 EPPASKVPEVPTAPATDAAPKrveiqMPKPAEAPTAPS------PAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQ 75
Cdd:PHA03307   78 EAPANESRSTPTWSLSTLAPA-----SPAREGSPTPPGpsspdpPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASP 152

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 164698500   76 EATEAAPSCVGDMADTPRDAGLKQAPASRNEKAPV 110
Cdd:PHA03307  153 PAAGASPAAVASDAASSRQAALPLSSPEETARAPS 187
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 129-310 4.50e-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: 40.52  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 129 MKQGFefnIMVVGQSGLGKSTLINTLFKSKISrksvqPTSeeRIPKTieiksiT-HDIeeKGVRMK----LTVIDTPGfg 203
Cdd:cd04163    1 FKSGF---VAIIGRPNVGKSTLLNALVGQKIS-----IVS--PKPQT------TrNRI--RGIYTDddaqIIFVDTPG-- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 204 dhinnencwqpIMKfindqYEKYLQEEVNINRKKRIPDtrVHCCLYFIPATgHSLRPLDIEFMKRLSKV-VNIVPVIAKA 282
Cdd:cd04163   61 -----------IHK-----PKKKLGERMVKAAWSALKD--VDLVLFVVDAS-EWIGEGDEFILELLKKSkTPVILVLNKI 121

                        170       180
                 ....*....|....*....|....*...
gi 164698500 283 DTLTLEERVhFKQRITADLLSNGIDVYP 310
Cdd:cd04163  122 DLVKDKEDL-LPLLEKLKELHPFAEIFP 148
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 3-109 4.90e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPkrveiqmPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAAP 82
Cdd:PRK07764 386 GVAGGAGAPAAAAPSAAAA-------APAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP 458

                         90       100
                 ....*....|....*....|....*..
gi 164698500  83 SCVGDMADTPRDAGLKQAPASRNEKAP 109
Cdd:PRK07764 459 AAAPSAQPAPAPAAAPEPTAAPAPAPP 485
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 3-95 4.95e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPT----APATDAAPKRVEIQMPKPAEAP-TAPSPAQTLENSEPAPVSQLQSRLEPKPQP-PVAEATPRSQE 76
Cdd:PRK07764 399 PSAAAAAPAAApapaAAAPAAAAAPAPAAAPQPAPAPaPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPaPAPAAAPEPTA 478

                         90
                 ....*....|....*....
gi 164698500  77 ATEAAPSCVGDMADTPRDA 95
Cdd:PRK07764 479 APAPAPPAAPAPAAAPAAP 497
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-103 5.19e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.62  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    3 PPASKVPEVPTAPATDAAPKRVeiqmPKPAEAPTAPSPAqtlenSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAAP 82
Cdd:PHA03247 2736 PAAPAPPAVPAGPATPGGPARP----ARPPTTAGPPAPA-----PPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPAD 2806

                          90       100
                  ....*....|....*....|.
gi 164698500   83 SCVGDMADTPRDAGlKQAPAS 103
Cdd:PHA03247 2807 PPAAVLAPAAALPP-AASPAG 2826
PLN03118 PLN03118
Rab family protein; Provisional
 135-201 5.26e-04

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 41.19  E-value: 5.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164698500 135 FNIMVVGQSGLGKSTLINTLFKSKIsrKSVQPTseerIPKTIEIKSITHDieekGVRMKLTVIDTPG 201
Cdd:PLN03118  15 FKILLIGDSGVGKSSLLVSFISSSV--EDLAPT----IGVDFKIKQLTVG----GKRLKLTIWDTAG 71
PHA03369 PHA03369
capsid maturational protease; Provisional
 1-90 5.82e-04

capsid maturational protease; Provisional


Pssm-ID: 223061 [Multi-domain]  Cd Length: 663  Bit Score: 42.29  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASKVPEVPTAPATDAAPKRVE-IQMPKPAEAPTAPSPAQTLENSEPAPVSQLQsrlepkPQPPVAEATPRSQEATE 79
Cdd:PHA03369 364 AKVAVIAAPQTHTGPADRQRPQRPDgIPYSVPARSPMTAYPPVPQFCGDPGLVSPYN------PQSPGTSYGPEPVGPVP 437

                         90
                 ....*....|.
gi 164698500  80 AAPSCVGDMAD 90
Cdd:PHA03369 438 PQPTNPYVMPI 448
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
116-202 6.78e-04

