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Conserved domains on  [gi|49480166|ref|YP_034834|]
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methyl-accepting chemotaxis protein [[Bacillus thuringiensis] serovar konkukian str. 97-27]

Protein Classification

HAMP and MCP_signal domain-containing protein (domain architecture ID 10893899)

protein containing domains Tar_Tsr_LBD, Cache_1, HAMP, and MCP_signal

Graphical summary

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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 ...
411-603 5.87e-54

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: 184.36  E-value: 5.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 411 QQVNAAIQDVNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQT 490
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 491 NLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSGEIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVS 570
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 49480166 571 FTEILSSTTHIVSQVNEMVETTKRIAGDANEVT 603
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIA 193
Cache_1 super family cl24147
Cache domain;
152-223 9.78e-19

Cache domain;


The actual alignment was detected with superfamily member pfam02743:

Pssm-ID: 280839  Cd Length: 79  Bit Score: 81.96  E-value: 9.78e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49480166   152 VTAPYQSASTKNMVVTIAKEVKDGK---GVIGINLNLDNILKISKMINIGEKGYAVILDQNKQIVSHPSRKPGAK 223
Cdd:pfam02743   1 VTEPYVDASTGDMVVTIAQPVKDDGdglGVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLAHPNHKPVTK 75
HAMP pfam00672
HAMP domain;
283-352 7.31e-16

HAMP domain;


:

Pssm-ID: 279063  Cd Length: 69  Bit Score: 73.37  E-value: 7.31e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   283 TFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITiHSKDDIGKLGNSFNEMSASLQD 352
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLE-SGRDEIGELARAFNQMAERLRE 69
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
7-143 4.70e-10

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 pfam02203:

Pssm-ID: 294096  Cd Length: 171  Bit Score: 58.10  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166     7 WVKCMSIKKKL--IISFFLILTIPGLIIGGVSYQTAKTNFEQQITGKAKENI---------------------------- 56
Cdd:pfam02203   1 MFKRISISTRLllVLAFLGVLLLVSGGLGLSGLQSANDALDEVYTNSLQQQAaladawvlllqarlaldraallgdapds 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    57 -SILNTvISQNIEEKFVDAAYFADILTEDTY-PNGQEEiVRTKLAQYIKLH-PEVEGIYIGTQTGKFIREPFIQMSDGYN 133
Cdd:pfam02203  81 aELLDR-ARESLAQSEKAWKAYLALPKTAPEeEALADE-LKAKYKQYLQDGlAPLIAALRAGDLDAFFDQPTQKMQPLFN 158
                         170
                  ....*....|
gi 49480166   134 PTDRDWYKEA 143
Cdd:pfam02203 159 ALTRAWYAQA 168
MCP_signal super family cl23763
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
334-428 1.48e-03

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: 304920  Cd Length: 200  Bit Score: 39.14  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 334 DDIGKLGNSFNEMSASLQDVITQISFSAEHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQV 413
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 49480166 414 NAAIQDVNGSAESIS 428
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
285-660 3.73e-67

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 227.57  E-value: 3.73e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 285 IVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVITQISFSAEHV 364
Cdd:COG0840  64 ISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEAL 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 365 AASAEELTASVQQandatdqitiameqVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEGEDL 444
Cdd:COG0840 144 SGASEEIAASATE--------------LSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEE 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 445 VEQTATQMQSISRSVSEsdaIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQ 524
Cdd:COG0840 210 VRQAVEQMQEIAEELAE---VVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAER 286
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 525 SGESSGEIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVtn 604
Cdd:COG0840 287 SADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEI-- 364
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 49480166 605 aideiaaaaeenTASMQSVAASTEEQVNSMEEISSASQNLAEMAEELQAMTSKFKV 660
Cdd:COG0840 365 ------------NASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
411-603 5.87e-54

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: 184.36  E-value: 5.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 411 QQVNAAIQDVNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQT 490
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 491 NLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSGEIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVS 570
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 49480166 571 FTEILSSTTHIVSQVNEMVETTKRIAGDANEVT 603
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIA 193
Cache_1 pfam02743
Cache domain;
152-223 9.78e-19

Cache domain;


