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Conserved domains on  [gi|86360197|ref|YP_472086|]
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methyl-accepting chemotaxis protein [Rhizobium etli CFN 42]

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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 ...
380-579 1.56e-57

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: 194.38  E-value: 1.56e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 380 EQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQT 459
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 460 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGN 539
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86360197 540 VGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEAT 579
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
220-268 2.12e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 36.84  E-value: 2.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 86360197 220 IVGPLTKLQLSLNAMAEGNLDgdRRLEARG-DEIGKLARAVAGLRDAISA 268
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLD--VRLPVTGrDEIGELARAFNQMAERLRE 48
Tar_Tsr_LBD super family cl00144
ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate ...
6-184 1.40e-12

ligand binding domain of Tar- and Tsr-related chemoreceptors; E.coli Tar (taxis to aspartate and repellents) and Tsr (taxis to serine and repellents) are homologous chemoreceptors that have a high specificity for aspartate and serine, respectively. Both are homodimeric receptors and contain an N-terminal periplasmic ligand binding domain, a transmembrane region, a HAMP domain and a C-terminal cytosolic signaling domain.


The actual alignment was detected with superfamily member pfam12729:

Pssm-ID: 260214  Cd Length: 181  Bit Score: 66.09  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197     6 NSGIAVRLALGFSFLILLMAGLSIYSTVKVAEINSNLQTINDVNSVKQRFAINYRGSVHDRAIAIRDVTLVTSVDERKAA 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    86 EALIEKLAAsytENEKRMADMVASPagATDQERSILKEIADIQAKTNPLVAQIIALQEKGDGEAARKILLEQARPAFVAW 165
Cdd:pfam12729  81 LKDIEELRA---EIDKLLKKYEKTI--LTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170
                  ....*....|....*....
gi 86360197   166 LGAINKFIDYQEALNKSIG 184
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAY 174
MCP_signal super family cl19050
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
292-397 1.75e-03

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: 267403  Cd Length: 200  Bit Score: 38.76  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 292 ADERRTLAEQTDRAVGQLGSALqaladGDLTQQIGTpfipSLEKLRADfNSAVEKLRAAMQKVAENASAIAAGAQEIRSA 371
Cdd:cd11386 105 ADEVRKLAEESAEAAKEIEELI-----EEIQEQTEE----AVEAMEET-SEEVEEGVELVEETGRAFEEIVASVEEVADG 174
                        90       100
                ....*....|....*....|....*.
gi 86360197 372 SDDLAKRTEQQAASVEETAAALEEIT 397
Cdd:cd11386 175 IQEISAATQEQSASTQEIAAAVEEIA 200
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
353-599 2.25e-71

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: 233.72  E-value: 2.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    353 KVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAV 432
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    433 DAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELIN------ 506
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    507 --------ASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEA 578
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 86360197    579 TAAAHKLAKEADALFQLLGQF 599
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
380-579 1.56e-57

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: 194.38  E-value: 1.56e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 380 EQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQT 459
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 460 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGN 539
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86360197 540 VGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEAT 579
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
220-268 2.12e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 36.84  E-value: 2.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 86360197 220 IVGPLTKLQLSLNAMAEGNLDgdRRLEARG-DEIGKLARAVAGLRDAISA 268
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLD--VRLPVTGrDEIGELARAFNQMAERLRE 48
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
6-184 1.40e-12

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors.


Pssm-ID: 193205  Cd Length: 181  Bit Score: 66.09  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197     6 NSGIAVRLALGFSFLILLMAGLSIYSTVKVAEINSNLQTINDVNSVKQRFAINYRGSVHDRAIAIRDVTLVTSVDERKAA 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    86 EALIEKLAAsytENEKRMADMVASPagATDQERSILKEIADIQAKTNPLVAQIIALQEKGDGEAARKILLEQARPAFVAW 165
Cdd:pfam12729  81 LKDIEELRA---EIDKLLKKYEKTI--LTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170
                  ....*....|....*....
gi 86360197   166 LGAINKFIDYQEALNKSIG 184
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAY 174
HAMP pfam00672
HAMP domain;
199-268 1.51e-08

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 52.23  E-value: 1.51e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   199 LTALGIAALLSVLAAVVTARTIVGPLTKLQLSLNAMAEGNLDgDRRLEARGDEIGKLARAVAGLRDAISA 268
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLD-DRVPVSGPDEIGELARAFNQMADRLRE 70
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
292-397 1.75e-03

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: 38.76  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 292 ADERRTLAEQTDRAVGQLGSALqaladGDLTQQIGTpfipSLEKLRADfNSAVEKLRAAMQKVAENASAIAAGAQEIRSA 371
Cdd:cd11386 105 ADEVRKLAEESAEAAKEIEELI-----EEIQEQTEE----AVEAMEET-SEEVEEGVELVEETGRAFEEIVASVEEVADG 174
                        90       100
                ....*....|....*....|....*.
gi 86360197 372 SDDLAKRTEQQAASVEETAAALEEIT 397
Cdd:cd11386 175 IQEISAATQEQSASTQEIAAAVEEIA 200
ApoLp-III pfam07464
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ...
290-418 4.21e-03

Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolizm. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.


Pssm-ID: 191748  Cd Length: 155  Bit Score: 37.16  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   290 QDADE-RRTLAEQTDRAVGQLgSALQALADGDLTQQIGTpFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQ-E 367
Cdd:pfam07464  23 KDTQEvNKAIKEGSDKVLQQL-KALSASLQEALKDANGK-AKEALEQLRQNIEETAEELRKAHPEVEQQAQELRDKLQaA 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 86360197   368 IRSASDDLAKRTEQQAASVEETAAALEE-ITTTVADSSNRAQEAGQLVRKTK 418
Cdd:pfam07464 101 VQSTVQESQKLAKEVASNVEGTNEKLAPkIKQAYDDFVKNAEEVQKKLHEAA 152
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
218-271 5.38e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 35.69  E-value: 5.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86360197    218 RTIVGPLTKLQLSLNAMAEGNLdgDRRLEARG-DEIGKLARAVAGLRDAISAKAE 271
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDL--TVRLPVDGrDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
353-599 2.25e-71

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: 233.72  E-value: 2.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    353 KVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAV 432
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    433 DAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELIN------ 506
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    507 --------ASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEA 578
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 86360197    579 TAAAHKLAKEADALFQLLGQF 599
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
231-601 7.90e-67

