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Conserved domains on  [gi|89895084|ref|YP_518571|]
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hypothetical protein DSY2338 [Desulfitobacterium hafniense Y51]

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List of domain hits

Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
193-240 1.02e-03

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: 37.23  E-value: 1.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 89895084 193 ISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTLNELSAQLR 240
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGD-LDVRLPVTGRDEIGELARAFNQMAERLR 47
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
300-507 4.85e-32

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


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 121.96  E-value: 4.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 300 EEIDAALTSISQRAEEGAvsshEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMI----HLLSEINAI 375
Cdd:cd11386   1 EELSASIEEVAASADQVA----ETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSaeigEIVEVIDDI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 376 ADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEEDVLANYD 455
Cdd:cd11386  77 AEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 89895084 456 NMVSVgakyasdaKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASA 507
Cdd:cd11386 157 TGRAF--------EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
2-92 7.08e-26

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


:

Pssm-ID: 214995  Cd Length: 91  Bit Score: 101.56  E-value: 7.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084      2 LYDDYDNVIKSEVETAVHLVDFYYKQFQEGLMTEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRR 81
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAAGKLTEEEAQAQAKAALRALRYGGDGYFFVYDSDGVMLMHPAKPELEGKNLS 80
                           90
                   ....*....|.
gi 89895084     82 ELTDPNGVKLI 92
Cdd:smart01049  81 DLKDPNGKYLF 91
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
250-324 6.25e-04

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


The actual alignment was detected with superfamily member cd11386:

Pssm-ID: 206779  Cd Length: 200  Bit Score: 39.91  E-value: 6.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 250 VQDLTQQANDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSSHEVS 324
Cdd:cd11386 126 IEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
140-528 1.62e-44

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 162.85  E-value: 1.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 140 ISTGNYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIyIQEINH 219
Cdd:COG0840  31 DELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDL-TKRIDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 220 TSQDEIGLLAKTLNELSAQLRNFISGAQNGVQDLTQQANDFTSLAGRvedtvqdsaektarINELMEAVAASTGEITRAI 299
Cdd:COG0840 110 SSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATE--------------LSARADQQAESLEEVASAI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 300 EEIDAALTSISQRAEEGAVSSHEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMIHLlseINAIADQT 379
Cdd:COG0840 176 EELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKKLSESSQEIEEITSV---INSIAEQT 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 380 DLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEE------DVLAN 453
Cdd:COG0840 253 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEgvklveETGSS 332
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 454 YDNMVSVGAKYASDAKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASAESIEGIFQQTEMILNHMKEIK 528
Cdd:COG0840 333 LGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFK 407
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
193-240 1.02e-03

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: 37.23  E-value: 1.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 89895084 193 ISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTLNELSAQLR 240
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGD-LDVRLPVTGRDEIGELARAFNQMAERLR 47
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
300-507 4.85e-32

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: 121.96  E-value: 4.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 300 EEIDAALTSISQRAEEGAvsshEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMI----HLLSEINAI 375
Cdd:cd11386   1 EELSASIEEVAASADQVA----ETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSaeigEIVEVIDDI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 376 ADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEEDVLANYD 455
Cdd:cd11386  77 AEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 89895084 456 NMVSVgakyasdaKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASA 507
Cdd:cd11386 157 TGRAF--------EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
2-92 7.08e-26

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995  Cd Length: 91  Bit Score: 101.56  E-value: 7.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084      2 LYDDYDNVIKSEVETAVHLVDFYYKQFQEGLMTEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRR 81
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAAGKLTEEEAQAQAKAALRALRYGGDGYFFVYDSDGVMLMHPAKPELEGKNLS 80
                           90
                   ....*....|.
gi 89895084     82 ELTDPNGVKLI 92
Cdd:smart01049  81 DLKDPNGKYLF 91
Cache_2 pfam08269
Cache domain;
10-93 7.81e-26

Cache domain;


Pssm-ID: 254697  Cd Length: 95  Bit Score: 101.61  E-value: 7.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    10 IKSEVETAVHLVDFYYKQFQEGLMTEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRRELTDPNGV 89
Cdd:pfam08269  12 LKAVVESALSIIKEYYQQAQKGKLTREEAQAQAKALLRALRYDGDGYFFAYDSNGTNVMHPIKPELVGKNLSNLKDPNGN 91

