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Conserved domains on  [gi|30260716|ref|NP_843093|]
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methyl-accepting chemotaxis protein [Bacillus anthracis str. Ames]

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List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
409-608 3.15e-65

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: 215.18  E-value: 3.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 409 EEVTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESVSQSDKVIVLLDDKSKQIGAILEVIQHIAEQT 488
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 489 NLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQS 568
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30260716 569 FAEILKSTDDTVVQIDNMVDVAKQMTVDARQVSASINEIA 608
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
303-350 4.05e-12

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 62.27  E-value: 4.05e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 30260716 303 IISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHH 350
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
Cache_1 super family cl03691
Cache domain;
150-221 1.41e-16

Cache domain;


The actual alignment was detected with superfamily member pfam02743:

Pssm-ID: 251508  Cd Length: 80  Bit Score: 75.76  E-value: 1.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30260716   150 ITAPYKSSTTGNIVITIAKQ---NEDKSGVLGIDLIINDIVNTSKMVNIGKTGFVAIFDQSKHVIAHPTIKPGDK 221
Cdd:pfam02743   1 VTEPYVDAATGDLVITIAQPvydNGDLLGVIGLDVPLEDLLKITKSIKLGKTGYAFIIDNNGKVLAHPNHEPVTK 75
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
34-149 1.71e-05

ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate and repellents) and Tsr (taxis to serine and repellents) are homologous chemoreceptors that have a high specificity for aspartate and serine, respectively. Both are homodimeric receptors and contain an N-terminal periplasmic ligand binding domain, a transmembrane region, a HAMP domain and a C-terminal cytosolic signaling domain.


The actual alignment was detected with superfamily member smart00319:

Pssm-ID: 260214  Cd Length: 135  Bit Score: 43.61  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716     34 SYQQAKTNFNETILQSAEDNVKILNNVINK---EIDSKKVDAVYFTKL----FNGVSY-----GTDQLQNVQNKLEE--- 98
Cdd:smart00319   4 SYQQAALSLSRVLLLQARNNLNRAGIRMMQnniGSKAKKLMTAASESLkqaeKNYKSYenmtaLPRADRALDAELKEkfq 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30260716     99 -YNKLHPEIEAIYTGSSTGQFIQSPSIQMPDGYNPTERDWYKEAAKKSGEVV 149
Cdd:smart00319  84 qYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQAV 135
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
382-657 3.91e-65

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: 217.15  E-value: 3.91e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    382 QITQAIEQVSSGAEIQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESVSQSD 461
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    462 KVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQFDI 541
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    542 KETVSSMKLVGTEVQSGLVVANETKQSFAEILKSTDDTVVQIDNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNI 621
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 30260716    622 AGSSEEqlasvdeinaaavhLSQMAEELQEMIGKFK 657
Cdd:smart00283 241 SAAAEE--------------LSGLAEELDELVERFK 262
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
409-608 3.15e-65

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: 215.18  E-value: 3.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 409 EEVTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESVSQSDKVIVLLDDKSKQIGAILEVIQHIAEQT 488
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 489 NLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQS 568
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30260716 569 FAEILKSTDDTVVQIDNMVDVAKQMTVDARQVSASINEIA 608
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
303-350 4.05e-12

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 62.27  E-value: 4.05e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 30260716 303 IISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHH 350
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
HAMP pfam00672
HAMP domain;
282-350 2.74e-17

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 77.27  E-value: 2.74e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30260716   282 LTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHH 350
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
Cache_1 pfam02743
Cache domain;
150-221 1.41e-16

Cache domain;


Pssm-ID: 251508  Cd Length: 80  Bit Score: 75.76  E-value: 1.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30260716   150 ITAPYKSSTTGNIVITIAKQ---NEDKSGVLGIDLIINDIVNTSKMVNIGKTGFVAIFDQSKHVIAHPTIKPGDK 221
Cdd:pfam02743   1 VTEPYVDAATGDLVITIAQPvydNGDLLGVIGLDVPLEDLLKITKSIKLGKTGYAFIIDNNGKVLAHPNHEPVTK 75
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
302-353 3.16e-12

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640  Cd Length: 53  Bit Score: 62.65  E-value: 3.16e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30260716    302 SIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVIS 353
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
289-348 1.60e-06

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 46.60  E-value: 1.60e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 289 LIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASL 348
Cdd:COG2770  16 VLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL 75
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
34-149 1.71e-05

Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the wild-type bacterial aspartate receptor, Tar.