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 226.41  E-value: 7.90e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 231 LNAMAEGNLDGDRRLEARGDEIGKLARAVAGLRDAISAKAEREADAEAKRAVAER-HRLEQDADERRTLAEQTDRAVGQL 309
Cdd:COG0840  12 IELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLlVAIIVVLVLAILLLRAILEPISDL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 310 GSALQALADGDLTQQIGTPFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEET 389
Cdd:COG0840  92 LEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 390 AAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIE-----------SSATEIGSIIGVIDEIAFQ 458
Cdd:COG0840 172 ASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEITSVINSIAEQ 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 459 TNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELI--------------NASNGHVKNGVALVGETGK 524
Cdd:COG0840 252 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIeeiqneaadavehmEESASEVSEGVKLVEETGS 331
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86360197 525 ALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNI 601
Cdd:COG0840 332 SLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
309-601 3.93e-66

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 228.03  E-value: 3.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  309 LGSALQALADGDLTQQIGTPFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEE 388
Cdd:PRK09793 221 IGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQ 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  389 TAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGV 468
Cdd:PRK09793 301 TAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAV 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  469 EAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQ 548
Cdd:PRK09793 381 EAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASE 460
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 86360197  549 EQATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNI 601
Cdd:PRK09793 461 EQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
405-602 4.78e-49

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: 171.09  E-value: 4.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   405 NRAQEAGQLVRKT-KDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVV 483
Cdd:pfam00015   1 AQASDLAQLASEEaLDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   484 AQEVRELAQRSAKAAKEIKELINAS--------------NGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQE 549
Cdd:pfam00015  81 ADEVRKLAERSAQAAKEIEALIEEIvkqtndstasiqqtRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 86360197   550 QATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNIG 602
Cdd:pfam00015 161 QSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
64-327 3.79e-07

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 52.08  E-value: 3.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  64 HDRAIAIRdvTLVTSVDERKAAEALIEKLAASYTENekrmADMVASPAGATDQERSILK----EIADIQAKTNPLVAQII 139
Cdd:COG5000 158 LDPAGFTD--LLNTEAAGRALLEAALLRADGRIVAQ----SYLDFDFPFPAPPEDSIKKadlgKPVLIEPDNTNIRGALI 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 140 ALQEKGDgeaaRKILLEQARPafvawlgaiNKFIDYQEALNKsIGGDVRSTASGFKPI----VLTALGIAaLLSVLAAVV 215
Cdd:COG5000 232 KLKEIED----VYLYVVRPVD---------PKVAEHADLTEG-AAAEYRELEAGRDGLqiafALLYLSTA-LLVLLAAIW 296
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 216 T----ARTIVGPLTKLQLSLNAMAEGNLDGDRRLEARGDEIGKLARA----VAGLRDAisakaeREADAEAKRAVAERHR 287
Cdd:COG5000 297 TaiafARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKAfnkmTEQLSSQ------QEALERAKDALEQRRR 370
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 86360197 288 LEQDA-----------DERRTLAEQTDRAVGQLGSALQALADGDLTQQIGT 327
Cdd:COG5000 371 FLEAVlsgltagvigfDNRGCITTVNPSAEQILGKPFDQLLGQSLSAIAPE 421
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
257-504 8.22e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 8.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    257 RAVAGLRDAISAKAEREADAEAKRAVAeRHRLEQDADERRTLAEQTDRAVGQLGSALQALADGDLTQQIGTPFIPSLEKL 336
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    337 RADFNsavEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRK 416
Cdd:TIGR02168  756 LTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    417 TKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTN-LLALNAGVEAARAgEAGKGFAVVAQEVRELAQRSA 495
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEaLLNERASLEEALA-LLRSELEELSEELRELESKRS 911

                   ....*....
gi 86360197    496 KAAKEIKEL 504
Cdd:TIGR02168  912 ELRRELEEL 920
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-423 5.21e-04

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


Pssm-ID: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    251 EIGKLARAVAGLRDAISAKAEREADAEAKRA--VAERHRLEQDADERRTLAEQTDRAVGQLGSALQALAD--GDLTQQig 326
Cdd:TIGR02169  295 KIGELEAEIASLERSIAEKERELEDAEERLAklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEelEDLRAE-- 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    327 tpfipsLEKLRADFNSAVEKLRAAMQKVAENASAIaagaQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNR 406
Cdd:TIGR02169  373 ------LEEVDKEFAETRDELKDYREKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
                          170
                   ....*....|....*..
gi 86360197    407 AQEAGQLVRKTKDNAER 423
Cdd:TIGR02169  443 KEDKALEIKKQEWKLEQ 459
valS PRK14900
valyl-tRNA synthetase; Provisional
205-432 7.58e-04

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 41.52  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   205 AALLSVLAAVVTARTIVGPLT---KLQLSLNAMAE-GNLDGDRRLEARGDEIGKLARaVAGLRDA-ISAKAEREADAEAK 279
Cdd:PRK14900  743 AAFRPVLGIIDAVRNIRGEMGipwKVKLGAQAPVEiAVADPALRDLLQAGELARVHR-VAGVEGSrLVVAAATAPAPQSA 821
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   280 RAVAERHRLEQDADERRTLAEQTDRAVGQLGSALQALADgdLTQQIGTP-FIPS-----LEKLRAdfnsAVEKLRAAMQK 353
Cdd:PRK14900  822 VGVGPGFEVRVPLAGVIDLAAETARVDKEIGKVDQDLAV--LERKLQNPsFVQNappavVEKDRA----RAEELREKRGK 895
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   354 VaENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSG-SVVRDAV 432
Cdd:PRK14900  896 L-EAHRAMLSGSEANSARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGiEKVAEAV 974
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
274-423 2.90e-03

