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Conserved domains on  [gi|46581485|ref|YP_012293|]
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methyl-accepting chemotaxis protein [Desulfovibrio vulgaris str. Hildenborough]

Protein Classification

DUF3365 and MCP_signal domain-containing protein (domain architecture ID 12112053)

protein containing domains DUF3365, HAMP, and MCP_signal

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
321-581 1.19e-69

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


:

Pssm-ID: 214599  Cd Length: 262  Bit Score: 228.71  E-value: 1.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    321 ALAAQVDQVSAGAEQQSARTAETATAMEEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQ 400
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    401 GAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGA 480
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    481 RGNMQGMEKAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQA 560
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 46581485    561 ASAVTRLAQLARELEGLIEKL 581
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
DUF3365 pfam11845
Protein of unknown function (DUF3365); This family of proteins are functionally ...
4-174 9.39e-40

Protein of unknown function (DUF3365); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 198 to 657 amino acids in length.


:

Pssm-ID: 314675  Cd Length: 186  Bit Score: 144.44  E-value: 9.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485     4 LVVAAIMAWQRVGDIREGADEAILEKSRAIVLMAEATRNEMARKLEIGLMKPFDQLPPDKVLDAVPVVTAMRMAGQNAKE 83
Cdd:pfam11845   3 LLLLGLLLAGSLLSQRQQAEEEALEKARLLLEQLEAVRDYVAKNLRPLLYPLLAHEDGFIPEIPSPAYAAREIGEVFSEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    84 A-GYEFRVPKVRPRNPANTPTELELKVLKQL-----EEKNLPELVIYEKDKIRYFRPIRLTSECLYCHGDP--AGERDVM 155
Cdd:pfam11845  83 RpGYTYRRVSLNPRNPRNEPDEFEREALERFrnnpeLKEPSGEREIDGKRYFRYARPIRIEESCLACHGTPedAPKSLIE 162
                         170       180
                  ....*....|....*....|..
gi 46581485   156 G-GTKE--GWKVGEMHGAFEVI 174
Cdd:pfam11845 163 RyGDKDgfGWKVGDVRGAISIS 184
HAMP pfam00672
HAMP domain;
191-260 6.15e-04

HAMP domain;


:

Pssm-ID: 307012  Cd Length: 69  Bit Score: 39.48  E-value: 6.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   191 VAGWTAGILAVLGVVAWTLLRTgIITPLERIRGFASTVASGKLDArPEGEFYAELGEVKGAIETMVDNLK 260
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARR-ILRPLRRLAEAARRIASGDLDV-PLESGRDEIGELARAFNQMAERLR 68
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
321-581 1.19e-69

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599  Cd Length: 262  Bit Score: 228.71  E-value: 1.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    321 ALAAQVDQVSAGAEQQSARTAETATAMEEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQ 400
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    401 GAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGA 480
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    481 RGNMQGMEKAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQA 560
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 46581485    561 ASAVTRLAQLARELEGLIEKL 581
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
195-583 1.53e-60

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 209.08  E-value: 1.53e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 195 TAGILAVLGVVAWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLkvkmgeaeshgreaa 274
Cdd:COG0840  65 SLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNL--------------- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 275 aearraeealavarqqeervssllgqmQQVAKQAVGIAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATAMEEMNATV 354
Cdd:COG0840 130 ---------------------------RQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETV 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 355 LEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVhtqAQELQGAMSTLGRQTEDISRIMDVISDIADQTNLLALNA 434
Cdd:COG0840 183 KEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEI---AEELAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNA 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 435 AIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEALKRIVSL 514
Cdd:COG0840 260 AIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAA 339
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46581485 515 SEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLARELEGLIEKLEV 583
Cdd:COG0840 340 IEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
348-547 4.56e-51

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: 176.66  E-value: 4.56e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 348 EEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDVISDIADQT 427
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 428 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEA 507
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46581485 508 LKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVS 547
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
384-580 1.71e-47

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


Pssm-ID: 278444  Cd Length: 207  Bit Score: 166.85  E-value: 1.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   384 EAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTM 463
Cdd:pfam00015  10 EALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   464 TATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAV 543
Cdd:pfam00015  90 QAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAV 169
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 46581485   544 EDVSRIASETADGMTQAASAVTRLAQLARELEGLIEK 580
Cdd:pfam00015 170 ARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQ 206
DUF3365 pfam11845
Protein of unknown function (DUF3365); This family of proteins are functionally ...
4-174 9.39e-40

Protein of unknown function (DUF3365); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 198 to 657 amino acids in length.


