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Conserved domains on  [gi|46580989|ref|YP_011797|]
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methyl-accepting chemotaxis protein [Desulfovibrio vulgaris str. Hildenborough]

Protein Classification

HAMP and MA domain-containing protein (domain architecture ID 11653791)

protein containing domains dCache_2, HAMP, and MA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
368-624 2.37e-67

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  Cd Length: 262  Bit Score: 223.32  E-value: 2.37e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    368 VRVAAEGAGRQRARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRESMGA 447
Cdd:smart00283   6 VEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    448 LSKRADAIGQIMSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSR 527
Cdd:smart00283  86 LEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    528 NVDAASRAVGEAAEHARAAGESLGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLR 607
Cdd:smart00283 166 AMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAE 245
                          250
                   ....*....|....*..
gi 46580989    608 DLEGGTTNLTRLIERLK 624
Cdd:smart00283 246 ELSGLAEELDELVERFK 262
dCache_2 super family cl07034
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
54-223 3.58e-31

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


The actual alignment was detected with superfamily member pfam17200:

Pssm-ID: 323735  Cd Length: 152  Bit Score: 120.12  E-value: 3.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    54 LLAARGDALRNMIQNVDKLLQEYDARVQKGEFTREEGMKRAALRIGSMRYGN-NDYFWIND-TGTpyptMIMHPVATQLV 131
Cdd:pfam17200   1 LIDQKKDELKNLVETAISLIEAVYKQVESGKITEEEAQELAKELVRALRYGDgKGYFFVYDsDGT----MLVHPFNPQLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   132 GKVLDspNYQratgwrtapgeDFNaypaGKNLFQAFVDVVQRNGSGLVSYAWPKPlpGGGASSElynKESYVTLFRPWGW 211
Cdd:pfam17200  77 GKNLS--NLK-----------DAN----GKYFIRELIDTAKKAGGGFVDYLWKNP--GEGAVEP---KLAYVKYFPPWDW 134
                         170
                  ....*....|..
gi 46580989   212 IVGTGVYVDDIE 223
Cdd:pfam17200 135 VIGTGSYLDDIN 146
HAMP pfam00672
HAMP domain;
233-302 4.59e-09

HAMP domain;


:

Pssm-ID: 307012  Cd Length: 69  Bit Score: 54.88  E-value: 4.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   233 VLTLSGGILLLVCAFGWILIRSIRRPLDSLASYARKVADGDLGAHVSGSfIAEFGELKHSLETMVEALRT 302
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESG-RDEIGELARAFNQMAERLRE 69
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
368-624 2.37e-67

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  Cd Length: 262  Bit Score: 223.32  E-value: 2.37e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    368 VRVAAEGAGRQRARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRESMGA 447
Cdd:smart00283   6 VEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    448 LSKRADAIGQIMSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSR 527
Cdd:smart00283  86 LEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    528 NVDAASRAVGEAAEHARAAGESLGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLR 607
Cdd:smart00283 166 AMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAE 245
                          250
                   ....*....|....*..
gi 46580989    608 DLEGGTTNLTRLIERLK 624
Cdd:smart00283 246 ELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
219-624 4.72e-63

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 216.78  E-value: 4.72e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 219 VDDIERDVTALRLRVLTLSGGILLLVCAFGWILIRSIRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVE 298
Cdd:COG0840  48 ASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMIL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 299 ALRTKIAEAQEKTDEASimarraeeqthaaeaareeaerarsegmvDAANQLEAIVRDVgraasaltglvrvaAEGAGRQ 378
Cdd:COG0840 128 NLRQIIDAVQDNAEALS-----------------------------GASEEIAASATEL--------------SARADQQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 379 RARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREaasLRESMGALSKRADAIGQI 458
Cdd:COG0840 165 AESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEE---LAEVVKKLSESSQEIEEI 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 459 MSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSRNVDAASRAVGE 538
Cdd:COG0840 242 TSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSE 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 539 AAEHARAAGESLGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLRDLEGGTTNLTR 618
Cdd:COG0840 322 GVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLE 401

                ....*.
gi 46580989 619 LIERLK 624
Cdd:COG0840 402 LVAKFK 407
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
390-589 1.22e-58

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: 197.84  E-value: 1.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 390 EEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRESMGALSKRADAIGQIMSVISDIADQT 469
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 470 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSRNVDAASRAVGEAAEHARAAGES 549
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46580989 550 LGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVA 589
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
403-622 2.23e-45