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


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 41.25  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 116 GIDSILEQMRRKamkqgfefNIMVVGQSGLGKSTLINTLFKskisrKSVQPTSE--ERIPK----TieiksiTH----DI 185
Cdd:COG1162  156 GLDELRELLKGK--------TSVLVGQSGVGKSTLINALLP-----DADLATGEisEKLGRgrhtT------THaelyPL 216

                         90
                 ....*....|....*..
gi 164698500 186 EEKGVrmkltVIDTPGF 202
Cdd:COG1162  217 PGGGW-----LIDTPGF 228
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
 136-204 7.50e-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: 41.04  E-value: 7.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698500 136 NIMVVGQSGLGKSTLINT-LFKSK-ISRK-------SVQPTSEERIPKTIEIKSITHDIEEKGVrmKLTVIDTPGFGD 204
Cdd:cd04170    1 NIALVGHSGSGKTTLAEAlLYATGaIDRLgrvedgnTVSDYDPEEKKRKMSIETSVAPLEWNGH--KINLIDTPGYAD 76
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 2-114 7.86e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.77  E-value: 7.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKV--PEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATE 79
Cdd:PRK07994 367 EPEVPPQsaAPAASAQATAAPTAAVAPPQAPAVPPPPASAPQQAPAVPLPETTSQLLAARQQLQRAQGATKAKKSEPAAA 446

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 164698500  80 AAPSCVGDMADtpRDAGLKQAPASRNEKAPVDFGY 114
Cdd:PRK07994 447 SRARPVNSALE--RLASVRPAPSALEKAPAKKEAY 479
era TIGR00436
GTP-binding protein Era; Era is an essential GTPase in Escherichia coli and many other ...
 137-331 8.28e-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: 40.83  E-value: 8.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  137 IMVVGQSGLGKSTLINTLFKSKISRKSvqptseeRIPKTIEIKSITHDIEEKGvrmKLTVIDTPGFGD--HINNENCWQP 214
Cdd:TIGR00436   3 VAILGRPNVGKSTLLNQLHGQKISITS-------PKAQTTRNRISGIHTTGAS---QIIFIDTPGFHEkkHSLNRLMMKE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  215 IMK---------FINDQYEKYLQEE--VNINRKKRIPdtrVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPViakaD 283
Cdd:TIGR00436  73 ARSaiggvdlilFVVDSDQWNGDGEfvLTKLQNLKRP---VVLTRNKLDNKFKDKLLPLIDKYAILEDFKDIVPI----S 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 164698500  284 TLTLEERVHFKQRITADlLSNGIDVYPQKEFDEDSEDRLVNEKFREMI 331
Cdd:TIGR00436 146 ALTGDNTSFLAAFIEVH-LPEGPFRYPEDYVTDQPDRFKISEIIREKI 192
AIG1 cd01852
AvrRpt2-Induced Gene 1 (AIG1); This group represents Arabidoposis protein AIG1 ...
 136-204 1.00e-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: 1.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164698500 136 NIMVVGQSGLGKSTLINTL-----FKSKISRKSVqptseeripkTIEIKSITHDIEEKgvrmKLTVIDTPGFGD 204
Cdd:cd01852    2 RLVLVGKTGNGKSATGNTIlgrkvFESKLSASGV----------TKTCQKESAVWDGR----RVNVIDTPGLFD 61
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
3-110 1.01e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.40  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTlensePAPVSQLQSRLEPKPQpPVAEATPRSQEATEAAP 82
Cdd:PRK12323 375 ATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAA-----ARAVAAAPARRSPAPE-ALAAARQASARGPGGAP 448

                         90       100
                 ....*....|....*....|....*...
gi 164698500  83 SCVGDMADTPrdaglkqAPASRNEKAPV 110
Cdd:PRK12323 449 APAPAPAAAP-------AAAARPAAAGP 469
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 4-72 1.02e-03

