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Conserved domains on  [gi|333936158|emb|CBY99288|]
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nonidentical kinase-1, partial [Gelasinospora brevispora]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
 166-253 9.22e-20

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 87.98  E-value: 9.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 166 GEMDELKKKINQMVYNL---RDSIQRNT-QA----REA-----------------AELANKTKSEFLANMSHEIRTPMNG 220
Cdd:PRK11107 231 GELDMLKNGINAMAMSLsayHEEMQQNIdQAtsdlRETleqmeiqnveldlakkrAQEAARIKSEFLANMSHELRTPLNG 310

                         90       100       110
                 ....*....|....*....|....*....|...
gi 333936158 221 IIGMTQLTLDTDLTQYQREMLNIVNSLANSLLT 253
Cdd:PRK11107 311 VIGFTRQTLKTPLTPTQRDYLQTIERSANNLLA 343
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 46-90 7.29e-07

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 Af1503 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: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 44.74  E-value: 7.29e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 333936158  46 TSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
135-187 2.26e-05

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


:

Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 41.08  E-value: 2.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 333936158   135 NNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRDSIQ 187
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 166-253 9.22e-20

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 87.98  E-value: 9.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 166 GEMDELKKKINQMVYNL---RDSIQRNT-QA----REA-----------------AELANKTKSEFLANMSHEIRTPMNG 220
Cdd:PRK11107 231 GELDMLKNGINAMAMSLsayHEEMQQNIdQAtsdlRETleqmeiqnveldlakkrAQEAARIKSEFLANMSHELRTPLNG 310

                         90       100       110
                 ....*....|....*....|....*....|...
gi 333936158 221 IIGMTQLTLDTDLTQYQREMLNIVNSLANSLLT 253
Cdd:PRK11107 311 VIGFTRQTLKTPLTPTQRDYLQTIERSANNLLA 343
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
 167-253 3.61e-19

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 86.37  E-value: 3.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158  167 EMDELKKKINQMVYNLRdsiqrntQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNS 246
Cdd:TIGR02956 435 ELAETNERLNAEVKNHA-------KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINR 507


                  ....*..
gi 333936158  247 LANSLLT 253
Cdd:TIGR02956 508 SGESLLD 514
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
182-252 5.70e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 67.24  E-value: 5.70e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333936158 182 LRDSIQRNTQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLtLDTDLTQYQREMLNIVNSLANSLL 252
Cdd:COG0642   89 LLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLEL-LLEELDEEQREYLETILRSADRLL 158
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
 203-252 2.06e-12

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 60.66  E-value: 2.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 333936158   203 KSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLANSLL 252
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLL 51
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
 203-252 2.61e-12

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 60.30  E-value: 2.61e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 333936158  203 KSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLANSLL 252
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLL 51
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
 200-253 1.84e-10

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 55.30  E-value: 1.84e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333936158 200 NKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDL-TQYQREMLNIVNSLANSLLT 253
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLR 55
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 46-90 7.29e-07

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 Af1503 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: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 44.74  E-value: 7.29e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 333936158  46 TSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
44-90 3.01e-06

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 43.39  E-value: 3.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 333936158    44 NLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
HAMP pfam00672
HAMP domain;
41-90 3.19e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 43.38  E-value: 3.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 333936158   41 MASNLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:pfam00672   2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
133-218 3.28e-06

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 47.51  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 133 MANNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLrdsiQRNTQAREAaelanktkseFLANMSH 212
Cdd:NF012163 184 LARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLASTL----EKNEQMRRD----------FMADISH 249


                 ....*.
gi 333936158 213 EIRTPM 218
Cdd:NF012163 250 ELRTPL 255
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
135-187 2.26e-05

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 41.08  E-value: 2.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 333936158   135 NNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRDSIQ 187
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
153-221 3.44e-04

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 41.55  E-value: 3.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333936158 153 DGDFTKLVEVEASGEMDELKKKINQMVynlrDSIQRntQAREAAELANkTKSEFLANMSHEIRTPMNGI 221
Cdd:NF040691 228 AGDLSERMPVKGEDDLARLARSFNQMA----DSLQR--QIRQLEELSR-LQQRFVSDVSHELRTPLTTI 289
HAMP pfam00672
HAMP domain;
133-184 3.50e-03

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 34.91  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333936158  133 MANNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRD 184
Cdd:pfam00672   2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
 166-253 9.22e-20

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 87.98  E-value: 9.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 166 GEMDELKKKINQMVYNL---RDSIQRNT-QA----REA-----------------AELANKTKSEFLANMSHEIRTPMNG 220
Cdd:PRK11107 231 GELDMLKNGINAMAMSLsayHEEMQQNIdQAtsdlRETleqmeiqnveldlakkrAQEAARIKSEFLANMSHELRTPLNG 310

                         90       100       110
                 ....*....|....*....|....*....|...
gi 333936158 221 IIGMTQLTLDTDLTQYQREMLNIVNSLANSLLT 253
Cdd:PRK11107 311 VIGFTRQTLKTPLTPTQRDYLQTIERSANNLLA 343
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
 167-253 3.61e-19