Pssm-ID: 314675  Cd Length: 186  Bit Score: 144.44  E-value: 9.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485     4 LVVAAIMAWQRVGDIREGADEAILEKSRAIVLMAEATRNEMARKLEIGLMKPFDQLPPDKVLDAVPVVTAMRMAGQNAKE 83
Cdd:pfam11845   3 LLLLGLLLAGSLLSQRQQAEEEALEKARLLLEQLEAVRDYVAKNLRPLLYPLLAHEDGFIPEIPSPAYAAREIGEVFSEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    84 A-GYEFRVPKVRPRNPANTPTELELKVLKQL-----EEKNLPELVIYEKDKIRYFRPIRLTSECLYCHGDP--AGERDVM 155
Cdd:pfam11845  83 RpGYTYRRVSLNPRNPRNEPDEFEREALERFrnnpeLKEPSGEREIDGKRYFRYARPIRIEESCLACHGTPedAPKSLIE 162
                         170       180
                  ....*....|....*....|..
gi 46581485   156 G-GTKE--GWKVGEMHGAFEVI 174
Cdd:pfam11845 163 RyGDKDgfGWKVGDVRGAISIS 184
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
198-574 8.00e-33

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 132.39  E-value: 8.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  198 ILAVLGVV--AWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLKVKMGEAESHgreaaa 275
Cdd:PRK15041 200 MIVVLAVIfaVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNG------ 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  276 earraeealavarqqeervssllgqmqqvakqavgiAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATAMEEMNATVL 355
Cdd:PRK15041 274 ------------------------------------ANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVK 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  356 EVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQElqgamstlgrqtedISRIMDVISDIADQTNLLALNAA 435
Cdd:PRK15041 318 QNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQK--------------IADIISVIDGIAFQTNILALNAA 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  436 IEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIqtiqtgargnmqgmEKAALAVERATTLAHESGEALKRIVSLS 515
Cdd:PRK15041 384 VEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLI--------------EDSVGKVDVGSTLVESAGETMAEIVSAV 449
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 46581485  516 EENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLAREL 574
Cdd:PRK15041 450 TRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRL 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
285-581 1.14e-04

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: 274008  Cd Length: 1179  Bit Score: 45.05  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    285 AVARQQEERVSSLLGQMQQVAKqavgIAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATA---MEEMNATVLEVARSS 361
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEE----LEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    362 SSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDvisdiADQTNLLALNAAIEAARA 441
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-----QLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    442 --GEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIqtgaRGNMQGMEKAALAVERATTLAHESGEALKrivSLSEENS 519
Cdd:TIGR02168  811 elTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----EELSEDIESLAAEIEELEELIEELESELE---ALLNERA 883
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46581485    520 DQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLARELEGLIEKL 581
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
HAMP pfam00672
HAMP domain;
191-260 6.15e-04

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 39.48  E-value: 6.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   191 VAGWTAGILAVLGVVAWTLLRTgIITPLERIRGFASTVASGKLDArPEGEFYAELGEVKGAIETMVDNLK 260
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARR-ILRPLRRLAEAARRIASGDLDV-PLESGRDEIGELARAFNQMAERLR 68
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
187-267 1.83e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 38.13  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 187 AQVSVAGWTAGILAVLGVVAWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLKVKMGEA 266
Cdd:COG2770   3 STAPIFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALSAL 82

                .
gi 46581485 267 E 267
Cdd:COG2770  83 E 83
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
214-260 9.72e-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: 35.69  E-value: 9.72e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 46581485 214 IITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLK 260
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
 
Name Accession Description Interval E-value
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
321-581 1.19e-69

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599  Cd Length: 262  Bit Score: 228.71  E-value: 1.19e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    321 ALAAQVDQVSAGAEQQSARTAETATAMEEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQ 400
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    401 GAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGA 480
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    481 RGNMQGMEKAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQA 560
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250       260
                   ....*....|....*....|.
gi 46581485    561 ASAVTRLAQLARELEGLIEKL 581
Cdd:smart00283 241 SAAAEELSGLAEELDELVERF 261
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
195-583 1.53e-60