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 39.37  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698500   4 PASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQlqsrlePKPQPPVAEATP 72
Cdd:COG3147    1 PAEEAAAAPAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAAAA------AAPAAKAAAPAG 63
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 139-202 1.05e-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: 1.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164698500  139 VVGQSGLGKSTLINTLfkskisrksvQPTSEERipktieiksiTHDIEEKGVRMKLT--------------VIDTPGF 202
Cdd:pfam03193 111 LAGQSGVGKSTLLNAL----------LPELDLR----------TGEISEKLGRGRHTtthvelfplpggglLIDTPGF 168
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 2-119 1.09e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    2 EPPAskvPEVPTAPATDAAPKRVEI------------QMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAE 69
Cdd:PHA03307  116 PPPP---TPPPASPPPSPAPDLSEMlrpvgspgpppaASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAE 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 164698500   70 ATPRSQeATEAAPSC------VGDMADTPRDAGLKQAPASRNEKAPVDFGYVGIDS 119
Cdd:PHA03307  193 PPPSTP-PAAASPRPprrsspISASASSPAPAPGRSAADDAGASSSDSSSSESSGC 247
PRK07994 PRK07994
DNA polymerase III subunits gamma and tau; Validated
 1-109 1.16e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236138 [Multi-domain]  Cd Length: 647  Bit Score: 41.00  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASKVPEVPTAPATDAAPK-RVEIQMPKPAEAPTAPSPAQTlenSEPAPVSQLQSRLEPK-PQPPVAEATPRSQEAT 78
Cdd:PRK07994 403 PASAPQQAPAVPLPETTSQLLAaRQQLQRAQGATKAKKSEPAAA---SRARPVNSALERLASVrPAPSALEKAPAKKEAY 479

                         90       100       110
                 ....*....|....*....|....*....|.
gi 164698500  79 EAAPSCVGDMADTPRDAGLKQAPASRNEKAP 109
Cdd:PRK07994 480 RWKATNPVEVKKEPVATPKALKKALEHEKTP 510
PRK00098 PRK00098
GTPase RsgA; Reviewed
 119-209 1.42e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 40.19  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500 119 SILEQMRRKAMKQGFEFNI-MVVGQSGLGKSTLINTLfkskisrksvqptseerIPKtIEIKsiTHDIEEKGVRMKLT-- 195
Cdd:PRK00098 148 SAKEGEGLDELKPLLAGKVtVLAGQSGVGKSTLLNAL-----------------APD-LELK--TGEISEALGRGKHTtt 207

                         90       100       110
                 ....*....|....*....|....*....|
gi 164698500 196 ------------VIDTPGFG----DHINNE 209
Cdd:PRK00098 208 hvelydlpggglLIDTPGFSsfglHDLEAE 237
PRK11901 PRK11901
hypothetical protein; Reviewed
 12-104 1.49e-03

hypothetical protein; Reviewed


Pssm-ID: 237015 [Multi-domain]  Cd Length: 327  Bit Score: 40.44  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  12 PTAPATDAAPKrveiQMPKPAEAPTAPSPAQTLENSEPAPVsqlqsrlePKPQPPVA-EATPRSQEATEAAPScvgdmad 90
Cdd:PRK11901 175 PTAPATVAPSK----GAKVPATAETHPTPPQKPATKKPAVN--------HHKTATVAvPPATSGKPKSGAASA------- 235

                         90
                 ....*....|....
gi 164698500  91 tprdAGLKQAPASR 104
Cdd:PRK11901 236 ----RALSSAPASH 245
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
2-102 1.60e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.63  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPtAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAA 81
Cdd:PRK12323 417 RAVAAAPARRSPAPEALAAARQASARGPGGAPAP-APAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDD 495

                         90       100
                 ....*....|....*....|.
gi 164698500  82 PSCVGDMADTPRDAGLKQAPA 102
Cdd:PRK12323 496 PPPWEELPPEFASPAPAQPDA 516
PRK10905 PRK10905
cell division protein DamX; Validated
 3-103 1.85e-03

cell division protein DamX; Validated


Pssm-ID: 236792 [Multi-domain]  Cd Length: 328  Bit Score: 40.31  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAP--SPAQTLENSEPA------PVSQLQSRLEPKPQPPVAEATPRS 74
Cdd:PRK10905 140 RQTAKTQTAERPATTRPARKQAVIEPKKPQATAKTEpkPVAQTPKRTEPAapvastKAPAATSTPAPKETATTAPVQTAS 219

                         90       100       110
                 ....*....|....*....|....*....|
gi 164698500  75 QEATEAAPSCVGDMADtprDAG-LKQAPAS 103
Cdd:PRK10905 220 PAQTTATPAAGGKTAG---NVGsLKSAPSS 246
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 13-104 2.10e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 40.22  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  13 TAPATDAAPKRVEI-QMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQ--PPVAEATPRSQE------------A 77
Cdd:COG3266  265 SAPATTSLGEQQEVsLPPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAaaPQPTAAKPVVTEtaapaapapeaaA 344

