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Conserved domains on  [gi|16264180|ref|NP_436972|]
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regulatory protein (plasmid) [Sinorhizobium meliloti 1021]

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List of domain hits

Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
591-785 1.14e-43

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


:

Pssm-ID: 284611  Cd Length: 190  Bit Score: 156.64  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   591 GKRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGeMEPAQFLNRVNRAIYKNLVRTRTnKHLSLAFLDYDGARLTLSG 670
Cdd:pfam07228   1 DGRVALVIGDVMGHGLPAALLMGMLRTALRALAAEG-LDPAEVLKRLNRLLQRNLEEDMF-ATAVLAVYDPETGTLEYAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   671 QHEELIVIRDLERVERIDTLDLGLPIGLEPDisAFVATREISFGRGDMIILHTDGVTEAESGTGELFGIERLCESARCRY 750
Cdd:pfam07228  79 AGHPPPLLLRPDGGVVELLESTGLPLGILPD--ADYEVVELELEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERH 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16264180   751 GSSAEDVKSGIIEDLMAHiGTQKIHDDITLVVMRH 785
Cdd:pfam07228 157 GLPPEELLDALLEALLRL-GGGELEDDITLLVLRV 190
Cache_1 super family cl24147
Cache domain;
251-317 4.78e-13

Cache domain;


The actual alignment was detected with superfamily member pfam02743:

Pssm-ID: 280839  Cd Length: 79  Bit Score: 65.78  E-value: 4.78e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16264180   251 TAPYTDAITGKLIVSFFQPLwsRDRSRVLGAAGTDITLDQLAEIVENVKVAETGFGFLTMSDGNVVA 317
Cdd:pfam02743   2 TEPYVDASTGDMVVTIAQPV--KDDGDGLGVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLA 66
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
435-510 5.22e-12

HAMP domain [Signal transduction mechanisms];


:

Pssm-ID: 225359  Cd Length: 83  Bit Score: 63.16  E-value: 5.22e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16264180 435 QVLALLVSLFFVIAAV--FAISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEISFHTENLE 510
Cdd:COG2770   6 PIFGLLVLALVLILAVllLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALSALE 83
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
499-786 2.39e-80

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


:

Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 264.26  E-value: 2.39e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 499 AEEISFHTENLEQLVEDRTKEIEEANLQISALNQQLRSENLRLGAELAVARRIQMMVLPKAGELEEIAELEIAAYmrPAD 578
Cdd:COG2208  82 LSEEIKHWRGGLPLVAELLVEINRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILV--PAS 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 579 EVGGDYYDVLQDG-KRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGEMEPAQFLNRVNRAIYKNLVRTRtNKHLSLA 657
Cdd:COG2208 160 EVGGDYYDFIQLGeKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPLDPADVLETLNRVLKQNLEEDM-FVTLFLG 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 658 FLDYDGARLTL-SGQHEELIVIRDLERVERIDTLDLGLPIGLEPDISAFVATREISfgRGDMIILHTDGVTEAESGTGEL 736
Cdd:COG2208 239 VYDLDSGELTYsNAGHEPALILSADGEIEVEDLTALGLPIGLLPDYQYEVASLQLE--PGDLLVLYTDGVTEARNSDGEF 316
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16264180 737 FGIERLCESARCRYGSSAEDVKSGIIEDLMAHIGTQKIHDDITLVVMRHR 786
Cdd:COG2208 317 FGLERLLKILGRLLGQPAEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
591-785 1.14e-43

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 284611  Cd Length: 190  Bit Score: 156.64  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   591 GKRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGeMEPAQFLNRVNRAIYKNLVRTRTnKHLSLAFLDYDGARLTLSG 670
Cdd:pfam07228   1 DGRVALVIGDVMGHGLPAALLMGMLRTALRALAAEG-LDPAEVLKRLNRLLQRNLEEDMF-ATAVLAVYDPETGTLEYAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   671 QHEELIVIRDLERVERIDTLDLGLPIGLEPDisAFVATREISFGRGDMIILHTDGVTEAESGTGELFGIERLCESARCRY 750
Cdd:pfam07228  79 AGHPPPLLLRPDGGVVELLESTGLPLGILPD--ADYEVVELELEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERH 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16264180   751 GSSAEDVKSGIIEDLMAHiGTQKIHDDITLVVMRH 785
Cdd:pfam07228 157 GLPPEELLDALLEALLRL-GGGELEDDITLLVLRV 190
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
573-767 3.59e-30