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  Cd Length: 207  Bit Score: 161.46  E-value: 2.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   403 AGQAATTSEAARAKAQQGAGGVEQVVasvaqvereaaslrESMGALSKRADAIGQIMSVISDIADQTNLLALNAAIEAAR 482
Cdd:pfam00015   1 SDLAQLASEEALDEMSQIGQVVDDAV--------------ETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAAR 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   483 AGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSRNVDAASRAVGEAAEHARAAGESLGEIVRLAEQVSD 562
Cdd:pfam00015  67 AGEQGRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIAD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   563 QIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLRDLEGGTTNLTRLIER 622
Cdd:pfam00015 147 IVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQ 206
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
230-570 2.25e-32

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 131.67  E-value: 2.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  230 RLRVLTLSGGILLLVCAFGwiLIRSIRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVEALRTKIAEAQE 309
Cdd:PRK15048 193 QLAVIALVVVLILLVAWYG--IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVRE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  310 KTDeaSIMARRAEeqthaaeaareeaeraRSEGMVDAANQLEaivrdvgRAASALTglvrvaaegagrqrarvgETSVSM 389
Cdd:PRK15048 271 GSD--AIYAGTRE----------------IAAGNTDLSSRTE-------QQASALE------------------ETAASM 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  390 EEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVasvaqvereaaslrESMGALSKRADAIGQIMSVISDIADQT 469
Cdd:PRK15048 308 EQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVV--------------KTMHEIADSSKKIADIISVIDGIAFQT 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  470 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRgiqqgtgESSRNVDAASRAVgeaaehaRAAGES 549
Cdd:PRK15048 374 NILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE-------DSVSRVDTGSVLV-------ESAGET 439
                        330       340
                 ....*....|....*....|.
gi 46580989  550 LGEIVRLAEQVSDQIRSIATA 570
Cdd:PRK15048 440 MNNIVNAVTRVTDIMGEIASA 460
sCache_2 pfam17200
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ...
54-223 3.58e-31

Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain.


Pssm-ID: 319218  Cd Length: 152  Bit Score: 120.12  E-value: 3.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    54 LLAARGDALRNMIQNVDKLLQEYDARVQKGEFTREEGMKRAALRIGSMRYGN-NDYFWIND-TGTpyptMIMHPVATQLV 131
Cdd:pfam17200   1 LIDQKKDELKNLVETAISLIEAVYKQVESGKITEEEAQELAKELVRALRYGDgKGYFFVYDsDGT----MLVHPFNPQLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   132 GKVLDspNYQratgwrtapgeDFNaypaGKNLFQAFVDVVQRNGSGLVSYAWPKPlpGGGASSElynKESYVTLFRPWGW 211
Cdd:pfam17200  77 GKNLS--NLK-----------DAN----GKYFIRELIDTAKKAGGGFVDYLWKNP--GEGAVEP---KLAYVKYFPPWDW 134
                         170
                  ....*....|..
gi 46580989   212 IVGTGVYVDDIE 223
Cdd:pfam17200 135 VIGTGSYLDDIN 146
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
54-145 1.44e-18

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: 82.69  E-value: 1.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989     54 LLAARGDALRNMIQNVDKLLQEYDARVQKGEFTREEGMKRAALRIGSMRYGNNDYFWINDTGtpyPTMIMHPVATQLVGK 133
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAAGKLTEEEAQAQAKAALRALRYGGDGYFFVYDSD---GVMLMHPAKPELEGK 77
                           90
                   ....*....|..
gi 46580989    134 VLDspNYQRATG 145
Cdd:smart01049  78 NLS--DLKDPNG 87
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms];
49-233 7.13e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 226930  Cd Length: 459  Bit Score: 64.46  E-value: 7.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  49 TVEQRLLAARGDALRNMIQNVDKLLQEYDARVQKGEftrEEGMKRAALRIGSMRYGNNDYFWINDTGTpypTMIMHPVAT 128
Cdd:COG4564  40 IFEANMLEAKETELLNLVNLALSAIRLVYNNAGPSD---EAAKQEVKAILTNLDYGSDGYFFVYDYQG---TNLVHPRQP 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 129 QLVGKVLdspnyqratgWRTAPgedfnayPAGKNLFQAFVdVVQRNGSGLVSYAWPKPlpgggASSELYNKESYVTLFRP 208
Cdd:COG4564 114 ELVGQNL----------WQLTD-------PRGDRVIQALI-AKAQEGGGLHQYLWEKP-----SSHETVDKLSYAAGLDK 170
                       170       180
                ....*....|....*....|....*
gi 46580989 209 WGWIVGTGVYVDDIERDVTALRLRV 233
Cdd:COG4564 171 WEWMIGTGLYLDDVSAETAAAQAAV 195
HAMP pfam00672
HAMP domain;
233-302 4.59e-09