Pssm-ID: 280839  Cd Length: 79  Bit Score: 81.96  E-value: 9.78e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49480166   152 VTAPYQSASTKNMVVTIAKEVKDGK---GVIGINLNLDNILKISKMINIGEKGYAVILDQNKQIVSHPSRKPGAK 223
Cdd:pfam02743   1 VTEPYVDASTGDMVVTIAQPVKDDGdglGVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLAHPNHKPVTK 75
HAMP pfam00672
HAMP domain;
283-352 7.31e-16

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 73.37  E-value: 7.31e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   283 TFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITiHSKDDIGKLGNSFNEMSASLQD 352
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLE-SGRDEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
303-355 7.49e-12

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 61.50  E-value: 7.49e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 49480166    303 KSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVIT 355
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
305-352 2.12e-11

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: 59.96  E-value: 2.12e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 49480166 305 ITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQD 352
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
TarH pfam02203
Tar ligand binding domain homologue;
7-143 4.70e-10

Tar ligand binding domain homologue;


Pssm-ID: 280382  Cd Length: 171  Bit Score: 58.10  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166     7 WVKCMSIKKKL--IISFFLILTIPGLIIGGVSYQTAKTNFEQQITGKAKENI---------------------------- 56
Cdd:pfam02203   1 MFKRISISTRLllVLAFLGVLLLVSGGLGLSGLQSANDALDEVYTNSLQQQAaladawvlllqarlaldraallgdapds 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    57 -SILNTvISQNIEEKFVDAAYFADILTEDTY-PNGQEEiVRTKLAQYIKLH-PEVEGIYIGTQTGKFIREPFIQMSDGYN 133
Cdd:pfam02203  81 aELLDR-ARESLAQSEKAWKAYLALPKTAPEeEALADE-LKAKYKQYLQDGlAPLIAALRAGDLDAFFDQPTQKMQPLFN 158
                         170
                  ....*....|
gi 49480166   134 PTDRDWYKEA 143
Cdd:pfam02203 159 ALTRAWYAQA 168
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
280-351 6.20e-09

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 53.53  E-value: 6.20e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49480166 280 FYKTFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQ 351
Cdd:COG2770   5 APIFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQ 76
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
36-150 1.90e-07

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: 49.77  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166     36 SYQTAKTNFEQQITGKAKENISILNTVISQN-IEEKFVDA-AYFADILTEDTY---------------PNGQEEIvRTKL 98
Cdd:smart00319   4 SYQQAALSLSRVLLLQARNNLNRAGIRMMQNnIGSKAKKLmTAASESLKQAEKnyksyenmtalpradRALDAEL-KEKF 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 49480166     99 AQYIKLHPEVEGIYIGTQTGKFIREPFIQMSDGYNPTDRDWYKEAHENKGKV 150
Cdd:smart00319  83 QQYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQA 134
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
334-428 1.48e-03

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: 39.14  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 334 DDIGKLGNSFNEMSASLQDVITQISFSAEHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQV 413
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 49480166 414 NAAIQDVNGSAESIS 428
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
aro_clust_Mycop TIGR04313
aromatic cluster surface protein; Members of this family are absolutely restricted to the ...
11-104 8.37e-03

aromatic cluster surface protein; Members of this family are absolutely restricted to the Mollicutes (Mycoplasma and Ureaplasma). All have a signal peptide, usually of the lipoprotein type, suggesting surface expression. Most members have lengths of about 280 residues but some members have a nearly full-length duplication. The mostly nearly invariant residue, a Trp,is part of a strongly conserved 9-residue motif, [ND]-W-[LY]-[WF]-X-[LF]-X-N-[LI], where X usually is hydrophobic. Because the hydrophobic six-residue core of this motif almost always contains three to four aromatic residues, we name this family aromatic cluster surface protein. Multiple paralogs may occur in a given Mycoplasma, usually clustered on the genome.