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


Pssm-ID: 223910  Cd Length: 408  Bit Score: 209.08  E-value: 1.53e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 195 TAGILAVLGVVAWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLkvkmgeaeshgreaa 274
Cdd:COG0840  65 SLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRIDESSNDEFGQLAKSFNEMILNL--------------- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 275 aearraeealavarqqeervssllgqmQQVAKQAVGIAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATAMEEMNATV 354
Cdd:COG0840 130 ---------------------------RQIIDAVQDNAEALSGASEEIAASATELSARADQQAESLEEVASAIEELSETV 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 355 LEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVhtqAQELQGAMSTLGRQTEDISRIMDVISDIADQTNLLALNA 434
Cdd:COG0840 183 KEVAFNAKEAAALASEASQVAEEGGEEVRQAVEQMQEI---AEELAEVVKKLSESSQEIEEITSVINSIAEQTNLLALNA 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 435 AIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEALKRIVSL 514
Cdd:COG0840 260 AIEAARAGEAGRGFAVVADEVRKLAERSADSAKEIGLLIEEIQNEAADAVEHMEESASEVSEGVKLVEETGSSLGEIAAA 339
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46581485 515 SEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLARELEGLIEKLEV 583
Cdd:COG0840 340 IEEVSQLISEIAAATEEQTAVLEEINASIEELDDVTQENAAAVEELAAASEELKELAEKLLELVAKFKL 408
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
348-547 4.56e-51

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: 176.66  E-value: 4.56e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 348 EEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDVISDIADQT 427
Cdd:cd11386   1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 428 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEA 507
Cdd:cd11386  81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 46581485 508 LKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVS 547
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
384-580 1.71e-47

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


Pssm-ID: 278444  Cd Length: 207  Bit Score: 166.85  E-value: 1.71e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   384 EAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTM 463
Cdd:pfam00015  10 EALDEMSQIGQVVDDAVETMEELETSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   464 TATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAV 543
Cdd:pfam00015  90 QAAKEIEALIEEIVKQTNDSTASIQQTRTEVEVGSTIVESTGEALKEIVEAVAEIADIVQEIAAASDEQSAGIDQVNQAV 169
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 46581485   544 EDVSRIASETADGMTQAASAVTRLAQLARELEGLIEK 580
Cdd:pfam00015 170 ARIDQVTQQNAALVEESAAAAETLEEQAEELTASVAQ 206
DUF3365 pfam11845
Protein of unknown function (DUF3365); This family of proteins are functionally ...
4-174 9.39e-40

Protein of unknown function (DUF3365); This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 198 to 657 amino acids in length.


Pssm-ID: 314675  Cd Length: 186  Bit Score: 144.44  E-value: 9.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485     4 LVVAAIMAWQRVGDIREGADEAILEKSRAIVLMAEATRNEMARKLEIGLMKPFDQLPPDKVLDAVPVVTAMRMAGQNAKE 83
Cdd:pfam11845   3 LLLLGLLLAGSLLSQRQQAEEEALEKARLLLEQLEAVRDYVAKNLRPLLYPLLAHEDGFIPEIPSPAYAAREIGEVFSEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    84 A-GYEFRVPKVRPRNPANTPTELELKVLKQL-----EEKNLPELVIYEKDKIRYFRPIRLTSECLYCHGDP--AGERDVM 155
Cdd:pfam11845  83 RpGYTYRRVSLNPRNPRNEPDEFEREALERFrnnpeLKEPSGEREIDGKRYFRYARPIRIEESCLACHGTPedAPKSLIE 162
                         170       180
                  ....*....|....*....|..
gi 46581485   156 G-GTKE--GWKVGEMHGAFEVI 174
Cdd:pfam11845 163 RyGDKDgfGWKVGDVRGAISIS 184
PRK15041 PRK15041
methyl-accepting chemotaxis protein I; Provisional
198-574 8.00e-33

