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Conserved domains on  [gi|56478990|ref|YP_160579|]
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membrane-associated methyl-accepting chemotaxis protein [Aromatoleum aromaticum EbN1]

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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. ...
341-385 2.55e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the 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: 48.40  E-value: 2.55e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 56478990 341 ILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAES 385
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAER 45
MCP_signal super family cl21547
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
433-632 9.09e-43

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: 153.16  E-value: 9.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 433 QALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQCIVDDIAAAVAAVLALEERSRTIDRVAYVIAEIAEQT 512
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 513 NLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSARVGESSVLFAKVLSA 592
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 56478990 593 LDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMA 632
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
258-668 5.48e-58

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


:

Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 202.53  E-value: 5.48e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 258 VQEYLTTKLINTSDFDIAPASYHAKGSAALEAGIAFAARLIpgIDQLMATREQETRSAFQSALLAFAIAVALIAYLFAGA 337
Cdd:COG0840   3 LEAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLI--LDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 338 YTSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIAKVAGAAGNTRSAASELTDQVAQVTAA 417
Cdd:COG0840  81 LRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 418 SARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQcivDDIAAAVAAVLALEERSRT 497
Cdd:COG0840 161 ADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQ---EIAEELAEVVKKLSESSQE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 498 IDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSA 577
Cdd:COG0840 238 IEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESAS 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 578 RVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMADENHGTARRTGTAISDLLQLSD 657
Cdd:COG0840 318 EVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAE 397
                       410
                ....*....|.
gi 56478990 658 SLRVAIAELRV 668
Cdd:COG0840 398 KLLELVAKFKL 408
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
341-385 2.55e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the 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: 48.40  E-value: 2.55e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 56478990 341 ILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAES 385
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAER 45
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
433-632 9.09e-43

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: 153.16  E-value: 9.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 433 QALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQCIVDDIAAAVAAVLALEERSRTIDRVAYVIAEIAEQT 512
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 513 NLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSARVGESSVLFAKVLSA 592
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 56478990 593 LDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMA 632
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
319-385 1.52e-08

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 52.23  E-value: 1.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56478990   319 ALLAFAIAVALIAYLFAGaytSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAES 385
Cdd:pfam00672   4 VLLIALLLLLLLAWLLAR---RLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADR 67
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
340-391 1.19e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 46.47  E-value: 1.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 56478990    340 SILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIA 391
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
258-668 5.48e-58

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 202.53  E-value: 5.48e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 258 VQEYLTTKLINTSDFDIAPASYHAKGSAALEAGIAFAARLIpgIDQLMATREQETRSAFQSALLAFAIAVALIAYLFAGA 337
Cdd:COG0840   3 LEAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLI--LDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 338 YTSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIAKVAGAAGNTRSAASELTDQVAQVTAA 417
Cdd:COG0840  81 LRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 418 SARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQcivDDIAAAVAAVLALEERSRT 497
Cdd:COG0840 161 ADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQ---EIAEELAEVVKKLSESSQE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 498 IDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSA 577
Cdd:COG0840 238 IEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESAS 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 578 RVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMADENHGTARRTGTAISDLLQLSD 657
Cdd:COG0840 318 EVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAE 397
                       410
                ....*....|.
gi 56478990 658 SLRVAIAELRV 668
Cdd:COG0840 398 KLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
406-667 7.91e-47

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: 166.69  E-value: 7.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990    406 ELTDQVAQVTAASARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQCIVDDIAAAV 485
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990    486 AAVLALEERSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGI 565
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990    566 QDVVAGIRQGSARVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMADENHGTARRT 645
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 56478990    646 GTAISDLLQLSDSLRVAIAELR 667
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
454-668 4.35e-32

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: 123.71  E-value: 4.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990   454 RQAAELSADGRAIADQAaagMQCIVDDIAAAVAAVLALEERSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGF 533
Cdd:pfam00015   1 AQASDLAQLASEEALDE---MSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990   534 AVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSARVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSV 613
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56478990   614 TRAQTDASHDIARSIETMAVMADENHGTARRTGTAISDLLQLSDSLRVAIAELRV 668
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
316-668 2.05e-28

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 118.96  E-value: 2.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  316 FQSALLAFAIAVALIAYLFaGAYTSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIAKVAG 395
Cdd:PRK15048 192 WQLAVIALVVVLILLVAWY-GIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVRE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  396 AAGNTRSAASELTDQVAQVTAASARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQ 475
Cdd:PRK15048 271 GSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMH 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  476 civddiaaavaavlALEERSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIA 555
Cdd:PRK15048 351 --------------EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIK 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  556 ATiremrngIQDVVagirqgsARVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMA 635
Cdd:PRK15048 417 AL-------IEDSV-------SRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVT 482
                        330       340       350
                 ....*....|....*....|....*....|...
gi 56478990  636 DENHGTARRTGTAISDLLQLSDSLRVAIAELRV 668
Cdd:PRK15048 483 QQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
341-385 2.55e-07