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


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 38.19  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   274 ADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGQLGSALQAladgdlTQQIGTPFIPSLEKLRADFNSAVEKLRAAmqk 353
Cdd:pfam00015  63 AAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIEE------IVKQTNDSTASIQQTRTEVEVGSTIVEST--- 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   354 vAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAER 423
Cdd:pfam00015 134 -GEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEE 202
PHA00430 PHA00430
tail fiber protein
238-440 6.29e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 38.33  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  238 NLDGDrrLEARGDEIGKLARAVAGlRDAISAKAEREADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGqlGSALQALA 317
Cdd:PHA00430 124 NNDGH--LDARGRRIVNLADAVDD-GDAVPLGQIKTWNQSAWNARNEANRSRNEADRARNQAERFNNESG--ASATNTKQ 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  318 DGDLTqqigtpfipsleklrADFNSAVEklRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEit 397
Cdd:PHA00430 199 WRSEA---------------DGSNSEAN--RFKGYADSMTSSVEAAKGQAESSSKEANTAGDYATKAAASASAAHASE-- 259
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 86360197  398 TTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIES 440
Cdd:PHA00430 260 VNAANSATAAATSANRAKQQADRAKTEADKLGNMNGFAGAIEK 302
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
292-410 9.79e-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 [Multi-domain]  Cd Length: 262  Bit Score: 36.88  E-value: 9.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    292 ADERRTLAEQTDRAVGQLGSALQALadgdltQQIGTPFIPSLEKLRadfnSAVEKLRAAMQKVAENASAIAAGAQEIRSA 371
Cdd:smart00283 132 ADEVRKLAERSAESAKEIESLIKEI------QEETNEAVAAMEESS----SEVEEGVELVEETGDALEEIVDSVEEIADL 201
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 86360197    372 SDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEA 410
Cdd:smart00283 202 VQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
 
Name Accession Description Interval E-value
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
380-579 1.56e-57

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: 194.38  E-value: 1.56e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 380 EQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQT 459
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 460 NLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGN 539
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 86360197 540 VGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEAT 579
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
220-268 2.12e-03

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 100122  Cd Length: 48  Bit Score: 36.84  E-value: 2.12e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 86360197 220 IVGPLTKLQLSLNAMAEGNLDgdRRLEARG-DEIGKLARAVAGLRDAISA 268
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLD--VRLPVTGrDEIGELARAFNQMAERLRE 48
4HB_MCP_1 pfam12729
Four helix bundle sensory module for signal transduction; This family is a four helix bundle ...
6-184 1.40e-12

Four helix bundle sensory module for signal transduction; This family is a four helix bundle that operates as a ubiquitous sensory module in prokaryotic signal-transduction. The 4HB_MCP is always found between two predicted transmembrane helices indicating that it detects only extracellular signals. In many cases the domain is associated with a cytoplasmic HAMP domain suggesting that most proteins carrying the bundle might share the mechanism of transmembrane signalling which is well-characterized in E coli chemoreceptors.


Pssm-ID: 193205  Cd Length: 181  Bit Score: 66.09  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197     6 NSGIAVRLALGFSFLILLMAGLSIYSTVKVAEINSNLQTINDVNSVKQRFAINYRGSVHDRAIAIRDVTLVTSVDERKAA 85
Cdd:pfam12729   1 NLKIRTKLILLFLLLALLLIIVGIVGLYSLKKINKNSETMYEDRLLPIKWLGEIRSNLREIRANLLELILTTDPAERDEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    86 EALIEKLAAsytENEKRMADMVASPagATDQERSILKEIADIQAKTNPLVAQIIALQEKGDGEAARKILLEQARPAFVAW 165
Cdd:pfam12729  81 LKDIEELRA---EIDKLLKKYEKTI--LTEEEKKLFNEFKEQLKAYRKVRNKVLDLAKAGKNDEAYALYLTELEPARDAV 155
                         170
                  ....*....|....*....
gi 86360197   166 LGAINKFIDYQEALNKSIG 184
Cdd:pfam12729 156 IEALDELIDYNLKVAKEAY 174
HAMP pfam00672
HAMP domain;
199-268 1.51e-08

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 52.23  E-value: 1.51e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   199 LTALGIAALLSVLAAVVTARTIVGPLTKLQLSLNAMAEGNLDgDRRLEARGDEIGKLARAVAGLRDAISA 268
Cdd:pfam00672   2 LLVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLD-DRVPVSGPDEIGELARAFNQMADRLRE 70
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
292-397 1.75e-03

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: 38.76  E-value: 1.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 292 ADERRTLAEQTDRAVGQLGSALqaladGDLTQQIGTpfipSLEKLRADfNSAVEKLRAAMQKVAENASAIAAGAQEIRSA 371
Cdd:cd11386 105 ADEVRKLAEESAEAAKEIEELI-----EEIQEQTEE----AVEAMEET-SEEVEEGVELVEETGRAFEEIVASVEEVADG 174
                        90       100
                ....*....|....*....|....*.
gi 86360197 372 SDDLAKRTEQQAASVEETAAALEEIT 397
Cdd:cd11386 175 IQEISAATQEQSASTQEIAAAVEEIA 200
ApoLp-III pfam07464
Apolipophorin-III precursor (apoLp-III); This family consists of several insect ...
290-418 4.21e-03

Apolipophorin-III precursor (apoLp-III); This family consists of several insect apolipoprotein-III sequences. Exchangeable apolipoproteins constitute a functionally important family of proteins that play critical roles in lipid transport and lipoprotein metabolizm. Apolipophorin III (apoLp-III) is a prototypical exchangeable apolipoprotein found in many insect species that functions in transport of diacylglycerol (DAG) from the fat body lipid storage depot to flight muscles in the adult life stage.


Pssm-ID: 191748  Cd Length: 155  Bit Score: 37.16  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   290 QDADE-RRTLAEQTDRAVGQLgSALQALADGDLTQQIGTpFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQ-E 367
Cdd:pfam07464  23 KDTQEvNKAIKEGSDKVLQQL-KALSASLQEALKDANGK-AKEALEQLRQNIEETAEELRKAHPEVEQQAQELRDKLQaA 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 86360197   368 IRSASDDLAKRTEQQAASVEETAAALEE-ITTTVADSSNRAQEAGQLVRKTK 418
Cdd:pfam07464 101 VQSTVQESQKLAKEVASNVEGTNEKLAPkIKQAYDDFVKNAEEVQKKLHEAA 152
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
218-271 5.38e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 35.69  E-value: 5.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 86360197    218 RTIVGPLTKLQLSLNAMAEGNLdgDRRLEARG-DEIGKLARAVAGLRDAISAKAE 271
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDL--TVRLPVDGrDEIGELARAFNEMADRLEETIA 53
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
353-599 2.25e-71