Pssm-ID: 275118  Cd Length: 293  Bit Score: 37.37  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    11 MSIKKKLIISFFLILTIPGLIIGGVSYQTAKTNFEQQITgKAKENISILNTVISQNIEEKFVDAAYFADILTEDTYPNGQ 90
Cdd:TIGR04313   1 MKKKKKKLLIIFSLILASLSLISCSSKSLNKIIKNKIDT-KKDKKDKKWQVFLNNKYINNLLNLVFKNDEDEKNKYIKSQ 79
                          90
                  ....*....|....
gi 49480166    91 EEIVRTKLAQYIKL 104
Cdd:TIGR04313  80 KNLNDELYLKLLKL 93
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
285-660 3.73e-67

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 227.57  E-value: 3.73e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 285 IVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVITQISFSAEHV 364
Cdd:COG0840  64 ISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEAL 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 365 AASAEELTASVQQandatdqitiameqVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEGEDL 444
Cdd:COG0840 144 SGASEEIAASATE--------------LSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEE 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 445 VEQTATQMQSISRSVSEsdaIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQ 524
Cdd:COG0840 210 VRQAVEQMQEIAEELAE---VVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAER 286
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 525 SGESSGEIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVtn 604
Cdd:COG0840 287 SADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEI-- 364
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 49480166 605 aideiaaaaeenTASMQSVAASTEEQVNSMEEISSASQNLAEMAEELQAMTSKFKV 660
Cdd:COG0840 365 ------------NASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
384-659 4.26e-62

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: 209.06  E-value: 4.26e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    384 QITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSVSESD 463
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    464 AIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSGEIANLIAEIKADI 543
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    544 EHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVTNaideiaaaaeentaSMQSV 623
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNA--------------AIDEI 226
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 49480166    624 AASTEEQVNSMEEISSASQNLAEMAEELQAMTSKFK 659
Cdd:smart00283 227 AQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
451-658 5.90e-44

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: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 156.45  E-value: 5.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   451 QMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSG 530
Cdd:pfam00015  14 EMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   531 EIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVtnaideia 610
Cdd:pfam00015  94 EIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQV-------- 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 49480166   611 aaaeeNTASMQsVAASTEEQVNSMEEISSASQNLAEMAEELQAMTSKF 658
Cdd:pfam00015 166 -----NQAVAR-IDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
267-640 2.22e-37

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 145.53  E-value: 2.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  267 MFDEEITQAANPVFYKTFIVIAIAIVFGSVLI---YFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSF 343
Cdd:PRK15048 175 LYRDIVTDNADDYRFAQWQLAVIALVVVLILLvawYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSV 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  344 NEMSASLQDVITQisfsaehvaasaeeltasVQQANDA----TDQITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQD 419
Cdd:PRK15048 255 SHMQRSLTDTVTH------------------VREGSDAiyagTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQ 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  420 VNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSvsesdaiiklldekSKQVGAISEAIQNIATQTNLLALNAAI 499
Cdd:PRK15048 317 NADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAV 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  500 EAARAGEQGRGFAIVADEVRKLAEQSgessgeiANLIAEIKADIEHTVKAMDNvngevqqGLDVVTKTKVSFTEILSSTT 579
Cdd:PRK15048 383 EAARAGEQGRGFAVVAGEVRNLASRS-------AQAAKEIKALIEDSVSRVDT-------GSVLVESAGETMNNIVNAVT 448
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49480166  580 HIVSQVNEMVETTKRIAGDANEVTNAIDEIAAAAEENTASMQ---SVAASTEEQVNSMEEISSA 640
Cdd:PRK15048 449 RVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQesaAAAAALEEQASRLTQAVSA 512
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
206-351 1.90e-05

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 46.16  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  206 LDQNKQIVSHPSRKPGAKVTDPWIKpiyeDKQGNV-----AYTEKDDKKNLIFATNEKTGWKVVGVMfdEEITQAANPVF 280
Cdd:PRK10549  85 FEQDNDSKPGPGMPPHGWRTQFWVV----DQNNKVlvgprGPIPPDGTRRPILVNGAEVGWVIASPV--ERLTRNTDINF 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49480166  281 YK-----TFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQ 351
Cdd:PRK10549 159 DKqqrrtSWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTLE 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
362-539 2.71e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    362 EHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEG 441
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    442 EDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQgrgFAIVADEVRKL 521
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR---IAATERRLEDL 843
                          170
                   ....*....|....*...
gi 49480166    522 AEQSGESSGEIANLIAEI 539
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEI 861
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
411-603 5.87e-54

