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Conserved domains on  [gi|205830900|sp|P03528|]
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RecName: Full=Outer capsid protein sigma-1; Short=Sigma1; AltName: Full=Cell attachment protein; AltName: Full=Hemagglutinin

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Reo_sigma1 pfam01664
Reovirus viral attachment protein sigma 1; This family consists of the reovirus sigma 1 ...
 242-454 2.65e-116

Reovirus viral attachment protein sigma 1; This family consists of the reovirus sigma 1 hemagglutinin, cell attachment protein. This glycoprotein is a minor capsid protein and also determines the serotype-specific humoral immune response. Sigma 1 consist of a fibrous tail and a globular head. The head has important roles in the cell attachment function of sigma 1 and determinant of the type-specific humoral immune response. Reovirus is part of the orthoreovirus group of retroviruses with, a dsRNA genome. Also present in this family is bacteriophage SF6 Lysozyme.


:

Pssm-ID: 366748  Cd Length: 216  Bit Score: 339.63  E-value: 2.65e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  242 INSRIGATEQSYVASAVTPLRLNSS--TKVLDMLIDSSTLEI-NSSGQLTVRSTSPNLRYPIADVSGG--IGMSPNYRFR 316
Cdd:pfam01664   1 LNSRIGSLEQSYIDSVVPPLRLNSSsgTRVLDMLYDSSDFEIiNSVLQLRVRSTSPTLRYPLELVSAGnrVGMSPNYRFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  317 QSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHndVVTYGA 396
Cdd:pfam01664  81 QGMWIGQLSYSGPGLNWRAQVTSNLMIVDDWLHLSFPAFDTFSIAAGGKFVLNFVTGLSPGWLTGDTEPSFT--VVPLST 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 205830900  397 QTVAIGLSSGGAPQYMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSF 454
Cdd:pfam01664 159 TFAAIQFSNGGQRQDAFRILGVEEWQDGELEIRNEGGTYTTHTNVKWAPMTIMYPCSF 216
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
62-134 6.52e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 47.13  E-value: 6.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205830900  62 ALEQSRDDLvasvsdAQLAISR---LESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAE 134
Cdd:COG1842   77 ALEKGREDL------AREALERkaeLEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAK 146
Crescentin super family cl41192
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 4-161 4.75e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


The actual alignment was detected with superfamily member pfam19220:

Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 45.44  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    4 RLREEVVRLIiALTSDNGASLSKgLESRVSALEKTsqihsdtilritqgLDDANKRIIALEQSrddLVASVSDAQLAISR 83
Cdd:pfam19220 171 LLEQENRRLQ-ALSEEQAAELAE-LTRRLAELETQ--------------LDATRARLRALEGQ---LAAEQAERERAEAQ 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   84 LESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRvdhDNLVAR---VDTAERNIGSLTTELSTLTLRVTSIQADFES 160
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEAR---NQLRDRdeaIRAAERRLKEASIERDTLERRLAGLEADLER 308


                  .
gi 205830900  161 R 161
Cdd:pfam19220 309 R 309
 
Name Accession Description Interval E-value
Reo_sigma1 pfam01664
Reovirus viral attachment protein sigma 1; This family consists of the reovirus sigma 1 ...
 242-454 2.65e-116

Reovirus viral attachment protein sigma 1; This family consists of the reovirus sigma 1 hemagglutinin, cell attachment protein. This glycoprotein is a minor capsid protein and also determines the serotype-specific humoral immune response. Sigma 1 consist of a fibrous tail and a globular head. The head has important roles in the cell attachment function of sigma 1 and determinant of the type-specific humoral immune response. Reovirus is part of the orthoreovirus group of retroviruses with, a dsRNA genome. Also present in this family is bacteriophage SF6 Lysozyme.


Pssm-ID: 366748  Cd Length: 216  Bit Score: 339.63  E-value: 2.65e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  242 INSRIGATEQSYVASAVTPLRLNSS--TKVLDMLIDSSTLEI-NSSGQLTVRSTSPNLRYPIADVSGG--IGMSPNYRFR 316
Cdd:pfam01664   1 LNSRIGSLEQSYIDSVVPPLRLNSSsgTRVLDMLYDSSDFEIiNSVLQLRVRSTSPTLRYPLELVSAGnrVGMSPNYRFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  317 QSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHndVVTYGA 396
Cdd:pfam01664  81 QGMWIGQLSYSGPGLNWRAQVTSNLMIVDDWLHLSFPAFDTFSIAAGGKFVLNFVTGLSPGWLTGDTEPSFT--VVPLST 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 205830900  397 QTVAIGLSSGGAPQYMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSF 454
Cdd:pfam01664 159 TFAAIQFSNGGQRQDAFRILGVEEWQDGELEIRNEGGTYTTHTNVKWAPMTIMYPCSF 216
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
62-134 6.52e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 47.13  E-value: 6.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205830900  62 ALEQSRDDLvasvsdAQLAISR---LESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAE 134
Cdd:COG1842   77 ALEKGREDL------AREALERkaeLEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAK 146
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 4-161 4.75e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 45.44  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    4 RLREEVVRLIiALTSDNGASLSKgLESRVSALEKTsqihsdtilritqgLDDANKRIIALEQSrddLVASVSDAQLAISR 83
Cdd:pfam19220 171 LLEQENRRLQ-ALSEEQAAELAE-LTRRLAELETQ--------------LDATRARLRALEGQ---LAAEQAERERAEAQ 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   84 LESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRvdhDNLVAR---VDTAERNIGSLTTELSTLTLRVTSIQADFES 160
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEAR---NQLRDRdeaIRAAERRLKEASIERDTLERRLAGLEADLER 308