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: 233.72  E-value: 2.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    353 KVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAV 432
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    433 DAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELIN------ 506
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKeiqeet 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    507 --------ASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEA 578
Cdd:smart00283 161 neavaameESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 86360197    579 TAAAHKLAKEADALFQLLGQF 599
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction ...
231-601 7.90e-67

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 226.41  E-value: 7.90e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 231 LNAMAEGNLDGDRRLEARGDEIGKLARAVAGLRDAISAKAEREADAEAKRAVAER-HRLEQDADERRTLAEQTDRAVGQL 309
Cdd:COG0840  12 IELAAGEADAGLLKLKKLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLlVAIIVVLVLAILLLRAILEPISDL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 310 GSALQALADGDLTQQIGTPFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEET 389
Cdd:COG0840  92 LEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNLRQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 390 AAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIE-----------SSATEIGSIIGVIDEIAFQ 458
Cdd:COG0840 172 ASAIEELSETVKEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEIAeelaevvkklsESSQEIEEITSVINSIAEQ 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 459 TNLLALNAGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELI--------------NASNGHVKNGVALVGETGK 524
Cdd:COG0840 252 TNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIeeiqneaadavehmEESASEVSEGVKLVEETGS 331
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86360197 525 ALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNI 601
Cdd:COG0840 332 SLGEIAAAIEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
309-601 3.93e-66

methyl-accepting protein IV; Provisional


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 228.03  E-value: 3.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  309 LGSALQALADGDLTQQIGTPFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEE 388
Cdd:PRK09793 221 IGSHFDSIAAGNLARPIAVYGRNEITAIFASLKTMQQALRGTVSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAASLAQ 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  389 TAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGV 468
Cdd:PRK09793 301 TAASMEQLTATVGQNADNARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAV 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  469 EAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQ 548
Cdd:PRK09793 381 EAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKGLIEESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASE 460
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 86360197  549 EQATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNI 601
Cdd:PRK09793 461 EQRRGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRVAVFTL 513
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
308-627 1.87e-65

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 226.76  E-value: 1.87e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  308 QLGSALQALADGDLTQQIGTPFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVE 387
Cdd:PRK15041 224 RLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLE 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  388 ETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAG 467
Cdd:PRK15041 304 ETAASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIDGIAFQTNILALNAA 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  468 VEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGAS 547
Cdd:PRK15041 384 VEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAEIVSAVTRVTDIMGEIASAS 463
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  548 QEQATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNIGGAAASRRISQPAAAAQHAQPVPSPA 627
Cdd:PRK15041 464 DEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTEAVAVFRIQQQQQQQRETSAVVKTVTPATPRKMA 543
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
306-628 4.91e-64

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 222.57  E-value: 4.91e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  306 VGQLGSALQALADGDLTQQIGTPFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAAS 385
Cdd:PRK15048 220 LAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASA 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  386 VEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTNLLALN 465
Cdd:PRK15048 300 LEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALN 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  466 AGVEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVG 545
Cdd:PRK15048 380 AAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIAS 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  546 ASQEQATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNIggaaASRRISQPAAAAQHAQPVPS 625
Cdd:PRK15048 460 ASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRL----AASPLTNKPQTPSRPASEQP 535

                 ...
gi 86360197  626 PAR 628
Cdd:PRK15048 536 PAQ 538
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
405-602 4.78e-49

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: 171.09  E-value: 4.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   405 NRAQEAGQLVRKT-KDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTNLLALNAGVEAARAGEAGKGFAVV 483
Cdd:pfam00015   1 AQASDLAQLASEEaLDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   484 AQEVRELAQRSAKAAKEIKELINAS--------------NGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQE 549
Cdd:pfam00015  81 ADEVRKLAERSAQAAKEIEALIEEIvkqtndstasiqqtRTEVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 86360197   550 QATGLKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFNIG 602
Cdd:pfam00015 161 QSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQFRIK 213
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
64-327 3.79e-07

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 52.08  E-value: 3.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  64 HDRAIAIRdvTLVTSVDERKAAEALIEKLAASYTENekrmADMVASPAGATDQERSILK----EIADIQAKTNPLVAQII 139
Cdd:COG5000 158 LDPAGFTD--LLNTEAAGRALLEAALLRADGRIVAQ----SYLDFDFPFPAPPEDSIKKadlgKPVLIEPDNTNIRGALI 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 140 ALQEKGDgeaaRKILLEQARPafvawlgaiNKFIDYQEALNKsIGGDVRSTASGFKPI----VLTALGIAaLLSVLAAVV 215
Cdd:COG5000 232 KLKEIED----VYLYVVRPVD---------PKVAEHADLTEG-AAAEYRELEAGRDGLqiafALLYLSTA-LLVLLAAIW 296
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 216 T----ARTIVGPLTKLQLSLNAMAEGNLDGDRRLEARGDEIGKLARA----VAGLRDAisakaeREADAEAKRAVAERHR 287
Cdd:COG5000 297 TaiafARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEDVGRLSKAfnkmTEQLSSQ------QEALERAKDALEQRRR 370
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 86360197 288 LEQDA-----------DERRTLAEQTDRAVGQLGSALQALADGDLTQQIGT 327
Cdd:COG5000 371 FLEAVlsgltagvigfDNRGCITTVNPSAEQILGKPFDQLLGQSLSAIAPE 421
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
257-504 8.22e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].


Pssm-ID: 233757 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 8.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    257 RAVAGLRDAISAKAEREADAEAKRAVAeRHRLEQDADERRTLAEQTDRAVGQLGSALQALADGDLTQQIGTPFIPSLEKL 336
Cdd:TIGR02168  677 REIEELEEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    337 RADFNsavEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRK 416
Cdd:TIGR02168  756 LTELE---AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    417 TKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIAFQTN-LLALNAGVEAARAgEAGKGFAVVAQEVRELAQRSA 495
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEaLLNERASLEEALA-LLRSELEELSEELRELESKRS 911

                   ....*....
gi 86360197    496 KAAKEIKEL 504
Cdd:TIGR02168  912 ELRRELEEL 920
PRK02224 PRK02224
chromosome segregation protein; Provisional
246-600 1.57e-05