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: 184.36  E-value: 5.87e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 411 QQVNAAIQDVNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQT 490
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 491 NLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSGEIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVS 570
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190
                ....*....|....*....|....*....|...
gi 49480166 571 FTEILSSTTHIVSQVNEMVETTKRIAGDANEVT 603
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIA 193
Cache_1 pfam02743
Cache domain;
152-223 9.78e-19

Cache domain;


Pssm-ID: 280839  Cd Length: 79  Bit Score: 81.96  E-value: 9.78e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 49480166   152 VTAPYQSASTKNMVVTIAKEVKDGK---GVIGINLNLDNILKISKMINIGEKGYAVILDQNKQIVSHPSRKPGAK 223
Cdd:pfam02743   1 VTEPYVDASTGDMVVTIAQPVKDDGdglGVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLAHPNHKPVTK 75
HAMP pfam00672
HAMP domain;
283-352 7.31e-16

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 73.37  E-value: 7.31e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   283 TFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITiHSKDDIGKLGNSFNEMSASLQD 352
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLE-SGRDEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
303-355 7.49e-12

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 61.50  E-value: 7.49e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 49480166    303 KSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVIT 355
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
305-352 2.12e-11

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: 59.96  E-value: 2.12e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 49480166 305 ITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQD 352
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
TarH pfam02203
Tar ligand binding domain homologue;
7-143 4.70e-10

Tar ligand binding domain homologue;


Pssm-ID: 280382  Cd Length: 171  Bit Score: 58.10  E-value: 4.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166     7 WVKCMSIKKKL--IISFFLILTIPGLIIGGVSYQTAKTNFEQQITGKAKENI---------------------------- 56
Cdd:pfam02203   1 MFKRISISTRLllVLAFLGVLLLVSGGLGLSGLQSANDALDEVYTNSLQQQAaladawvlllqarlaldraallgdapds 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    57 -SILNTvISQNIEEKFVDAAYFADILTEDTY-PNGQEEiVRTKLAQYIKLH-PEVEGIYIGTQTGKFIREPFIQMSDGYN 133
Cdd:pfam02203  81 aELLDR-ARESLAQSEKAWKAYLALPKTAPEeEALADE-LKAKYKQYLQDGlAPLIAALRAGDLDAFFDQPTQKMQPLFN 158
                         170
                  ....*....|
gi 49480166   134 PTDRDWYKEA 143
Cdd:pfam02203 159 ALTRAWYAQA 168
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
280-351 6.20e-09

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 53.53  E-value: 6.20e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49480166 280 FYKTFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQ 351
Cdd:COG2770   5 APIFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQ 76
TarH smart00319
Homologues of the ligand binding domain of Tar; Homologues of the ligand binding domain of the ...
36-150 1.90e-07

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: 49.77  E-value: 1.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166     36 SYQTAKTNFEQQITGKAKENISILNTVISQN-IEEKFVDA-AYFADILTEDTY---------------PNGQEEIvRTKL 98
Cdd:smart00319   4 SYQQAALSLSRVLLLQARNNLNRAGIRMMQNnIGSKAKKLmTAASESLKQAEKnyksyenmtalpradRALDAEL-KEKF 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 49480166     99 AQYIKLHPEVEGIYIGTQTGKFIREPFIQMSDGYNPTDRDWYKEAHENKGKV 150
Cdd:smart00319  83 QQYITALQELIQILGNGNLGAFFDQPTQGMQDGFDPAYRDWLQQAVALKGQA 134
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
334-428 1.48e-03

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: 39.14  E-value: 1.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 334 DDIGKLGNSFNEMSASLQDVITQISFSAEHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQV 413
Cdd:cd11386 106 DEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQ 185
                        90
                ....*....|....*
gi 49480166 414 NAAIQDVNGSAESIS 428
Cdd:cd11386 186 SASTQEIAAAVEEIA 200
aro_clust_Mycop TIGR04313
aromatic cluster surface protein; Members of this family are absolutely restricted to the ...
11-104 8.37e-03

aromatic cluster surface protein; Members of this family are absolutely restricted to the Mollicutes (Mycoplasma and Ureaplasma). All have a signal peptide, usually of the lipoprotein type, suggesting surface expression. Most members have lengths of about 280 residues but some members have a nearly full-length duplication. The mostly nearly invariant residue, a Trp,is part of a strongly conserved 9-residue motif, [ND]-W-[LY]-[WF]-X-[LF]-X-N-[LI], where X usually is hydrophobic. Because the hydrophobic six-residue core of this motif almost always contains three to four aromatic residues, we name this family aromatic cluster surface protein. Multiple paralogs may occur in a given Mycoplasma, usually clustered on the genome.


