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Conserved domains on  [gi|119395758|ref|NP_005210|]
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protein diaphanous homolog 1 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
769-1145 1.03e-133

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 413.59  E-value: 1.03e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   769 PKKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 848
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDR-GTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   849 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMG 928
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   929 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 1008
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  1009 DTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVE 1088
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119395758  1089 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMF 1145
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 274-464 1.66e-64

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


:

Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 217.14  E-value: 1.66e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   274 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGT--TIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDL 350
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSEndNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   351 REIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 430
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 119395758   431 YKLIEECISQIVLHKNGADPDFKCR-HLQIEIEGL 464
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 84-268 7.17e-42

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


The actual alignment was detected with superfamily member pfam06371:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 152.09  E-value: 7.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    84 LQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYT--SKAGMSQKESSK-----SAMMYIQELRSGL 156
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKDDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   157 RDmplLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEEtaGSYDSRNKHEIIRCLKAFMNNKFGIKTML 235
Cdd:pfam06371   81 IS---SKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQ--EEEDLDREYEILKCLKALMNNKFGLDHVL 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 119395758   236 ETEEGILLLVRAMDPAVPNMMIDAAKLLSALCI 268
Cdd:pfam06371  156 GHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 590-704 8.09e-17

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


:

Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 79.14  E-value: 8.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   590 GDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGdatippppplpeGVGIPSPSSL 669
Cdd:pfam06346    8 GDSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPG------------AASIPPPPPL 75

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 119395758   670 PGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPP 704
Cdd:pfam06346   76 PGSTGIPPPPPLPGGAGIPPPPPPLPGGAGVPPPP 110
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 429-570 1.88e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   429 QYYKLIEECISQIVLHKngadpdFKCRHLQIEIEGLIDQM--------IDKTKVEKSEAKAAELEKKLDS---ELTARHE 497
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395758   498 LQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAI 570
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
769-1145 1.03e-133

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 413.59  E-value: 1.03e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   769 PKKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 848
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDR-GTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   849 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMG 928
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   929 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 1008
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  1009 DTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVE 1088
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119395758  1089 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMF 1145
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 770-1207 2.29e-133

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 413.67  E-value: 2.29e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    770 KKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEdrfENNELFAKLTLTFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 849
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    850 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDE-YDDLAESEQFGVVMG 928
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    929 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 1008
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   1009 DTKSTDQKMTLLHFLAELCENDYpdvlkfpdelahvekasrvsaenlqknldqmkkqisdverdVQNFPAATDEKDKFVE 1088
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   1089 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1168
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352

                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 119395758   1169 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1207
Cdd:smart00498  353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 274-464 1.66e-64

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 217.14  E-value: 1.66e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   274 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGT--TIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDL 350
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSEndNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   351 REIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 430
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 119395758   431 YKLIEECISQIVLHKNGADPDFKCR-HLQIEIEGL 464
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 84-268 7.17e-42

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 152.09  E-value: 7.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    84 LQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYT--SKAGMSQKESSK-----SAMMYIQELRSGL 156
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKDDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   157 RDmplLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEEtaGSYDSRNKHEIIRCLKAFMNNKFGIKTML 235
Cdd:pfam06371   81 IS---SKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQ--EEEDLDREYEILKCLKALMNNKFGLDHVL 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 119395758   236 ETEEGILLLVRAMDPAVPNMMIDAAKLLSALCI 268
Cdd:pfam06371  156 GHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 590-704 8.09e-17

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 79.14  E-value: 8.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   590 GDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGdatippppplpeGVGIPSPSSL 669
Cdd:pfam06346    8 GDSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPG------------AASIPPPPPL 75

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 119395758   670 PGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPP 704
Cdd:pfam06346   76 PGSTGIPPPPPLPGGAGIPPPPPPLPGGAGVPPPP 110
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 429-570 1.88e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   429 QYYKLIEECISQIVLHKngadpdFKCRHLQIEIEGLIDQM--------IDKTKVEKSEAKAAELEKKLDS---ELTARHE 497
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395758   498 LQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAI 570
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 455-569 3.23e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  455 RHLQIEIEGLIDQM-IDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDF---EQKLQDLQGEKDALHSEKQQI 530
Cdd:COG1196   249 EELEAELEELEAELaELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAEL 328

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119395758  531 ATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAA 569
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 497-686 4.94e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  497 ELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSV 576
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  577 PSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGDATIPPPPP 656
Cdd:COG3883   220 AAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAA 299