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 54.88  E-value: 4.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   233 VLTLSGGILLLVCAFGWILIRSIRRPLDSLASYARKVADGDLGAHVSGSfIAEFGELKHSLETMVEALRT 302
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESG-RDEIGELARAFNQMAERLRE 69
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
253-305 6.30e-07

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 48.40  E-value: 6.30e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 46580989    253 RSIRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVEALRTKIA 305
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
255-302 8.32e-06

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: 44.93  E-value: 8.32e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 46580989 255 IRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVEALRT 302
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
234-300 1.87e-04

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846  Cd Length: 475  Bit Score: 44.06  E-value: 1.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46580989  234 LTLSGGILLLVCAFGWILIRSIRRpldsLASYARKVADGDLGA--HVSGSfiaEFGELKHSLETMVEAL 300
Cdd:PRK11100 189 ALLLGIALLIGAGVVWWLNRSIRR----LTRYADAVTEGKPVPlpKLGSS---ELRELAQALESMRVKL 250
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
298-488 2.13e-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  Cd Length: 1353  Bit Score: 40.94  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    298 EALRTKIAEAQEKTDEASIMARRAEEQTHAAEAAREEAERARSEGMVDAANQ--------LEAIVRDV---GRAASALTG 366
Cdd:TIGR02680  786 RSLRAAHRRAAEAERQAESAERELARAARKAAAAAAAWKQARRELERDAADLdlptdpdaLEAVGLALkrfGDHLHTLEV 865
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    367 LVR---VAAEGAGRQRARVGETSVSMEEMNAtvlDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRE 443
Cdd:TIGR02680  866 AVRelrHAATRAAEQRARAARAESDAREAAE---DAAEARAEAEEASLRLRTLEESVGAMVDEIRARLAETRAALASGGR 942
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 46580989    444 SMGALSK-RADAIGQIMSVISDIADQTNLLalnAAIEAARAGEAGR 488
Cdd:TIGR02680  943 ELPRLAEaLATAEEARGRAEEKRAEADATL---DERAEARDHAIGQ 985
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
368-624 2.37e-67

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  Cd Length: 262  Bit Score: 223.32  E-value: 2.37e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    368 VRVAAEGAGRQRARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRESMGA 447
Cdd:smart00283   6 VEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAVSAVEE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    448 LSKRADAIGQIMSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSR 527
Cdd:smart00283  86 LEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEETNEAVA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    528 NVDAASRAVGEAAEHARAAGESLGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLR 607
Cdd:smart00283 166 AMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAE 245
                          250
                   ....*....|....*..
gi 46580989    608 DLEGGTTNLTRLIERLK 624
Cdd:smart00283 246 ELSGLAEELDELVERFK 262
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
219-624 4.72e-63

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 216.78  E-value: 4.72e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 219 VDDIERDVTALRLRVLTLSGGILLLVCAFGWILIRSIRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVE 298
Cdd:COG0840  48 ASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMIL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 299 ALRTKIAEAQEKTDEASimarraeeqthaaeaareeaerarsegmvDAANQLEAIVRDVgraasaltglvrvaAEGAGRQ 378
Cdd:COG0840 128 NLRQIIDAVQDNAEALS-----------------------------GASEEIAASATEL--------------SARADQQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 379 RARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREaasLRESMGALSKRADAIGQI 458
Cdd:COG0840 165 AESLEEVASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAEE---LAEVVKKLSESSQEIEEI 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 459 MSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSRNVDAASRAVGE 538
Cdd:COG0840 242 TSVINSIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSE 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 539 AAEHARAAGESLGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLRDLEGGTTNLTR 618
Cdd:COG0840 322 GVKLVEETGSSLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLE 401

                ....*.
gi 46580989 619 LIERLK 624
Cdd:COG0840 402 LVAKFK 407
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
390-589 1.22e-58