Pssm-ID: 275118  Cd Length: 293  Bit Score: 37.37  E-value: 8.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    11 MSIKKKLIISFFLILTIPGLIIGGVSYQTAKTNFEQQITgKAKENISILNTVISQNIEEKFVDAAYFADILTEDTYPNGQ 90
Cdd:TIGR04313   1 MKKKKKKLLIIFSLILASLSLISCSSKSLNKIIKNKIDT-KKDKKDKKWQVFLNNKYINNLLNLVFKNDEDEKNKYIKSQ 79
                          90
                  ....*....|....
gi 49480166    91 EEIVRTKLAQYIKL 104
Cdd:TIGR04313  80 KNLNDELYLKLLKL 93
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
285-660 3.73e-67

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 227.57  E-value: 3.73e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 285 IVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVITQISFSAEHV 364
Cdd:COG0840  64 ISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEAL 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 365 AASAEELTASVQQandatdqitiameqVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEGEDL 444
Cdd:COG0840 144 SGASEEIAASATE--------------LSARADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEE 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 445 VEQTATQMQSISRSVSEsdaIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQ 524
Cdd:COG0840 210 VRQAVEQMQEIAEELAE---VVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAER 286
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 525 SGESSGEIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVtn 604
Cdd:COG0840 287 SADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEI-- 364
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 49480166 605 aideiaaaaeenTASMQSVAASTEEQVNSMEEISSASQNLAEMAEELQAMTSKFKV 660
Cdd:COG0840 365 ------------NASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
384-659 4.26e-62

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: 209.06  E-value: 4.26e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    384 QITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSVSESD 463
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    464 AIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSGEIANLIAEIKADI 543
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    544 EHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVTNaideiaaaaeentaSMQSV 623
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNA--------------AIDEI 226
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 49480166    624 AASTEEQVNSMEEISSASQNLAEMAEELQAMTSKFK 659
Cdd:smart00283 227 AQVTQETAAMSEEISAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
451-658 5.90e-44

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: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 156.45  E-value: 5.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   451 QMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLAEQSGESSG 530
Cdd:pfam00015  14 EMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   531 EIANLIAEIKADIEHTVKAMDNVNGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEVtnaideia 610
Cdd:pfam00015  94 EIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQV-------- 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 49480166   611 aaaeeNTASMQsVAASTEEQVNSMEEISSASQNLAEMAEELQAMTSKF 658
Cdd:pfam00015 166 -----NQAVAR-IDQVTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
267-640 2.22e-37

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 145.53  E-value: 2.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  267 MFDEEITQAANPVFYKTFIVIAIAIVFGSVLI---YFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSF 343
Cdd:PRK15048 175 LYRDIVTDNADDYRFAQWQLAVIALVVVLILLvawYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSV 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  344 NEMSASLQDVITQisfsaehvaasaeeltasVQQANDA----TDQITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQD 419
Cdd:PRK15048 255 SHMQRSLTDTVTH------------------VREGSDAiyagTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQ 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  420 VNGSAESISISSLHARERAKEGEDLVEQTATQMQSISRSvsesdaiiklldekSKQVGAISEAIQNIATQTNLLALNAAI 499
Cdd:PRK15048 317 NADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADS--------------SKKIADIISVIDGIAFQTNILALNAAV 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  500 EAARAGEQGRGFAIVADEVRKLAEQSgessgeiANLIAEIKADIEHTVKAMDNvngevqqGLDVVTKTKVSFTEILSSTT 579
Cdd:PRK15048 383 EAARAGEQGRGFAVVAGEVRNLASRS-------AQAAKEIKALIEDSVSRVDT-------GSVLVESAGETMNNIVNAVT 448
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49480166  580 HIVSQVNEMVETTKRIAGDANEVTNAIDEIAAAAEENTASMQ---SVAASTEEQVNSMEEISSA 640
Cdd:PRK15048 449 RVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQesaAAAAALEEQASRLTQAVSA 512
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
279-660 1.45e-36