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 46.96  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  246 EARGDEIGKLARAVAGLRDAISAkAEREADAEAKRAVAERHRLEQDADERRTLAEQTDravgqlgsaLQALADGDLTQQI 325
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAE-TEREREELAEEVRDLRERLEELEEERDDLLAEAG---------LDDADAEAVEARR 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  326 GTpfipsLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADssn 405
Cdd:PRK02224 317 EE-----LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEE--- 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  406 raqeagqLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIafQTNLLALNAGVEAARA-GEAGK------ 478
Cdd:PRK02224 389 -------LEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAEL--EATLRTARERVEEAEAlLEAGKcpecgq 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  479 -----GFAVVAQEVRELAQRSAKAAKEIKELINASNGHVkngvalvgETGKALQEIAVQVQQVDGNVGAIVGASQEQATG 553
Cdd:PRK02224 460 pvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERL--------ERAEDLVEAEDRIERLEERREDLEELIAERRET 531
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 86360197  554 LKEINTAVNRMDQGTQQNAAMVEEATAAAHKLAKEADALFQLLGQFN 600
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
DUF390 pfam04094
Protein of unknown function (DUF390); This is a family of long proteins currently only found ...
221-595 3.32e-05

Protein of unknown function (DUF390); This is a family of long proteins currently only found in the rice genome. They have no known function. However they may be some kind of transposable element.


Pssm-ID: 112890 [Multi-domain]  Cd Length: 843  Bit Score: 45.58  E-value: 3.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   221 VGPLTKLQLsLNAMAEGN---LDG-DRRLEARGDEIGKLARAVAGLRDAisaKAEREADAEAKRAVAERHRLEQDAdERR 296
Cdd:pfam04094 379 AAPLNAEPL-LQALAAANttvLDGlSAQMEALQAERAELDAAWARVEEG---RRSVEAMVEAGRKAHRRHTSELEA-RKK 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   297 TLAEQTDRAVGQLGSALQALADGDLTQqigtpfipslEKLRADFNSAVEKLRAAMQkvAENASAIAAGAQEIRSASDDLA 376
Cdd:pfam04094 454 DLAEIAKEVEEEREAALIATTVLNEAQ----------DDLRLQYGSRAAELEKKLD--AAQGVLDAAAAREQRAAENEAA 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   377 KRTEQQAasVEETAAALEEITTTVA-DSSNRaqEAGQLVRKTKDNAERSGSVVRDAvdAMGKIESSATEIGSIIGVIDEI 455
Cdd:pfam04094 522 SRQREEA--LEARAMALEERACAKErDLADR--EAAVAIREATLAAHEAACAEEEF--ALRLREDALTERERALEEAEAA 595
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   456 AFQ-TNLLALNagvEAARAGEAGKGFAVVAQEVRELAQRSAKAAKEIKELinasNGHVKNGVALVGET------GKALQE 528
Cdd:pfam04094 596 AQQlADSLFLR---EAAQEEQARRNLEGARAERAALDQRAAELEARAKEL----DARAHSGGAAAGDGdlaarlAAAEHS 668
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86360197   529 IAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQ-------NAAMVEEATAAAHKLAKEADALFQL 595
Cdd:pfam04094 669 IADLQCALDSSAGEVEALRLAGEVGPGMLRDAVSRLDCAGRQaglwggrCAKYAANQGGLAQRLSEMAGALQRL 742
PRK02224 PRK02224
chromosome segregation protein; Provisional
242-494 9.00e-05

chromosome segregation protein; Provisional


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 9.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  242 DRRLEARGDEIGKLARAVAGLRDAISAKAEREADAEAKRAVAERHRLE-----QDADERRTLAEQTDRAVGQLGSALQAL 316
Cdd:PRK02224 369 ESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEElreerDELREREAELEATLRTARERVEEAEAL 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  317 ADGDLTQQIGTPF---------------IPSLEKLRADFNSAVEKLRAAMQKvAENASAIAAGAQEIRSASDDLAKRTEQ 381
Cdd:PRK02224 449 LEAGKCPECGQPVegsphvetieedrerVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERREDLEELIAE 527
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  382 QAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAErsgsvvrDAVDAMGKIESSATEIGSIIGVIDEIAFQTNL 461
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAE-------EAREEVAELNSKLAELKERIESLERIRTLLAA 600
                        250       260       270
                 ....*....|....*....|....*....|....
gi 86360197  462 LAlNAGVEAARAGEAGKGFAVVAQEVRE-LAQRS 494
Cdd:PRK02224 601 IA-DAEDEIERLREKREALAELNDERRErLAEKR 633
COG1511 COG1511
Predicted membrane protein [Function unknown]
420-592 4.72e-04

Predicted membrane protein [Function unknown]


Pssm-ID: 224428 [Multi-domain]  Cd Length: 780  Bit Score: 42.11  E-value: 4.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 420 NAERSGSVVRDAVDAMGKIESSATEigSIIGVIDEIAFQTNLLALNAGVEAARAGeagkgfavvAQEVRELAQRSAKAAK 499
Cdd:COG1511 134 NEKLNAVAPKITEKAADKLLNEISK--ELTETYTKVVAFPTIYDLGGGVKGAADG---------AEKLKDGTDEASNGNK 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 500 EIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMDQGTQQNAAMVEEAT 579
Cdd:COG1511 203 KLSDLLNTLNNSSATFSDGLNALTSGLTTLTDGLNQLDSGLGTLAAGIGELKQGAEQLNEGIGEFSSGLSELNSGVQDLA 282
                       170
                ....*....|...
gi 86360197 580 AAAHKLAKEADAL 592
Cdd:COG1511 283 AGVPQLNQGISAL 295
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
251-423 5.21e-04

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


Pssm-ID: 233758 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 5.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    251 EIGKLARAVAGLRDAISAKAEREADAEAKRA--VAERHRLEQDADERRTLAEQTDRAVGQLGSALQALAD--GDLTQQig 326
Cdd:TIGR02169  295 KIGELEAEIASLERSIAEKERELEDAEERLAklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEelEDLRAE-- 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    327 tpfipsLEKLRADFNSAVEKLRAAMQKVAENASAIaagaQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNR 406
Cdd:TIGR02169  373 ------LEEVDKEFAETRDELKDYREKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
                          170
                   ....*....|....*..
gi 86360197    407 AQEAGQLVRKTKDNAER 423
Cdd:TIGR02169  443 KEDKALEIKKQEWKLEQ 459
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
242-444 5.31e-04