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: 197.84  E-value: 1.22e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 390 EEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRESMGALSKRADAIGQIMSVISDIADQT 469
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 470 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSRNVDAASRAVGEAAEHARAAGES 549
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46580989 550 LGEIVRLAEQVSDQIRSIATASEEQSSSSESIAHALDGVA 589
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
403-622 2.23e-45

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  Cd Length: 207  Bit Score: 161.46  E-value: 2.23e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   403 AGQAATTSEAARAKAQQGAGGVEQVVasvaqvereaaslrESMGALSKRADAIGQIMSVISDIADQTNLLALNAAIEAAR 482
Cdd:pfam00015   1 SDLAQLASEEALDEMSQIGQVVDDAV--------------ETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAAR 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   483 AGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRGIQQGTGESSRNVDAASRAVGEAAEHARAAGESLGEIVRLAEQVSD 562
Cdd:pfam00015  67 AGEQGRGFAVVADEVRKLAERSAQAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIAD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   563 QIRSIATASEEQSSSSESIAHALDGVAGVADDTSRAMDDAMHSLRDLEGGTTNLTRLIER 622
Cdd:pfam00015 147 IVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQ 206
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
230-570 2.25e-32

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 131.67  E-value: 2.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  230 RLRVLTLSGGILLLVCAFGwiLIRSIRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVEALRTKIAEAQE 309
Cdd:PRK15048 193 QLAVIALVVVLILLVAWYG--IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVRE 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  310 KTDeaSIMARRAEeqthaaeaareeaeraRSEGMVDAANQLEaivrdvgRAASALTglvrvaaegagrqrarvgETSVSM 389
Cdd:PRK15048 271 GSD--AIYAGTRE----------------IAAGNTDLSSRTE-------QQASALE------------------ETAASM 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  390 EEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVasvaqvereaaslrESMGALSKRADAIGQIMSVISDIADQT 469
Cdd:PRK15048 308 EQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVV--------------KTMHEIADSSKKIADIISVIDGIAFQT 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  470 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRgiqqgtgESSRNVDAASRAVgeaaehaRAAGES 549
Cdd:PRK15048 374 NILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIE-------DSVSRVDTGSVLV-------ESAGET 439
                        330       340
                 ....*....|....*....|.
gi 46580989  550 LGEIVRLAEQVSDQIRSIATA 570
Cdd:PRK15048 440 MNNIVNAVTRVTDIMGEIASA 460
sCache_2 pfam17200
Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which ...
54-223 3.58e-31

Single Cache domain 2; This entry represents the single Cache domain 2 (sCache_2), which contains the long N-terminal helix domain.


Pssm-ID: 319218  Cd Length: 152  Bit Score: 120.12  E-value: 3.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    54 LLAARGDALRNMIQNVDKLLQEYDARVQKGEFTREEGMKRAALRIGSMRYGN-NDYFWIND-TGTpyptMIMHPVATQLV 131
Cdd:pfam17200   1 LIDQKKDELKNLVETAISLIEAVYKQVESGKITEEEAQELAKELVRALRYGDgKGYFFVYDsDGT----MLVHPFNPQLE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   132 GKVLDspNYQratgwrtapgeDFNaypaGKNLFQAFVDVVQRNGSGLVSYAWPKPlpGGGASSElynKESYVTLFRPWGW 211
Cdd:pfam17200  77 GKNLS--NLK-----------DAN----GKYFIRELIDTAKKAGGGFVDYLWKNP--GEGAVEP---KLAYVKYFPPWDW 134
                         170
                  ....*....|..
gi 46580989   212 IVGTGVYVDDIE 223
Cdd:pfam17200 135 VIGTGSYLDDIN 146
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
377-570 1.03e-30

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 126.61  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  377 RQRARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAGGVEQVVasvaqvereaaslrESMGALSKRADAIG 456
Cdd:PRK15041 297 QQAASLEETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVV--------------QTMRDISTSSQKIA 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  457 QIMSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRgiqqgtgESSRNVDAASRAV 536
Cdd:PRK15041 363 DIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIE-------DSVGKVDVGSTLV 435
                        170       180       190
                 ....*....|....*....|....*....|....
gi 46580989  537 geaaehaRAAGESLGEIVRLAEQVSDQIRSIATA 570
Cdd:PRK15041 436 -------ESAGETMAEIVSAVTRVTDIMGEIASA 462
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
350-620 7.52e-30

