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Conserved domains on  [gi|39996135|ref|NP_952086|]
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methyl-accepting chemotaxis sensory transducer, class 40H [Geobacter sulfurreducens PCA]

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List of domain hits

Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
286-485 1.70e-56

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: 191.30  E-value: 1.70e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 286 EEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTIGAMERITERVRDTARTVEALGARSDQIGEIVGTIQDIADQT 365
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 366 NLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDA 445
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 39996135 446 LREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQIT 485
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
CZB pfam13682
Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in ...
536-602 2.30e-16

Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in bacterial signal transduction proteins - most frequently receptors involved in chemotaxis and motility, but also in c-di-GMP signalling and nitrate/nitrite-sensing. Originally discovered in the cytoplasmic chemoreceptor TlpD from Helicobacter pylori, it is often found C-terminal to the MCPsignal domain in cytoplasmic chemoreceptor proteins. The CZB domain contains a core sequence motif, Hxx[WFYL]x21-28Cx[LFMVI]Gx[WFLVI]x18-27HxxxH. The highly-conserved H-C-H-H residues of this motif are believed to coordinate zinc; mutating the latter two histidines of the motif to alanines abolishes Zn binding. This domain binds zinc with high affinity, with a Kd in the femtomolar range. Although the function of the CZB domain is not yet known, scientists have speculated that it may function as either an unknown signal input domain, based on its frequent association with signalling output domains, or as a domain that helps to stabilize protein tertiary or quaternary structure.


:

Pssm-ID: 290405  Cd Length: 66  Bit Score: 74.86  E-value: 2.30e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39996135   536 HSGFVTTVEAVLVGRRRmEAGELSTHHTCRFGKWYEGDGRQLCGHLASYKAIYAPHERIHSLARDVV 602
Cdd:pfam13682   1 HLLWKSRLYKALEGGEV-DPEDLADHHQCRLGKWYYGEGGEGKGHLPAFKELEEPHKEVHELAAEIV 66
HAMP pfam00672
HAMP domain;
173-241 2.50e-07

HAMP domain;


:

Pssm-ID: 279063  Cd Length: 69  Bit Score: 48.72  E-value: 2.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39996135   173 AVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIRaDDELGDMGRTFNRMVENFEH 241
Cdd:pfam00672   2 LLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESG-RDEIGELARAFNQMAERLRE 69
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
259-520 3.38e-73

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: 238.34  E-value: 3.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    259 TLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTIGAMERITERVRDTA 338
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    339 RTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQET 418
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    419 RGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITEVVGHTAREAGES 498
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 39996135    499 ADAATGLATLADELQTEVRTFK 520
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
286-485 1.70e-56

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: 191.30  E-value: 1.70e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 286 EEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTIGAMERITERVRDTARTVEALGARSDQIGEIVGTIQDIADQT 365
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 366 NLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDA 445
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 39996135 446 LREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQIT 485
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
CZB pfam13682
Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in ...
536-602 2.30e-16

Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in bacterial signal transduction proteins - most frequently receptors involved in chemotaxis and motility, but also in c-di-GMP signalling and nitrate/nitrite-sensing. Originally discovered in the cytoplasmic chemoreceptor TlpD from Helicobacter pylori, it is often found C-terminal to the MCPsignal domain in cytoplasmic chemoreceptor proteins. The CZB domain contains a core sequence motif, Hxx[WFYL]x21-28Cx[LFMVI]Gx[WFLVI]x18-27HxxxH. The highly-conserved H-C-H-H residues of this motif are believed to coordinate zinc; mutating the latter two histidines of the motif to alanines abolishes Zn binding. This domain binds zinc with high affinity, with a Kd in the femtomolar range. Although the function of the CZB domain is not yet known, scientists have speculated that it may function as either an unknown signal input domain, based on its frequent association with signalling output domains, or as a domain that helps to stabilize protein tertiary or quaternary structure.