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 118.60  E-value: 3.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180    573 YMRPADEVGGDYYDVLQDG-KRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGEmEPAQFLNRVNRAIYKNLVRTR-- 649
Cdd:smart00331   9 YYEDATQVGGDFYDVVKLPeGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGI-SLSQILERLNRAIYENGEDGMfa 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180    650 TnkhLSLAFLDYDGARLTL-SGQHEELIVIRDLERVErIDTLDLGLPIGLEPDISafVATREISFGRGDMIILHTDGVTE 728
Cdd:smart00331  88 T---LFLALYDFAGGTLSYaNAGHSPPYLLRADGGLV-EDLDDLGAPLGLEPDVE--VDVRELTLEPGDLLLLYTDGLTE 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 16264180    729 AESGTGelfGIERLCESArcryGSSAEDVKSGIIEDLMA 767
Cdd:smart00331 162 ARNPER---LEELLEELL----GSPPAEIAQRILEELLE 193
Cache_1 pfam02743
Cache domain;
251-317 4.78e-13

Cache domain;


Pssm-ID: 280839  Cd Length: 79  Bit Score: 65.78  E-value: 4.78e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16264180   251 TAPYTDAITGKLIVSFFQPLwsRDRSRVLGAAGTDITLDQLAEIVENVKVAETGFGFLTMSDGNVVA 317
Cdd:pfam02743   2 TEPYVDASTGDMVVTIAQPV--KDDGDGLGVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLA 66
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
435-510 5.22e-12

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 63.16  E-value: 5.22e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16264180 435 QVLALLVSLFFVIAAV--FAISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEISFHTENLE 510
Cdd:COG2770   6 PIFGLLVLALVLILAVllLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALSALE 83
HAMP pfam00672
HAMP domain;
436-502 2.04e-09

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 55.27  E-value: 2.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16264180   436 VLALLVSLFFVIAAVFAISKRITGGISALANAAKRIEAKDYSVRVDiPTRDEVGDAGAAFNRMAEEI 502
Cdd:pfam00672   2 LLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLE-SGRDEIGELARAFNQMAERL 67
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
455-502 5.07e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 50.71  E-value: 5.07e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 16264180    455 KRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEI 502
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
457-502 7.94e-08

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: 49.94  E-value: 7.94e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16264180 457 ITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEI 502
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERL 46
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
499-786 2.39e-80

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 264.26  E-value: 2.39e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 499 AEEISFHTENLEQLVEDRTKEIEEANLQISALNQQLRSENLRLGAELAVARRIQMMVLPKAGELEEIAELEIAAYmrPAD 578
Cdd:COG2208  82 LSEEIKHWRGGLPLVAELLVEINRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILV--PAS 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 579 EVGGDYYDVLQDG-KRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGEMEPAQFLNRVNRAIYKNLVRTRtNKHLSLA 657
Cdd:COG2208 160 EVGGDYYDFIQLGeKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPLDPADVLETLNRVLKQNLEEDM-FVTLFLG 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 658 FLDYDGARLTL-SGQHEELIVIRDLERVERIDTLDLGLPIGLEPDISAFVATREISfgRGDMIILHTDGVTEAESGTGEL 736
Cdd:COG2208 239 VYDLDSGELTYsNAGHEPALILSADGEIEVEDLTALGLPIGLLPDYQYEVASLQLE--PGDLLVLYTDGVTEARNSDGEF 316
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16264180 737 FGIERLCESARCRYGSSAEDVKSGIIEDLMAHIGTQKIHDDITLVVMRHR 786
Cdd:COG2208 317 FGLERLLKILGRLLGQPAEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
418-534 3.84e-11