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 123.64  E-value: 7.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  350 LEAIVRDVGRAASAL-TGLVRVAA------EGAGRQRARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQGAG 422
Cdd:PRK09793 259 LRGTVSDVRKGSQEMhIGIAEIVAgnndlsSRTEQQAASLAQTAASMEQLTATVGQNADNARQASELAKNAATTAQAGGV 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  423 gveqvvasvaqverEAASLRESMGALSKRADAIGQIMSVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAE 502
Cdd:PRK09793 339 --------------QVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAS 404
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  503 KTMNATKEVDSAIRgiqqgtgESSRNVDAASRAVGEAAeharaagESLGEIVRLAEQVSDQIRSIATASEEQSSSSESIA 582
Cdd:PRK09793 405 RSAQAAKEIKGLIE-------ESVNRVQQGSKLVNNAA-------ATMTDIVSSVTRVNDIMGEIASASEEQRRGIEQVA 470
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 46580989  583 HALDGVAGVADDTSRAMDDAMHSLRDLEGGTTNLTRLI 620
Cdd:PRK09793 471 QAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRV 508
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
51-226 6.74e-28

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


Pssm-ID: 311945  Cd Length: 296  Bit Score: 114.76  E-value: 6.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    51 EQRLLAARGDALRNMIQNVDKLLQEYDARvQKGEFTREEGMKRA--ALRigSMRY-GNNDYFWINDTgtpYPTMIMHPVA 127
Cdd:pfam08269  39 KNNLEESLKESLKSRVEEAYSIAESIYEK-YKNKLSEEEIKKLIkeALR--SIRYnGGTGYYFIIDS---KGTLILHPDS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   128 TQLVGKVLDspNYQratgwrtapgedfnaYPAGKNLFQAFVDVVQRNGSGLVSYAWPKPLPgggassELYNKESYVTLFR 207
Cdd:pfam08269 113 PSLEGKNLL--DLK---------------DKNGRYIIREMIKLARKKGEGFVEYLWPKPPK------TPYKKISYVKYFE 169
                         170
                  ....*....|....*....
gi 46580989   208 PWGWIVGTGVYVDDIERDV 226
Cdd:pfam08269 170 PYDWIIGTGAYLDDIEEEL 188
dCache_2 pfam08269
Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 ...
71-223 1.23e-25

Cache domain; Double Cache domain 2 (dCache_2) may be a result of single Cache domain 2 (sCache_2) duplication.


Pssm-ID: 311945  Cd Length: 296  Bit Score: 108.21  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    71 KLLQEYDARVQKGEFT--REEGMKRAALR-IGSMRYGNNDYFWINDTGtpyPTMIMHPVATQLVGKVLDSpnyqratgwr 147
Cdd:pfam08269 166 KYFEPYDWIIGTGAYLddIEEELKQELLKqLASIRYGNNGYFFIYDTD---GNMILHPLKPELDGKNLTD---------- 232
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46580989   148 tapgedfNAYPAGKNLFQAFVDVVQRNGSGLVSYAWPKPlpgggASSELYNKESYVTLFRPWGWIVGTGVYVDDIE 223
Cdd:pfam08269 233 -------VKDKKGVEIFQELLDAAKKGGEGFVTYKWPKP-----GGDKPRPKISYVRYFPPWGWIIGTGVYLDEIE 296
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
54-145 1.44e-18

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: 82.69  E-value: 1.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989     54 LLAARGDALRNMIQNVDKLLQEYDARVQKGEFTREEGMKRAALRIGSMRYGNNDYFWINDTGtpyPTMIMHPVATQLVGK 133
Cdd:smart01049   1 LLEERKAELKNLVEIAVSIVEAYYAQAAAGKLTEEEAQAQAKAALRALRYGGDGYFFVYDSD---GVMLMHPAKPELEGK 77
                           90
                   ....*....|..
gi 46580989    134 VLDspNYQRATG 145
Cdd:smart01049  78 NLS--DLKDPNG 87
COG4564 COG4564
Signal transduction histidine kinase [Signal transduction mechanisms];
49-233 7.13e-11