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: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 42.10  E-value: 5.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    242 DRRLEARGDEIGKLARAVAGLRDAI--------SAKAEREADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGQLGSAL 313
Cdd:TIGR02680  748 DARLAAVDDELAELARELRALGARQraladelaGAPSDRSLRAAHRRAAEAERQAESAERELARAARKAAAAAAAWKQAR 827
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    314 QALADGdlTQQIGTPFIP-SLEKLRADFNS----------AVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRtEQQ 382
Cdd:TIGR02680  828 RELERD--AADLDLPTDPdALEAVGLALKRfgdhlhtlevAVRELRHAATRAAEQRARAARAESDAREAAEDAAEA-RAE 904
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86360197    383 AASVEETAAALEE-ITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATE 444
Cdd:TIGR02680  905 AEEASLRLRTLEEsVGAMVDEIRARLAETRAALASGGRELPRLAEALATAEEARGRAEEKRAE 967
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
252-590 5.93e-04

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: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 41.72  E-value: 5.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    252 IGKLARAvaglrdaiSAKAEREADAEAkravaerhRLEQDADERRTLAeqtdRAVGQLGSALQALADgdltQQIGTPFIP 331
Cdd:TIGR02680  731 IGAAARE--------RARLRRIAELDA--------RLAAVDDELAELA----RELRALGARQRALAD----ELAGAPSDR 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    332 SLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVeeTAAALEEITTTVADSSNRAQEAG 411
Cdd:TIGR02680  787 SLRAAHRRAAEAERQAESAERELARAARKAAAAAAAWKQARRELERDAADLDLPT--DPDALEAVGLALKRFGDHLHTLE 864
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    412 QLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGSIIGVIDEIafQTNLLALNAGVeAARAGEagkgfavVAQEVRELA 491
Cdd:TIGR02680  865 VAVRELRHAATRAAEQRARAARAESDAREAAEDAAEARAEAEEA--SLRLRTLEESV-GAMVDE-------IRARLAETR 934
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    492 QRSAKAAKEIKELINASNGHVKngvALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKEI---NTAVNRMDQGT 568
Cdd:TIGR02680  935 AALASGGRELPRLAEALATAEE---ARGRAEEKRAEADATLDERAEARDHAIGQLREFALTGLLEDalpDTEVPELDAKW 1011
                          330       340
                   ....*....|....*....|...
gi 86360197    569 QQNAAM-VEEATAAAHKLAKEAD 590
Cdd:TIGR02680 1012 TIEAALkVARRTEAALLQVADDD 1034
Ttg2C COG1463
ABC-type transport system involved in resistance to organic solvents, periplasmic component ...
296-438 6.42e-04

ABC-type transport system involved in resistance to organic solvents, periplasmic component [Secondary metabolites biosynthesis, transport, and catabolism]


Pssm-ID: 224380 [Multi-domain]  Cd Length: 359  Bit Score: 40.91  E-value: 6.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 296 RTLAEQTDRAVGQLGSALQALADGdLTQQIGTpFIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDL 375
Cdd:COG1463 150 LLLGGLDPDRLNAILNEAAAALAG-TGPQLNA-LLDNLAQFTDALNARDGDIGALIANLNQLLDSLAAASDQLDRLLDNL 227
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86360197 376 AKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKI 438
Cdd:COG1463 228 ATLTAALAARRDALDDALAALSALAATVNDLLAENRPNLNQALANLRPLATLLVDYLPGLEQL 290
TIGR02680 TIGR02680
TIGR02680 family protein; Members of this protein family belong to a conserved gene four-gene ...
250-556 6.63e-04

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: 233973 [Multi-domain]  Cd Length: 1353  Bit Score: 41.72  E-value: 6.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    250 DEIGKLARAVAGLRDAISAKAEREADAEAKRAVAERHRLEQdadeRRTLAEQTDRAVGQLGSALQALAD-GDLTQQigtp 328
Cdd:TIGR02680  220 DELTDVADALEQLDEYRDELERLEALERALRNFLQRYRRYA----RTMLRRRATRLRSAQTQYDQLSRDlGRARDE---- 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    329 fipsLEKLRADFNSAVEKLRAAmQKVAENASAIAAGAQEIRSASDdlAKRTEQQAASVEETAAALEEITTTVADSSNRAQ 408
Cdd:TIGR02680  292 ----LETAREEERELDARTEAL-EREADALRTRLEALQGSPAYQD--AEELERARADAEALQAAAADARQAIREAESRLE 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    409 EAGqlvRKTKDNAERSGSVVRDAVDAMGKIESSATEIGsiigvIDEIAFQTNLLALNAGVE------AARAGEAGKGFAV 482
Cdd:TIGR02680  365 EER---RRLDEEAGRLDDAERELRAAREQLARAAERAG-----LSPAHTAEPDAALAAQELqelgalDARRQDADRVIAQ 436
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86360197    483 VAQEVRELAQRSakAAKEIKELINASNGHVKNGVALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKE 556
Cdd:TIGR02680  437 RSEQVALLRRRD--DVADRAEATHAAARARRDELDEEAEQAAARAELADEAVHREGARLAWVDAWQAQLRELTI 508
valS PRK14900
valyl-tRNA synthetase; Provisional
205-432 7.58e-04

valyl-tRNA synthetase; Provisional


Pssm-ID: 237855 [Multi-domain]  Cd Length: 1052  Bit Score: 41.52  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   205 AALLSVLAAVVTARTIVGPLT---KLQLSLNAMAE-GNLDGDRRLEARGDEIGKLARaVAGLRDA-ISAKAEREADAEAK 279
Cdd:PRK14900  743 AAFRPVLGIIDAVRNIRGEMGipwKVKLGAQAPVEiAVADPALRDLLQAGELARVHR-VAGVEGSrLVVAAATAPAPQSA 821
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   280 RAVAERHRLEQDADERRTLAEQTDRAVGQLGSALQALADgdLTQQIGTP-FIPS-----LEKLRAdfnsAVEKLRAAMQK 353
Cdd:PRK14900  822 VGVGPGFEVRVPLAGVIDLAAETARVDKEIGKVDQDLAV--LERKLQNPsFVQNappavVEKDRA----RAEELREKRGK 895
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   354 VaENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSG-SVVRDAV 432
Cdd:PRK14900  896 L-EAHRAMLSGSEANSARRDTMEIQNEQKPTQDGPAAEAQPAQENTVVESAEKAVAAVSEAAQQAATAVASGiEKVAEAV 974
COG5283 COG5283
Phage-related tail protein [Function unknown]
84-597 8.75e-04