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the 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: 48.40  E-value: 2.55e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 56478990 341 ILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAES 385
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAER 45
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
433-632 9.09e-43

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: 153.16  E-value: 9.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 433 QALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQCIVDDIAAAVAAVLALEERSRTIDRVAYVIAEIAEQT 512
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 513 NLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSARVGESSVLFAKVLSA 592
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 56478990 593 LDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMA 632
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP pfam00672
HAMP domain;
319-385 1.52e-08

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 52.23  E-value: 1.52e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56478990   319 ALLAFAIAVALIAYLFAGaytSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAES 385
Cdd:pfam00672   4 VLLIALLLLLLLAWLLAR---RLLRPLRRLAEAARRIASGDLDDRVPVSGPDEIGELARAFNQMADR 67
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
340-391 1.19e-06

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 46.47  E-value: 1.19e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 56478990    340 SILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIA 391
Cdd:smart00304   2 RLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
258-668 5.48e-58

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 202.53  E-value: 5.48e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 258 VQEYLTTKLINTSDFDIAPASYHAKGSAALEAGIAFAARLIpgIDQLMATREQETRSAFQSALLAFAIAVALIAYLFAGA 337
Cdd:COG0840   3 LEAPLNLELIELAAGEADAGLLKLKKLIDELGKLLLSLNLI--LDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 338 YTSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIAKVAGAAGNTRSAASELTDQVAQVTAA 417
Cdd:COG0840  81 LRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSAR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 418 SARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQcivDDIAAAVAAVLALEERSRT 497
Cdd:COG0840 161 ADQQAESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQ---EIAEELAEVVKKLSESSQE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 498 IDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSA 577
Cdd:COG0840 238 IEEITSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESAS 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 578 RVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMADENHGTARRTGTAISDLLQLSD 657
Cdd:COG0840 318 EVSEGVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAE 397
                       410
                ....*....|.
gi 56478990 658 SLRVAIAELRV 668
Cdd:COG0840 398 KLLELVAKFKL 408
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
406-667 7.91e-47

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: 166.69  E-value: 7.91e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990    406 ELTDQVAQVTAASARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQCIVDDIAAAV 485
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990    486 AAVLALEERSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIAATIREMRNGI 565
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990    566 QDVVAGIRQGSARVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMADENHGTARRT 645
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|..
gi 56478990    646 GTAISDLLQLSDSLRVAIAELR 667
Cdd:smart00283 241 SAAAEELSGLAEELDELVERFK 262
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
454-668 4.35e-32

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: 123.71  E-value: 4.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990   454 RQAAELSADGRAIADQAaagMQCIVDDIAAAVAAVLALEERSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGF 533
Cdd:pfam00015   1 AQASDLAQLASEEALDE---MSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990   534 AVVADEVRKLANRTGSSTREIAATIREMRNGIQDVVAGIRQGSARVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSV 613
Cdd:pfam00015  78 AVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 56478990   614 TRAQTDASHDIARSIETMAVMADENHGTARRTGTAISDLLQLSDSLRVAIAELRV 668
Cdd:pfam00015 158 SDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRI 212
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
316-668 2.05e-28

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 118.96  E-value: 2.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  316 FQSALLAFAIAVALIAYLFaGAYTSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIAKVAG 395
Cdd:PRK15048 192 WQLAVIALVVVLILLVAWY-GIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVRE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  396 AAGNTRSAASELTDQVAQVTAASARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRAIADQAAAGMQ 475
Cdd:PRK15048 271 GSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMH 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  476 civddiaaavaavlALEERSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLANRTGSSTREIA 555
Cdd:PRK15048 351 --------------EIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIK 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  556 ATiremrngIQDVVagirqgsARVGESSVLFAKVLSALDAIHYEVTRSAMLVGDIVSVTRAQTDASHDIARSIETMAVMA 635
Cdd:PRK15048 417 AL-------IEDSV-------SRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVT 482
                        330       340       350
                 ....*....|....*....|....*....|...
gi 56478990  636 DENHGTARRTGTAISDLLQLSDSLRVAIAELRV 668
Cdd:PRK15048 483 QQNASLVQESAAAAAALEEQASRLTQAVSAFRL 515
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
301-667 7.39e-28