Pssm-ID: 128614  Cd Length: 135  Bit Score: 43.61  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716     34 SYQQAKTNFNETILQSAEDNVKILNNVINK---EIDSKKVDAVYFTKL----FNGVSY-----GTDQLQNVQNKLEE--- 98
Cdd:smart00319   4 SYQQAALSLSRVLLLQARNNLNRAGIRMMQnniGSKAKKLMTAASESLkqaeKNYKSYenmtaLPRADRALDAELKEkfq 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30260716     99 -YNKLHPEIEAIYTGSSTGQFIQSPSIQMPDGYNPTERDWYKEAAKKSGEVV 149
Cdd:smart00319  84 qYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQAV 135
TarH pfam02203
Tar ligand binding domain homologue;
28-143 1.22e-04

Tar ligand binding domain homologue;


Pssm-ID: 251153  Cd Length: 146  Bit Score: 41.20  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    28 IVIGWTSYQQAKTNFNETILQS-----------------------------AEDNVKILNNvINKEIDSKKVDAVYFTKL 78
Cdd:pfam02203   1 GGLGLSGLQSANDALDEVYTNSlqqqaaladawvlllqarltldraallpdAPDAAELLDR-ARESLAQSEKAWKAYLAL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30260716    79 FNGVSYGTDQLQNVQNKLEEYNKLH-PEIEAIYTGSSTGQFIQSPSIQMPDGYNPTERDWYKEAAK 143
Cdd:pfam02203  80 PKSAPEEEALADELKAKYKQYLQDGlDPLAAALRAGDLDAFFDQPTQKMQPLFNALTRAWYAQAVK 145
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
382-657 3.91e-65

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: 217.15  E-value: 3.91e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    382 QITQAIEQVSSGAEIQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESVSQSD 461
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    462 KVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQFDI 541
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    542 KETVSSMKLVGTEVQSGLVVANETKQSFAEILKSTDDTVVQIDNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNI 621
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 30260716    622 AGSSEEqlasvdeinaaavhLSQMAEELQEMIGKFK 657
Cdd:smart00283 241 SAAAEE--------------LSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
282-658 6.09e-70

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 234.88  E-value: 6.09e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 282 LTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVISNINTSASH 361
Cdd:COG0840  63 LISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 362 VAASSEELTASMKQTSEATEQITQAIEQVSSGaeiqtkeveegatlLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGK 441
Cdd:COG0840 143 LSGASEEIAASATELSARADQQAESLEEVASA--------------IEELSETVKEVAFNAKEAAALASEASQVAEEGGE 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 442 LVEQTVNQMQLIHESVsqsDKVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAE 521
Cdd:COG0840 209 EVRQAVEQMQEIAEEL---AEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAE 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 522 QSGQSSTEIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQSFAEILKSTDDTVVQIDnmvdvakqmtvdarQVS 601
Cdd:COG0840 286 RSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLIS--------------EIA 351
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30260716 602 ASINEIAATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:COG0840 352 AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
449-658 3.08e-49

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: 171.47  E-value: 3.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   449 QMQLIHESVSQSDKVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSST 528
Cdd:pfam00015  17 EMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   529 EIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQSFAEILkstdDTVVQIDNMVDvakqmtvdarQVSASINEIA 608
Cdd:pfam00015  97 EIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIV----DAVAEIADIVQ----------EIAAASDEQS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 30260716   609 ATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:pfam00015 163 AGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
267-658 3.78e-42

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 159.40  E-value: 3.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  267 SKEIIEAANPIFYKTLTVIGISLIIGGVLI---YFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNE 343
Cdd:PRK15048 177 RDIVTDNADDYRFAQWQLAVIALVVVLILLvawYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSH 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  344 MAASLHHVISNINTSASHVAASSEELTASMKQTSEATEQitqaieqvssgaeiQTKEVEEGATLLEEVTEGIQRVADSSS 423
Cdd:PRK15048 257 MQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQ--------------QASALEETAASMEQLTATVKQNADNAR 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  424 LVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESvsqsdkvivllddkSKQIGAILEVIQHIAEQTNLLALNAAIEAARAG 503
Cdd:PRK15048 323 QASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAVEAARAG 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  504 EQGRGFAIVADEVRKLAEQSGQSSTEIGKLvkeiqfdIKETVSSMKLVGTEVQSglvvANETkqsfaeilkstddtvvqI 583
Cdd:PRK15048 389 EQGRGFAVVAGEVRNLASRSAQAAKEIKAL-------IEDSVSRVDTGSVLVES----AGET-----------------M 440
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30260716  584 DNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:PRK15048 441 NNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
280-491 3.89e-08

