|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
16-561 |
8.50e-78 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 254.95 E-value: 8.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 16 ILFVSILGFSSFIYYKTDQSYKALLTKEVKLYQTSLELEALLQKQEAQIKTYVVVQDAENLQKIEQTYEEINKKTTEASK 95
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 96 MSTVKQAKNLLDQISEKNYLYYTSTNRLFNSLNMQNQKEFNTRLSQELQPIEQEIHTFTKEFAQTQLKQRDQKISQLNEE 175
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 176 SNQLLLTLILVSAAIIVGFLVIGTRFVHR-MTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQL 254
Cdd:COG0840 176 AAALALALLAAALLALVALAIILALLLSRsITRPLRELLEVLERIAEGDLT-VRIDVDSKDEIGQLADAFNRMIENLREL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 255 ILQVQNGSRQLAdsaaqfeetisqtiSASEQTSSSIEQVSEASREQSDAVGKVASAIQEVSTGMHNAAEHTSDVSGHSIS 334
Cdd:COG0840 255 VGQVRESAEQVA--------------SASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 335 VTEKAEEGASLIQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAV 414
Cdd:COG0840 321 ASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 415 VADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTE 494
Cdd:COG0840 401 VADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515927287 495 QISASTEEISQTIgvieegakrnseetEYMSAAVEESLAANEEMKAAAEDLKSLSQSLKTSISSFKI 561
Cdd:COG0840 481 EQSAGTEEVNQAI--------------EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
285-553 |
3.52e-53 |
|
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: 181.72 E-value: 3.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 285 QTSSSIEQVSEASREQSDAVGKVASAIQEVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEHH 364
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 365 STMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDT 444
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 445 ERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQISASTEEISQTIGVIEEGAKRNseeteym 524
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQET------- 233
|
250 260
....*....|....*....|....*....
gi 515927287 525 SAAVEESLAANEEMKAAAEDLKSLSQSLK 553
Cdd:smart00283 234 AAMSEEISAAAEELSGLAEELDELVERFK 262
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
312-510 |
4.87e-48 |
|
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: 165.87 E-value: 4.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 312 QEVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQT 391
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 392 NLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQS 471
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 515927287 472 FQEILAAIRDISMKAEELSATTEQISASTEEISQTIGVI 510
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
336-507 |
9.73e-36 |
|
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: 131.79 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 336 TEKAEEGASLIQQFVKQMSSIKESVNEhhstmanvqvqftgIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVV 415
Cdd:pfam00015 8 SEEAQDGGKEVANVVGQMEQIAQSSKK--------------ISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 416 ADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQ 495
Cdd:pfam00015 74 ADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 153
|
170
....*....|..
gi 515927287 496 ISASTEEISQTI 507
Cdd:pfam00015 154 QSAGIDQVNQAV 165
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
144-519 |
9.37e-30 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 123.14 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 144 QPIEQEIHTFTKEFAQTQLKQR---DQKISQLNEESNQLLLTLILVSAAIIVGFLVIGTRFVHRMTKPIVSVTHAARRMA 220
Cdd:PRK15041 154 QPTQGYQDGFEKQYVAYMEQNDrlyDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 221 DGDLtLEEIEVTSKNEIGQLGTAFNQMTAHLRQLILQVQNGSRQLADSAAQFEETISQTISASEQTSSSIEQVseasreq 300