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 117.09  E-value: 7.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  301 IDQLMATREQETRSAFQSALLAFAIAVALIAYLFAGAY----TSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVG 376
Cdd:PRK09793 170 INHVLEAASAQSQRNYQISALVFISMIIVAAIYISSALwwtrKMIVQPLAIIGSHFDSIAAGNLARPIAVYGRNEITAIF 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  377 NGFNAMAESFSALIAKVAGAAGNTRSAASELTDQVAQVTAASARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQA 456
Cdd:PRK09793 250 ASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNA 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  457 AELSADGRAIADQAAAGMQCIVDDiaaavaavlaleerSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVV 536
Cdd:PRK09793 330 ATTAQAGGVQVSTMTHTMQEIATS--------------SQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVV 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  537 ADEVRKLANRTGSSTREIAATIREMRNGIQdvvagirQGSARVGESSVLFAKVLSAldaihyeVTRSAMLVGDIVSVTRA 616
Cdd:PRK09793 396 AGEVRNLASRSAQAAKEIKGLIEESVNRVQ-------QGSKLVNNAAATMTDIVSS-------VTRVNDIMGEIASASEE 461
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 56478990  617 QTDASHDIARSIETMAVMADENHGTARRTGTAISDLLQLSDSL--RVAIAELR 667
Cdd:PRK09793 462 QRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLssRVAVFTLE 514
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
309-668 4.65e-27

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 114.67  E-value: 4.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  309 EQETRSAFQSALLAFAIAVALIAYLFA---GAYTSILRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAES 385
Cdd:PRK15041 183 SDNNASYSQAMWILVGVMIVVLAVIFAvwfGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGE 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  386 FSALIAKVAGAAGNTRSAASELTDQVAQVTAASARQSESAARSSSSVQALAVSVQQVATHAEDTNRITRQAAELSADGRA 465
Cdd:PRK15041 263 LMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGK 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  466 IADQAAAGMQCIVDDiaaavaavlaleerSRTIDRVAYVIAEIAEQTNLLALNAAIEAARAGEVGRGFAVVADEVRKLAN 545
Cdd:PRK15041 343 VVDNVVQTMRDISTS--------------SQKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQ 408
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990  546 RTGSSTREIAATiremrngIQDVVAGIRQGSARVGESSVLFAKVLSAldaihyeVTRSAMLVGDIVSVTRAQTDASHDIA 625
Cdd:PRK15041 409 RSAQAAREIKSL-------IEDSVGKVDVGSTLVESAGETMAEIVSA-------VTRVTDIMGEIASASDEQSRGIDQVG 474
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 56478990  626 RSIETMAVMADENHGTARRTGTAISDLLQLSDSLRVAIAELRV 668
Cdd:PRK15041 475 LAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRI 517
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
295-421 8.88e-05

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 44.26  E-value: 8.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 295 ARLIPGIDQLM------ATREQETRSAFQSA--LLAFAIAVALIAYLfagaYTSILRSIHELEVAARAMAAGDLRARVMV 366
Cdd:COG3850 125 ADFVAQIDQFVlalqrfAERKTILLVLVQLAgmLLILLLVVFTIYWL----RRRVVRPLNQLTSAAQRIGRRQFDQRPTD 200
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 56478990 367 RTHDEIGHVGNGFNAMAESFSALIAKVAGAAgNTRSAASELTDQVAQVTAASARQ 421
Cdd:COG3850 201 TGRNELGLLGRAFNQMSGELKKLYADLEQRV-EEKTRDLEQKNQRLSFLYQSSRR 254
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
290-387 1.29e-03

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 40.52  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56478990 290 GIAFAARLIPGIDQLMATREQE---TRSAFQSALLAFAIAVALIAYLFAGAYT-SILRSIHELEVAARAMAAGDLRARVM 365
Cdd:COG5000 250 KVAEHADLTEGAAAEYRELEAGrdgLQIAFALLYLSTALLVLLAAIWTAIAFArRIVRPIRKLIEAADEVADGDLDVQVP 329
                        90       100
                ....*....|....*....|...
gi 56478990 366 VRTHDE-IGHVGNGFNAMAESFS 387
Cdd:COG5000 330 VRRVDEdVGRLSKAFNKMTEQLS 352
PRK10604 PRK10604
sensor protein RstB; Provisional
319-391 2.98e-03

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 39.20  E-value: 2.98e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56478990  319 ALLAF-AIAVALIAYLFAGAYtsiLRSIHELEVAARAMAAGDLRARVMVRTHDEIGHVGNGFNAMAESFSALIA 391
Cdd:PRK10604 140 ALLALiGLSLAFPVFLWMRPH---WQDMLKLEAAAQRLGDGHLAERIHFDEGSSLERLGVAFNQMADNINALIA 210
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
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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