                  .
gi 205830900  161 R 161
Cdd:pfam19220 309 R 309
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-190 2.68e-04

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: 43.51  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    28 LESRVSALEKTSQIHSDTILRITQGLDDANKRIIALEQSRDDLvasvsdaQLAISRLESSIGALQTVVNGLDSSVTQLGA 107
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-------AEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   108 RVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTELSTLTLRVTSIQA---DFESRISTLERTAVTSAGAPLSIRNNRM 184
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrreRLQQEIEELLKKLEEAELKELQAELEEL 445


                   ....*.
gi 205830900   185 TMGLND 190
Cdd:TIGR02168  446 EEELEE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-169 9.01e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    4 RLREEVVRL---IIALTSDNGA--SLSKGLESRVSALEKTSQIHSDTIlritqGLDDANKRIIALEQSRDDLVASVSDaq 78
Cdd:COG4913   614 ALEAELAELeeeLAEAEERLEAleAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSDD-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   79 laISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTEL-------STLTLRV 151
Cdd:COG4913   687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaaALGDAVE 764

                         170
                  ....*....|....*...
gi 205830900  152 TSIQADFESRISTLERTA 169
Cdd:COG4913   765 RELRENLEERIDALRARL 782
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 34-133 3.49e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.89  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   34 ALEKTSQIHSDTILRITQGLDDANKR----IIALEQSRDDLVASVSdAQLAisRLESSIGALQTVVNGLDSSVTQLGARV 109
Cdd:pfam04012  44 ALAQTIARQKQLERRLEQQTEQAKKLeekaQAALTKGNEELAREAL-AEKK--SLEKQAEALETQLAQQRSAVEQLRKQL 120

                          90       100
                  ....*....|....*....|....
gi 205830900  110 GQLETGLAELRVDHDNLVARVDTA 133
Cdd:pfam04012 121 AALETKIQQLKAKKNLLKARLKAA 144
 
Name Accession Description Interval E-value
Reo_sigma1 pfam01664
Reovirus viral attachment protein sigma 1; This family consists of the reovirus sigma 1 ...
 242-454 2.65e-116

Reovirus viral attachment protein sigma 1; This family consists of the reovirus sigma 1 hemagglutinin, cell attachment protein. This glycoprotein is a minor capsid protein and also determines the serotype-specific humoral immune response. Sigma 1 consist of a fibrous tail and a globular head. The head has important roles in the cell attachment function of sigma 1 and determinant of the type-specific humoral immune response. Reovirus is part of the orthoreovirus group of retroviruses with, a dsRNA genome. Also present in this family is bacteriophage SF6 Lysozyme.


Pssm-ID: 366748  Cd Length: 216  Bit Score: 339.63  E-value: 2.65e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  242 INSRIGATEQSYVASAVTPLRLNSS--TKVLDMLIDSSTLEI-NSSGQLTVRSTSPNLRYPIADVSGG--IGMSPNYRFR 316
Cdd:pfam01664   1 LNSRIGSLEQSYIDSVVPPLRLNSSsgTRVLDMLYDSSDFEIiNSVLQLRVRSTSPTLRYPLELVSAGnrVGMSPNYRFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  317 QSMWIGIVSYSGSGLNWRVQVNSDIFIVDDYIHICLPAFDGFSIADGGDLSLNFVTGLLPPLLTGDTEPAFHndVVTYGA 396
Cdd:pfam01664  81 QGMWIGQLSYSGPGLNWRAQVTSNLMIVDDWLHLSFPAFDTFSIAAGGKFVLNFVTGLSPGWLTGDTEPSFT--VVPLST 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 205830900  397 QTVAIGLSSGGAPQYMSKNLWVEQWQDGVLRLRVEGGGSITHSNSKWPAMTVSYPRSF 454
Cdd:pfam01664 159 TFAAIQFSNGGQRQDAFRILGVEEWQDGELEIRNEGGTYTTHTNVKWAPMTIMYPCSF 216
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
62-134 6.52e-06