                  ....
gi 89895084    90 KLIQ 93
Cdd:pfam08269  92 NVFV 95
HAMP pfam00672
HAMP domain;
171-241 1.07e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 55.31  E-value: 1.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89895084   171 SVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIYiQEINHTSQDEIGLLAKTLNELSAQLRN 241
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLD-DRVPVSGPDEIGELARAFNQMADRLRE 70
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
170-244 7.87e-07

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 46.99  E-value: 7.87e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 170 VSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTLNELSAQLRNFIS 244
Cdd:COG2770   7 IFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGD-LSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
191-244 1.59e-04

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 39.92  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 89895084    191 RRISDPLNALVKAFEKDANGQIYiQEINHTSQDEIGLLAKTLNELSAQLRNFIS 244
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLT-VRLPVDGRDEIGELARAFNEMADRLEETIA 53
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
250-324 6.25e-04

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: 39.91  E-value: 6.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 250 VQDLTQQANDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSSHEVS 324
Cdd:cd11386 126 IEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
140-528 1.62e-44

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 162.85  E-value: 1.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 140 ISTGNYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIyIQEINH 219
Cdd:COG0840  31 DELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDL-TKRIDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 220 TSQDEIGLLAKTLNELSAQLRNFISGAQNGVQDLTQQANDFTSLAGRvedtvqdsaektarINELMEAVAASTGEITRAI 299
Cdd:COG0840 110 SSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATE--------------LSARADQQAESLEEVASAI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 300 EEIDAALTSISQRAEEGAVSSHEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMIHLlseINAIADQT 379
Cdd:COG0840 176 EELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKKLSESSQEIEEITSV---INSIAEQT 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 380 DLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEE------DVLAN 453
Cdd:COG0840 253 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEgvklveETGSS 332
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 454 YDNMVSVGAKYASDAKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASAESIEGIFQQTEMILNHMKEIK 528
Cdd:COG0840 333 LGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFK 407
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
281-549 9.68e-37

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: 137.03  E-value: 9.68e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    281 INELMEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSSHEVSDRAQKLQD---DSNHSIKKTKAIYDTTRSGVEQAIS 357
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEaaeEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    358 EVKKVEEMI----HLLSEINAIADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVD 433
Cdd:smart00283  82 AVEELEESSdeigEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    434 KLVDNIRQVlvfieedvlanyDNMVSVGAKYASDA----KHINAIMLELSSTSEEISASTNEVSTRTGEVSGSIsasaES 509
Cdd:smart00283 162 EAVAAMEES------------SSEVEEGVELVEETgdalEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAI----DE 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 89895084    510 IEGIFQQTEmilNHMKEIKSNSENNLATVTDLKQYIDKFK 549
Cdd:smart00283 226 IAQVTQETA---AMSEEISAAAEELSGLAEELDELVERFK 262
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms]
34-239 3.69e-27

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 226930 [Multi-domain]  Cd Length: 459  Bit Score: 113.00  E-value: 3.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  34 TEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRRELTDPNGVKLIQQLLKAAQenENGGYSDYMWE 113
Cdd:COG4564  74 SDEAAKQEVKAILTNLDYGSDGYFFVYDYQGTNLVHPRQPELVGQNLWQLTDPRGDRVIQALIAKAQ--EGGGLHQYLWE 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 114 KPNdvgTNELSPKRAYSKEFQPWNWVISTGNYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRi 193
Cdd:COG4564 152 KPS---SHETVDKLSYAAGLDKWEWMIGTGLYLDDVSAETAAAQAAVRANIDTTFLIVVLIAVVAVLLVFATCLALNLR- 227
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 89895084 194 sdplnalvKAFEKDANGQIYIQEINHTSQDEIGLLAKTLNELSAQL 239
Cdd:COG4564 228 --------EHRLADKKLKELAQRVVDTQEDERARLARELHDGISQN 265
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
327-550 3.44e-23

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


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 97.52  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   327 AQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEV-KKVEEMIHLLSEINAIADQTDLLALNAAIESARAGEAGRGFAVVAD 405
Cdd:pfam00015   3 ASDLAQLASEEALDEMSQIGQVVDDAVETMEELeTSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   406 EIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEEDVlANYDNMVSVGAKYASDAKHINAIMLELSSTSEEI 485
Cdd:pfam00015  83 EVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGS-TIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084   486 SASTNEVSTRTGEVSGSisasaesiegifqqTEMILNHMKEIKSNSENNLATVTDLKQYIDKFKI 550
Cdd:pfam00015 162 SAGIDQVNQAVARIDQV--------------TQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
144-511 2.03e-22