                         170       180       190
                  ....*....|....*....|....*....|
gi 119395758  657 LPEGVGIPSPSSLPGGTAIPPPPPLPGSAR 686
Cdd:COG3883   300 SGGSGGGSGGAGGVGSGGGAGAVVGGASAG 329
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 475-566 8.91e-04

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 43.09  E-value: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   475 EKSEAKAAELEKKLDSELTARHELQVEMkkmesdFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLtgeVAKLTKE 554
Cdd:pfam04849  141 SETESSCSTPLRRNESFSSLHGCVQLDA------LQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL---MSDCVEQ 211

                           90
                   ....*....|..
gi 119395758   555 LEDAKKEMASLS 566
Cdd:pfam04849  212 LSEANQQMAELS 223
BimA_first NF040984
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ...
 593-670 9.26e-04

trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.


Pssm-ID: 468914 [Multi-domain]  Cd Length: 517  Bit Score: 43.32  E-value: 9.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119395758  593 GTIIP-PPPAPGdsttppppppppppppplpGGVCISSPPSLPGGTAISPPPPlsgdatippppPLPEGVGIPSPSSLP 670
Cdd:NF040984   48 GTNIPvPPPMPG-------------------GGANIPVPPPMPGGGANIPPPP-----------PPPGGIGGATPSPPP 96
46 PHA02562
endonuclease subunit; Provisional
 473-566 2.07e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  473 KVEKSEAKAAELEKKLDSELTARHELQVEMkkmeSDFEQKLQDLQGEKDALHSEKQQIAT---EKQDLEAEVSQL----- 544
Cdd:PHA02562  300 RITKIKDKLKELQHSLEKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITlvdKAKKVKAAIEELqaefv 375

                          90       100
                  ....*....|....*....|....
gi 119395758  545 --TGEVAKLTKELEDAKKEMASLS 566
Cdd:PHA02562  376 dnAEELAKLQDELDKIVKTKSELV 399
BimA_first NF040984
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ...
 628-675 2.12e-03

trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.


Pssm-ID: 468914 [Multi-domain]  Cd Length: 517  Bit Score: 42.17  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 119395758  628 SSPPSLPGGTAISPPPPLSGDatippppplpeGVGIPSPSSLPGGTAI 675
Cdd:NF040984   40 ANPPEPPGGTNIPVPPPMPGG-----------GANIPVPPPMPGGGAN 76
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 471-674 3.12e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  471 KTKVEKSEAKAAELEKKLDseltarhelqvEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAK 550
Cdd:COG3883   139 KADKAELEAKKAELEAKLA-----------ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  551 LTKELEDakkemASLSAAAITVPPSVPSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSP 630
Cdd:COG3883   208 AEAAAAA-----AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAA 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 119395758  631 PSLPGGTAISPPPPLSGDATIPPPPPLPEGVGIPSPSSLPGGTA 674
Cdd:COG3883   283 GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGA 326
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 451-565 3.32e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 3.32e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    451 DFKCRHLQIEIEGL---IDQM-IDKTKVEKSEAKAAELEKKL-DSELTARHELQvEMKKMESDFEQKLQ-DLQGEKDALH 524
Cdd:smart00787  136 EWRMKLLEGLKEGLdenLEGLkEDYKLLMKELELLNSIKPKLrDRKDALEEELR-QLKQLEDELEDCDPtELDRAKEKLK 214

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 119395758    525 SEKQQIATEKQ---DLEAEVSQLTGEVAKLTKELEDAKKEMASL 565
Cdd:smart00787  215 KLLQEIMIKVKkleELEEELQELESKIEDLTNKKSELNTEIAEA 258
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 329-570 4.19e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.57  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  329 DFRVHIRSELMRLglHQVLQDLREIENE---DMRVQLN-----VFDEQGEEDSYDLKGRLDDIRMEMddFNEVFQIllnt 400
Cdd:PTZ00108  901 DYKEFLESETLKE--KDVIVDYRDYSTAntvHFTVKLNdgvleQWEEEGIEKVFKLKSTISTTNMVL--FDENGKI---- 972

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  401 VKDSKAEPhflsILQHLLLVRND-YEARPQYykLIEECISQIVLHKNgadpdfKCRHLQIEIEGLIDqmIDKtkvekseA 479
Cdd:PTZ00108  973 KKYSDALD----ILKEFYLVRLDlYKKRKEY--LLGKLERELARLSN------KVRFIKHVINGELV--ITN-------A 1031