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 65.06  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 418 FAAQA-----GISEATNRILIYQVLALLVSLFFVIAAVFA----ISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEV 488
Cdd:COG3850 127 FVAQIdqfvlALQRFAERKTILLVLVQLAGMLLILLLVVFtiywLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNEL 206
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16264180 489 GDAGAAFNRMAEEISFHTENLEQLVEDRTKEIEEANLQISAL---NQQL 534
Cdd:COG3850 207 GLLGRAFNQMSGELKKLYADLEQRVEEKTRDLEQKNQRLSFLyqsSRRL 255
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
432-536 1.05e-07

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 53.91  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180  432 LIYQVLALLvSLFFVIAAVFAISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEISFHTENLEQ 511
Cdd:PRK10600 125 LVHRVFAVF-MALLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQ 203
                         90       100
                 ....*....|....*....|....*...
gi 16264180  512 LVEDRTKEIEEANLQISAL---NQQLRS 536
Cdd:PRK10600 204 RVQEKTAGLEQKNQILSFLwqaNRRLHS 231
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
579-784 3.01e-04

stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs. [Cellular processes, Sporulation and germination]


Pssm-ID: 274328 [Multi-domain]  Cd Length: 764  Bit Score: 42.76  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   579 EVGGDYYDV--LQDGKrLKIGIGDVTGHG----LESGVLMLMVQSVARAlqemgEMEPAQFLNRVNRAIyknLVRTRTNK 652
Cdd:TIGR02865 565 LVSGDSYSFgkLSAGK-YAVAISDGMGSGpeaaQESSACVRLLEKFLES-----GFDREVAIKTVNSIL---SLRSTDEK 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   653 H--LSLAFLDydgarlTLSGQHEELIV------IRDLERVERIDTLDLglPIGLEPDISAFVATREIsfGRGDMIILHTD 724
Cdd:TIGR02865 636 FstLDLSVID------LYTGQAEFVKVgavpsfIKRGAKVEVIRSSNL--PIGILDEVDVELVRKKL--KNGDLIVMVSD 705
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16264180   725 GVTEAESgtgELFGIERLCesarCRYGSSAEDVKSGII-EDLMAH---IGTQKIHDDITLVVMR 784
Cdd:TIGR02865 706 GVLEGEK---EVEGKVLWL----VRKLKETNTNDPEEIaEYLLEKakeLRSGKIKDDMTVIVAK 762
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
420-529 6.06e-04

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 42.07  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   420 AQAGISEATNRILIYQVLALLVSLFFVIAAVFAISKRITGGISALAN----AAKRIEAKDYSVRVDIPTRDE---VGDAG 492
Cdd:TIGR02956 315 TEAAVSDLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNqhtqALLRLALGDLDISLDARGDDElahMGRAI 394
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16264180   493 AAFNRMA--------------EEISFHTENLEQLVEDRTKEIEEANLQISA 529
Cdd:TIGR02956 395 EAFRDTAahnlklqaderqvaQELQEHKESLEQLVAQRTQELAETNERLNA 445
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
591-785 1.14e-43

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 284611  Cd Length: 190  Bit Score: 156.64  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   591 GKRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGeMEPAQFLNRVNRAIYKNLVRTRTnKHLSLAFLDYDGARLTLSG 670
Cdd:pfam07228   1 DGRVALVIGDVMGHGLPAALLMGMLRTALRALAAEG-LDPAEVLKRLNRLLQRNLEEDMF-ATAVLAVYDPETGTLEYAN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   671 QHEELIVIRDLERVERIDTLDLGLPIGLEPDisAFVATREISFGRGDMIILHTDGVTEAESGTGELFGIERLCESARCRY 750
Cdd:pfam07228  79 AGHPPPLLLRPDGGVVELLESTGLPLGILPD--ADYEVVELELEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERH 156
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 16264180   751 GSSAEDVKSGIIEDLMAHiGTQKIHDDITLVVMRH 785
Cdd:pfam07228 157 GLPPEELLDALLEALLRL-GGGELEDDITLLVLRV 190
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
573-767 3.59e-30