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 99.64  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  144 NYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIyIQEINHTSQD 223
Cdd:PRK15041 169 AYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDL-VKPIEVDGSN 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  224 EIGLLAKTLNELSAQLRNFISGAQNGvqdltqqANDFTSLAGRVEDTVQDSAEKTarinelmEAVAASTGEITRAIEEID 303
Cdd:PRK15041 248 EMGQLAESLRHMQGELMRTVGDVRNG-------ANAIYSGASEIATGNNDLSSRT-------EQQAASLEETAASMEQLT 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  304 AaltSISQRAEEGAVSSH---EVSDRAQKLQDDSNHSIKKTKAIydttrSGVEQAISEVkkveemihlLSEINAIADQTD 380
Cdd:PRK15041 314 A---TVKQNAENARQASHlalSASETAQRGGKVVDNVVQTMRDI-----STSSQKIADI---------ISVIDGIAFQTN 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  381 LLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDklvdnIRQVLVFIEEDVLANYDNMVSv 460
Cdd:PRK15041 377 ILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVD-----VGSTLVESAGETMAEIVSAVT- 450
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 89895084  461 gakyasdakHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASAESIE 511
Cdd:PRK15041 451 ---------RVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVE 492
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
161-325 6.81e-04

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: 40.88  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   161 GDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFekDANGQIYIQEINHTSQDEIGLLAKTLNELSAQLR 240
Cdd:TIGR03785 402 NSALEKLFNVILAIMSIGTLALFGFASWISWRIRRLSDDAEAAI--DSQGRISGAIPASRSRDEIGDLSRSFAQMVARLR 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   241 NFISGAQNGVQDLTQQANdfTSLAgrvedTVQDSAEKTarinELMEAVAASTGEITRA---IEEIDAALTSISQRAE-EG 316
Cdd:TIGR03785 480 QYTHYLENMSSRLSHELR--TPVA-----VVRSSLENL----ELQALEQEKQKYLERAregTERLSMILNNMSEATRlEQ 548

                  ....*....
gi 89895084   317 AVSSHEVSD 325
Cdd:TIGR03785 549 AIQSAEVED 557
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
193-240 1.02e-03

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: 37.23  E-value: 1.02e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 89895084 193 ISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTLNELSAQLR 240
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGD-LDVRLPVTGRDEIGELARAFNQMAERLR 47
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
300-507 4.85e-32

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: 121.96  E-value: 4.85e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 300 EEIDAALTSISQRAEEGAvsshEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMI----HLLSEINAI 375
Cdd:cd11386   1 EELSASIEEVAASADQVA----ETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSaeigEIVEVIDDI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 376 ADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEEDVLANYD 455
Cdd:cd11386  77 AEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEE 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 89895084 456 NMVSVgakyasdaKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASA 507
Cdd:cd11386 157 TGRAF--------EEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
2-92 7.08e-26

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995  Cd Length: 91  Bit Score: 101.56  E-value: 7.08e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084      2 LYDDYDNVIKSEVETAVHLVDFYYKQFQEGLMTEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRR 81
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAAGKLTEEEAQAQAKAALRALRYGGDGYFFVYDSDGVMLMHPAKPELEGKNLS 80
                           90
                   ....*....|.
gi 89895084     82 ELTDPNGVKLI 92
Cdd:smart01049  81 DLKDPNGKYLF 91
Cache_2 pfam08269
Cache domain;
10-93 7.81e-26

Cache domain;


Pssm-ID: 254697  Cd Length: 95  Bit Score: 101.61  E-value: 7.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    10 IKSEVETAVHLVDFYYKQFQEGLMTEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRRELTDPNGV 89
Cdd:pfam08269  12 LKAVVESALSIIKEYYQQAQKGKLTREEAQAQAKALLRALRYDGDGYFFAYDSNGTNVMHPIKPELVGKNLSNLKDPNGN 91

                  ....
gi 89895084    90 KLIQ 93
Cdd:pfam08269  92 NVFV 95
HAMP pfam00672
HAMP domain;
171-241 1.07e-09