Phage-related tail protein [Function unknown]


Pssm-ID: 227608 [Multi-domain]  Cd Length: 1213  Bit Score: 41.07  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   84 AAEALIEKLAASYTENEKRMADMVASPAGATDQERSILKEIADIQAKTNplvaqiialqekgdgeAARKILLEQARpafv 163
Cdd:COG5283   89 ASKKAYQEYNAQYTQAENKLRSLSGQFGVASEQLMLQQKEIQRLQYAIS----------------TLNKSMAAQAR---- 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  164 AWLGAINKFIDYQEALNKSIGGDVRSTASGFKPIVLTALGIAALLSVLAAVVTA--RTIVGPLTKLQLSLNAMAEGNLDG 241
Cdd:COG5283  149 LLEQTGNKFGTADAKVVGLRESFGRQTEALNKQLERTKKVADALTYVLDEAQQKlsQALSARLERLQESRTQMSQSSGQL 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  242 DRRLEARGDEIGKLAR---AVAGLRDAISAKAEREA-DAEAKRAVAERHRLEQDADERRT-----LAEQTDRAVGQLGSA 312
Cdd:COG5283  229 GKRLETDKAGAGALGLlgaALAGSFAAIGAAVRRTAqMNGELMDKTKQVKGARDNLGKVTsqgeeMSDAIQETAEHIKDS 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  313 LQALADGDLTQQIG-------------------TPFIPSLEKLRADFNSAVEKLRAAMQKVAEN----ASAIAAGAQEIR 369
Cdd:COG5283  309 GRELSKAAAIGAAAamgvaagkfptgqeakptlKEMARVAALTATAFNLPADELNDNLAKWAGElkfpASDAISGGSLLA 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  370 SASDDLakrTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAV---DAMGKIESSATEIG 446
Cdd:COG5283  389 MLTDLL---QGKGGDLKKVSDAAGAGAVETLGLSADAAANLATTFGTLGASAERAGDTLTKALlrlLDIVKKNTDGFALG 465
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  447 SIIG-----VIDEIAFQTNLLALNAGVEAARAGEAGKGFAVVAQEV-RELAQRSAKAAKEIKE----LINASNGHVKNGV 516
Cdd:COG5283  466 VTLDyltgaEAQKLMVTFAESAAMLIMLANKGLPVEDSAGTMADAFgKKLGEALKKLADAIAElfqsLADNRGKIANGSM 545
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  517 ALVGET-GKALQEIAVQVQQVDGNVGAIVGASQEQA--TGLKEINTAVNRMDQGTQQNA----AMVEEATAAAHKLAKEA 589
Cdd:COG5283  546 EEELLTlYKATAGIWQIYKSGVTEFSDAKGEQLKVGinDLVAMAGGVIESLGKEVEKLTgllkAAAGEADNLAGKMATVA 625

                 ....*...
gi 86360197  590 DALFQLLG 597
Cdd:COG5283  626 AGALKKAG 633
COG4372 COG4372
Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]
330-629 1.95e-03

Uncharacterized protein conserved in bacteria with the myosin-like domain [Function unknown]


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 39.62  E-value: 1.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 330 IPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQE 409
Cdd:COG4372  73 VFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQTR 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 410 AGQLVRKTKDNAERSGSVVRDAVDAMGKIEssateigsiigvideiafQTNLLALNAGVEAARAgeagkgfavvAQEVRE 489
Cdd:COG4372 153 LKTLAEQRRQLEAQAQSLQASQKQLQASAT------------------QLKSQVLDLKLRSAQI----------EQEAQN 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 490 LAQRSAKAAKEIKELINASnghvkngvALVGETGKALQEIAVQVQQVDGNVGAIVGASQEQATGLKEINTAVNRMdqgtQ 569
Cdd:COG4372 205 LATRANAAQARTEELARRA--------AAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARL----E 272
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 570 QNAAMVEEATAAAHKLAKEADALfqLLGQFNIGGAaasRRISQPAAAAQHAQPVPSPARQ 629
Cdd:COG4372 273 QEVAQLEAYYQAYVRLRQQAAAT--QRGQVLAGAA---QRVAQAQAQAQAQAQLLSSANR 327
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
197-288 2.55e-03

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 39.33  E-value: 2.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197 197 IVLTALGIAALLSVLAAVVTARTIVGPLTKLQLSLNAMAEGNLdgDRRLEARG-DEIGKLAravaglrDAISAKAEREAD 275
Cdd:COG5002  31 ILISGTLIALIITALLGILLARTITKPITDMRKQAVDMARGNY--SRKVKVYGtDEIGELA-------DSFNDLTKRVQE 101
                        90
                ....*....|...
gi 86360197 276 AEAKRAvAERHRL 288
Cdd:COG5002 102 AQANTE-QERRKL 113
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
274-423 2.90e-03

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


Pssm-ID: 249510 [Multi-domain]  Cd Length: 213  Bit Score: 38.19  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   274 ADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGQLGSALQAladgdlTQQIGTPFIPSLEKLRADFNSAVEKLRAAmqk 353
Cdd:pfam00015  63 AAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIEE------IVKQTNDSTASIQQTRTEVEVGSTIVEST--- 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   354 vAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVRKTKDNAER 423
Cdd:pfam00015 134 -GEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVARIDQVTQQNAALVEESAAAAETLEEQAEE 202
EspB pfam05802
Enterobacterial EspB protein; EspB is a type-III-secreted pore-forming protein of ...
338-472 3.54e-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: 114524 [Multi-domain]  Cd Length: 317  Bit Score: 38.51  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   338 ADFNSAVEKLRAAMQKVAENASAIAAGAQEIrsASDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEAGQLVrkt 417
Cdd:pfam05802 117 AAINSATKGASDIAQKATSASSKAVNAASEV--ATKALVKATESVADAAEEASSTMQQAMATATKAASRTSGVADDV--- 191
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 86360197   418 KDNAERSGSVVRDAVDAMGKiessATEIGSIIGVIDEIAFQTNLLALNAGVEAAR 472
Cdd:pfam05802 192 ATSAQKASQVAEEAADAAQK----ASRLSRFTAAVDKITGSTAFVAVTSLAEGTK 242
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
197-295 3.73e-03