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 226930  Cd Length: 459  Bit Score: 64.46  E-value: 7.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  49 TVEQRLLAARGDALRNMIQNVDKLLQEYDARVQKGEftrEEGMKRAALRIGSMRYGNNDYFWINDTGTpypTMIMHPVAT 128
Cdd:COG4564  40 IFEANMLEAKETELLNLVNLALSAIRLVYNNAGPSD---EAAKQEVKAILTNLDYGSDGYFFVYDYQG---TNLVHPRQP 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989 129 QLVGKVLdspnyqratgWRTAPgedfnayPAGKNLFQAFVdVVQRNGSGLVSYAWPKPlpgggASSELYNKESYVTLFRP 208
Cdd:COG4564 114 ELVGQNL----------WQLTD-------PRGDRVIQALI-AKAQEGGGLHQYLWEKP-----SSHETVDKLSYAAGLDK 170
                       170       180
                ....*....|....*....|....*
gi 46580989 209 WGWIVGTGVYVDDIERDVTALRLRV 233
Cdd:COG4564 171 WEWMIGTGLYLDDVSAETAAAQAAV 195
HAMP pfam00672
HAMP domain;
233-302 4.59e-09

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 54.88  E-value: 4.59e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   233 VLTLSGGILLLVCAFGWILIRSIRRPLDSLASYARKVADGDLGAHVSGSfIAEFGELKHSLETMVEALRT 302
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLESG-RDEIGELARAFNQMAERLRE 69
Cache_3-Cache_2 pfam17201
Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of ...
94-230 1.71e-07

Cache 3/Cache 2 fusion domain; The Cache_3-Cache_2 domain likely originated as a fusion of sCache_3 and sCache_2 domains.


Pssm-ID: 319219  Cd Length: 291  Bit Score: 53.09  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    94 AALR--IGSMRYGNNDYFWI-NDTGTPYPTMIMHPvatqlvgkvldspnyqratgwrtapgedfnaYPAGKNLFQ----- 165
Cdd:pfam17201 182 ASLRkaIGKAKIGKTGYLYVlDGKGDEKGKFIIHP-------------------------------TLKGKNLLDdadgq 230
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46580989   166 --AFVDVVQRNgSGLVSYAWPKPLPGGgasselyNKESYVTLFRPWGWIVGTGVYVDDIERDVTALR 230
Cdd:pfam17201 231 rdFVKKMLAKK-DGSLEYTWKDDAKGR-------EKIAVFTYFEPWDWVIVASVYEDEFLAETNRVR 289
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
253-305 6.30e-07

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 48.40  E-value: 6.30e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 46580989    253 RSIRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVEALRTKIA 305
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRLEETIA 53
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
255-302 8.32e-06

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: 44.93  E-value: 8.32e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 46580989 255 IRRPLDSLASYARKVADGDLGAHVSGSFIAEFGELKHSLETMVEALRT 302
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLRE 48
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
234-300 1.87e-04

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846  Cd Length: 475  Bit Score: 44.06  E-value: 1.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46580989  234 LTLSGGILLLVCAFGWILIRSIRRpldsLASYARKVADGDLGA--HVSGSfiaEFGELKHSLETMVEAL 300
Cdd:PRK11100 189 ALLLGIALLIGAGVVWWLNRSIRR----LTRYADAVTEGKPVPlpKLGSS---ELRELAQALESMRVKL 250
PRK07735 PRK07735
NADH dehydrogenase subunit C; Validated
292-546 3.97e-04

NADH dehydrogenase subunit C; Validated


Pssm-ID: 236081  Cd Length: 430  Bit Score: 43.05  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  292 SLETMVEALRTKIAEAQEKTDEASIMARRAEEQTHAAEAAREEAERARSEGMVDAANQLEaivrdvgRAASAltglVRVA 371
Cdd:PRK07735   2 DPEKDLEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKR-------RAAAA----AKAK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  372 AEGAGRQRaRVGETSVSMEEMnatvldvarnAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRESMGALSKR 451
Cdd:PRK07735  71 AAALAKQK-REGTEEVTEEEK----------AKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKA 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989  452 ADAIGQIMSVISDIADQTNLL--------------ALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMNATKEVDSAIRG 517
Cdd:PRK07735 140 AALAKQKREGTEEVTEEEEETdkekakakaaaaakAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALA 219
                        250       260
                 ....*....|....*....|....*....
gi 46580989  518 IQQGTGESSRNVDAASRAVGEAAEHARAA 546
Cdd:PRK07735 220 KQKASQGNGDSGDEDAKAKAIAAAKAKAA 248
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
298-488 2.13e-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  Cd Length: 1353  Bit Score: 40.94  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    298 EALRTKIAEAQEKTDEASIMARRAEEQTHAAEAAREEAERARSEGMVDAANQ--------LEAIVRDV---GRAASALTG 366
Cdd:TIGR02680  786 RSLRAAHRRAAEAERQAESAERELARAARKAAAAAAAWKQARRELERDAADLdlptdpdaLEAVGLALkrfGDHLHTLEV 865
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    367 LVR---VAAEGAGRQRARVGETSVSMEEMNAtvlDVARNAGQAATTSEAARAKAQQGAGGVEQVVASVAQVEREAASLRE 443
Cdd:TIGR02680  866 AVRelrHAATRAAEQRARAARAESDAREAAE---DAAEARAEAEEASLRLRTLEESVGAMVDEIRARLAETRAALASGGR 942
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 46580989    444 SMGALSK-RADAIGQIMSVISDIADQTNLLalnAAIEAARAGEAGR 488
Cdd:TIGR02680  943 ELPRLAEaLATAEEARGRAEEKRAEADATL---DERAEARDHAIGQ 985
PTZ00121 PTZ00121
MAEBL; Provisional
285-565 4.68e-03