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 86.37  E-value: 3.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158  167 EMDELKKKINQMVYNLRdsiqrntQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNS 246
Cdd:TIGR02956 435 ELAETNERLNAEVKNHA-------KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINR 507


                  ....*..
gi 333936158  247 LANSLLT 253
Cdd:TIGR02956 508 SGESLLD 514
PRK15347 PRK15347
two component system sensor kinase;
169-253 1.44e-15

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 75.83  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 169 DELKKKINQMVYNLrdsiqrnTQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLA 248
Cdd:PRK15347 371 DTLENKVAERTQAL-------AEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCT 443


                 ....*
gi 333936158 249 NSLLT 253
Cdd:PRK15347 444 LSLLA 448
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
 191-253 4.98e-13

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 68.39  E-value: 4.98e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 333936158 191 QAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLANSLLT 253
Cdd:PRK11466 432 QARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLT 494
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
182-252 5.70e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 67.24  E-value: 5.70e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333936158 182 LRDSIQRNTQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLtLDTDLTQYQREMLNIVNSLANSLL 252
Cdd:COG0642   89 LLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLEL-LLEELDEEQREYLETILRSADRLL 158
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
 203-252 2.06e-12

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 60.66  E-value: 2.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 333936158   203 KSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLANSLL 252
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLL 51
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
 183-251 2.17e-12

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 66.50  E-value: 2.17e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333936158 183 RDSIQRNtQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLANSL 251
Cdd:PRK11091 264 RDITERK-RYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITL 331
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
 203-252 2.61e-12

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 60.30  E-value: 2.61e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 333936158  203 KSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQREMLNIVNSLANSLL 252
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLL 51
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
191-253 1.70e-11

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 62.23  E-value: 1.70e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333936158 191 QAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLD--TDLTQYQREMLNIVNSLANSLLT 253
Cdd:COG2205    4 EALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLR 68
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
 200-253 1.84e-10

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 55.30  E-value: 1.84e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 333936158 200 NKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDL-TQYQREMLNIVNSLANSLLT 253
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLR 55
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
159-223 1.02e-07

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 52.28  E-value: 1.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 333936158 159 LVEVEASGEMDElkkkinqmvynlrdSIQRNTQAreaAELANKTKSEFLANMSHEIRTPMNGIIG 223
Cdd:PRK10841 420 LVDVSARVKMEE--------------SLQEMAQA---AEQASQSKSMFLATVSHELRTPLYGIIG 467
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
146-253 2.70e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 50.71  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 146 DITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRDSIQRNTQAREAAElanKTKSEFLANMSHEIRTPMNGIIGMT 225
Cdd:COG5002  111 LILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLE---QMRREFVANVSHELRTPLTSIRGYL 187

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 333936158 226 QLTLD--TDLTQYQREMLNIV-------NSLANSLLT 253
Cdd:COG5002  188 ELLLDgaADDPEERREYLEIIleeaerlSRLVNDLLD 224
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 157-238 4.29e-07

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 50.36  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 157 TKLVEVEASGEMDELKKKINQMVynLRDsiqrNTQAREAAELANKTK-----SEFLANMSHEIRTPMNGIIGMTQLTLDT 231
Cdd:COG5809  225 WRLLEASGAPIKKNGEVDGIVII--FRD----ITERKKLEELLRKSEklsvvGELAAGIAHEIRNPLTSLKGFIQLLKDT 298


                 ....*..
gi 333936158 232 DLTQYQR 238
Cdd:COG5809  299 IDEEQKT 305
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
177-252 6.71e-07

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 50.12  E-value: 6.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 333936158  177 QMVYNLRDSIQRNTQAREAAELANKTKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQYQR-EMLNIVNSLANSLL 252
Cdd:PRK09959  686 QDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLL 762
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 46-90 7.29e-07

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 Af1503 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: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 44.74  E-value: 7.29e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 333936158  46 TSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSKDEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
44-90 3.01e-06

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 43.39  E-value: 3.01e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 333936158    44 NLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
HAMP pfam00672
HAMP domain;
41-90 3.19e-06

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 43.38  E-value: 3.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 333936158   41 MASNLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL 90
Cdd:pfam00672   2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERL 51
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
133-218 3.28e-06

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 47.51  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 133 MANNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLrdsiQRNTQAREAaelanktkseFLANMSH 212
Cdd:NF012163 184 LARGLLAPVKRLVEATHRLAAGDYTTRVTPTSNDELGKLAQDFNQLASTL----EKNEQMRRD----------FMADISH 249


                 ....*.
gi 333936158 213 EIRTPM 218
Cdd:NF012163 250 ELRTPL 255
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
135-187 2.26e-05

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


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 41.08  E-value: 2.26e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 333936158   135 NNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRDSIQ 187
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
133-218 2.51e-05

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 45.01  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 133 MANNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQmvynLRDSIQRNTQAREAaelanktkseFLANMSH 212
Cdd:PRK10549 184 LARGLLAPVKRLVEGTHKLAAGDFTTRVTPTSRDELGRLAQDFNQ----LASTLEKNEQMRRD----------FMADISH 249