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


Pssm-ID: 234070 [Multi-domain]  Cd Length: 968  Bit Score: 38.99  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   197 IVLTALGIAALLSVLAAVVTaRTIVGPLTKLQLSLNAMAEGNLDGDrrLEARGD-EIGKLARAVAGLRDAISAKAEREAD 275
Cdd:TIGR02956 334 LITGMLGLVILVFIMWRVVY-RSVILRLNQHTQALLRLALGDLDIS--LDARGDdELAHMGRAIEAFRDTAAHNLKLQAD 410
                          90       100
                  ....*....|....*....|..
gi 86360197   276 AEAKRAVAERHR--LEQDADER 295
Cdd:TIGR02956 411 ERQVAQELQEHKesLEQLVAQR 432
DUF390 pfam04094
Protein of unknown function (DUF390); This is a family of long proteins currently only found ...
246-586 5.45e-03

Protein of unknown function (DUF390); This is a family of long proteins currently only found in the rice genome. They have no known function. However they may be some kind of transposable element.


Pssm-ID: 112890 [Multi-domain]  Cd Length: 843  Bit Score: 38.64  E-value: 5.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   246 EARGDEIGKLARAVAGLRDAISAKAEREADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGQ--LGSALQALADGDLTQ 323
Cdd:pfam04094 267 EAAREEAARARQAEEAAREAEAAFRADEAAATSEAARDEAAGAQLAPDPSGDAAATTSEAAGDeaAGALLGPDPSGDAQD 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   324 QIGTPFIPsleklradfnsaveklraamqkvaENASAIaAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVADS 403
Cdd:pfam04094 347 EPAPGGAP------------------------DSGTSI-GGPSRAAPSPRRLFPLPSAAPLNAEPLLQALAAANTTVLDG 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   404 SNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIESSATEIGsiigvIDEIAFQTNLLAlnagvEAARAGEAGKGFAVV 483
Cdd:pfam04094 402 LSAQMEALQAERAELDAAWARVEEGRRSVEAMVEAGRKAHRRH-----TSELEARKKDLA-----EIAKEVEEEREAALI 471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197   484 AQEVRELAQRSAKA-----AKEIKELINASNGHVKNGVALvgETGKALQEIAVQVQQVdgnvgaivgASQEQATGLKEIN 558
Cdd:pfam04094 472 ATTVLNEAQDDLRLqygsrAAELEKKLDAAQGVLDAAAAR--EQRAAENEAASRQREE---------ALEARAMALEERA 540
                         330       340
                  ....*....|....*....|....*...
gi 86360197   559 TAVNRmDQGTQQNAAMVEEATAAAHKLA 586
Cdd:pfam04094 541 CAKER-DLADREAAVAIREATLAAHEAA 567
PHA00430 PHA00430
tail fiber protein
238-440 6.29e-03

tail fiber protein


Pssm-ID: 222790 [Multi-domain]  Cd Length: 568  Bit Score: 38.33  E-value: 6.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  238 NLDGDrrLEARGDEIGKLARAVAGlRDAISAKAEREADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGqlGSALQALA 317
Cdd:PHA00430 124 NNDGH--LDARGRRIVNLADAVDD-GDAVPLGQIKTWNQSAWNARNEANRSRNEADRARNQAERFNNESG--ASATNTKQ 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  318 DGDLTqqigtpfipsleklrADFNSAVEklRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEit 397
Cdd:PHA00430 199 WRSEA---------------DGSNSEAN--RFKGYADSMTSSVEAAKGQAESSSKEANTAGDYATKAAASASAAHASE-- 259
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 86360197  398 TTVADSSNRAQEAGQLVRKTKDNAERSGSVVRDAVDAMGKIES 440
Cdd:PHA00430 260 VNAANSATAAATSANRAKQQADRAKTEADKLGNMNGFAGAIEK 302
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
342-402 9.12e-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 [Multi-domain]  Cd Length: 262  Bit Score: 36.88  E-value: 9.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86360197    342 SAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQAASVEETAAALEEITTTVAD 402
Cdd:smart00283 193 DSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAAAEELSGLAEE 253
Smc COG1196
Chromosome segregation ATPases [Cell division and chromosome partitioning]
243-504 9.15e-03

Chromosome segregation ATPases [Cell division and chromosome partitioning]


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 37.77  E-value: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  243 RRLEARGDEIGKLARAVAGLRDAIsakaeREADAEAKRAVAERHRLEQDADERRTLAEQTDRAVGQLGSALQALadgdlt 322
Cdd:COG1196  660 RSSLAQKRELKELEEELAELEAQL-----EKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAAL------ 728
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  323 qqigtpfIPSLEKLRADFNSAVEKLRAAMQKVAENASAIAAGAQEIRSASDDLAKRTEQQaasvEETAAALEEITTTVAD 402
Cdd:COG1196  729 -------EEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEI----EELEEKRQALQEELEE 797
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197  403 SSNRAQEAGQLVRKTKDNAErsgSVVRDAVDAMGKIESSATEIGSIIGVIDEIafQTNLLALNAGVEAARAGEAGKgfav 482
Cdd:COG1196  798 LEEELEEAERRLDALERELE---SLEQRRERLEQEIEELEEEIEELEEKLDEL--EEELEELEKELEELKEELEEL---- 868
                        250       260
                 ....*....|....*....|..
gi 86360197  483 vAQEVRELAQRSAKAAKEIKEL 504
Cdd:COG1196  869 -EAEKEELEDELKELEEEKEEL 889
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
292-410 9.79e-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 [Multi-domain]  Cd Length: 262  Bit Score: 36.88  E-value: 9.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86360197    292 ADERRTLAEQTDRAVGQLGSALQALadgdltQQIGTPFIPSLEKLRadfnSAVEKLRAAMQKVAENASAIAAGAQEIRSA 371
Cdd:smart00283 132 ADEVRKLAERSAESAKEIESLIKEI------QEETNEAVAAMEESS----SEVEEGVELVEETGDALEEIVDSVEEIADL 201
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 86360197    372 SDDLAKRTEQQAASVEETAAALEEITTTVADSSNRAQEA 410
Cdd:smart00283 202 VQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
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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