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 55.05  E-value: 3.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 280 KTLTVIGISLIIGG-------VLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVI 352
Cdd:COG3850 145 KTILLVLVQLAGMLlilllvvFTIYWLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLY 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 353 SNI--------------NTSASHVAASSEELTASmKQTSEATEQITQAIeQVSSGAEIQTKEVEEGATLLE--------E 410
Cdd:COG3850 225 ADLeqrveektrdleqkNQRLSFLYQSSRRLHTS-QIDDERLRHVLNRL-QNLTGLAAVRLELYGGDDERNhqehaeqwD 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 411 VTEGIQRVADSSSLVSTASMYTKKKAE--DGGKLVEqtvNQMQLIhESVSQsdkvivllddkskQIGAILEVIQHIAEQT 488
Cdd:COG3850 303 ISEGDQPSGLKWPQEDPLTQQGHLLGTlpWQRSLPE---DDQQLL-DTLVQ-------------QLGRTLALNKQQEQQQ 365

                ...
gi 30260716 489 NLL 491
Cdd:COG3850 366 QLL 368
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
243-348 2.86e-07

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 51.94  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  243 DGDDRNITFiTNKQTGWKIAGimPSKEIIEAANPIFYK-----TLTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKI 317
Cdd:PRK10549 126 DGTRRPILV-NGAEVGWVIAS--PVERLTRNTDINFDKqqrrtSWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKL 202
                         90       100       110
                 ....*....|....*....|....*....|.
gi 30260716  318 SEGDLTETITVHSKDEIGQLGESFNEMAASL 348
Cdd:PRK10549 203 AAGDFTTRVTPTSRDELGRLAQDFNQLASTL 233
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
251-426 5.07e-07

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 51.67  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   251 FITNKQTGWKIAGiMPSKEIIEAANPIFYKTLTVIgISLIIGGVLIYFIIASIIS----PLKQLVISSKKiSEGDLTETI 326
Cdd:TIGR03785 379 WIDTEVLGAVIAE-QTTNGIRTLRNSALEKLFNVI-LAIMSIGTLALFGFASWISwrirRLSDDAEAAID-SQGRISGAI 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   327 TV-HSKDEIGQLGESFNEMAASL---HHVISNINTSASH-------VAASSEELTASMKQTSEATEQITQAIEQVSSGAE 395
Cdd:TIGR03785 456 PAsRSRDEIGDLSRSFAQMVARLrqyTHYLENMSSRLSHelrtpvaVVRSSLENLELQALEQEKQKYLERAREGTERLSM 535
                         170       180       190
                  ....*....|....*....|....*....|..
gi 30260716   396 IQTKEVEegATLLEEVTEGIQRVA-DSSSLVS 426
Cdd:TIGR03785 536 ILNNMSE--ATRLEQAIQSAEVEDfDLSEVLS 565
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
331-445 6.90e-04

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: 40.73  E-value: 6.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    331 KDEIGQLGESFNEMAASLHHVISNINTSASHVaassEELTASMKQTSEATEQITQAIEQVSSGAEIQTKEVEEGATLLEE 410
Cdd:smart00283 150 ESLIKEIQEETNEAVAAMEESSSEVEEGVELV----EETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDE 225
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30260716    411 VTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQ 445
Cdd:smart00283 226 IAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
362-653 8.81e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    362 VAASSEELTASMKQTSEATEQITQAIEQVSSGAEIQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGK 441
Cdd:TIGR02168  661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    442 LVEQTVNQMQLIHESVSQSDKVIVLLDDK-SKQIGAILEVIQHIAE--------QTNLLALNAAIEAARA--GEQGRGFA 510
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEEleaqieqlKEELKALREALDELRAelTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    511 IVADEVRKLAEQSGQSSTEIGKLVKEIQfDIKETVSSMKLV-------GTEVQSGLVVANETKQSFAEILKST----DDT 579
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEieeleelIEELESELEALLNERASLEEALALLrselEEL 899
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30260716    580 VVQIDNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNIAgsseEQLASVDEINAaavhlsQMAEELQEMI 653
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ----ERLSEEYSLTL------EEAEALENKI 963
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
409-608 3.15e-65