methyl-accepting chemotaxis protein I; Provisional


Pssm-ID: 185001  Cd Length: 554  Bit Score: 132.39  E-value: 8.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  198 ILAVLGVV--AWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLKVKMGEAESHgreaaa 275
Cdd:PRK15041 200 MIVVLAVIfaVWFGIKASLVAPMNRLIDSIRHIAGGDLVKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNG------ 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  276 earraeealavarqqeervssllgqmqqvakqavgiAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATAMEEMNATVL 355
Cdd:PRK15041 274 ------------------------------------ANAIYSGASEIATGNNDLSSRTEQQAASLEETAASMEQLTATVK 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  356 EVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQElqgamstlgrqtedISRIMDVISDIADQTNLLALNAA 435
Cdd:PRK15041 318 QNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQK--------------IADIISVIDGIAFQTNILALNAA 383
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  436 IEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIqtiqtgargnmqgmEKAALAVERATTLAHESGEALKRIVSLS 515
Cdd:PRK15041 384 VEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLI--------------EDSVGKVDVGSTLVESAGETMAEIVSAV 449
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 46581485  516 EENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLAREL 574
Cdd:PRK15041 450 TRVTDIMGEIASASDEQSRGIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRL 508
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
192-587 2.43e-31

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008  Cd Length: 553  Bit Score: 128.20  E-value: 2.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  192 AGWTAGILAV----LGVVAWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDnlkvkmgeae 267
Cdd:PRK15048 190 AQWQLAVIALvvvlILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQR---------- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  268 shgreaaaearraeealavarqqeervsSLLGQMQQVAKQAVGIAQQVSmaaeALAAQVDQVSAGAEQQSARTAETATAM 347
Cdd:PRK15048 260 ----------------------------SLTDTVTHVREGSDAIYAGTR----EIAAGNTDLSSRTEQQASALEETAASM 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  348 EEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQElqgamstlgrqtedISRIMDVISDIADQT 427
Cdd:PRK15048 308 EQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKK--------------IADIISVIDGIAFQT 373
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  428 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSAIqtiqtgargnmqgmEKAALAVERATTLAHESGEA 507
Cdd:PRK15048 374 NILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALI--------------EDSVSRVDTGSVLVESAGET 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  508 LKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLARELEGLIEKLEVAGRA 587
Cdd:PRK15048 440 MNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASP 519
PRK09793 PRK09793
methyl-accepting protein IV; Provisional
298-578 2.83e-31

methyl-accepting protein IV; Provisional


Pssm-ID: 182079  Cd Length: 533  Bit Score: 127.50  E-value: 2.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  298 LGQMQQVAKQAVGIAQQVSMAAEA----LAAQVDQVSAGAEQQSARTAETATAMEEMNATVlevarsssssatsaDQARN 373
Cdd:PRK09793 252 LKTMQQALRGTVSDVRKGSQEMHIgiaeIVAGNNDLSSRTEQQAASLAQTAASMEQLTATV--------------GQNAD 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  374 QALQGEKVVTEAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVAD 453
Cdd:PRK09793 318 NARQASELAKNAATTAQAGGVQVSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAG 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485  454 EVRKLAEKTMTATKEVGSAIqtiqtgargnmqgmEKAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQS 533
Cdd:PRK09793 398 EVRNLASRSAQAAKEIKGLI--------------EESVNRVQQGSKLVNNAAATMTDIVSSVTRVNDIMGEIASASEEQR 463
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 46581485  534 ATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLARELEGLI 578
Cdd:PRK09793 464 RGIEQVAQAVSQMDQVTQQNASLVEEAAVATEQLANQADHLSSRV 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
285-581 1.14e-04

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: 274008  Cd Length: 1179  Bit Score: 45.05  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    285 AVARQQEERVSSLLGQMQQVAKqavgIAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATA---MEEMNATVLEVARSS 361
Cdd:TIGR02168  660 VITGGSAKTNSSILERRREIEE----LEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    362 SSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDvisdiADQTNLLALNAAIEAARA 441
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE-----QLKEELKALREALDELRA 810
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    442 --GEAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIqtgaRGNMQGMEKAALAVERATTLAHESGEALKrivSLSEENS 519
Cdd:TIGR02168  811 elTLLNEEAANLRERLESLERRIAATERRLEDLEEQI----EELSEDIESLAAEIEELEELIEELESELE---ALLNERA 883
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46581485    520 DQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGMTQAASAVTRLAQLARELEGLIEKL 581
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
329-582 3.33e-04