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 55.31  E-value: 1.07e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 89895084   171 SVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIYiQEINHTSQDEIGLLAKTLNELSAQLRN 241
Cdd:pfam00672   1 LLLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLD-DRVPVSGPDEIGELARAFNQMADRLRE 70
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
170-244 7.87e-07

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 46.99  E-value: 7.87e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 170 VSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTLNELSAQLRNFIS 244
Cdd:COG2770   7 IFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGD-LSAEIPQPMLDEIGELAKAFNRMRDSLQRALS 80
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
191-244 1.59e-04

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 39.92  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 89895084    191 RRISDPLNALVKAFEKDANGQIYiQEINHTSQDEIGLLAKTLNELSAQLRNFIS 244
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLT-VRLPVDGRDEIGELARAFNEMADRLEETIA 53
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
250-324 6.25e-04

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: 39.91  E-value: 6.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 250 VQDLTQQANDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSSHEVS 324
Cdd:cd11386 126 IEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRAFEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
140-528 1.62e-44

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 162.85  E-value: 1.62e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 140 ISTGNYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIyIQEINH 219
Cdd:COG0840  31 DELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDL-TKRIDE 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 220 TSQDEIGLLAKTLNELSAQLRNFISGAQNGVQDLTQQANDFTSLAGRvedtvqdsaektarINELMEAVAASTGEITRAI 299
Cdd:COG0840 110 SSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATE--------------LSARADQQAESLEEVASAI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 300 EEIDAALTSISQRAEEGAVSSHEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMIHLlseINAIADQT 379
Cdd:COG0840 176 EELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEELAEVVKKLSESSQEIEEITSV---INSIAEQT 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 380 DLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEE------DVLAN 453
Cdd:COG0840 253 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEgvklveETGSS 332
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084 454 YDNMVSVGAKYASDAKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASAESIEGIFQQTEMILNHMKEIK 528
Cdd:COG0840 333 LGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFK 407
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
281-549 9.68e-37

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: 137.03  E-value: 9.68e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    281 INELMEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSSHEVSDRAQKLQD---DSNHSIKKTKAIYDTTRSGVEQAIS 357
Cdd:smart00283   2 VSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEaaeEGREAVEDAITAMDQIREVVEEAVS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    358 EVKKVEEMI----HLLSEINAIADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVD 433
Cdd:smart00283  82 AVEELEESSdeigEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETN 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    434 KLVDNIRQVlvfieedvlanyDNMVSVGAKYASDA----KHINAIMLELSSTSEEISASTNEVSTRTGEVSGSIsasaES 509
Cdd:smart00283 162 EAVAAMEES------------SSEVEEGVELVEETgdalEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAI----DE 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 89895084    510 IEGIFQQTEmilNHMKEIKSNSENNLATVTDLKQYIDKFK 549
Cdd:smart00283 226 IAQVTQETA---AMSEEISAAAEELSGLAEELDELVERFK 262
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms]
34-239 3.69e-27

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 226930 [Multi-domain]  Cd Length: 459  Bit Score: 113.00  E-value: 3.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  34 TEAEAQETAKKAVKGLRYGSEGYFWIDDVHGILVAHPMLPDQEGTDRRELTDPNGVKLIQQLLKAAQenENGGYSDYMWE 113
Cdd:COG4564  74 SDEAAKQEVKAILTNLDYGSDGYFFVYDYQGTNLVHPRQPELVGQNLWQLTDPRGDRVIQALIAKAQ--EGGGLHQYLWE 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 114 KPNdvgTNELSPKRAYSKEFQPWNWVISTGNYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRi 193
Cdd:COG4564 152 KPS---SHETVDKLSYAAGLDKWEWMIGTGLYLDDVSAETAAAQAAVRANIDTTFLIVVLIAVVAVLLVFATCLALNLR- 227
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 89895084 194 sdplnalvKAFEKDANGQIYIQEINHTSQDEIGLLAKTLNELSAQL 239
Cdd:COG4564 228 --------EHRLADKKLKELAQRVVDTQEDERARLARELHDGISQN 265
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
327-550 3.44e-23

