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Conserved domains on  [gi|30018860|ref|NP_830491.1|]
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methyl-accepting chemotaxis protein [Bacillus cereus ATCC 14579]

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List of domain hits

Name Accession Description Interval E-value
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
107-264 8.96e-44

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 150.47  E-value: 8.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 107 SNEGKESVHRLLIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANE 186
Cdd:cd11386  28 AEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADE 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30018860 187 VRKLAESTAESTKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQ 264
Cdd:cd11386 108 VRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
DD_cGKI super family cl17044
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
8-49 9.02e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


The actual alignment was detected with superfamily member cd12083:

Pssm-ID: 213458  Cd Length: 48  Bit Score: 33.31  E-value: 9.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30018860   8 LQHTISQLEERIQELELELKQKDIEKQETISTIhDRVQSVVQ 49
Cdd:cd12083   7 KTEELRKKDERIRELEQELQEKDEEIQELRSQL-DKFQSVLP 47
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
59-311 2.21e-40

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


:

Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 143.20  E-value: 2.21e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     59 NTLQSLVQQLSSCFENVSTRTTHSNELNNEMLQKEQSLIQSIAEIIDCSNEGKESVHRLLIVINKLGEQSQRTSNSMNHL 138
Cdd:smart00283   7 EEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    139 SERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLTKKIQEEIEKAYDN 218
Cdd:smart00283  87 EESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    219 TKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQKSCNDDILREFANTQQMFQKlNTTIMNHIHDAEK 298
Cdd:smart00283 167 MEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQE-TAAMSEEISAAAE 245
                          250
                   ....*....|...
gi 30018860    299 VDVQLSKSLQETV 311
Cdd:smart00283 246 ELSGLAEELDELV 258
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
107-264 8.96e-44

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 150.47  E-value: 8.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 107 SNEGKESVHRLLIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANE 186
Cdd:cd11386  28 AEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADE 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30018860 187 VRKLAESTAESTKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQ 264
Cdd:cd11386 108 VRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
8-49 9.02e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373  Cd Length: 48  Bit Score: 33.31  E-value: 9.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30018860   8 LQHTISQLEERIQELELELKQKDIEKQETISTIhDRVQSVVQ 49
Cdd:cd12083   7 KTEELRKKDERIRELEQELQEKDEEIQELRSQL-DKFQSVLP 47
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
59-311 2.21e-40

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 143.20  E-value: 2.21e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     59 NTLQSLVQQLSSCFENVSTRTTHSNELNNEMLQKEQSLIQSIAEIIDCSNEGKESVHRLLIVINKLGEQSQRTSNSMNHL 138
Cdd:smart00283   7 EEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    139 SERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLTKKIQEEIEKAYDN 218
Cdd:smart00283  87 EESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    219 TKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQKSCNDDILREFANTQQMFQKlNTTIMNHIHDAEK 298
Cdd:smart00283 167 MEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQE-TAAMSEEISAAAE 245
                          250
                   ....*....|...
gi 30018860    299 VDVQLSKSLQETV 311
Cdd:smart00283 246 ELSGLAEELDELV 258
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
25-312 2.24e-32

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 123.95  E-value: 2.24e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860  25 ELKQKDIEKQETISTIHDRVQSVVQEHQLVNNQHNTLQSLVQQLSSCFENVSTRTTHSNELNNEMLQKEQSLIQSIAEII 104
Cdd:COG0840 114 EFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAA 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 105 DCSNEGKESVHRLLIVINKLGEQSQRTSNSMNH----LSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGF 180
Cdd:COG0840 194 ALASEASQVAEEGGEEVRQAVEQMQEIAEELAEvvkkLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGF 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 181 AVVANEVRKLAESTAESTKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKA 260
Cdd:COG0840 274 AVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAA 353
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 30018860 261 IENQKSCNDDILREFANTQQMFQKlNTTIMNHIHDAEKVDVQLSKSLQETVT 312
Cdd:COG0840 354 TEEQTAVLEEINASIEELDDVTQE-NAAAVEELAAASEELKELAEKLLELVA 404
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
118-271 1.58e-29

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 112.54  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860   118 LIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAES 197
Cdd:pfam00015  15 LDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQA 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30018860   198 TKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQKSCNDDI 271
Cdd:pfam00015  95 AKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 168
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
82-220 2.94e-19