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 142.90  E-value: 1.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  279 VFYKTFIVIAiAIVFGSVLIYfITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVITQIS 358
Cdd:PRK09793 190 LVFISMIIVA-AIYISSALWW-TRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVR 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  359 FSAEHVAASAEELTASvqqANDatdqitiameqVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERA 438
Cdd:PRK09793 268 KGSQEMHIGIAEIVAG---NND-----------LSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTA 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  439 KEGEDLVEQTATQMQSISRSvsesdaiiklldekSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEV 518
Cdd:PRK09793 334 QAGGVQVSTMTHTMQEIATS--------------SQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEV 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  519 RKLAEQSGESSGEIANLIAEikadiehtvkamdNVNgEVQQGLDVVTKTKVSFTEILSStthiVSQVNEmvettkrIAGD 598
Cdd:PRK09793 400 RNLASRSAQAAKEIKGLIEE-------------SVN-RVQQGSKLVNNAAATMTDIVSS----VTRVND-------IMGE 454
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49480166  599 ANEVTNAIDEIAAAAEENTASMQSVaasTEEQVNSMEEISSASQNLAEMAEELQAMTSKFKV 660
Cdd:PRK09793 455 IASASEEQRRGIEQVAQAVSQMDQV---TQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
284-660 4.72e-33

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 132.77  E-value: 4.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  284 FIVIAIAIVFGSVLIYF-ITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQDVITQISFSAE 362
Cdd:PRK15041 196 LVGVMIVVLAVIFAVWFgIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGAN 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  363 HVAASAEEltasvqqandatdqITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEGE 442
Cdd:PRK15041 276 AIYSGASE--------------IATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGG 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  443 DLVEQTATQMQSISRSvsesdaiiklldekSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQGRGFAIVADEVRKLA 522
Cdd:PRK15041 342 KVVDNVVQTMRDISTS--------------SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLA 407
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  523 EQSGESSGEIANLIAeikadiehtvkamDNVnGEVQQGLDVVTKTKVSFTEILSSTTHIVSQVNEMVETTKRIAGDANEV 602
Cdd:PRK15041 408 QRSAQAAREIKSLIE-------------DSV-GKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDEQSRGIDQV 473
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 49480166  603 tnaideiaaaaEENTASMQSVaasTEEQVNSMEEISSASQNLAEMAEELQAMTSKFKV 660
Cdd:PRK15041 474 -----------GLAVAEMDRV---TQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
283-540 1.46e-08

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 56.32  E-value: 1.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 283 TFIVIAIAIVFGsvlIYFiTKSITRPLRKIADSAYKISKGDLTEKITIHSKD-DIGKLGNSFNEMSASLQdvitqisfsa 361
Cdd:COG5000 287 ALLVLLAAIWTA---IAF-ARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDeDVGRLSKAFNKMTEQLS---------- 352
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 362 ehvaasaeELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEgaatlqqvNAAIQDVNGSAESIsisslharerakeg 441
Cdd:COG5000 353 --------SQQEALERAKDALEQRRRFLEAVLSGLTAGVIGFDN--------RGCITTVNPSAEQI-------------- 402
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 442 edlVEQTATQM--QSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQTNLLalnaaIEAAR-AGEQGRGFAIVADEV 518
Cdd:COG5000 403 ---LGKPFDQLlgQSLSAIAPELEEVFAEAGAAARTDKRVEVKLAREGEERTLN-----VQATRePEDNGNGYVVTFDDI 474
                       250       260
                ....*....|....*....|....
gi 49480166 519 RKL-AEQSGESSGEIANLIA-EIK 540
Cdd:COG5000 475 TDLvIAQRSAAWGDVARRIAhEIK 498
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms];
284-352 3.01e-08

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 55.13  E-value: 3.01e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 49480166 284 FIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQD 352
Cdd:COG5002  33 ISGTLIALIITALLGILLARTITKPITDMRKQAVDMARGNYSRKVKVYGTDEIGELADSFNDLTKRVQE 101
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
286-379 1.74e-07