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  480 KAAELEKKLDSELTARHElQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQD----LEAEVSQLTGE-VAKLTKE 554
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFK-DIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydylLSMPIWSLTKEkVEKLNAE 1110

                         250
                  ....*....|....*.
gi 119395758  555 LEDAKKEMASLSAAAI 570
Cdd:PTZ00108 1111 LEKKEKELEKLKNTTP 1126
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
769-1145 1.03e-133

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 413.59  E-value: 1.03e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   769 PKKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 848
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDR-GTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   849 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMG 928
Cdd:pfam02181   79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   929 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 1008
Cdd:pfam02181  155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  1009 DTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVE 1088
Cdd:pfam02181  235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 119395758  1089 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMF 1145
Cdd:pfam02181  315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 770-1207 2.29e-133

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 413.67  E-value: 2.29e-133
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    770 KKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEdrfENNELFAKLTLTFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 849
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    850 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDE-YDDLAESEQFGVVMG 928
Cdd:smart00498   75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    929 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 1008
Cdd:smart00498  155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   1009 DTKSTDQKMTLLHFLAELCENDYpdvlkfpdelahvekasrvsaenlqknldqmkkqisdverdVQNFPAATDEKDKFVE 1088
Cdd:smart00498  235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   1089 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1168
Cdd:smart00498  274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352

                           410       420       430       440
                    ....*....|....*....|....*....|....*....|
gi 119395758   1169 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1207
Cdd:smart00498  353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 274-464 1.66e-64

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 217.14  E-value: 1.66e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   274 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGT--TIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDL 350
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSEndNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   351 REIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 430
Cdd:pfam06367   81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 119395758   431 YKLIEECISQIVLHKNGADPDFKCR-HLQIEIEGL 464
Cdd:pfam06367  161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 84-268 7.17e-42

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 152.09  E-value: 7.17e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    84 LQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYT--SKAGMSQKESSK-----SAMMYIQELRSGL 156
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKDDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   157 RDmplLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEEtaGSYDSRNKHEIIRCLKAFMNNKFGIKTML 235
Cdd:pfam06371   81 IS---SKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQ--EEEDLDREYEILKCLKALMNNKFGLDHVL 155

                          170       180       190
                   ....*....|....*....|....*....|...
gi 119395758   236 ETEEGILLLVRAMDPAVPNMMIDAAKLLSALCI 268
Cdd:pfam06371  156 GHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 590-704 8.09e-17

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 79.14  E-value: 8.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   590 GDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGdatippppplpeGVGIPSPSSL 669
Cdd:pfam06346    8 GDSSTIPLPPGACIPTPPPLPGGGGPPPPPPLPGSAAIPPPPPLPGGTSIPPPPPLPG------------AASIPPPPPL 75

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 119395758   670 PGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPP 704
Cdd:pfam06346   76 PGSTGIPPPPPLPGGAGIPPPPPPLPGGAGVPPPP 110
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 567-675 1.67e-08

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 54.88  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   567 AAAITVPPSVPSRAPVPPAPPLPGDSGtIIPPPPAPGDSttppppppppppppplpgGVcISSPPSLPGGTAIS-PPPPL 645
Cdd:pfam06346   54 GTSIPPPPPLPGAASIPPPPPLPGSTG-IPPPPPLPGGA------------------GI-PPPPPPLPGGAGVPpPPPPL 113

                           90       100       110
                   ....*....|....*....|....*....|
gi 119395758   646 SGdatippppplpeGVGIPSPSSLPGGTAI 675
Cdd:pfam06346  114 PG------------GPGIPPPPPFPGGPGI 131
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 429-570 1.88e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   429 QYYKLIEECISQIVLHKngadpdFKCRHLQIEIEGLIDQM--------IDKTKVEKSEAKAAELEKKLDS---ELTARHE 497
Cdd:TIGR02168  292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395758   498 LQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAI 570
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 455-569 3.23e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  455 RHLQIEIEGLIDQM-IDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDF---EQKLQDLQGEKDALHSEKQQI 530
Cdd:COG1196   249 EELEAELEELEAELaELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAEL 328

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 119395758  531 ATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAA 569
Cdd:COG1196   329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 497-686 4.94e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  497 ELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSV 576
Cdd:COG3883   140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  577 PSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGDATIPPPPP 656
Cdd:COG3883   220 AAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAA 299