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: 215.18  E-value: 3.15e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 409 EEVTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESVSQSDKVIVLLDDKSKQIGAILEVIQHIAEQT 488
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 489 NLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQS 568
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 30260716 569 FAEILKSTDDTVVQIDNMVDVAKQMTVDARQVSASINEIA 608
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
303-350 4.05e-12

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 62.27  E-value: 4.05e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 30260716 303 IISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHH 350
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
HAMP pfam00672
HAMP domain;
282-350 2.74e-17

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 77.27  E-value: 2.74e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30260716   282 LTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHH 350
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADRLRE 70
Cache_1 pfam02743
Cache domain;
150-221 1.41e-16

Cache domain;


Pssm-ID: 251508  Cd Length: 80  Bit Score: 75.76  E-value: 1.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30260716   150 ITAPYKSSTTGNIVITIAKQ---NEDKSGVLGIDLIINDIVNTSKMVNIGKTGFVAIFDQSKHVIAHPTIKPGDK 221
Cdd:pfam02743   1 VTEPYVDAATGDLVITIAQPvydNGDLLGVIGLDVPLEDLLKITKSIKLGKTGYAFIIDNNGKVLAHPNHEPVTK 75
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
302-353 3.16e-12

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640  Cd Length: 53  Bit Score: 62.65  E-value: 3.16e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30260716    302 SIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVIS 353
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
289-348 1.60e-06

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 46.60  E-value: 1.60e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 289 LIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASL 348
Cdd:COG2770  16 VLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSL 75
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
34-149 1.71e-05

Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the wild-type bacterial aspartate receptor, Tar.


Pssm-ID: 128614  Cd Length: 135  Bit Score: 43.61  E-value: 1.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716     34 SYQQAKTNFNETILQSAEDNVKILNNVINK---EIDSKKVDAVYFTKL----FNGVSY-----GTDQLQNVQNKLEE--- 98
Cdd:smart00319   4 SYQQAALSLSRVLLLQARNNLNRAGIRMMQnniGSKAKKLMTAASESLkqaeKNYKSYenmtaLPRADRALDAELKEkfq 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 30260716     99 -YNKLHPEIEAIYTGSSTGQFIQSPSIQMPDGYNPTERDWYKEAAKKSGEVV 149
Cdd:smart00319  84 qYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQAV 135
TarH pfam02203
Tar ligand binding domain homologue;
28-143 1.22e-04

Tar ligand binding domain homologue;


Pssm-ID: 251153  Cd Length: 146  Bit Score: 41.20  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    28 IVIGWTSYQQAKTNFNETILQS-----------------------------AEDNVKILNNvINKEIDSKKVDAVYFTKL 78
Cdd:pfam02203   1 GGLGLSGLQSANDALDEVYTNSlqqqaaladawvlllqarltldraallpdAPDAAELLDR-ARESLAQSEKAWKAYLAL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30260716    79 FNGVSYGTDQLQNVQNKLEEYNKLH-PEIEAIYTGSSTGQFIQSPSIQMPDGYNPTERDWYKEAAK 143
Cdd:pfam02203  80 PKSAPEEEALADELKAKYKQYLQDGlDPLAAALRAGDLDAFFDQPTQKMQPLFNALTRAWYAQAVK 145
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
382-657 3.91e-65

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: 217.15  E-value: 3.91e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    382 QITQAIEQVSSGAEIQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESVSQSD 461
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    462 KVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQFDI 541
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    542 KETVSSMKLVGTEVQSGLVVANETKQSFAEILKSTDDTVVQIDNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNI 621
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 30260716    622 AGSSEEqlasvdeinaaavhLSQMAEELQEMIGKFK 657
Cdd:smart00283 241 SAAAEE--------------LSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
282-658 6.09e-70

Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms]