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 86.66  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860   82 SNELNNEMLQKEQSLIQSIAEI----------IDCSNEGKESVHRLLIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEV 151
Cdd:PRK09793 284 NNDLSSRTEQQAASLAQTAASMeqltatvgqnADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISV 363
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30018860  152 IQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLtkkIQEEIEKAYDNTK 220
Cdd:PRK09793 364 IDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGL---IEESVNRVQQGSK 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-217 1.72e-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: 38.50  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     12 ISQLEERIQELE---LELKQKDIEKQETISTIHDRVQSVVQEHQLVNNQHNTLQSLVQQLSSCFENVSTRTTHSNELNNE 88
Cdd:TIGR02168  679 IEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     89 MLQKEQSLIQSIAEIIDCSNEGKEsvhrlliVINKLGEQSQRTSNSMNHLSERSKEIEQIVEViQNIAAQTNLLALNASi 168
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESL- 829
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30018860    169 eAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLTK---KIQEEIEKAYD 217
Cdd:TIGR02168  830 -ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieELESELEALLN 880
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
107-264 8.96e-44

Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis proteins (MCPs or chemotaxis receptors) are an integral part of the transmembrane protein complex that controls bacterial chemotaxis, together with the histidine kinase CheA, the receptor-coupling protein CheW, receptor-modification enzymes, and localized phosphatases. MCPs contain a four helix trans membrane region, an N-terminal periplasmic ligand binding domain, and a C-terminal HAMP domain followed by a cytoplasmic signaling domain. This C-terminal signaling domain dimerizes into a four-helix bundle and interacts with CheA through the adaptor protein CheW.


Pssm-ID: 206779  Cd Length: 200  Bit Score: 150.47  E-value: 8.96e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 107 SNEGKESVHRLLIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANE 186
Cdd:cd11386  28 AEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADE 107
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30018860 187 VRKLAESTAESTKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQ 264
Cdd:cd11386 108 VRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
DD_cGKI cd12083
Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent ...
8-49 9.02e-03

Dimerization/Docking domain of Cyclic GMP-dependent Protein Kinase I; Cyclic GMP-dependent Protein Kinase I (PKG1 or cGKI) is a Serine/Threonine Kinase (STK), catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. They contain an N-terminal regulatory domain containing a dimerization/docking region and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. It is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. The dimerization/docking (D/D) domain is a leucine/isoleucine zipper that mediates both homodimerization and interaction with isotype-specific G-kinase-anchoring proteins (GKAPs). The D/D domain of the two variants (alpha and beta) differ, allowing their targeting to different subcellular compartments and intracellular substrates.


Pssm-ID: 213373  Cd Length: 48  Bit Score: 33.31  E-value: 9.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 30018860   8 LQHTISQLEERIQELELELKQKDIEKQETISTIhDRVQSVVQ 49
Cdd:cd12083   7 KTEELRKKDERIRELEQELQEKDEEIQELRSQL-DKFQSVLP 47
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
59-311 2.21e-40

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 143.20  E-value: 2.21e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     59 NTLQSLVQQLSSCFENVSTRTTHSNELNNEMLQKEQSLIQSIAEIIDCSNEGKESVHRLLIVINKLGEQSQRTSNSMNHL 138
Cdd:smart00283   7 EEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    139 SERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLTKKIQEEIEKAYDN 218
Cdd:smart00283  87 EESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVAA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    219 TKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQKSCNDDILREFANTQQMFQKlNTTIMNHIHDAEK 298
Cdd:smart00283 167 MEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQE-TAAMSEEISAAAE 245
                          250
                   ....*....|...
gi 30018860    299 VDVQLSKSLQETV 311
Cdd:smart00283 246 ELSGLAEELDELV 258
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
25-312 2.24e-32

Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 123.95  E-value: 2.24e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860  25 ELKQKDIEKQETISTIHDRVQSVVQEHQLVNNQHNTLQSLVQQLSSCFENVSTRTTHSNELNNEMLQKEQSLIQSIAEII 104
Cdd:COG0840 114 EFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAKEAA 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 105 DCSNEGKESVHRLLIVINKLGEQSQRTSNSMNH----LSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGF 180
Cdd:COG0840 194 ALASEASQVAEEGGEEVRQAVEQMQEIAEELAEvvkkLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGF 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 181 AVVANEVRKLAESTAESTKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKA 260
Cdd:COG0840 274 AVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAA 353
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 30018860 261 IENQKSCNDDILREFANTQQMFQKlNTTIMNHIHDAEKVDVQLSKSLQETVT 312
Cdd:COG0840 354 TEEQTAVLEEINASIEELDDVTQE-NAAAVEELAAASEELKELAEKLLELVA 404
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
118-271 1.58e-29

Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to transduce the signal to CheA since it is highly conserved in very diverse MCPs.