                         170       180       190
                  ....*....|....*....|....*....|
gi 119395758  657 LPEGVGIPSPSSLPGGTAIPPPPPLPGSAR 686
Cdd:COG3883   300 SGGSGGGSGGAGGVGSGGGAGAVVGGASAG 329
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 455-567 7.52e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   455 RHLQIEIEGL-IDQMIDK-TKVEKSEAKAAELEKKLDSELTARH----ELQVEMKKMESDFEQ---KLQDLQGEKDALHS 525
Cdd:TIGR02168  223 RELELALLVLrLEELREElEELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEElqkELYALANEISRLEQ 302

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 119395758   526 EKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSA 567
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 471-567 1.30e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  471 KTKVEKSEAKAAELEKKLDSELTAR------HELQvEMKKMESDFEQKLQDLQGEKDALHSE----KQQIATEKQDLEAE 540
Cdd:COG1579    65 ELEIEEVEARIKKYEEQLGNVRNNKeyealqKEIE-SLKRRISDLEDEILELMERIEELEEElaelEAELAELEAELEEK 143

                          90       100
                  ....*....|....*....|....*..
gi 119395758  541 VSQLTGEVAKLTKELEDAKKEMASLSA 567
Cdd:COG1579   144 KAELDEELAELEAELEELEAEREELAA 170
Drf_FH1 pfam06346
Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs) ...
 597-766 2.05e-04

Formin Homology Region 1; This region is found in some of the Diaphanous related formins (Drfs). It consists of low complexity repeats of around 12 residues.


Pssm-ID: 461881 [Multi-domain]  Cd Length: 157  Bit Score: 43.32  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   597 PPPPAPGDSTTPPPPppppppppplpGGVCISSPPSLPGGTAISPPPPLSGdatippppplpeGVGIPSPSSLPGgtaip 676
Cdd:pfam06346    2 PPPPLPGDSSTIPLP-----------PGACIPTPPPLPGGGGPPPPPPLPG------------SAAIPPPPPLPG----- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   677 pppplpgsaripppppplpgsagipppppplpgeagmpppppplpggpgipppppfpggpgipppppgmgmpppppfGFG 756
Cdd:pfam06346   54 -----------------------------------------------------------------------------GTS 56

                          170
                   ....*....|
gi 119395758   757 VPAAPVLPFG 766
Cdd:pfam06346   57 IPPPPPLPGA 66
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 473-568 2.31e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.15  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  473 KVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDFEQK-------------------LQDLQGEKDALHSEKQQIATE 533
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyeeqlgnvrnnkeYEALQKEIESLKRRISDLEDE 111

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 119395758  534 KQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAA 568
Cdd:COG1579   112 ILELMERIEELEEELAELEAELAELEAELEEKKAE 146
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 489-569 3.36e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  489 DSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAA 568
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94


                  .
gi 119395758  569 A 569
Cdd:COG3883    95 L 95
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 475-566 8.91e-04

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 43.09  E-value: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   475 EKSEAKAAELEKKLDSELTARHELQVEMkkmesdFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLtgeVAKLTKE 554
Cdd:pfam04849  141 SETESSCSTPLRRNESFSSLHGCVQLDA------LQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL---MSDCVEQ 211

                           90
                   ....*....|..
gi 119395758   555 LEDAKKEMASLS 566
Cdd:pfam04849  212 LSEANQQMAELS 223
BimA_first NF040984
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ...
 593-670 9.26e-04

trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.


Pssm-ID: 468914 [Multi-domain]  Cd Length: 517  Bit Score: 43.32  E-value: 9.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119395758  593 GTIIP-PPPAPGdsttppppppppppppplpGGVCISSPPSLPGGTAISPPPPlsgdatippppPLPEGVGIPSPSSLP 670
Cdd:NF040984   48 GTNIPvPPPMPG-------------------GGANIPVPPPMPGGGANIPPPP-----------PPPGGIGGATPSPPP 96
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
471-567 1.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  471 KTKVEKSEAKAAELEKKLDSELTARHELQVEMKKME---SDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGE 547
Cdd:COG4372    72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151