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 234.88  E-value: 6.09e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 282 LTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVISNINTSASH 361
Cdd:COG0840  63 LISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 362 VAASSEELTASMKQTSEATEQITQAIEQVSSGaeiqtkeveegatlLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGK 441
Cdd:COG0840 143 LSGASEEIAASATELSARADQQAESLEEVASA--------------IEELSETVKEVAFNAKEAAALASEASQVAEEGGE 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 442 LVEQTVNQMQLIHESVsqsDKVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAE 521
Cdd:COG0840 209 EVRQAVEQMQEIAEEL---AEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAE 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 522 QSGQSSTEIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQSFAEILKSTDDTVVQIDnmvdvakqmtvdarQVS 601
Cdd:COG0840 286 RSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLIS--------------EIA 351
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30260716 602 ASINEIAATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:COG0840 352 AATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
449-658 3.08e-49

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: 171.47  E-value: 3.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   449 QMQLIHESVSQSDKVIVLLDDKSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSST 528
Cdd:pfam00015  17 EMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   529 EIGKLVKEIQFDIKETVSSMKLVGTEVQSGLVVANETKQSFAEILkstdDTVVQIDNMVDvakqmtvdarQVSASINEIA 608
Cdd:pfam00015  97 EIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIV----DAVAEIADIVQ----------EIAAASDEQS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 30260716   609 ATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:pfam00015 163 AGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
267-658 3.78e-42

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 159.40  E-value: 3.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  267 SKEIIEAANPIFYKTLTVIGISLIIGGVLI---YFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNE 343
Cdd:PRK15048 177 RDIVTDNADDYRFAQWQLAVIALVVVLILLvawYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSH 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  344 MAASLHHVISNINTSASHVAASSEELTASMKQTSEATEQitqaieqvssgaeiQTKEVEEGATLLEEVTEGIQRVADSSS 423
Cdd:PRK15048 257 MQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQ--------------QASALEETAASMEQLTATVKQNADNAR 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  424 LVSTASMYTKKKAEDGGKLVEQTVNQMQLIHESvsqsdkvivllddkSKQIGAILEVIQHIAEQTNLLALNAAIEAARAG 503
Cdd:PRK15048 323 QASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAVEAARAG 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  504 EQGRGFAIVADEVRKLAEQSGQSSTEIGKLvkeiqfdIKETVSSMKLVGTEVQSglvvANETkqsfaeilkstddtvvqI 583
Cdd:PRK15048 389 EQGRGFAVVAGEVRNLASRSAQAAKEIKAL-------IEDSVSRVDTGSVLVES----AGET-----------------M 440
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30260716  584 DNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:PRK15048 441 NNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
284-658 1.11e-39

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 152.03  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  284 VIGISLIIGGVLI---YFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVISNINTSAS 360
Cdd:PRK15041 196 LVGVMIVVLAVIFavwFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGAN 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  361 HVAASSEELTASMKQTSEATEQitqaieqvssgaeiQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGG 440
Cdd:PRK15041 276 AIYSGASEIATGNNDLSSRTEQ--------------QAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGG 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  441 KLVEQTVNQMQLIHESvsqsdkvivllddkSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLA 520
Cdd:PRK15041 342 KVVDNVVQTMRDISTS--------------SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLA 407
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  521 EQSGQSSTEIGKLvkeiqfdIKETVSSMKLVGTEVQSglvvANETkqsfaeilkstddtvvqIDNMVDVAKQMTVDARQV 600
Cdd:PRK15041 408 QRSAQAAREIKSL-------IEDSVGKVDVGSTLVES----AGET-----------------MAEIVSAVTRVTDIMGEI 459
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 30260716  601 SASINEIAATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:PRK15041 460 ASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
282-658 1.39e-33

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 134.04  E-value: 1.39e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  282 LTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVISNINTSASH 361
Cdd:PRK09793 193 ISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQE 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  362 VAASSEELTASMKQTSEATEQitqaieqvssgaeiQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGK 441
Cdd:PRK09793 273 MHIGIAEIVAGNNDLSSRTEQ--------------QAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGV 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  442 LVEQTVNQMQLIHESvsqsdkvivllddkSKQIGAILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAE 521
Cdd:PRK09793 339 QVSTMTHTMQEIATS--------------SQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAS 404
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  522 QSGQSSteigklvKEIQFDIKETVSsmklvgtEVQSGLVVANETKQSFAEILKStddtVVQIDNMVDvakqmtvdarQVS 601
Cdd:PRK09793 405 RSAQAA-------KEIKGLIEESVN-------RVQQGSKLVNNAAATMTDIVSS----VTRVNDIMG----------EIA 456
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30260716  602 ASINEIAATIEENAASVQNIAGSSEEQLASVDEINAAAVHLSQMAEELQEMIGKFKV 658
Cdd:PRK09793 457 SASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
280-491 3.89e-08