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 112.54  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860   118 LIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAES 197
Cdd:pfam00015  15 LDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQA 94
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30018860   198 TKNIGNLTKKIQEEIEKAYDNTKDNLHLVDEGVEMSADTNARIENILVMIQTLQNGATNVIKAIENQKSCNDDI 271
Cdd:pfam00015  95 AKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQV 168
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
82-220 2.94e-19

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 86.66  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860   82 SNELNNEMLQKEQSLIQSIAEI----------IDCSNEGKESVHRLLIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEV 151
Cdd:PRK09793 284 NNDLSSRTEQQAASLAQTAASMeqltatvgqnADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISV 363
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30018860  152 IQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLtkkIQEEIEKAYDNTK 220
Cdd:PRK09793 364 IDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGL---IEESVNRVQQGSK 429
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
133-204 7.81e-19

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 85.44  E-value: 7.81e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30018860  133 NSMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNL 204
Cdd:PRK15048 347 KTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKAL 418
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
134-204 7.57e-17

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 79.61  E-value: 7.57e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30018860  134 SMNHLSERSKEIEQIVEVIQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNL 204
Cdd:PRK15041 350 TMRDISTSSQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSL 420
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
6-298 1.30e-05

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.48  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860    6 KSLQHTISQLEERIQELELELKQKDIEKQEtistIHDRVQSVVQEHQLVNNQHNTLQSLVQQLSSCFENVSTRTTHSNEL 85
Cdd:COG1196  691 KSLKNELRSLEDLLEELRRQLEELERQLEE----LKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEE 766
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860   86 NNEMLQKEQSLIQSIAEIIDCSNEGKESVHRLLIVINKLGEQSQRTSNSMNHLSER----SKEIEQIVEVIQNIAAQTNL 161
Cdd:COG1196  767 LESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRrerlEQEIEELEEEIEELEEKLDE 846
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860  162 LALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLTKKIQEEIEKAYDNTKDNLHLVD---EGVEMSADTNA 238
Cdd:COG1196  847 LEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRErleELEAKLERLEV 926
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30018860  239 RIENILVMIQ-----TLQNGATNVIKAIENQ----KSCNDDILREFANTQQMFQKLNTTIMNHIHDAEK 298
Cdd:COG1196  927 ELPELEEELEeeyedTLETELEREIERLEEEiealGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEK 995
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
1-221 1.42e-05

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 45.02  E-value: 1.42e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860   1 MFTQKKSLQHTISQLEE---RIQELELELKQKDIEKQETIS---TIHDRVQSVVQEHQLVNNQhntLQSLVQQLSSCFEN 74
Cdd:COG4372  62 LFLLNRNLRSGVFQLDDirpQLRALRTELGTAQGEKRAAETereAARSELQKARQEREAVRQE---LAAARQNLAKAQQE 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860  75 VSTRTTHSNELNNEMLQKEQSLIQSIAEIIDCSNEGKE---SVHRLLIVINKLGEQSQRTSNSMNHLSERSKEIEQIVEV 151
Cdd:COG4372 139 LARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQlqaSATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEE 218
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860 152 IQNIAAQTNLLALNASIEAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLtKKIQEEIEKAYDNTKD 221
Cdd:COG4372 219 LARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARL-EQEVAQLEAYYQAYVR 287
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-217 1.72e-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: 38.50  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     12 ISQLEERIQELE---LELKQKDIEKQETISTIHDRVQSVVQEHQLVNNQHNTLQSLVQQLSSCFENVSTRTTHSNELNNE 88
Cdd:TIGR02168  679 IEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30018860     89 MLQKEQSLIQSIAEIIDCSNEGKEsvhrlliVINKLGEQSQRTSNSMNHLSERSKEIEQIVEViQNIAAQTNLLALNASi 168
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESL- 829
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30018860    169 eAARAGEHGKGFAVVANEVRKLAESTAESTKNIGNLTK---KIQEEIEKAYD 217
Cdd:TIGR02168  830 -ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieELESELEALLN 880
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.14
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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