                          90       100
                  ....*....|....*....|
gi 119395758  548 VAKLTKELEDAKKEMASLSA 567
Cdd:COG4372   152 LKELEEQLESLQEELAALEQ 171
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 475-569 1.29e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  475 EKSEAKAAELEKkLDSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKE 554
Cdd:COG4942    20 DAAAEAEAELEQ-LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90
                  ....*....|....*
gi 119395758  555 LEDAKKEMASLSAAA 569
Cdd:COG4942    99 LEAQKEELAELLRAL 113
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 473-572 1.55e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   473 KVEKSEAKAAELEKKLDselTARHELQvEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLT 552
Cdd:TIGR02168  685 KIEELEEKIAELEKALA---ELRKELE-ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100
                   ....*....|....*....|
gi 119395758   553 KELEDAKKEMASLSAAAITV 572
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEA 780
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
452-567 1.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  452 FKCRHLQIEIEGLIDQMIDKTK-VEKSEAKAAELEKKLDS---ELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEK 527
Cdd:COG4372    38 FELDKLQEELEQLREELEQAREeLEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 119395758  528 QQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSA 567
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
461-565 1.92e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  461 IEGLIDQMIDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKkmESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAE 540
Cdd:COG4717   384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAE 461

                          90       100
                  ....*....|....*....|....*..
gi 119395758  541 VSQL--TGEVAKLTKELEDAKKEMASL 565
Cdd:COG4717   462 LEQLeeDGELAELLQELEELKAELREL 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 476-570 2.05e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  476 KSEAKAAELEKKLDSELTARhELQVEMKKMEsDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKEL 555
Cdd:COG1196   206 ERQAEKAERYRELKEELKEL-EAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283

                          90
                  ....*....|....*
gi 119395758  556 EDAKKEMASLSAAAI 570
Cdd:COG1196   284 EEAQAEEYELLAELA 298
46 PHA02562
endonuclease subunit; Provisional
 473-566 2.07e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.31  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  473 KVEKSEAKAAELEKKLDSELTARHELQVEMkkmeSDFEQKLQDLQGEKDALHSEKQQIAT---EKQDLEAEVSQL----- 544
Cdd:PHA02562  300 RITKIKDKLKELQHSLEKLDTAIDELEEIM----DEFNEQSKKLLELKNKISTNKQSLITlvdKAKKVKAAIEELqaefv 375

                          90       100
                  ....*....|....*....|....
gi 119395758  545 --TGEVAKLTKELEDAKKEMASLS 566
Cdd:PHA02562  376 dnAEELAKLQDELDKIVKTKSELV 399
BimA_first NF040984
trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular ...
 628-675 2.12e-03

trimeric autotransporter actin-nucleating factor BimA; BimA (B. pseudomallei intracellular motility protein A) is a trimeric autotransporter, homologous in its C-terminal half to a number of trimeric autotransporter adhesins. It is a virulence factor that nucleates actin, so that actin polymerization can drive escape by B. pseudomallei out of one cell and into a neighboring cell. HMM NF040983 describes a homolog with similar activity but substantial difference in sequence architecture in the N-terminal region.


Pssm-ID: 468914 [Multi-domain]  Cd Length: 517  Bit Score: 42.17  E-value: 2.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 119395758  628 SSPPSLPGGTAISPPPPLSGDatippppplpeGVGIPSPSSLPGGTAI 675
Cdd:NF040984   40 ANPPEPPGGTNIPVPPPMPGG-----------GANIPVPPPMPGGGAN 76
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 471-570 2.74e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  471 KTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDF---EQKLQDLQGEKDALHSEKQQI-------ATEKQDLEAE 540
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELeelELELEEAQAEEYELLAELARLeqdiarlEERRRELEER 317

                          90       100       110
                  ....*....|....*....|....*....|
gi 119395758  541 VSQLTGEVAKLTKELEDAKKEMASLSAAAI 570
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELE 347
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 471-674 3.12e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  471 KTKVEKSEAKAAELEKKLDseltarhelqvEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAK 550
Cdd:COG3883   139 KADKAELEAKKAELEAKLA-----------ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  551 LTKELEDakkemASLSAAAITVPPSVPSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSP 630
Cdd:COG3883   208 AEAAAAA-----AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAA 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 119395758  631 PSLPGGTAISPPPPLSGDATIPPPPPLPEGVGIPSPSSLPGGTA 674
Cdd:COG3883   283 GGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGA 326
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 451-565 3.32e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 41.16  E-value: 3.32e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758    451 DFKCRHLQIEIEGL---IDQM-IDKTKVEKSEAKAAELEKKL-DSELTARHELQvEMKKMESDFEQKLQ-DLQGEKDALH 524
Cdd:smart00787  136 EWRMKLLEGLKEGLdenLEGLkEDYKLLMKELELLNSIKPKLrDRKDALEEELR-QLKQLEDELEDCDPtELDRAKEKLK 214