                 ....*.
gi 333936158 213 EIRTPM 218
Cdd:PRK10549 250 ELRTPL 255
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
 157-235 3.65e-05

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: 44.30  E-value: 3.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333936158  157 TKLVEVEASGEMDELKKKINQMVYNLRDSIQRntqareaaelanktKSEFLANMSHEIRTPMNGIIGMTQLTLDTDLTQ 235
Cdd:TIGR01386 209 QRLDPSRAPAELRELAQSFNAMLGRLEDAFQR--------------LSQFSADLAHELRTPLTNLLGQTQVALSQPRTG 273
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 41-227 5.44e-05

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 43.80  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158  41 MASNLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRL--SIFCNEVQRVAKDVGVDGIMGGqadVAG 118
Cdd:COG5000   29 LARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLkeQREELEERRRYLETILENLPAG---VIV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 119 LKGRWKeITTdVNTMANNLTAQVRA---------------FGDITNAATDGDFTKLVEVEASGEmdelkKKINQMVYNLR 183
Cdd:COG5000  106 LDADGR-ITL-ANPAAERLLGIPLEeligkpleellpeldLAELLREALERGWQEEIELTRDGR-----RTLLVRASPLR 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 333936158 184 D-----SIQRNTQAREAAELAnkTKSEFLANMSHEIRTPMNGIIGMTQL 227
Cdd:COG5000  179 DdgyviVFDDITELLRAERLA--AWGELARRIAHEIKNPLTPIQLSAER 225
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
41-196 9.70e-05

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 43.09  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158  41 MASNLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRLSIFCNEVQRVAKDV--GVDGIMGGQADVAG 118
Cdd:COG0840  202 LSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVasASEELAASAEELAA 281

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 333936158 119 LKGRWKEITTDVNTMANNLTAQVRAFGDITNAATdgdftklvevEASGEMDELKKKINQMVYNLRDSIQRNTQAREAA 196
Cdd:COG0840  282 GAEEQAASLEETAAAMEELSATVQEVAENAQQAA----------ELAEEASELAEEGGEVVEEAVEGIEEIRESVEET 349
HAMP_2 pfam18947
HAMP domain;
28-88 2.12e-04

HAMP domain;


Pssm-ID: 465927 [Multi-domain]  Cd Length: 67  Bit Score: 38.62  E-value: 2.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 333936158   28 EGKWKDLTENVNTMASNLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVD 88
Cdd:pfam18947   3 QGDFRKIVEGVNNTLDAIITPLNEAADYVDRISKGDIPEKITDEYKGDFNEIKNNLNALID 63
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
153-221 3.44e-04

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 41.55  E-value: 3.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 333936158 153 DGDFTKLVEVEASGEMDELKKKINQMVynlrDSIQRntQAREAAELANkTKSEFLANMSHEIRTPMNGI 221
Cdd:NF040691 228 AGDLSERMPVKGEDDLARLARSFNQMA----DSLQR--QIRQLEELSR-LQQRFVSDVSHELRTPLTTI 289
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
206-253 4.53e-04

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 41.15  E-value: 4.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 333936158 206 FLANMSHEIRTPMNGIIGMTQLTLDTDLT--------QYQREMLNIVNSLANSLLT 253
Cdd:PRK11006 207 FFANVSHELRTPLTVLQGYLEMMQDQPLEgalrekalHTMREQTQRMEGLVKQLLT 262
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
186-253 9.64e-04

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 39.83  E-value: 9.64e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 333936158 186 IQRNTQAREAAELAnktkSEFLANMSHEIRTPMNGIIGMTQLtLDTDLT-QYQREMLNIV-------NSLANSLLT 253
Cdd:COG3852  122 LERELRRAEKLAAV----GELAAGLAHEIRNPLTGIRGAAQL-LERELPdDELREYTQLIieeadrlNNLVDRLLS 192
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
30-214 1.85e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 39.23  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158  30 KWKDLTENVNTMASNLTSQVRGISTVTQAIANGDMSRKIEVEAKGEILILKETINNMVDRLSIFCNEVQRVAKDVGVDGI 109
Cdd:COG0840   99 ALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 333936158 110 MGGQADVAGLKGRWKEITTDVNTMANNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRDSIQrn 189
Cdd:COG0840  179 LALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVG-- 256

                        170       180
                 ....*....|....*....|....*
gi 333936158 190 tQAREAAElANKTKSEFLANMSHEI 214
Cdd:COG0840  257 -QVRESAE-QVASASEELAASAEEL 279
HAMP pfam00672
HAMP domain;
133-184 3.50e-03

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 34.91  E-value: 3.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 333936158  133 MANNLTAQVRAFGDITNAATDGDFTKLVEVEASGEMDELKKKINQMVYNLRD 184
Cdd:pfam00672   2 LARRILRPLRRLAEAARRIASGDLDVRLPVSGRDEIGELARAFNQMAERLRE 53
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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