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 55.05  E-value: 3.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 280 KTLTVIGISLIIGG-------VLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASLHHVI 352
Cdd:COG3850 145 KTILLVLVQLAGMLlilllvvFTIYWLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELKKLY 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 353 SNI--------------NTSASHVAASSEELTASmKQTSEATEQITQAIeQVSSGAEIQTKEVEEGATLLE--------E 410
Cdd:COG3850 225 ADLeqrveektrdleqkNQRLSFLYQSSRRLHTS-QIDDERLRHVLNRL-QNLTGLAAVRLELYGGDDERNhqehaeqwD 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 411 VTEGIQRVADSSSLVSTASMYTKKKAE--DGGKLVEqtvNQMQLIhESVSQsdkvivllddkskQIGAILEVIQHIAEQT 488
Cdd:COG3850 303 ISEGDQPSGLKWPQEDPLTQQGHLLGTlpWQRSLPE---DDQQLL-DTLVQ-------------QLGRTLALNKQQEQQQ 365

                ...
gi 30260716 489 NLL 491
Cdd:COG3850 366 QLL 368
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
243-348 2.86e-07

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 51.94  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716  243 DGDDRNITFiTNKQTGWKIAGimPSKEIIEAANPIFYK-----TLTVIGISLIIGGVLIYFIIASIISPLKQLVISSKKI 317
Cdd:PRK10549 126 DGTRRPILV-NGAEVGWVIAS--PVERLTRNTDINFDKqqrrtSWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKL 202
                         90       100       110
                 ....*....|....*....|....*....|.
gi 30260716  318 SEGDLTETITVHSKDEIGQLGESFNEMAASL 348
Cdd:PRK10549 203 AAGDFTTRVTPTSRDELGRLAQDFNQLASTL 233
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
251-426 5.07e-07

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 51.67  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   251 FITNKQTGWKIAGiMPSKEIIEAANPIFYKTLTVIgISLIIGGVLIYFIIASIIS----PLKQLVISSKKiSEGDLTETI 326
Cdd:TIGR03785 379 WIDTEVLGAVIAE-QTTNGIRTLRNSALEKLFNVI-LAIMSIGTLALFGFASWISwrirRLSDDAEAAID-SQGRISGAI 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716   327 TV-HSKDEIGQLGESFNEMAASL---HHVISNINTSASH-------VAASSEELTASMKQTSEATEQITQAIEQVSSGAE 395
Cdd:TIGR03785 456 PAsRSRDEIGDLSRSFAQMVARLrqyTHYLENMSSRLSHelrtpvaVVRSSLENLELQALEQEKQKYLERAREGTERLSM 535
                         170       180       190
                  ....*....|....*....|....*....|..
gi 30260716   396 IQTKEVEegATLLEEVTEGIQRVA-DSSSLVS 426
Cdd:TIGR03785 536 ILNNMSE--ATRLEQAIQSAEVEDfDLSEVLS 565
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
282-393 5.46e-07

Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms]


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 51.31  E-value: 5.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 282 LTVIGISLIIGGVLIYFIIA---SIISPLKQLVISSKKISEGDLTETITVHSKDE-IGQLGESFNEMAASLhhvisnint 357
Cdd:COG5000 281 LLYLSTALLVLLAAIWTAIAfarRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQL--------- 351
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30260716 358 sashvaassEELTASMKQTSEATEQITQAIEQVSSG 393
Cdd:COG5000 352 ---------SSQQEALERAKDALEQRRRFLEAVLSG 378
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
284-349 2.88e-06

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 49.08  E-value: 2.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30260716  284 VIGISLIIGGVL--IYFIIASIISPLKQLVISSKKISEGDLTE-TITVHSKDEIGQLGESFNEMAASLH 349
Cdd:PRK10935 155 LLGLILILTLVFftVRFTRRQVVAPLNQLVTASQQIEKGQFDHiPLDTTLPNELGLLAKAFNQMSSELH 223
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
285-348 1.10e-04

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 43.89  E-value: 1.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30260716  285 IGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEMAASL 348
Cdd:PRK10600 131 AVFMALLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAEL 194
COG1511 COG1511
Predicted membrane protein [Function unknown]
300-653 6.28e-04

Predicted membrane protein [Function unknown]