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 119395758    525 SEKQQIATEKQ---DLEAEVSQLTGEVAKLTKELEDAKKEMASL 565
Cdd:smart00787  215 KLLQEIMIKVKkleELEEELQELESKIEDLTNKKSELNTEIAEA 258
PRK13729 PRK13729
conjugal transfer pilus assembly protein TraB; Provisional
 463-607 4.16e-03

conjugal transfer pilus assembly protein TraB; Provisional


Pssm-ID: 184281 [Multi-domain]  Cd Length: 475  Bit Score: 41.35  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  463 GLIDQMIDKtKVEKS-----EAKAAELEKKLDselTARHELQVeMKKMESDFEQKLQDLqgekdalhsekqqiatekqdl 537
Cdd:PRK13729   56 GVVDTTFDD-KVRQHattemQVTAAQMQKQYE---EIRRELDV-LNKQRGDDQRRIEKL--------------------- 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119395758  538 EAEVSQLTGEVAKLTKELEDAKKEMASLSAAAitvPPSVPSRAPVPPAPPLPGDSGTIIPPPPA---PGDSTT 607
Cdd:PRK13729  110 GQDNAALAEQVKALGANPVTATGEPVPQMPAS---PPGPEGEPQPGNTPVSFPPQGSVAVPPPTafyPGNGVT 179
PTZ00108 PTZ00108
DNA topoisomerase 2-like protein; Provisional
 329-570 4.19e-03

DNA topoisomerase 2-like protein; Provisional


Pssm-ID: 240271 [Multi-domain]  Cd Length: 1388  Bit Score: 41.57  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  329 DFRVHIRSELMRLglHQVLQDLREIENE---DMRVQLN-----VFDEQGEEDSYDLKGRLDDIRMEMddFNEVFQIllnt 400
Cdd:PTZ00108  901 DYKEFLESETLKE--KDVIVDYRDYSTAntvHFTVKLNdgvleQWEEEGIEKVFKLKSTISTTNMVL--FDENGKI---- 972

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  401 VKDSKAEPhflsILQHLLLVRND-YEARPQYykLIEECISQIVLHKNgadpdfKCRHLQIEIEGLIDqmIDKtkvekseA 479
Cdd:PTZ00108  973 KKYSDALD----ILKEFYLVRLDlYKKRKEY--LLGKLERELARLSN------KVRFIKHVINGELV--ITN-------A 1031

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  480 KAAELEKKLDSELTARHElQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQD----LEAEVSQLTGE-VAKLTKE 554
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFK-DIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydylLSMPIWSLTKEkVEKLNAE 1110

                         250
                  ....*....|....*.
gi 119395758  555 LEDAKKEMASLSAAAI 570
Cdd:PTZ00108 1111 LEKKEKELEKLKNTTP 1126
Spc24 pfam08286
Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved ...
 523-576 4.42e-03

Spc24 subunit of Ndc80; Spc24 is a component of the evolutionarily conserved kinetochore-associated Ndc80 complex and is involved in chromosome segregation


Pssm-ID: 429899 [Multi-domain]  Cd Length: 107  Bit Score: 37.96  E-value: 4.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 119395758   523 LHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSV 576
Cdd:pfam08286    2 LDNEKFRLAKELNDLESELERLESELAKLKEELEELEEQGVEVDEEDERSEDET 55
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 494-569 5.51e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 5.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119395758  494 ARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAA 569
Cdd:COG4942   147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
 467-555 8.04e-03

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 40.43  E-value: 8.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758   467 QMIDKTKVEKSEAKAAeLEKKLDSELTArhELQVEMKKMESdFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTG 546
Cdd:pfam13166  383 EITDNFEEEKNKAKKK-LRLHLVEEFKS--EIDEYKDKYAG-LEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKP 458


                   ....*....
gi 119395758   547 EVAKLTKEL 555
Cdd:pfam13166  459 GADEINKLL 467
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
455-561 8.98e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119395758  455 RHLQIEIEGLIDQMID-KTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATE 533
Cdd:COG4717   135 EALEAELAELPERLEElEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214

                          90       100
                  ....*....|....*....|....*...
gi 119395758  534 KQDLEAEVSQLTGEVAKLTKELEDAKKE 561
Cdd:COG4717   215 LEEAQEELEELEEELEQLENELEAAALE 242
 
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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