Pssm-ID: 290405  Cd Length: 66  Bit Score: 74.86  E-value: 2.30e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39996135   536 HSGFVTTVEAVLVGRRRmEAGELSTHHTCRFGKWYEGDGRQLCGHLASYKAIYAPHERIHSLARDVV 602
Cdd:pfam13682   1 HLLWKSRLYKALEGGEV-DPEDLADHHQCRLGKWYYGEGGEGKGHLPAFKELEEPHKEVHELAAEIV 66
HAMP pfam00672
HAMP domain;
173-241 2.50e-07

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 48.72  E-value: 2.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39996135   173 AVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIRaDDELGDMGRTFNRMVENFEH 241
Cdd:pfam00672   2 LLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESG-RDEIGELARAFNQMAERLRE 69
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
197-241 2.41e-05

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: 42.62  E-value: 2.41e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 39996135 197 RLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNRMVENFEH 241
Cdd:cd06225   4 PLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
192-238 2.77e-05

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 42.24  E-value: 2.77e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 39996135    192 RRFVFRLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNRMVEN 238
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADR 47
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
259-520 3.38e-73

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: 238.34  E-value: 3.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    259 TLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTIGAMERITERVRDTA 338
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    339 RTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQET 418
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    419 RGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITEVVGHTAREAGES 498
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 39996135    499 ADAATGLATLADELQTEVRTFK 520
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
141-521 9.93e-72

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 239.51  E-value: 9.93e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 141 AAVKEMEKAARQSFGDSRAALAASSKRLLVGQAVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIR 220
Cdd:COG0840  31 DELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDES 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 221 ADDELGDMGRTFNRMVENFEHMLTSIQNAVLNLSESARTLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCS 300
Cdd:COG0840 111 SNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAK 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 301 TAADVARNASASARSGAAVVQQTIGAMERITERVrdtARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAG 380
Cdd:COG0840 191 EAAALASEASQVAEEGGEEVRQAVEQMQEIAEEL---AEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAG 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 381 EQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQV 460
Cdd:COG0840 268 EAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLI 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39996135 461 AQIATAAEQQTATTSEITMNIQQITEVVGHTAREAGESADAATGLATLADELQTEVRTFKT 521
Cdd:COG0840 348 SEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
327-519 4.76e-46

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


Pssm-ID: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 162.23  E-value: 4.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   327 MERITERVRDTARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATRE 406
Cdd:pfam00015  15 MSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   407 IAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITE 486
Cdd:pfam00015  95 IEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQ 174
                         170       180       190
                  ....*....|....*....|....*....|...
gi 39996135   487 VVGHTAREAGESADAATGLATLADELQTEVRTF 519
Cdd:pfam00015 175 VTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
173-526 2.43e-39

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 150.93  E-value: 2.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  173 AVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNrmvenfeHMLTSIQNAVLN 252
Cdd:PRK15048 195 AVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVS-------HMQRSLTDTVTH 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  253 LSESARTLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTigameriTE 332
Cdd:PRK15048 268 VREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHG-------GK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  333 RVRDTARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIk 412
Cdd:PRK15048 341 VVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALI- 419
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  413 siqqetrgavasmEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITEVVGHTA 492
Cdd:PRK15048 420 -------------EDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNA 486
                        330       340       350
                 ....*....|....*....|....*....|....
gi 39996135  493 REAGESADAATGLATLADELQTEVRTFKTSGSEL 526
Cdd:PRK15048 487 SLVQESAAAAAALEEQASRLTQAVSAFRLAASPL 520
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
133-270 1.28e-05

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 47.07  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 133 RGIDRPLEAAVKEMEKAAR--QSFGDSRAALAASSKRLLVGqavFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVAD 210
Cdd:COG5000 245 RPVDPKVAEHADLTEGAAAeyRELEAGRDGLQIAFALLYLS---TALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVAD 321
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39996135 211 SDLTARV-VIRADDELGDMGRTFNRMVENfehmLTSIQNAVLNLSESARTLSVTSEQIATG 270
Cdd:COG5000 322 GDLDVQVpVRRVDEDVGRLSKAFNKMTEQ----LSSQQEALERAKDALEQRRRFLEAVLSG 378
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
2-259 2.90e-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: 45.46  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135     2 AGLTVLGLAAVTALSLYGVNRQVAETE-TIVQVDAAQVDVALKSQVSLAEAVRAyknyLVRKddkhvtgFRESIGTFEkN 80
Cdd:TIGR01386  13 AAVTALVFALSGFMLYSSLERHFEERDrEELQGKLEQVRRFLRDPADLDEDIKR----LQEK-------IDDLLVGHS-D 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    81 IaeFEKLANTDGEKAAVGKAKEELGKYRgcidelVAARGASDDVAAIDRNLARGIDRPLEAAVKEMEKAAR------QSF 154
Cdd:TIGR01386  81 L--ALSILNPDGRLLFERAQGAALVPAV------AANDALLELDQADAKMTHYRSILRSVAALPGGKGRKPvqitvaLDI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   155 GDSRAALAASSKRLLVGQAVFSVIVALLAAGfgfnTARRFVFRLGKFSEMIARVADSDLTARV-VIRADDELGDMGRTFN 233
Cdd:TIGR01386 153 NAHTHLLDALRKWLILIAVLLVLLTALLGWW----ITRLGLEPLRRLSAVAARISPESLDQRLdPSRAPAELRELAQSFN 228
                         250       260
                  ....*....|....*....|....*.
gi 39996135   234 RMVENFEHMLTSIQNAVLNLSESART 259
Cdd:TIGR01386 229 AMLGRLEDAFQRLSQFSADLAHELRT 254
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
286-485 1.70e-56