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 52.73  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 286 VIAIAIVFGSVL-IYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQdvitQISFSAEHv 364
Cdd:COG3850 155 AGMLLILLLVVFtIYWLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGELK----KLYADLEQ- 229
                        90
                ....*....|....*
gi 49480166 365 aaSAEELTASVQQAN 379
Cdd:COG3850 230 --RVEEKTRDLEQKN 242
PRK10549 PRK10549
signal transduction histidine-protein kinase BaeS; Provisional
206-351 1.90e-05

signal transduction histidine-protein kinase BaeS; Provisional


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 46.16  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  206 LDQNKQIVSHPSRKPGAKVTDPWIKpiyeDKQGNV-----AYTEKDDKKNLIFATNEKTGWKVVGVMfdEEITQAANPVF 280
Cdd:PRK10549  85 FEQDNDSKPGPGMPPHGWRTQFWVV----DQNNKVlvgprGPIPPDGTRRPILVNGAEVGWVIASPV--ERLTRNTDINF 158
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49480166  281 YK-----TFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLQ 351
Cdd:PRK10549 159 DKqqrrtSWLIVALSTLLAALATFLLARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQLASTLE 234
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
282-380 2.29e-05

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 46.20  E-value: 2.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  282 KTFIVI-AIAIVFGsvlIYFITKSITRPLRKIADSAYKISKGDLTEKITIHSKDDIGKLGNSFNEMSASLqdvitqiSFS 360
Cdd:PRK10600 128 RVFAVFmALLLVFT---IIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAEL-------AES 197
                         90       100
                 ....*....|....*....|
gi 49480166  361 AEHVAASAEELTASVQQAND 380
Cdd:PRK10600 198 YAVLEQRVQEKTAGLEQKNQ 217
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
347-566 2.30e-04

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


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 42.70  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 347 SASLQDVITQISFSAEHVAA---SAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDvngs 423
Cdd:COG4372  42 TAVLVTVLTGMLISAATLAIlflLNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQE---- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 424 AESISISSLHARERAKEGEDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAAR 503
Cdd:COG4372 118 REAVRQELAAARQNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQ 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49480166 504 AGEQGRGFAIVADEVRKLAEqsgessgEIANLIAEIKA---DIEHTVKAMDNVNGEVQQGLDVVTK 566
Cdd:COG4372 198 IEQEAQNLATRANAAQARTE-------ELARRAAAAQQtaqAIQQRDAQISQKAQQIAARAEQIRE 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
362-539 2.71e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    362 EHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAESISISSLHARERAKEG 441
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    442 EDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQVGAISEAIQNIATQTNLLALNAAIEAARAGEQgrgFAIVADEVRKL 521
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR---IAATERRLEDL 843
                          170
                   ....*....|....*...
gi 49480166    522 AEQSGESSGEIANLIAEI 539
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEI 861
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
285-380 4.73e-04

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 41.76  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  285 IVIAIAIVFGSVLI--------YFITKSITRPLRKIADSAYKISKGDLTE-KITIHSKDDIGKLGNSFNEMSASLQdvit 355
Cdd:PRK10935 148 ILLAAISLLGLILIltlvfftvRFTRRQVVAPLNQLVTASQQIEKGQFDHiPLDTTLPNELGLLAKAFNQMSSELH---- 223
                         90       100
                 ....*....|....*....|....*
gi 49480166  356 QISFSAEHvaaSAEELTASVQQAND 380
Cdd:PRK10935 224 KLYRSLEA---SVEEKTRKLTQANR 245
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
335-447 5.31e-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: 41.12  E-value: 5.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    335 DIGKLGNSFNEMSASLQDVITQISFSAEHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQVN 414
Cdd:smart00283 148 EIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIA 227
                           90       100       110
                   ....*....|....*....|....*....|...
gi 49480166    415 AAIQDVNGSAESISISSLHARERAKEGEDLVEQ 447
Cdd:smart00283 228 QVTQETAAMSEEISAAAEELSGLAEELDELVER 260
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
350-475 7.50e-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: 40.35  E-value: 7.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166    350 LQDVITQISFSAEHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNgsaesisi 429
Cdd:smart00283 156 IQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIA-------- 227
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 49480166    430 sslharerakegeDLVEQTATQMQSISRSVSESDAIIKLLDEKSKQ 475
Cdd:smart00283 228 -------------QVTQETAAMSEEISAAAEELSGLAEELDELVER 260
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
350-646 1.15e-03