Cdd:PRK15041 234 GGDL-VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEET------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 301 sdavgkvASAIQEVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEhhstmanvqvqftgIQDL 380
Cdd:PRK15041 306 -------AASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQK--------------IADI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 381 LGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAE 460
Cdd:PRK15041 365 ISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAE 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927287 461 GVKVSQLSEQSFQEILAA-------IRDISMKAEELSATTEQISASTEEISQTIGVIEEGAKRNSE 519
Cdd:PRK15041 445 IVSAVTRVTDIMGEIASAsdeqsrgIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTE 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-558 |
1.17e-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 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 346 IQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGfavVADEVRKLAEE 425
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 426 SSQLTDQISQLLANVNKDTE---RSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQISASTEE 502
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515927287 503 ISQTIGVIEEGAKRNSEETEYMSAAVEESLAANEEMKAAAEDLKSLSQSLKTSISS 558
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
16-561 |
8.50e-78 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 254.95 E-value: 8.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 16 ILFVSILGFSSFIYYKTDQSYKALLTKEVKLYQTSLELEALLQKQEAQIKTYVVVQDAENLQKIEQTYEEINKKTTEASK 95
Cdd:COG0840 16 LLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 96 MSTVKQAKNLLDQISEKNYLYYTSTNRLFNSLNMQNQKEFNTRLSQELQPIEQEIHTFTKEFAQTQLKQRDQKISQLNEE 175
Cdd:COG0840 96 LALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 176 SNQLLLTLILVSAAIIVGFLVIGTRFVHR-MTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQL 254
Cdd:COG0840 176 AAALALALLAAALLALVALAIILALLLSRsITRPLRELLEVLERIAEGDLT-VRIDVDSKDEIGQLADAFNRMIENLREL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 255 ILQVQNGSRQLAdsaaqfeetisqtiSASEQTSSSIEQVSEASREQSDAVGKVASAIQEVSTGMHNAAEHTSDVSGHSIS 334
Cdd:COG0840 255 VGQVRESAEQVA--------------SASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 335 VTEKAEEGASLIQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAV 414
Cdd:COG0840 321 ASELAEEGGEVVEEAVEGIEEIRESVEETAETIEELGESSQEIGEIVDVIDDIAEQTNLLALNAAIEAARAGEAGRGFAV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 415 VADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTE 494
Cdd:COG0840 401 VADEVRKLAERSAEATKEIEELIEEIQSETEEAVEAMEEGSEEVEEGVELVEEAGEALEEIVEAVEEVSDLIQEIAAASE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515927287 495 QISASTEEISQTIgvieegakrnseetEYMSAAVEESLAANEEMKAAAEDLKSLSQSLKTSISSFKI 561
Cdd:COG0840 481 EQSAGTEEVNQAI--------------EQIAAAAQENAASVEEVAAAAEELAELAEELQELVSRFKL 533
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
285-553 |
3.52e-53 |
|
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: 181.72 E-value: 3.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 285 QTSSSIEQVSEASREQSDAVGKVASAIQEVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEHH 364
Cdd:smart00283 1 DVSEAVEEIAAGAEEQAEELEELAERMEELSASIEEVAANADEIAATAQSAAEAAEEGREAVEDAITAMDQIREVVEEAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 365 STMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDT 444
Cdd:smart00283 81 SAVEELEESSDEIGEIVSVIDDIADQTNLLALNAAIEAARAGEAGRGFAVVADEVRKLAERSAESAKEIESLIKEIQEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 445 ERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQISASTEEISQTIGVIEEGAKRNseeteym 524
Cdd:smart00283 161 NEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAIDEIAQVTQET------- 233
|
250 260
....*....|....*....|....*....