                         90       100
                 ....*....|....*....|....*...
gi 164698500  78 TEAAPSCVGDMADTPRDAG-LKQAPASR 104
Cdd:COG3266  345 AAAAPAAPAVAKKLAADEQwLASQPASH 372
PHA03378 PHA03378
EBNA-3B; Provisional
 1-108 2.48e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.44  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPAS---KVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTlenSEPAPVSQLQSRLEPKPQPPvAEATPRS-QE 76
Cdd:PHA03378 734 ARPPAAapgRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPP---PQAPPAPQQRPRGAPTPQPP-PQAGPTSmQL 809

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 164698500  77 ATEAAPSCVGDMADTPRD---AGLKQA-PASRNEKA 108
Cdd:PHA03378 810 MPRAAPGQQGPTKQILRQlltGGVKRGrPSLKKPAA 845
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 3-83 2.90e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.83  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVPEVPTAPATDAAPKRVE--IQMPKPAEAPTAPSPAQTLENSEPAPVSQLQsrlEPKPQPP-VAEATPRSQEATE 79
Cdd:COG3266  290 AAAAAQPSAVALPAAPAAAAAAAapAEAAAPQPTAAKPVVTETAAPAAPAPEAAAA---AAAPAAPaVAKKLAADEQWLA 366


                 ....
gi 164698500  80 AAPS 83
Cdd:COG3266  367 SQPA 370
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1-111 2.95e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 39.86  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLEnSEPAPVSQLQSRLEPKPQP-PVAEATPRSQEATE 79
Cdd:PRK12323 426 RSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGPR-PVAAAAAAAPARAAPAAAPaPADDDPPPWEELPP 504

                         90       100       110
                 ....*....|....*....|....*....|..
gi 164698500  80 AAPSCVGDMADtPRDAGLKQAPASRNEKAPVD 111
Cdd:PRK12323 505 EFASPAPAQPD-AAPAGWVAESIPDPATADPD 535
PHA03247 PHA03247
large tegument protein UL36; Provisional
 3-83 3.29e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.92  E-value: 3.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500    3 PPASKVPEVPTAPATDAAPKrvEIQMPKPAEAPTAPS----PAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSqeAT 78
Cdd:PHA03247 2760 PPTTAGPPAPAPPAAPAAGP--PRRLTRPAVASLSESreslPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTS--AQ 2835


                  ....*
gi 164698500   79 EAAPS 83
Cdd:PHA03247 2836 PTAPP 2840
flhF PRK06995
flagellar biosynthesis protein FlhF;
11-126 3.74e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 39.56  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  11 VPTAPATDAAPkrveiqMPKPAEAPTAPS-PAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAAPSCVGDMA 89
Cdd:PRK06995  52 APPAAAAPAAA------QPPPAAAPAAVSrPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAA 125

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 164698500  90 DTPRDAGLKQAPASRNEKAPVDFGYVGIDSILEQMRR 126
Cdd:PRK06995 126 ENAARRLARAAAAAPRPRVPADAAAAVADAVKARIER 162
GTPase_YsxC TIGR03598
ribosome biogenesis GTP-binding protein YsxC/EngB; Members of this protein family are a GTPase ...
 140-311 3.86e-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: 38.22  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  140 VGQSGLGKSTLINTLFKSK-ISRKSVQPTseeripKTIEIksITHDIEEkgvrmKLTVIDTPGFG-------DHINnenc 211
Cdd:TIGR03598  24 AGRSNVGKSSLINALTNRKkLARTSKTPG------RTQLI--NFFEVND-----GFRLVDLPGYGyakvskeEKEK---- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500  212 WQPIMkfindqyEKYLQEEVNInrkkripdtrvhCCLYFIPATGHSLRPLDIEFMKRL-SKVVNIVPVIAKADTLTLEER 290
Cdd:TIGR03598  87 WQKLI-------EEYLEKRENL------------KGVVLLMDIRHPLKELDLEMIEWLrERGIPVLIVLTKADKLKKSEL 147

                         170       180
                  ....*....|....*....|.
gi 164698500  291 VHFKQRITADLLSNGIDVYPQ 311
Cdd:TIGR03598 148 NKQLKKIKKALKKDADDPSVQ 168
PRK11633 PRK11633
cell division protein DedD; Provisional
 1-115 3.98e-03

cell division protein DedD; Provisional


Pssm-ID: 236940 [Multi-domain]  Cd Length: 226  Bit Score: 38.45  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   1 MEPPASkvPEVPTAPATDAAPkrvEIQMPKPAEAPTAPSPAQTlENSEPAPVSQLQSRLEPKPQPPVAEAtPRSQEATEA 80
Cdd:PRK11633  55 MMPAAT--QALPTQPPEGAAE---AVRAGDAAAPSLDPATVAP-PNTPVEPEPAPVEPPKPKPVEKPKPK-PKPQQKVEA 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 164698500  81 APscvgdmadTPRDAglkQAPASRNEKAPVDFGYV 115
Cdd:PRK11633 128 PP--------APKPE---PKPVVEEKAAPTGKAYV 151
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
2-98 5.34e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.06  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPKrveiqMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQP----PVAEATPRSQEA 77
Cdd:PRK07003 461 SRCDERDAQPPADSGSASAPA-----SDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREdapaAAAPPAPEARPP 535