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


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 97.52  E-value: 3.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   327 AQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEV-KKVEEMIHLLSEINAIADQTDLLALNAAIESARAGEAGRGFAVVAD 405
Cdd:pfam00015   3 ASDLAQLASEEALDEMSQIGQVVDDAVETMEELeTSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVAD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   406 EIRKLAESTALTVQKIEGISRQVIVSVDKLVDNIRQVLVFIEEDVlANYDNMVSVGAKYASDAKHINAIMLELSSTSEEI 485
Cdd:pfam00015  83 EVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGS-TIVESTGEALKEIVDAVAEIADIVQEIAAASDEQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 89895084   486 SASTNEVSTRTGEVSGSisasaesiegifqqTEMILNHMKEIKSNSENNLATVTDLKQYIDKFKI 550
Cdd:pfam00015 162 SAGIDQVNQAVARIDQV--------------TQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
144-511 2.03e-22

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 99.64  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  144 NYVDTIDALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQIyIQEINHTSQD 223
Cdd:PRK15041 169 AYMEQNDRLYDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIAGGDL-VKPIEVDGSN 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  224 EIGLLAKTLNELSAQLRNFISGAQNGvqdltqqANDFTSLAGRVEDTVQDSAEKTarinelmEAVAASTGEITRAIEEID 303
Cdd:PRK15041 248 EMGQLAESLRHMQGELMRTVGDVRNG-------ANAIYSGASEIATGNNDLSSRT-------EQQAASLEETAASMEQLT 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  304 AaltSISQRAEEGAVSSH---EVSDRAQKLQDDSNHSIKKTKAIydttrSGVEQAISEVkkveemihlLSEINAIADQTD 380
Cdd:PRK15041 314 A---TVKQNAENARQASHlalSASETAQRGGKVVDNVVQTMRDI-----STSSQKIADI---------ISVIDGIAFQTN 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  381 LLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDklvdnIRQVLVFIEEDVLANYDNMVSv 460
Cdd:PRK15041 377 ILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVD-----VGSTLVESAGETMAEIVSAVT- 450
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 89895084  461 gakyasdakHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISASAESIE 511
Cdd:PRK15041 451 ---------RVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVE 492
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
163-529 8.16e-21

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 94.75  E-value: 8.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  163 HLRQIVMVSVLITAAaliILAVISLQISRR-ISDPLNALVKAFEKDANGQIyIQEINHTSQDEIGLLAKTLNELSAQLRN 241
Cdd:PRK09793 186 QISALVFISMIIVAA---IYISSALWWTRKmIVQPLAIIGSHFDSIAAGNL-ARPIAVYGRNEITAIFASLKTMQQALRG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  242 FISGAQNGVQDLTQQANDFTslAGRvedtvQDSAEKTarinelmEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSSH 321
Cdd:PRK09793 262 TVSDVRKGSQEMHIGIAEIV--AGN-----NDLSSRT-------EQQAASLAQTAASMEQLTATVGQNADNARQASELAK 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  322 EVSDRAQKLQDDSNHSIKKTKAIYDTTrsgveQAISEVkkveemihlLSEINAIADQTDLLALNAAIESARAGEAGRGFA 401
Cdd:PRK09793 328 NAATTAQAGGVQVSTMTHTMQEIATSS-----QKIGDI---------ISVIDGIAFQTNILALNAAVEAARAGEQGRGFA 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  402 VVADEIRKLAESTALTVQKIEGISRQVIVSV---DKLVDNIRQVLVFIeedvlanydnmvsvgakyASDAKHINAIMLEL 478
Cdd:PRK09793 394 VVAGEVRNLASRSAQAAKEIKGLIEESVNRVqqgSKLVNNAAATMTDI------------------VSSVTRVNDIMGEI 455
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 89895084  479 SSTSEEISASTNEVSTRTGEVSGSISASAESIEGIFQQTEMILNHMKEIKS 529
Cdd:PRK09793 456 ASASEEQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSS 506
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
227-499 8.20e-20

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 91.61  E-value: 8.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  227 LLAKTLNELSAQLRNFISGaqNGVQDLTQQA-NDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEIT--------- 296
Cdd:PRK15048 215 MLLTPLAKIIAHIREIAGG--NLANTLTIDGrSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAagntdlssr 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  297 -----RAIEEIDAALTSISQRAEEGAVSSHEVSDRAQKLQDDSNHSIKKTKAIYDTtrsgVEQAISEVKKVEEMIhllSE 371
Cdd:PRK15048 293 teqqaSALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKT----MHEIADSSKKIADII---SV 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  372 INAIADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISRQVIVSVDKlvdniRQVLVFIEEDVL 451
Cdd:PRK15048 366 IDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDT-----GSVLVESAGETM 440
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 89895084  452 ANYDNMVSvgakyasdakHINAIMLELSSTSEEISASTNEVSTRTGEV 499
Cdd:PRK15048 441 NNIVNAVT----------RVTDIMGEIASASDEQSRGIDQVALAVSEM 478
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
144-259 4.11e-09