gi 515927287 525 SAAVEESLAANEEMKAAAEDLKSLSQSLK 553
Cdd:smart00283 234 AAMSEEISAAAEELSGLAEELDELVERFK 262
|
|
| MCP_signal |
cd11386 |
Methyl-accepting chemotaxis protein (MCP), signaling domain; Methyl-accepting chemotaxis ... |
312-510 |
4.87e-48 |
|
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: 165.87 E-value: 4.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 312 QEVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQT 391
Cdd:cd11386 1 EELSASIEEVAASADQVAETSQQAAELAEKGREAAEDAINQMNQIDESVDEAVSAVEELEESSAEIGEIVEVIDDIAEQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 392 NLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQS 471
Cdd:cd11386 81 NLLALNAAIEAARAGEAGRGFAVVADEVRKLAEESAEAAKEIEELIEEIQEQTEEAVEAMEETSEEVEEGVELVEETGRA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 515927287 472 FQEILAAIRDISMKAEELSATTEQISASTEEISQTIGVI 510
Cdd:cd11386 161 FEEIVASVEEVADGIQEISAATQEQSASTQEIAAAVEEI 199
|
|
| MCPsignal |
pfam00015 |
Methyl-accepting chemotaxis protein (MCP) signalling domain; This domain is thought to ... |
336-507 |
9.73e-36 |
|
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: 131.79 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 336 TEKAEEGASLIQQFVKQMSSIKESVNEhhstmanvqvqftgIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVV 415
Cdd:pfam00015 8 SEEAQDGGKEVANVVGQMEQIAQSSKK--------------ISDIISVIDEIAFQTNLLALNAAIEAARAGEQGRGFAVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 416 ADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQ 495
Cdd:pfam00015 74 ADEVRKLAERSAQAAKEIEALIIEIQKQTNDSTASIESTRQRVEVGSTIVESTGEALKEIVDAVAEIADIVQEIAAASDE 153
|
170
....*....|..
gi 515927287 496 ISASTEEISQTI 507
Cdd:pfam00015 154 QSAGIDQVNQAV 165
|
|
| PRK15041 |
PRK15041 |
methyl-accepting chemotaxis protein; |
144-519 |
9.37e-30 |
|
methyl-accepting chemotaxis protein;
Pssm-ID: 185001 [Multi-domain] Cd Length: 554 Bit Score: 123.14 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 144 QPIEQEIHTFTKEFAQTQLKQR---DQKISQLNEESNQLLLTLILVSAAIIVGFLVIGTRFVHRMTKPIVSVTHAARRMA 220
Cdd:PRK15041 154 QPTQGYQDGFEKQYVAYMEQNDrlyDIAVSDNNASYSQAMWILVGVMIVVLAVIFAVWFGIKASLVAPMNRLIDSIRHIA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 221 DGDLtLEEIEVTSKNEIGQLGTAFNQMTAHLRQLILQVQNGSRQLADSAAQFEETISQTISASEQTSSSIEQVseasreq 300
Cdd:PRK15041 234 GGDL-VKPIEVDGSNEMGQLAESLRHMQGELMRTVGDVRNGANAIYSGASEIATGNNDLSSRTEQQAASLEET------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 301 sdavgkvASAIQEVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEhhstmanvqvqftgIQDL 380
Cdd:PRK15041 306 -------AASMEQLTATVKQNAENARQASHLALSASETAQRGGKVVDNVVQTMRDISTSSQK--------------IADI 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 381 LGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAE 460
Cdd:PRK15041 365 ISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLAQRSAQAAREIKSLIEDSVGKVDVGSTLVESAGETMAE 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927287 461 GVKVSQLSEQSFQEILAA-------IRDISMKAEELSATTEQISASTEEISQTIGVIEEGAKRNSE 519
Cdd:PRK15041 445 IVSAVTRVTDIMGEIASAsdeqsrgIDQVGLAVAEMDRVTQQNAALVEESAAAAAALEEQASRLTE 510
|
|
| PRK15048 |
PRK15048 |
methyl-accepting chemotaxis protein II; Provisional |
72-516 |
9.81e-29 |
|
methyl-accepting chemotaxis protein II; Provisional
Pssm-ID: 185008 [Multi-domain] Cd Length: 553 Bit Score: 120.11 E-value: 9.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 72 DAENLQKIEQTYEEINKKTTEASKMSTVKQAKNLLDQ---------ISEKNYLYYTSTNRLFNSLNMQNQKEFntrLSQE 142
Cdd:PRK15048 77 DSSNQQSNAKVELLDSARKTLAQAATHYKKFKSMAPLpemvatsrnIDEKYKNYYTALTELIDYLDYGNTGAY---FAQP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 143 LQPIEQEIHTFTKEFAQTQLKQRDQKISQLNEESNQLLLTLILVSAAIIVGFLVIGTRFVHRMTKPIVSVTHAARRMADG 222