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: 191.30  E-value: 1.70e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 286 EEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTIGAMERITERVRDTARTVEALGARSDQIGEIVGTIQDIADQT 365
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 366 NLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDA 445
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 39996135 446 LREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQIT 485
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
CZB pfam13682
Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in ...
536-602 2.30e-16

Chemoreceptor zinc-binding domain; The chemoreceptor zinc-binding domain (CZB) is found in bacterial signal transduction proteins - most frequently receptors involved in chemotaxis and motility, but also in c-di-GMP signalling and nitrate/nitrite-sensing. Originally discovered in the cytoplasmic chemoreceptor TlpD from Helicobacter pylori, it is often found C-terminal to the MCPsignal domain in cytoplasmic chemoreceptor proteins. The CZB domain contains a core sequence motif, Hxx[WFYL]x21-28Cx[LFMVI]Gx[WFLVI]x18-27HxxxH. The highly-conserved H-C-H-H residues of this motif are believed to coordinate zinc; mutating the latter two histidines of the motif to alanines abolishes Zn binding. This domain binds zinc with high affinity, with a Kd in the femtomolar range. Although the function of the CZB domain is not yet known, scientists have speculated that it may function as either an unknown signal input domain, based on its frequent association with signalling output domains, or as a domain that helps to stabilize protein tertiary or quaternary structure.


Pssm-ID: 290405  Cd Length: 66  Bit Score: 74.86  E-value: 2.30e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39996135   536 HSGFVTTVEAVLVGRRRmEAGELSTHHTCRFGKWYEGDGRQLCGHLASYKAIYAPHERIHSLARDVV 602
Cdd:pfam13682   1 HLLWKSRLYKALEGGEV-DPEDLADHHQCRLGKWYYGEGGEGKGHLPAFKELEEPHKEVHELAAEIV 66
HAMP pfam00672
HAMP domain;
173-241 2.50e-07

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 48.72  E-value: 2.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39996135   173 AVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIRaDDELGDMGRTFNRMVENFEH 241
Cdd:pfam00672   2 LLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESG-RDEIGELARAFNQMAERLRE 69
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
197-241 2.41e-05

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: 42.62  E-value: 2.41e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 39996135 197 RLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNRMVENFEH 241
Cdd:cd06225   4 PLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
192-238 2.77e-05

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 42.24  E-value: 2.77e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 39996135    192 RRFVFRLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNRMVEN 238
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADR 47
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
259-520 3.38e-73

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: 238.34  E-value: 3.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    259 TLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTIGAMERITERVRDTA 338
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    339 RTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQET 418
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    419 RGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITEVVGHTAREAGES 498
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 39996135    499 ADAATGLATLADELQTEVRTFK 520
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
141-521 9.93e-72

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 239.51  E-value: 9.93e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 141 AAVKEMEKAARQSFGDSRAALAASSKRLLVGQAVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIR 220
Cdd:COG0840  31 DELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDES 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 221 ADDELGDMGRTFNRMVENFEHMLTSIQNAVLNLSESARTLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCS 300
Cdd:COG0840 111 SNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETVKEVAFNAK 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 301 TAADVARNASASARSGAAVVQQTIGAMERITERVrdtARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAG 380
Cdd:COG0840 191 EAAALASEASQVAEEGGEEVRQAVEQMQEIAEEL---AEVVKKLSESSQEIEEITSVINSIAEQTNLLALNAAIEAARAG 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 381 EQGRGFAVVADEVRALAERTTRATREIAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQV 460
Cdd:COG0840 268 EAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAAIEEVSQLI 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39996135 461 AQIATAAEQQTATTSEITMNIQQITEVVGHTAREAGESADAATGLATLADELQTEVRTFKT 521
Cdd:COG0840 348 SEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
327-519 4.76e-46

