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Conserved domains on  [gi|2502261906|ref|WP_281664874|]
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methyl-accepting chemotaxis protein [Paraburkholderia fungorum]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 11435591)

methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

CATH:  1.10.287.950
Gene Ontology:  GO:0006935
PubMed:  18165013|20738376
SCOP:  4003862

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
13-290 1.69e-35

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


:

Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 138.23  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  13 QTVVGDIAAQAGKLGIEICDVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQT 92
Cdd:COG0840   252 RELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEV 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  93 LEASLADIHGLVEGVTVIESQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAK 172
Cdd:COG0840   332 VEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAER 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 173 TAQATGQIETTLAQLTQQTEQLISEGSMNTARAHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEA 252
Cdd:COG0840   412 SAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQ 491
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2502261906 253 QVLEMASGVEDSSENFVQAKDRLGNLLGVSETLIELTA 290
Cdd:COG0840   492 AIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
13-290 1.69e-35

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 138.23  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  13 QTVVGDIAAQAGKLGIEICDVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQT 92
Cdd:COG0840   252 RELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEV 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  93 LEASLADIHGLVEGVTVIESQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAK 172
Cdd:COG0840   332 VEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAER 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 173 TAQATGQIETTLAQLTQQTEQLISEGSMNTARAHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEA 252
Cdd:COG0840   412 SAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQ 491
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2502261906 253 QVLEMASGVEDSSENFVQAKDRLGNLLGVSETLIELTA 290
Cdd:COG0840   492 AIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
32-290 4.93e-32

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: 123.16  E-value: 4.93e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906   32 DVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQTLEASLADIHGLVEGVTVIE 111
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  112 SQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETTLAQLTQQT 191
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  192 EQLISEGSMNTARAHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLEMASGVEDSSENFVQA 271
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250
                   ....*....|....*....
gi 2502261906  272 KDRLGNLLGVSETLIELTA 290
Cdd:smart00283 241 SAAAEELSGLAEELDELVE 259
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
68-265 9.29e-30

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 [Multi-domain]  Cd Length: 200  Bit Score: 115.03  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  68 IATAARAMRSVSAGAATGVQESQQTLEASLADIHGLVEGVTVIESQIGALRSALAHVSRVSEEISLIARQTHLLALNAAI 147
Cdd:cd11386    10 VAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 148 EAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETTLAQLTQQTEQliSEGSMntaraHRVREGTRKIGDVVHATGDAIT 227
Cdd:cd11386    90 EAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEE--AVEAM-----EETSEEVEEGVELVEETGRAFE 162
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2502261906 228 QLNDEAGQIAALTGEIETQCNGLEAQVLEMASGVEDSS 265
Cdd:cd11386   163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
112-262 2.44e-22

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: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 93.65  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 112 SQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETTLAQLTQQT 191
Cdd:pfam00015  23 GQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQT 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502261906 192 EQliSEGSMNTARAhRVREGTRKIGDvvhaTGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLEMASGVE 262
Cdd:pfam00015 103 ND--STASIESTRQ-RVEVGSTIVES----TGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVA 166
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
39-257 3.05e-16

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 81.21  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  39 EVAARVQHQAQvcrALRESAAqtlagnhriaTAARAMRSVSAGAATGVQESQQTLEASLADIHG--LVEGVTVIESQIGA 116
Cdd:PRK15048  288 DLSSRTEQQAS---ALEETAA----------SMEQLTATVKQNADNARQASQLAQSASDTAQHGgkVVDGVVKTMHEIAD 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 117 LRSALAHVSRVseeISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETtlaqLTQQTEQLIS 196
Cdd:PRK15048  355 SSKKIADIISV---IDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKA----LIEDSVSRVD 427
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502261906 197 EGSMNTARAhrvregtrkiGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLEM 257
Cdd:PRK15048  428 TGSVLVESA----------GETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEM 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-256 1.26e-05