MAEBL; Provisional


Pssm-ID: 173412  Cd Length: 2084  Bit Score: 40.12  E-value: 4.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   285 EFGELKHSLETMVEALRTKIAEAQEKTDEASIM-ARRAEEQTHAAEAAREEAERARSEgmvdaanqleaivrDVGRAASA 363
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEeARKAEEAKKKAEDARKAEEARKAE--------------DARKAEEA 1145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   364 ltglvRVAAEGAGRQRARVGETSVSMEEmnatvldvARNAGQAATTSEAARAkaqqgaggvEQVvasvaqveREAASLRE 443
Cdd:PTZ00121 1146 -----RKAEDAKRVEIARKAEDARKAEE--------ARKAEDAKKAEAARKA---------EEV--------RKAEELRK 1195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   444 SMGAlsKRADAIGQIMSVisdiadqtnllalNAAIEAARAGEAGRGFAV-VADEVRKLAEKTMNATKEVDSAirgiQQGT 522
Cdd:PTZ00121 1196 AEDA--RKAEAARKAEEE-------------RKAEEARKAEDAKKAEAVkKAEEAKKDAEEAKKAEEERNNE----EIRK 1256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 46580989   523 GESSRNVDAASRAVGEAAEHARAAGEslgeiVRLAEQV--SDQIR 565
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADE-----LKKAEEKkkADEAK 1296
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
340-446 6.73e-03

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  Cd Length: 262  Bit Score: 38.42  E-value: 6.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989    340 SEGMVDAANQLEAIVRDVGRAASALTGLVrvaaegagrqrARVGETSVSMEEMNATVLDVARNAGQAATTSEAARAKAQQ 419
Cdd:smart00283 164 VAAMEESSSEVEEGVELVEETGDALEEIV-----------DSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQE 232
                           90       100
                   ....*....|....*....|....*..
gi 46580989    420 GAGGVEQVVASVAQVEREAASLRESMG 446
Cdd:smart00283 233 TAAMSEEISAAAEELSGLAEELDELVE 259
EspB pfam05802
Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of ...
410-626 7.96e-03

Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of enteropathogenic Escherichia coli (EPEC) which is essential for EPEC pathogenesis. EspB is also found in Citrobacter rodentium.


Pssm-ID: 310415  Cd Length: 317  Bit Score: 38.52  E-value: 7.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   410 SEAARAKAQQGAGGVEQVVASVAQVEREAASlRESMGALSKRADAIgqimsviSDIADQTNLLALNAAIEAARAGEAGRG 489
Cdd:pfam05802 115 SFAAINSATKGASDIAQKATSASSKAVNAAS-EVATKALVKATESV-------ADAAEEASSTMQQAMATATKAASRTSG 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46580989   490 favVADEVRKLAEKTMNATKEVDSAirgiQQGTGESSRNVDAASR--------AVGEAAEHARAAGESLGEIVRLAEQVS 561
Cdd:pfam05802 187 ---VADDVATSAQKASQVAEEAADA----AQKASRLSRFTAAVDKitgstafvAVTSLAEGTKTLPTTISESVKSNHEIN 259
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46580989   562 DQ-IRSIATASEEQSSSsesiahaldgvagVADDTSRAMDDAMHSLRDLEGGTTNLTRLIERLKKS 626
Cdd:pfam05802 260 EQrAKSVENFQQGNLEL-------------YKQDVRRSQDDIASRLRDMTAAARDLNDLQNRMGQS 312
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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