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 57.56  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  144 NYVDTIDALIeeknQELGDHLRQIVMVSVLITAAALIILAVISL----QISRRISDPLNALVKAFEKDANGQIYIQEINH 219
Cdd:PRK10935 127 NYVDQIDLFV----LALQHFAERKLILLAAISLLGLILILTLVFftvrFTRRQVVAPLNQLVTASQQIEKGQFDHIPLDT 202
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 89895084  220 TSQDEIGLLAKTLNELSAQLRNFISGAQNGVQDLT---QQAND 259
Cdd:PRK10935 203 TLPNELGLLAKAFNQMSSELHKLYRSLEASVEEKTrklTQANR 245
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
83-258 1.43e-06

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 49.65  E-value: 1.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  83 LTDPNGVKLIQQLLKAAQENENGGYsdymwekPNDvgtnelSPKRAYSKEFQpwnwvistgNYVDTIDAL---IEEKNQe 159
Cdd:COG3850  87 WRVPLAVKTQYQQLIAYWRNMLKPL-------LLQ------GDRRPYQADLA---------DFVAQIDQFvlaLQRFAE- 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 160 lgdhlRQIVMVSVLITAAALIILAVISLQI---SRRISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTLNELS 236
Cdd:COG3850 144 -----RKTILLVLVQLAGMLLILLLVVFTIywlRRRVVRPLNQLTSAAQRIGRRQ-FDQRPTDTGRNELGLLGRAFNQMS 217
                       170       180
                ....*....|....*....|....*
gi 89895084 237 AQLRNFISGAQNGVQDLT---QQAN 258
Cdd:COG3850 218 GELKKLYADLEQRVEEKTrdlEQKN 242
COG1511 COG1511
Predicted membrane protein [Function unknown]
206-512 6.73e-05

Predicted membrane protein [Function unknown]


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 44.42  E-value: 6.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 206 KDANGQIY--IQEINHTSQDeIGLLAKTLNELSAQLRNFISGAQNGVQDLTQQANDFTSLAGRVEDTVQDSAEKTARINE 283
Cdd:COG1511 184 ADGAEKLKdgTDEASNGNKK-LSDLLNTLNNSSATFSDGLNALTSGLTTLTDGLNQLDSGLGTLAAGIGELKQGAEQLNE 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 284 LMEAVAASTGEITRAIEEIDAALTSISQRAEEGAVSShevsdraqKLQDDSNHSIKKTKAIYDTTRSGVEQAISEvkKVE 363
Cdd:COG1511 263 GIGEFSSGLSELNSGVQDLAAGVPQLNQGISALAAGL--------SLPDSLGDQFSSLQEALTQIAQGLKQKTSS--SLE 332
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 364 EMIHLLSEINAIADQTDLLALNAAIESARAGEAGRGFAVVADEIRKLAESTALTVQKIEGISR----------------- 426
Cdd:COG1511 333 AAQGSLSSLQSMLALSKSLDLTAEGATVDALGAPDGVQWLDESQKTLATLSELLSTGIDGVSEgldaleqasaqlaksla 412
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 427 QVIVSVDKLVDNIRQ-------------------VLVFIEEDVLANYDNMVSVGAKYASDAKHINaiMLELSSTSEEISA 487
Cdd:COG1511 413 KLKTAVAQIAASIAQllpgasevlktlkskgldkLLNQLNGALAKGSNALVQGLSDANDSFRSIT--SAQLKAGLNTLAD 490
                       330       340
                ....*....|....*....|....*
gi 89895084 488 STNEVSTRTGEVSGSISASAESIEG 512
Cdd:COG1511 491 GSNDLSSLGPGLGQLADGSKLLADG 515
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
229-332 3.82e-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: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    229 AKTLNELSAQLRNFISGAQNGVQDLTQQANDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITRAIEEIDAALTS 308
Cdd:smart00283 146 AKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDE 225
                           90       100
                   ....*....|....*....|....
gi 89895084    309 ISQRAEEGAVSSHEVSDRAQKLQD 332
Cdd:smart00283 226 IAQVTQETAAMSEEISAAAEELSG 249
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
150-240 5.70e-04