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 40.57  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 350 LQDVITQISFSAEHVAASAEELTASVQQANDATDQI---TIAMEQVSGGAESQSQGVEEGAATLQQVNAAIQDVNGSAES 426
Cdd:COG1511 253 LKQGAEQLNEGIGEFSSGLSELNSGVQDLAAGVPQLnqgISALAAGLSLPDSLGDQFSSLQEALTQIAQGLKQKTSSSLE 332
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 427 ISISSLHARERAKEGEDLVEQTATQMQSISRSVSESdaiIKLLDEKSKQVGAISEAI--QNIATQTNLLALNAAIEAARA 504
Cdd:COG1511 333 AAQGSLSSLQSMLALSKSLDLTAEGATVDALGAPDG---VQWLDESQKTLATLSELLstGIDGVSEGLDALEQASAQLAK 409
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166 505 GEQgrgfaIVADEVRKLAEQSGESSGEIANLIAEIKADIEHTVkaMDNVNGEVQQGLDVVTKTKVSFTEILSS--TTHIV 582
Cdd:COG1511 410 SLA-----KLKTAVAQIAASIAQLLPGASEVLKTLKSKGLDKL--LNQLNGALAKGSNALVQGLSDANDSFRSitSAQLK 482
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49480166 583 SQVNEMVETTKRIAGDANEVTNAIDEIAAAAEENTASMQSVAASTEEQVnsmeEISSASQNLAE 646
Cdd:COG1511 483 AGLNTLADGSNDLSSLGPGLGQLADGSKLLADGLSELNTGSAQLRDGLG----ELSDGLTELAD 542
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
268-362 2.02e-03

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 39.68  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   268 FDEEITQAanpvFYKTFIVIAIAIVFGSVLI-YFITKSITRPLRKIADSAYKISKGDLTEKITIHSK-DDIGKLGNSFNE 345
Cdd:TIGR01386 154 AHTHLLDA----LRKWLILIAVLLVLLTALLgWWITRLGLEPLRRLSAVAARISPESLDQRLDPSRApAELRELAQSFNA 229
                          90
                  ....*....|....*...
gi 49480166   346 MSASLQDVITQIS-FSAE 362
Cdd:TIGR01386 230 MLGRLEDAFQRLSqFSAD 247
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
252-393 2.78e-03

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: 39.34  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   252 IFATNEKTGWKVVgvmfdEEITQA----ANPVFYKTFIVIaIAIVFGSVLIYFITKS-----ITRpLRKIADSAYKiSKG 322
Cdd:TIGR03785 378 IWIDTEVLGAVIA-----EQTTNGirtlRNSALEKLFNVI-LAIMSIGTLALFGFASwiswrIRR-LSDDAEAAID-SQG 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166   323 DLTEKITI-HSKDDIGKLGNSFNEMSASLQDVITQI-SFSAE--H-------VAASAEELTASVQQANDATDQITIAMEQ 391
Cdd:TIGR03785 450 RISGAIPAsRSRDEIGDLSRSFAQMVARLRQYTHYLeNMSSRlsHelrtpvaVVRSSLENLELQALEQEKQKYLERAREG 529

                  ..
gi 49480166   392 VS 393
Cdd:TIGR03785 530 TE 531
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
345-412 5.34e-03

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: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 37.43  E-value: 5.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 49480166   345 EMSASLQDVITQISFSAEHVAASAEELTASVQQANDATDQITIAMEQVSGGAESQSQGVEEGAATLQQ 412
Cdd:pfam00015 139 EAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQ 206
cpxA PRK09470
two-component sensor protein; Provisional
277-355 7.40e-03

two-component sensor protein; Provisional


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 37.99  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49480166  277 NPVFYKTFIVIAIAIVFGSVLIYFITKSITRPLRKIADSAYKISKGDLTekitIHSKDDIG-----KLGNSFNEMSASLQ 351
Cdd:PRK09470 162 NLLFDRPLLLLLVTMLVSTPLLLWLAWSLAKPARKLKNAADEVAQGNLR----QHPELETGpqefrQAGASFNQMVTALE 237

                 ....
gi 49480166  352 DVIT 355
Cdd:PRK09470 238 RMMT 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
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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