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


Pssm-ID: 278444 [Multi-domain]  Cd Length: 207  Bit Score: 162.23  E-value: 4.76e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   327 MERITERVRDTARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATRE 406
Cdd:pfam00015  15 MSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   407 IAEMIKSIQQETRGAVASMEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITE 486
Cdd:pfam00015  95 IEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQ 174
                         170       180       190
                  ....*....|....*....|....*....|...
gi 39996135   487 VVGHTAREAGESADAATGLATLADELQTEVRTF 519
Cdd:pfam00015 175 VTQQNAALVEESAAAAETLEEQAEELTASVAQF 207
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
173-526 2.43e-39

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 150.93  E-value: 2.43e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  173 AVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNrmvenfeHMLTSIQNAVLN 252
Cdd:PRK15048 195 AVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVS-------HMQRSLTDTVTH 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  253 LSESARTLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNASASARSGAAVVQQTigameriTE 332
Cdd:PRK15048 268 VREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHG-------GK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  333 RVRDTARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIk 412
Cdd:PRK15048 341 VVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALI- 419
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  413 siqqetrgavasmEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITEVVGHTA 492
Cdd:PRK15048 420 -------------EDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNA 486
                        330       340       350
                 ....*....|....*....|....*....|....
gi 39996135  493 REAGESADAATGLATLADELQTEVRTFKTSGSEL 526
Cdd:PRK15048 487 SLVQESAAAAAALEEQASRLTQAVSAFRLAASPL 520
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
78-520 1.93e-38

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 148.18  E-value: 1.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   78 EKNIAEFEKLA-NTDGEKAAVGKAKEELGKYRGCIDELVAARGASddvaaidrNLARGIDRPLEAAVKEMEKA--ARQSF 154
Cdd:PRK15041 102 EKNWADYEALPrDPRQSTAAAAEIKRNYDIYHNALAELIQLLGAG--------KINEFFDQPTQGYQDGFEKQyvAYMEQ 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  155 GDSRAALAASSKRLLVGQAVF---SVIVALLAAGFG--FNTARRFVFRLGKFSEMIARVADSDLTARVVIRADDELGdmg 229
Cdd:PRK15041 174 NDRLYDIAVSDNNASYSQAMWilvGVMIVVLAVIFAvwFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMG--- 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  230 rtfnRMVENFEHMLTSIQNAVLNLSESARTLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNA 309
Cdd:PRK15041 251 ----QLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQA 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  310 SASARSGAAVVQQTIGAMERITERVRDTARTvealgarSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVV 389
Cdd:PRK15041 327 SHLALSASETAQRGGKVVDNVVQTMRDISTS-------SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVV 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  390 ADEVRALAERTTRATREIAEMIksiqqetrgavasmEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQ 469
Cdd:PRK15041 400 AGEVRNLAQRSAQAAREIKSLI--------------EDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASASDE 465
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 39996135  470 QTATTSEITMNIQQITEVVGHTAREAGESADAATGLATLADELQTEVRTFK 520
Cdd:PRK15041 466 QSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFR 516
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
173-533 1.56e-35

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 139.44  E-value: 1.56e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  173 AVFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNRMVENFEHMLTSIQNAVLN 252
Cdd:PRK09793 193 ISMIIVAAIYISSALWWTRKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQE 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  253 LSESARTLSVTSEQIATGAEEMASQTGTVATASEEMAATSQEIAQNCSTAADVARNASASArsgaavvqqtigamERITE 332
Cdd:PRK09793 273 MHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTA--------------QAGGV 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  333 RVRDTARTVEALGARSDQIGEIVGTIQDIADQTNLLALNAAIEAARAGEQGRGFAVVADEVRALAERTTRATREIAEMIk 412
Cdd:PRK09793 339 QVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLI- 417
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135  413 siqqetrgavasmEEGVVEVTQGSADAARSGDALREILDQIEQVTGQVAQIATAAEQQTATTSEITMNIQQITEVVGHTA 492
Cdd:PRK09793 418 -------------EESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVAQAVSQMDQVTQQNA 484
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 39996135  493 REAGESADAATGLATLADELQTEVRTFKTSGSELFILELAK 533
Cdd:PRK09793 485 SLVEEAAVATEQLANQADHLSSRVAVFTLEEHEVARHESAQ 525
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
133-270 1.28e-05