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 47.13  E-value: 6.52e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 205830900  62 ALEQSRDDLvasvsdAQLAISR---LESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAE 134
Cdd:COG1842   77 ALEKGREDL------AREALERkaeLEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAK 146
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 4-161 4.75e-05

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 45.44  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    4 RLREEVVRLIiALTSDNGASLSKgLESRVSALEKTsqihsdtilritqgLDDANKRIIALEQSrddLVASVSDAQLAISR 83
Cdd:pfam19220 171 LLEQENRRLQ-ALSEEQAAELAE-LTRRLAELETQ--------------LDATRARLRALEGQ---LAAEQAERERAEAQ 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   84 LESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRvdhDNLVAR---VDTAERNIGSLTTELSTLTLRVTSIQADFES 160
Cdd:pfam19220 232 LEEAVEAHRAERASLRMKLEALTARAAATEQLLAEAR---NQLRDRdeaIRAAERRLKEASIERDTLERRLAGLEADLER 308


                  .
gi 205830900  161 R 161
Cdd:pfam19220 309 R 309
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 48-136 1.72e-04

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: 43.60  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  48 RITQGLDDANKRIIALEQSRDDLVASVSDAQLAISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRvdhDNLV 127
Cdd:COG4942   31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---EELA 107


                 ....*....
gi 205830900 128 ARVDTAERN 136
Cdd:COG4942  108 ELLRALYRL 116
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 28-190 2.68e-04

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: 43.51  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    28 LESRVSALEKTSQIHSDTILRITQGLDDANKRIIALEQSRDDLvasvsdaQLAISRLESSIGALQTVVNGLDSSVTQLGA 107
Cdd:TIGR02168  293 LANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-------AEELAELEEKLEELKEELESLEAELEELEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   108 RVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTELSTLTLRVTSIQA---DFESRISTLERTAVTSAGAPLSIRNNRM 184
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDrreRLQQEIEELLKKLEEAELKELQAELEEL 445


                   ....*.
gi 205830900   185 TMGLND 190
Cdd:TIGR02168  446 EEELEE 451
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
4-169 9.01e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    4 RLREEVVRL---IIALTSDNGA--SLSKGLESRVSALEKTSQIHSDTIlritqGLDDANKRIIALEQSRDDLVASVSDaq 78
Cdd:COG4913   614 ALEAELAELeeeLAEAEERLEAleAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELERLDASSDD-- 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   79 laISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTEL-------STLTLRV 151
Cdd:COG4913   687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaaALGDAVE 764

                         170
                  ....*....|....*...
gi 205830900  152 TSIQADFESRISTLERTA 169
Cdd:COG4913   765 RELRENLEERIDALRARL 782
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 3-167 1.16e-03

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900     3 PRLREEVVRLIIALtSDNGASLSkglESRVSALEKTSQIHSDTILRITQGLDDANKRIIA-------LEQSRDDLVASVS 75
Cdd:TIGR02169  768 EELEEDLHKLEEAL-NDLEARLS---HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlekeyLEKEIQELQEQRI 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900    76 DAQLAISRLESSIGALQTVVNGLDSSVTQLGARVGQLETGLAELRVDHDNLVARVDTAERNIGSLTTELSTLTLRVTSIQ 155
Cdd:TIGR02169  844 DLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923

                          170
                   ....*....|....*
gi 205830900   156 ADFE---SRISTLER 167
Cdd:TIGR02169  924 AKLEaleEELSEIED 938
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 34-133 3.49e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.89  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900   34 ALEKTSQIHSDTILRITQGLDDANKR----IIALEQSRDDLVASVSdAQLAisRLESSIGALQTVVNGLDSSVTQLGARV 109
Cdd:pfam04012  44 ALAQTIARQKQLERRLEQQTEQAKKLeekaQAALTKGNEELAREAL-AEKK--SLEKQAEALETQLAQQRSAVEQLRKQL 120

                          90       100
                  ....*....|....*....|....
gi 205830900  110 GQLETGLAELRVDHDNLVARVDTA 133
Cdd:pfam04012 121 AALETKIQQLKAKKNLLKARLKAA 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 26-134 8.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 205830900  26 KGLESRVSALEKTSQIHSDTILRITQGLDDANKRIIALEQSRDDLVASVSDAQLAISRLESSIGALQTVVNGLDSSVTQL 105
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                         90       100
                 ....*....|....*....|....*....
gi 205830900 106 GARVGQLETGLAELRVDHDNLVARVDTAE 134
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELE 343
 
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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