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 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906   21 AQAGKLGIEICDVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQTLEASLADI 100
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  101 hglvegvtviESQIGALRSALahvSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQI 180
Cdd:TIGR02168  795 ----------KEELKALREAL---DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  181 ETTLAQLTQQTEQLISE----GSMNTARaHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLE 256
Cdd:TIGR02168  862 EELEELIEELESELEALlnerASLEEAL-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
 
Name Accession Description Interval E-value
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
13-290 1.69e-35

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 138.23  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  13 QTVVGDIAAQAGKLGIEICDVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQT 92
Cdd:COG0840   252 RELVGQVRESAEQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASELAEEGGEV 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  93 LEASLADIHGLVEGVTVIESQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAK 172
Cdd:COG0840   332 VEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAER 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 173 TAQATGQIETTLAQLTQQTEQLISEGSMNTARAHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEA 252
Cdd:COG0840   412 SAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASEEQSAGTEEVNQ 491
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2502261906 253 QVLEMASGVEDSSENFVQAKDRLGNLLGVSETLIELTA 290
Cdd:COG0840   492 AIEQIAAAAQENAASVEEVAAAAEELAELAEELQELVS 529
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
32-290 4.93e-32

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: 123.16  E-value: 4.93e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906   32 DVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQTLEASLADIHGLVEGVTVIE 111
Cdd:smart00283   1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  112 SQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETTLAQLTQQT 191
Cdd:smart00283  81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  192 EQLISEGSMNTARAHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLEMASGVEDSSENFVQA 271
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQETAAMSEEI 240
                          250
                   ....*....|....*....
gi 2502261906  272 KDRLGNLLGVSETLIELTA 290
Cdd:smart00283 241 SAAAEELSGLAEELDELVE 259
MCP_signal cd11386
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ...
68-265 9.29e-30

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 [Multi-domain]  Cd Length: 200  Bit Score: 115.03  E-value: 9.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  68 IATAARAMRSVSAGAATGVQESQQTLEASLADIHGLVEGVTVIESQIGALRSALAHVSRVSEEISLIARQTHLLALNAAI 147
Cdd:cd11386    10 VAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQTNLLALNAAI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 148 EAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETTLAQLTQQTEQliSEGSMntaraHRVREGTRKIGDVVHATGDAIT 227
Cdd:cd11386    90 EAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEE--AVEAM-----EETSEEVEEGVELVEETGRAFE 162
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2502261906 228 QLNDEAGQIAALTGEIETQCNGLEAQVLEMASGVEDSS 265
Cdd:cd11386   163 EIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEIA 200
MCPsignal pfam00015
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ...
112-262 2.44e-22

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: 333767 [Multi-domain]  Cd Length: 172  Bit Score: 93.65  E-value: 2.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 112 SQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETTLAQLTQQT 191
Cdd:pfam00015  23 GQMEQIAQSSKKISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVVADEVRKLAERSAQAAKEIEALIIEIQKQT 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502261906 192 EQliSEGSMNTARAhRVREGTRKIGDvvhaTGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLEMASGVE 262
Cdd:pfam00015 103 ND--STASIESTRQ-RVEVGSTIVES----TGEALKEIVDAVAEIADIVQEIAAASDEQSAGIDQVNQAVA 166
PRK15048 PRK15048
methyl-accepting chemotaxis protein II; Provisional
39-257 3.05e-16

methyl-accepting chemotaxis protein II; Provisional


Pssm-ID: 185008 [Multi-domain]  Cd Length: 553  Bit Score: 81.21  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  39 EVAARVQHQAQvcrALRESAAqtlagnhriaTAARAMRSVSAGAATGVQESQQTLEASLADIHG--LVEGVTVIESQIGA 116
Cdd:PRK15048  288 DLSSRTEQQAS---ALEETAA----------SMEQLTATVKQNADNARQASQLAQSASDTAQHGgkVVDGVVKTMHEIAD 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 117 LRSALAHVSRVseeISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQIETtlaqLTQQTEQLIS 196
Cdd:PRK15048  355 SSKKIADIISV---IDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKA----LIEDSVSRVD 427
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502261906 197 EGSMNTARAhrvregtrkiGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLEM 257
Cdd:PRK15048  428 TGSVLVESA----------GETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEM 478
PRK09793 PRK09793
methyl-accepting chemotaxis protein IV;
16-277 2.97e-14

methyl-accepting chemotaxis protein IV;