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 47.07  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 133 RGIDRPLEAAVKEMEKAAR--QSFGDSRAALAASSKRLLVGqavFSVIVALLAAGFGFNTARRFVFRLGKFSEMIARVAD 210
Cdd:COG5000 245 RPVDPKVAEHADLTEGAAAeyRELEAGRDGLQIAFALLYLS---TALLVLLAAIWTAIAFARRIVRPIRKLIEAADEVAD 321
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 39996135 211 SDLTARV-VIRADDELGDMGRTFNRMVENfehmLTSIQNAVLNLSESARTLSVTSEQIATG 270
Cdd:COG5000 322 GDLDVQVpVRRVDEDVGRLSKAFNKMTEQ----LSSQQEALERAKDALEQRRRFLEAVLSG 378
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
2-259 2.90e-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: 45.46  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135     2 AGLTVLGLAAVTALSLYGVNRQVAETE-TIVQVDAAQVDVALKSQVSLAEAVRAyknyLVRKddkhvtgFRESIGTFEkN 80
Cdd:TIGR01386  13 AAVTALVFALSGFMLYSSLERHFEERDrEELQGKLEQVRRFLRDPADLDEDIKR----LQEK-------IDDLLVGHS-D 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135    81 IaeFEKLANTDGEKAAVGKAKEELGKYRgcidelVAARGASDDVAAIDRNLARGIDRPLEAAVKEMEKAAR------QSF 154
Cdd:TIGR01386  81 L--ALSILNPDGRLLFERAQGAALVPAV------AANDALLELDQADAKMTHYRSILRSVAALPGGKGRKPvqitvaLDI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   155 GDSRAALAASSKRLLVGQAVFSVIVALLAAGfgfnTARRFVFRLGKFSEMIARVADSDLTARV-VIRADDELGDMGRTFN 233
Cdd:TIGR01386 153 NAHTHLLDALRKWLILIAVLLVLLTALLGWW----ITRLGLEPLRRLSAVAARISPESLDQRLdPSRAPAELRELAQSFN 228
                         250       260
                  ....*....|....*....|....*.
gi 39996135   234 RMVENFEHMLTSIQNAVLNLSESART 259
Cdd:TIGR01386 229 AMLGRLEDAFQRLSQFSADLAHELRT 254
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
173-296 1.74e-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: 43.19  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135   173 AVFSVIVALLAAG----FGFntARRFVFRLGKFSEMIARVADSD--LTARVVI-RADDELGDMGRTFNRMV--------- 236
Cdd:TIGR03785 407 KLFNVILAIMSIGtlalFGF--ASWISWRIRRLSDDAEAAIDSQgrISGAIPAsRSRDEIGDLSRSFAQMVarlrqythy 484
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39996135   237 -ENFEHMLT------------SIQNavLNLSESARTLSVTSEQIATGAEEMASQTGTVATASE-EMAATSQEIA 296
Cdd:TIGR03785 485 lENMSSRLShelrtpvavvrsSLEN--LELQALEQEKQKYLERAREGTERLSMILNNMSEATRlEQAIQSAEVE 556
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
162-262 3.36e-03

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 38.87  E-value: 3.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39996135 162 AASSKRLLVGQAVFSVIVALLAAGFGFNT--ARRFVFR-LGKFSEMIARVADSDLTARVVIRADDELGDMGRTFNRMVEN 238
Cdd:COG3850 140 RFAERKTILLVLVQLAGMLLILLLVVFTIywLRRRVVRpLNQLTSAAQRIGRRQFDQRPTDTGRNELGLLGRAFNQMSGE 219
                        90       100
                ....*....|....*....|....*...
gi 39996135 239 FEHMLTSIQNAVLN----LSESARTLSV 262
Cdd:COG3850 220 LKKLYADLEQRVEEktrdLEQKNQRLSF 247
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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