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 41.72  E-value: 6.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 300 IASIISPLKQLVISSKKISEGDLTetitvhSKDEIGQLGESFNEMAASLHHVISNINTSASHVAASSEELTasmkQTSEA 379
Cdd:COG1511 187 AEKLKDGTDEASNGNKKLSDLLNT------LNNSSATFSDGLNALTSGLTTLTDGLNQLDSGLGTLAAGIG----ELKQG 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 380 TEQITQAIEQVSSGAEIQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGgklveqtvnqmQLIHESVSQ 459
Cdd:COG1511 257 AEQLNEGIGEFSSGLSELNSGVQDLAAGVPQLNQGISALAAGLSLPDSLGDQFSSLQEAL-----------TQIAQGLKQ 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 460 SDKVIVLLDDKSKQigaILEVIQHIAEQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGQSSTEIGKLVKEIQF 539
Cdd:COG1511 326 KTSSSLEAAQGSLS---SLQSMLALSKSLDLTAEGATVDALGAPDGVQWLDESQKTLATLSELLSTGIDGVSEGLDALEQ 402
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 540 DIKETVSSMKLVGTEVqsGLVVANETKQSfaEILKSTDDTvVQIDNMVDVAKQMtvdARQVSASINEIAATIEENAASVQ 619
Cdd:COG1511 403 ASAQLAKSLAKLKTAV--AQIAASIAQLL--PGASEVLKT-LKSKGLDKLLNQL---NGALAKGSNALVQGLSDANDSFR 474
                       330       340       350
                ....*....|....*....|....*....|....
gi 30260716 620 NIAgsSEEQLASVDEINAAAVHLSQMAEELQEMI 653
Cdd:COG1511 475 SIT--SAQLKAGLNTLADGSNDLSSLGPGLGQLA 506
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
331-445 6.90e-04

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: 40.73  E-value: 6.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    331 KDEIGQLGESFNEMAASLHHVISNINTSASHVaassEELTASMKQTSEATEQITQAIEQVSSGAEIQTKEVEEGATLLEE 410
Cdd:smart00283 150 ESLIKEIQEETNEAVAAMEESSSEVEEGVELV----EETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDE 225
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 30260716    411 VTEGIQRVADSSSLVSTASMYTKKKAEDGGKLVEQ 445
Cdd:smart00283 226 IAQVTQETAAMSEEISAAAEELSGLAEELDELVER 260
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
362-653 8.81e-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: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    362 VAASSEELTASMKQTSEATEQITQAIEQVSSGAEIQTKEVEEGATLLEEVTEGIQRVADSSSLVSTASMYTKKKAEDGGK 441
Cdd:TIGR02168  661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    442 LVEQTVNQMQLIHESVSQSDKVIVLLDDK-SKQIGAILEVIQHIAE--------QTNLLALNAAIEAARA--GEQGRGFA 510
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERlEEAEEELAEAEAEIEEleaqieqlKEELKALREALDELRAelTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    511 IVADEVRKLAEQSGQSSTEIGKLVKEIQfDIKETVSSMKLV-------GTEVQSGLVVANETKQSFAEILKST----DDT 579
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIE-ELSEDIESLAAEieeleelIEELESELEALLNERASLEEALALLrselEEL 899
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30260716    580 VVQIDNMVDVAKQMTVDARQVSASINEIAATIEENAASVQNIAgsseEQLASVDEINAaavhlsQMAEELQEMI 653
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ----ERLSEEYSLTL------EEAEALENKI 963
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
285-344 1.14e-03

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 40.49  E-value: 1.14e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716 285 IGISLIIGGVLIYFIIASIISPLKQLVISSKKISEGDLTETITVHSKDEIGQLGESFNEM 344
Cdd:COG5002  36 TLIALIITALLGILLARTITKPITDMRKQAVDMARGNYSRKVKVYGTDEIGELADSFNDL 95
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
323-412 4.72e-03

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: 38.04  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30260716    323 TETITVHSKDEIGQLGESFNEMAASLHHV---ISNINTSASHVAASSEELTASMKQTSEATEQITQAIEQVSSGAEIQTK 399
Cdd:smart00283 170 SSSEVEEGVELVEETGDALEEIVDSVEEIadlVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSG 249
                           90
                   ....*....|...
gi 30260716    400 EVEEGATLLEEVT 412
Cdd:smart00283 250 LAEELDELVERFK 262
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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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