Pssm-ID: 182079 [Multi-domain]  Cd Length: 533  Bit Score: 74.72  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  16 VGDIAAQAGKLGIEICDVSGHVEEVAARVQHQAQvcralreSAAQTLAGNHRIATaaramrSVSAGAATGVQESQQTLEA 95
Cdd:PRK09793  263 VSDVRKGSQEMHIGIAEIVAGNNDLSSRTEQQAA-------SLAQTAASMEQLTA------TVGQNADNARQASELAKNA 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  96 SLADIHGLVEgVTVIESQIGALRSALAHVSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQ 175
Cdd:PRK09793  330 ATTAQAGGVQ-VSTMTHTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQ 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 176 ATGQIETTLAQLTQQTEQliSEGSMNTArahrvregTRKIGDVVhatgDAITQLNDEAGQIAALTGEietQCNGLE--AQ 253
Cdd:PRK09793  409 AAKEIKGLIEESVNRVQQ--GSKLVNNA--------AATMTDIV----SSVTRVNDIMGEIASASEE---QRRGIEqvAQ 471
                         250       260
                  ....*....|....*....|....*...
gi 2502261906 254 VLEMASGVEDSSENFVQ----AKDRLGN 277
Cdd:PRK09793  472 AVSQMDQVTQQNASLVEeaavATEQLAN 499
PRK15041 PRK15041
methyl-accepting chemotaxis protein;
16-265 4.38e-14

methyl-accepting chemotaxis protein;


Pssm-ID: 185001 [Multi-domain]  Cd Length: 554  Bit Score: 74.22  E-value: 4.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  16 VGDIAAQAGKLGIEICDVSGHVEEVAARVQHQAQvcrALRESAAqtlagnhriataarAMRSVSAGAATGVQESQQTLEA 95
Cdd:PRK15041  267 VGDVRNGANAIYSGASEIATGNNDLSSRTEQQAA---SLEETAA--------------SMEQLTATVKQNAENARQASHL 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  96 SLADIHGLVEGVTVIESQIGALRSALAHVSRVSEEISLI---ARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAK 172
Cdd:PRK15041  330 ALSASETAQRGGKVVDNVVQTMRDISTSSQKIADIISVIdgiAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQR 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906 173 TAQATGQIETtlaqLTQQTEQLISEGSMntarahRVREGTRKIGDVVhatgDAITQLNDEAGQIAALTGEIETQCNGLEA 252
Cdd:PRK15041  410 SAQAAREIKS----LIEDSVGKVDVGST------LVESAGETMAEIV----SAVTRVTDIMGEIASASDEQSRGIDQVGL 475
                         250       260
                  ....*....|....*....|
gi 2502261906 253 QVLEM-------ASGVEDSS 265
Cdd:PRK15041  476 AVAEMdrvtqqnAALVEESA 495
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
21-256 1.26e-05

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 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906   21 AQAGKLGIEICDVSGHVEEVAARVQHQAQVCRALRESAAQTLAGNHRIATAARAMRSVSAGAATGVQESQQTLEASLADI 100
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  101 hglvegvtviESQIGALRSALahvSRVSEEISLIARQTHLLALNAAIEAARAGDSGKSFAVVAAEVKNLSAKTAQATGQI 180
Cdd:TIGR02168  795 ----------KEELKALREAL---DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261906  181 ETTLAQLTQQTEQLISE----GSMNTARaHRVREGTRKIGDVVHATGDAITQLNDEAGQIAALTGEIETQCNGLEAQVLE 256
Cdd:TIGR02168  862 EELEELIEELESELEALlnerASLEEAL-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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