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: 274008  Cd Length: 1179  Bit Score: 43.51  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    329 VSAGAEQQSARTAETATAMEEMNATVLEVARSSSSSATSADQARNQALQGEKVVTEAVNAI----REVHTQAQELQGAMS 404
Cdd:TIGR02168  661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeelsRQISALRKDLARLEA 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    405 TLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAEKTMTATKEVGSA---IQTIQTGAR 481
Cdd:TIGR02168  741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELraeLTLLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    482 GNMQGME----KAALAVERATTLAHESGEALKRIVSLSEENSDQVRSIATAAEQQSATSEEINRAVEDVSRIASETADGM 557
Cdd:TIGR02168  821 NLRERLEslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
                          250       260
                   ....*....|....*....|....*
gi 46581485    558 TQAASAVTRLAQLARELEGLIEKLE 582
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLA 925
HAMP pfam00672
HAMP domain;
191-260 6.15e-04

HAMP domain;


Pssm-ID: 307012  Cd Length: 69  Bit Score: 39.48  E-value: 6.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485   191 VAGWTAGILAVLGVVAWTLLRTgIITPLERIRGFASTVASGKLDArPEGEFYAELGEVKGAIETMVDNLK 260
Cdd:pfam00672   1 LLLVLLIALLLALLLAWLLARR-ILRPLRRLAEAARRIASGDLDV-PLESGRDEIGELARAFNQMAERLR 68
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
295-579 7.01e-04

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 224428  Cd Length: 780  Bit Score: 42.49  E-value: 7.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 295 SSLLGQMQQVAKQAVGIAQQVSMAAEALAAQVDQVSAGAEQQSARTAETATAMEEMNATVLEVARSSSSSATSADQArNQ 374
Cdd:COG1511 219 SDGLNALTSGLTTLTDGLNQLDSGLGTLAAGIGELKQGAEQLNEGIGEFSSGLSELNSGVQDLAAGVPQLNQGISAL-AA 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 375 ALQGEKVVTEAVNAIREVHTQ-AQELQGAMSTLGRQTEDISRIMDVISDIADQTNLLALNAAIEAARAGEAGRGFAVVAD 453
Cdd:COG1511 298 GLSLPDSLGDQFSSLQEALTQiAQGLKQKTSSSLEAAQGSLSSLQSMLALSKSLDLTAEGATVDALGAPDGVQWLDESQK 377
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 454 EVRKLAEKTMTATKevgsAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEALKRIVS-----LSEENSDQV-----R 523
Cdd:COG1511 378 TLATLSELLSTGID----GVSEGLDALEQASAQLAKSLAKLKTAVAQIAASIAQLLPGASevlktLKSKGLDKLlnqlnG 453
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 46581485 524 SIATAAEQQSATSEEINRAVEDVSRIASETadGMTQAASAVTRLAQLARELEGLIE 579
Cdd:COG1511 454 ALAKGSNALVQGLSDANDSFRSITSAQLKA--GLNTLADGSNDLSSLGPGLGQLAD 507
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
284-549 1.70e-03

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: 274008  Cd Length: 1179  Bit Score: 41.20  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    284 LAVARQQ----EERVSSLLGQMQQVAKQAVGIAQQVSMA---AEALAAQVDQVSAGAEQQSARTAETATAMEEMNATVLE 356
Cdd:TIGR02168  700 LAELRKEleelEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    357 VARSSSSSATSADQARNQALQGEKVVTEAVNAIREVHTQAQELQGAMSTLGRQTEDISRIMDVISDIADQTN--LLALNA 434
Cdd:TIGR02168  780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedIESLAA 859
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485    435 AIEAARAG--EAGRGFAVVADEVRKLAEKTMTATKEVGSAIQTIQTGARGNMQGMEKAALAVERATTLAHESGEALKRIV 512
Cdd:TIGR02168  860 EIEELEELieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 46581485    513 SLSEE-NSDQVRSIATAAEQQSATSEEINRAVEDVSRI 549
Cdd:TIGR02168  940 NLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKRL 977
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
187-267 1.83e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 38.13  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46581485 187 AQVSVAGWTAGILAVLGVVAWTLLRTGIITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLKVKMGEA 266
Cdd:COG2770   3 STAPIFGLLVLALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALSAL 82

                .
gi 46581485 267 E 267
Cdd:COG2770  83 E 83
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
214-260 9.72e-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: 35.69  E-value: 9.72e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 46581485 214 IITPLERIRGFASTVASGKLDARPEGEFYAELGEVKGAIETMVDNLK 260
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERLR 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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