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 41.29  E-value: 5.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 150 DALIEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQI--SRRISDPLNALVKAFEKDANGQIYIQEINHTSQDEIGL 227
Cdd:COG5000 260 GAAAEYRELEAGRDGLQIAFALLYLSTALLVLLAAIWTAIafARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGR 339
                        90
                ....*....|...
gi 89895084 228 LAKTLNELSAQLR 240
Cdd:COG5000 340 LSKAFNKMTEQLS 352
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
161-325 6.81e-04

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: 40.88  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   161 GDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFekDANGQIYIQEINHTSQDEIGLLAKTLNELSAQLR 240
Cdd:TIGR03785 402 NSALEKLFNVILAIMSIGTLALFGFASWISWRIRRLSDDAEAAI--DSQGRISGAIPASRSRDEIGDLSRSFAQMVARLR 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   241 NFISGAQNGVQDLTQQANdfTSLAgrvedTVQDSAEKTarinELMEAVAASTGEITRA---IEEIDAALTSISQRAE-EG 316
Cdd:TIGR03785 480 QYTHYLENMSSRLSHELR--TPVA-----VVRSSLENL----ELQALEQEKQKYLERAregTERLSMILNNMSEATRlEQ 548

                  ....*....
gi 89895084   317 AVSSHEVSD 325
Cdd:TIGR03785 549 AIQSAEVED 557
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
145-262 9.57e-04

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 40.42  E-value: 9.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  145 YVDTIDALIEEKNQELGDHLRQIVMV-SVLITAAALIILAVIsLQISRRISDPLNALVKAFEKDANGQiYIQEINHTSQD 223
Cdd:PRK10600 101 FVAGLDALVSAFDHTTEMRIETVVLVhRVFAVFMALLLVFTI-IWLRRRLLQPWRQLLSMANAVSHRD-FTQRANISGRD 178
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 89895084  224 EIGLLAKTLNELSAQLRNFISGAQNGVQDLT---QQANDFTS 262
Cdd:PRK10600 179 EMAMLGTALNNMSAELAESYAVLEQRVQEKTaglEQKNQILS 220
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
250-332 1.14e-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: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 39.35  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084   250 VQDLTQQANDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITRAIEEIDAALTSISQ-------RAEEGAVSSHE 322
Cdd:pfam00015 116 IQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQvtqqnaaLVEESAAAAET 195
                          90
                  ....*....|
gi 89895084   323 VSDRAQKLQD 332
Cdd:pfam00015 196 LEEQAEELTA 205
chromosome_segregation_protein_related_ptotein TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
146-514 3.11e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.90  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    146 VDTIDALIEEKNQELG-------DHLRQIVMVSVLITAAALIILAviSLQISRRISDPLNALVKAFEKDANG-QIYIQEI 217
Cdd:TIGR02169  186 IERLDLIIDEKRQQLErlrrereKAERYQALLKEKREYEGYELLK--EKEALERQKEAIERQLASLEEELEKlTEEISEL 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    218 NhtsqDEIGLLAKTLNELSAQLRNFISGAQNGVQDltqqanDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITR 297
Cdd:TIGR02169  264 E----KRLEEIEQLLEELNKKIKDLGEEEQLRVKE------KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    298 AIEEIDaaltSISQRAEEGAVSSHEVSDRAQKLQDDSNHSIKKTKAIYDTTRSGVEQAISEVKKVEEMIHllsEINAIAD 377
Cdd:TIGR02169  334 LLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR---EINELKR 406
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    378 QTDLLalnaaiesarageagrgfavvADEIRKLAESTALTVQKIEGIsRQVIVSVDKLVDNIRQVLVFIEEDVLANYDNM 457
Cdd:TIGR02169  407 ELDRL---------------------QEELQRLSEELADLNAAIAGI-EAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    458 VSVGAKYASDAKHINAIMLELSSTSEEISASTNEVSTRTGEVSGSISAS---AESIEGIF 514
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEevlKASIQGVH 524
conserved_hypothetical_protein TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
229-412 4.32e-03

TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene neighborhood found sporadically in a phylogenetically broad range of bacteria: Nocardia farcinica, Symbiobacterium thermophilum, and Streptomyces avermitilis (Actinobacteria), Geobacillus kaustophilus (Firmicutes), Azoarcus sp. EbN1 and Ralstonia solanacearum (Betaproteobacteria). Proteins in this family average over 1400 amino acids in length. [Hypothetical proteins, Conserved]


Pssm-ID: 274256 [Multi-domain]  Cd Length: 1353  Bit Score: 38.63  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    229 AKTLNELSAQLRNfiSGAQNGVQDLTQQANDFTSLAGRVEDTVQDSAEKTARINELMEAVAASTGEITRAIEEIDAALTS 308
Cdd:TIGR02680  313 ADALRTRLEALQG--SPAYQDAEELERARADAEALQAAAADARQAIREAESRLEEERRRLDEEAGRLDDAERELRAAREQ 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084    309 ISQRAEEGAVSSHEvsdRAQKLQDDSNHSIKKTKAiYDTTRSGVEQAISEvkkVEEMIHLLSEINAIADQTDLlalnaai 388
Cdd:TIGR02680  391 LARAAERAGLSPAH---TAEPDAALAAQELQELGA-LDARRQDADRVIAQ---RSEQVALLRRRDDVADRAEA------- 456
                          170       180
                   ....*....|....*....|....
gi 89895084    389 ESARAGEAGRGFAVVADEIRKLAE 412
Cdd:TIGR02680  457 THAAARARRDELDEEAEQAAARAE 480
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
153-240 4.78e-03

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 38.18  E-value: 4.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084 153 IEEKNQELGDHLRQIVMVSVLITAAALIILAVISLQISRRISDPLNALVKAFEKDANGQiYIQEINHTSQDEIGLLAKTL 232
Cdd:COG5002  14 IEASIEDVYNQMNFINNILISGTLIALIITALLGILLARTITKPITDMRKQAVDMARGN-YSRKVKVYGTDEIGELADSF 92

                ....*...
gi 89895084 233 NELSAQLR 240
Cdd:COG5002  93 NDLTKRVQ 100
PRK03918 PRK03918
chromosome segregation protein; Provisional
197-422 8.34e-03

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 8.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  197 LNALVKAFEKDANGQIYIQEINHTSQDEIGLLAKTLNELSAQLRNF---ISGAQNGVQDLTQQANDFTSLAGRVEDTVQD 273
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreeLEKLEKEVKELEELKEEIEELEKELESLEGS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  274 SAEKTARINELMEAVAASTGEItRAIEEIDAALTSISQRAEEGAVSSHEVSDRAQKLQDdsnhsIKKTKAIYDTTRSGVE 353
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-----IEKRLSRLEEEINGIE 327
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 89895084  354 QAISE----VKKVEEMIHLLSEInaiadQTDLLALNaaiESARAGEAGRgfaVVADEIRKL-AESTALTVQKIE 422
Cdd:PRK03918 328 ERIKEleekEERLEELKKKLKEL-----EKRLEELE---ERHELYEEAK---AKKEELERLkKRLTGLTPEKLE 390
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
224-514 9.24e-03

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 37.39  E-value: 9.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  224 EIGLLAKTLNELSAQLRNFisgaqngVQDLTQQANDFTSLAGRVEDTVQDSAEKTARINEL---MEAVAASTGEITRAIE 300
Cdd:COG1196  226 ELALLLAKLKELRKELEEL-------EEELSRLEEELEELQEELEEAEKEIEELKSELEELreeLEELQEELLELKEEIE 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  301 EIDAALTSISQRAEEGAVSSHEVSDRAQKLQDDsnhsIKKTKAIYDTTRSGVEQAISEVKKVEEMIHLLSEINAIADQ-- 378
Cdd:COG1196  299 ELEGEISLLRERLEELENELEELEERLEELKEK----IEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEel 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 89895084  379 --------TDLLALNAAIESARA--GEAGRGFAVVADEIRKLAESTALTVQKIEGISRQvIVSVDKLVDNIRQVLVFIEE 448
Cdd:COG1196  375 eelfealrEELAELEAELAEIRNelEELKREIESLEERLERLSERLEDLKEELKELEAE-LEELQTELEELNEELEELEE 453
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 89895084  449 DVLANYDNMVSVGAKYASDAKHINAIMLELSSTSEEISASTNEVSTRTGeVSGSISASAESIEGIF 514
Cdd:COG1196  454 QLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQG-VRAVLEALESGLPGVY 518
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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