Cdd:PRK15048 154 TQGMQNAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGG 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 223 DLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQLILQVQNGSRQLADSAAQFEETISQTISASEQTSSSIEQVSeASREQSD 302
Cdd:PRK15048 234 NLA-NTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETA-ASMEQLT 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 303 AVGKvasaiqevstgmhNAAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEhhstmanvqvqftgIQDLLG 382
Cdd:PRK15048 312 ATVK-------------QNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKK--------------IADIIS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 383 NIHAIADQTNLLALNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLL----ANVNKDT---ERSSQSMTKVE 455
Cdd:PRK15048 365 VIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIedsvSRVDTGSvlvESAGETMNNIV 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927287 456 RDVAE-----GVKVSQLSEQSfqeilAAIRDISMKAEELSATTEQISASTEEISQTIGVIEEGAKR 516
Cdd:PRK15048 445 NAVTRvtdimGEIASASDEQS-----RGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASR 505
|
|
| PRK09793 |
PRK09793 |
methyl-accepting chemotaxis protein IV; |
94-548 |
5.09e-27 |
|
methyl-accepting chemotaxis protein IV;
Pssm-ID: 182079 [Multi-domain] Cd Length: 533 Bit Score: 114.78 E-value: 5.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 94 SKMSTVKQAKNLLDQISEKNYlyytstNRLFNSLNMQNQKEFNTRLSQELQ-PIEQEIHTFTKEFAQTQLK-----QRDQ 167
Cdd:PRK09793 105 MAMTAGNEHVRALQKETEKSF------ARWHNDLEHQATWLESNQLSDFLTaPVQGSQNAFDVNFEAWQLEinhvlEAAS 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 168 KISQLNEESNQLLLTLILVSAAIIVGFLVIGTRfvHRMTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQM 247
Cdd:PRK09793 179 AQSQRNYQISALVFISMIIVAAIYISSALWWTR--KMIVQPLAIIGSHFDSIAAGNLA-RPIAVYGRNEITAIFASLKTM 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 248 TAHLRQLILQVQNGSRQLadsaaqfEETISQTISASEQTSSSIEQvseasreQSDAVGKVASAIQEVSTGMHNAAEHTSD 327
Cdd:PRK09793 256 QQALRGTVSDVRKGSQEM-------HIGIAEIVAGNNDLSSRTEQ-------QAASLAQTAASMEQLTATVGQNADNARQ 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 328 VSGHSISVTEKAEEGASliqqfvkQMSSIKesvnehhSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGE 407
Cdd:PRK09793 322 ASELAKNAATTAQAGGV-------QVSTMT-------HTMQEIATSSQKIGDIISVIDGIAFQTNILALNAAVEAARAGE 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 408 HGRGFAVVADEVRKLAEESSQLTDQISQLLanvnkdtersSQSMTKVErdvaEGVKVSQLSEQSFQEILAAIRDISMKAE 487
Cdd:PRK09793 388 QGRGFAVVAGEVRNLASRSAQAAKEIKGLI----------EESVNRVQ----QGSKLVNNAAATMTDIVSSVTRVNDIMG 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515927287 488 ELSATTEQISASTEEISQTIGVIEEGAKRNseeteymSAAVEESLAANEEMKAAAEDLKSL 548
Cdd:PRK09793 454 EIASASEEQRRGIEQVAQAVSQMDQVTQQN-------ASLVEEAAVATEQLANQADHLSSR 507
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
206-251 |
1.10e-13 |
|
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 Af1503 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: 381743 [Multi-domain] Cd Length: 45 Bit Score: 65.16 E-value: 1.10e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 515927287 206 TKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHL 251
Cdd:cd06225 1 TRPLRRLTEAARRIAEGDLD-VRVPVRSKDEIGELARAFNQMAERL 45
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
178-282 |
8.47e-13 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 70.38 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 178 QLLLTLILVSAAIIVGFLVI--GTRFVHRMTKPIVSVTHAARRMADGDLTLeEIEVTSKNEIGQLGTAFNQMTAHLRQli 255
Cdd:COG5000 4 QILFLLLLLLIALLLLLLALwlALLLARRLTRPLRRLAEATRAVAAGDLSV-RLPVTGDDEIGELARAFNRMTDQLKE-- 80
|
90 100
....*....|....*....|....*..