                         90       100
                 ....*....|....*....|....*..
gi 164698500  78 TEAA---PSCVGDMA---DTPRDAGLK 98
Cdd:PRK07003 536 TPAAaapAARAGGAAaalDVLRNAGMR 562
PRK14948 PRK14948
DNA polymerase III subunit gamma/tau;
4-90 6.02e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237862 [Multi-domain]  Cd Length: 620  Bit Score: 38.79  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   4 PASKVPEVPTAPATdaAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSrlEPKPQPPVAEATPRSQEATEAAPS 83
Cdd:PRK14948 361 PSAFISEIANASAP--ANPTPAPNPSPPPAPIQPSAPKTKQAATTPSPPPAKAS--PPIPVPAEPTEPSPTPPANAANAP 436


                 ....*..
gi 164698500  84 CVGDMAD 90
Cdd:PRK14948 437 PSLNLEE 443
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 2-54 7.06e-03

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 36.68  E-value: 7.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164698500   2 EPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTlENSEPAPVSQ 54
Cdd:COG3147    8 APAAAAAPAAPAAAAAPAPAAAAAAAAPKPAAKPAAPKPAAA-AAAAPAAKAA 59
PHA03291 PHA03291
envelope glycoprotein I; Provisional
 8-81 7.90e-03

envelope glycoprotein I; Provisional


Pssm-ID: 223033 [Multi-domain]  Cd Length: 401  Bit Score: 38.40  E-value: 7.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164698500   8 VPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVA--EATPRSQEATEAA 81
Cdd:PHA03291 204 VPATPRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPAPPTPGGgeAPPANATPAPEAS 279
DUF3729 pfam12526
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ...
 1-79 8.02e-03

Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.


Pssm-ID: 372164 [Multi-domain]  Cd Length: 115  Bit Score: 36.21  E-value: 8.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164698500    1 MEPPAskvPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPvsqLQSRLEPKpqPPVAEATPRSQEATE 79
Cdd:pfam12526  38 DPPPP---VGDPRPPVVDTPPPVSAVWVLPPPSEPAAPEPDLVPPVTGPAG---PPSPLAPP--APAQKPPLPPPRPQR 108
DedD COG3147
Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, ...
 21-82 8.96e-03

Cell division protein DedD (periplasmic protein involved in septation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442381 [Multi-domain]  Cd Length: 140  Bit Score: 36.29  E-value: 8.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164698500  21 PKRVEIQMPKPAEAPTAPSPAqtlenSEPAPVSQLQSRlEPKPQPPVAEATPRSQEATEAAP 82
Cdd:COG3147    1 PAEEAAAAPAAAAAPAAPAAA-----AAPAPAAAAAAA-APKPAAKPAAPKPAAAAAAAPAA 56
flhF PRK06995
flagellar biosynthesis protein FlhF;
3-99 9.01e-03

flagellar biosynthesis protein FlhF;


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 38.02  E-value: 9.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   3 PPASKVP---EVPTAPATDAAPKRVEiqMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATE 79
Cdd:PRK06995  64 PPPAAAPaavSRPAAPAAEPAPWLVE--HAKRLTAQREQLVARAAAPAAPEAQAPAAPAERAAAENAARRLARAAAAAPR 141

                         90       100
                 ....*....|....*....|
gi 164698500  80 AAPScvGDMADTPRDAGLKQ 99
Cdd:PRK06995 142 PRVP--ADAAAAVADAVKAR 159
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 2-109 9.34e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.43  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164698500   2 EPPASKVPEVPTAPATDAAPkrveiqmPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQP-PVAEATPRSQEATEA 80
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAA-------AAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPaKAGGAAPAAPPPAPA 686

                         90       100
                 ....*....|....*....|....*....
gi 164698500  81 APSCVGDMADTPRDAGLKQAPASRNEKAP 109
Cdd:PRK07764 687 PAAPAAPAGAAPAQPAPAPAATPPAGQAD 715
 
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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