gi 515927287 256 lqvqngSRQLADSAAQFEETISQTISA 282
Cdd:COG5000 81 ------QREELEERRRYLETILENLPA 101
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
203-255 |
1.83e-11 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 59.18 E-value: 1.83e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 515927287 203 HRMTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQLI 255
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIADGDLT-VRLPVDGRDEIGELARAFNEMADRLEETI 52
|
|
| HAMP |
pfam00672 |
HAMP domain; |
200-253 |
3.01e-11 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 58.40 E-value: 3.01e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 515927287 200 RFVHRMTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQ 253
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIASGDLD-VRLPVSGRDEIGELARAFNQMAERLRE 53
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
170-268 |
4.19e-09 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 58.88 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 170 SQLNEESNQLLLTLILVSAAIIVGFLVIGTRFVHRMTKPIVSVTHAARRMADGDLTleEIEVTSKNEIGQLGTAFNQMTA 249
Cdd:COG2972 146 SELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLV--RLEVSGNDEIGILARSFNEMVE 223
|
90
....*....|....*....
gi 515927287 250 HLRQLILQVQNGSRQLADS 268
Cdd:COG2972 224 RIKELIEEVYELELEKKEA 242
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
1-554 |
1.75e-07 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 53.96 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 1 MRLKNQFLFGLIVICILFVSILGFSSFIYYKTDQSYKALLTKEVKLYQTSLELEALLQKQEAQIKTYVVVQDAENLQKIE 80
Cdd:COG2770 32 SLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 81 QTYEEINKKTTEASKMSTVKQAKNLLDQISEKNYLYYTSTNRLFNSLNMQNQKEFNTRLSQELQPIEQEIHTFTKEFAQT 160
Cdd:COG2770 112 LLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 161 QLKQRDQKISQLNEESNQLLLTLILVSAAIIVGFLVIGTRFVHRMTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQL 240
Cdd:COG2770 192 LLLLGGLLLVVLLEAALAALLLLLLLALLALLLALLLALLLARRITRPLRRLAEAARRIAAGDLD-VRIPVSRKDEIGEL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 241 GTAFNQMTAHLRQLILQVQNGSRQLADSAAQFEETISQTISASEQTSSSIEQVSEASREQSDAVGKVASAIQEVSTGMHN 320
Cdd:COG2770 271 ARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 321 AAEHTSDVSGHSISVTEKAEEGASLIQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAI 400
Cdd:COG2770 351 LLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 401 EAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIR 480
Cdd:COG2770 431 AEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEELL 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515927287 481 DISMKAEELSATTEQISASTEEISQTIGVIEEGAKRNSEETEYMSAAVEESLAANEEMKAAAEDLKSLSQSLKT 554
Cdd:COG2770 511 LLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAA 584
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
182-511 |
1.26e-06 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 51.04 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 182 TLILVSAAIIVGFLVIGTRFVHRMTKPIVSVTHAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQLILQVQNG 261
Cdd:COG3850 119 LALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFD-ARVPVSGRDELGTLARAFNRMADELQELYAELEEE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 262 SRQLADSAAQFEETISQTISASEQTSSSIEQVSEASREQSDAVGKVASAIQEVSTGMHNAAEHTSDVSGHSISVTEKAEE 341
Cdd:COG3850 198 EELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 342 gASLIQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGFAVVADEVRK 421
Cdd:COG3850 278 -LLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 422 LAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQISASTE 501
Cdd:COG3850 357 AAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSIIAGGEAIARGEAL 436
|
330
....*....|
gi 515927287 502 EISQTIGVIE 511
Cdd:COG3850 437 AARGLAAAAA 446
|
|
| PRK10935 |
PRK10935 |
nitrate/nitrite two-component system sensor histidine kinase NarQ; |
183-254 |
3.17e-05 |
|
nitrate/nitrite two-component system sensor histidine kinase NarQ;
Pssm-ID: 236800 [Multi-domain] Cd Length: 565 Bit Score: 46.77 E-value: 3.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515927287 183 LILVSAAIIVGFLVI------GTRFVHR-MTKPIVSVTHAARRMADGDLTLEEIEVTSKNEIGQLGTAFNQMTAHLRQL 254
Cdd:PRK10935 147 LILLAAISLLGLILIltlvffTVRFTRRqVVAPLNQLVTASQQIEKGQFDHIPLDTTLPNELGLLAKAFNQMSSELHKL 225
|
|
| MA |
smart00283 |
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ... |
233-349 |
3.47e-04 |
|
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: 42.66 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 233 SKNEIGQLGTAFNQMTAHLRQLILQVQNGSRQLADSAAQFEETISQTISASEQTSSSIEQVSEASREQSDAVGKVASAIQ 312
Cdd:smart00283 145 SAKEIESLIKEIQEETNEAVAAMEESSSEVEEGVELVEETGDALEEIVDSVEEIADLVQEIAAATDEQAAGSEEVNAAID 224
|
90 100 110
....*....|....*....|....*....|....*..
gi 515927287 313 EVSTGMHNAAEHTSDVSGHSISVTEKAEEGASLIQQF 349
Cdd:smart00283 225 EIAQVTQETAAMSEEISAAAEELSGLAEELDELVERF 261
|
|
| envZ |
PRK09467 |
osmolarity sensor protein; Provisional |
174-254 |
8.63e-04 |
|
osmolarity sensor protein; Provisional
Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 41.82 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 174 EESNQLLLTLILvsaaIIVGFLVI--GTRFVHRMTKPIVSVTHAARRMADGDL--------TLEEIEVTSkneigqlgtA 243
Cdd:PRK09467 148 HQGDFSPLFRYT----LAIGLLSVagGWLFIRIQNRPLVALEHAALQVGKGEIppplreygASEVRSVTR---------A 214
|
90
....*....|.
gi 515927287 244 FNQMTAHLRQL 254
Cdd:PRK09467 215 FNQMAAGIKQL 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-558 |
1.17e-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 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 346 IQQFVKQMSSIKESVNEHHSTMANVQVQFTGIQDLLGNIHAIADQTNLLALNAAIEAARAGEHGRGfavVADEVRKLAEE 425
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ---LEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 426 SSQLTDQISQLLANVNKDTE---RSSQSMTKVERDVAEGVKVSQLSEQSFQEILAAIRDISMKAEELSATTEQISASTEE 502
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515927287 503 ISQTIGVIEEGAKRNSEETEYMSAAVEESLAANEEMKAAAEDLKSLSQSLKTSISS 558
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
|
| PRK10604 |
PRK10604 |
sensor protein RstB; Provisional |
214-270 |
1.68e-03 |
|
sensor protein RstB; Provisional
Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 41.13 E-value: 1.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 515927287 214 HAARRMADGDLTlEEIEVTSKNEIGQLGTAFNQMTAHLRQLIlqvqNGSRQLADSAA 270
Cdd:PRK10604 169 AAAQRLGDGHLA-ERIHFDEGSSLERLGVAFNQMADNINALI----ASKKQLIDGIA 220
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
396-553 |
7.62e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.07 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 396 LNAAIEAARAGEHGRGFAVVADEVRKLAEESSQLTDQISQLLANVNKDTERSSQSMTKVERDVAEGV-------KVSQLS 468
Cdd:PLN03229 576 IKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTpppnlqeKIESLN 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927287 469 EQSFQEILAAIR--DISMKAEELSATTEQISASTE-EISQTIGVIEEGAKRNSEETEYMSAAVEESLAANEEMKAAAEDL 545
Cdd:PLN03229 656 EEINKKIERVIRssDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETA 735
|
....*...
gi 515927287 546 KSLSQSLK 553
Cdd:PLN03229 736 AESNGSLK 743
|
|
|