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 118.60  E-value: 3.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180    573 YMRPADEVGGDYYDVLQDG-KRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGEmEPAQFLNRVNRAIYKNLVRTR-- 649
Cdd:smart00331   9 YYEDATQVGGDFYDVVKLPeGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGI-SLSQILERLNRAIYENGEDGMfa 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180    650 TnkhLSLAFLDYDGARLTL-SGQHEELIVIRDLERVErIDTLDLGLPIGLEPDISafVATREISFGRGDMIILHTDGVTE 728
Cdd:smart00331  88 T---LFLALYDFAGGTLSYaNAGHSPPYLLRADGGLV-EDLDDLGAPLGLEPDVE--VDVRELTLEPGDLLLLYTDGLTE 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 16264180    729 AESGTGelfGIERLCESArcryGSSAEDVKSGIIEDLMA 767
Cdd:smart00331 162 ARNPER---LEELLEELL----GSPPAEIAQRILEELLE 193
Cache_1 pfam02743
Cache domain;
251-317 4.78e-13

Cache domain;


Pssm-ID: 280839  Cd Length: 79  Bit Score: 65.78  E-value: 4.78e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16264180   251 TAPYTDAITGKLIVSFFQPLwsRDRSRVLGAAGTDITLDQLAEIVENVKVAETGFGFLTMSDGNVVA 317
Cdd:pfam02743   2 TEPYVDASTGDMVVTIAQPV--KDDGDGLGVVGLDVSLEDLLEIINSIKVGGEGYAFIIDNNGKVLA 66
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
435-510 5.22e-12

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 225359  Cd Length: 83  Bit Score: 63.16  E-value: 5.22e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16264180 435 QVLALLVSLFFVIAAV--FAISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEISFHTENLE 510
Cdd:COG2770   6 PIFGLLVLALVLILAVllLAAARRVTRPLRRLADLAQNLALGDLSAEIPQPMLDEIGELAKAFNRMRDSLQRALSALE 83
HAMP pfam00672
HAMP domain;
436-502 2.04e-09

HAMP domain;


Pssm-ID: 279063  Cd Length: 69  Bit Score: 55.27  E-value: 2.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16264180   436 VLALLVSLFFVIAAVFAISKRITGGISALANAAKRIEAKDYSVRVDiPTRDEVGDAGAAFNRMAEEI 502
Cdd:pfam00672   2 LLVLLIALLLALLLAWLLARRILRPLRRLAEAARRIASGDLDVPLE-SGRDEIGELARAFNQMAERL 67
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
455-502 5.07e-08

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 50.71  E-value: 5.07e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 16264180    455 KRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEI 502
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGRDEIGELARAFNEMADRL 48
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
457-502 7.94e-08

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: 49.94  E-value: 7.94e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16264180 457 ITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEI 502
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGDLDVRLPVTGRDEIGELARAFNQMAERL 46
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
499-786 2.39e-80

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, Transcription];


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 264.26  E-value: 2.39e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 499 AEEISFHTENLEQLVEDRTKEIEEANLQISALNQQLRSENLRLGAELAVARRIQMMVLPKAGELEEIAELEIAAYmrPAD 578
Cdd:COG2208  82 LSEEIKHWRGGLPLVAELLVEINRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILV--PAS 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 579 EVGGDYYDVLQDG-KRLKIGIGDVTGHGLESGVLMLMVQSVARALQEMGEMEPAQFLNRVNRAIYKNLVRTRtNKHLSLA 657
Cdd:COG2208 160 EVGGDYYDFIQLGeKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPLDPADVLETLNRVLKQNLEEDM-FVTLFLG 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 658 FLDYDGARLTL-SGQHEELIVIRDLERVERIDTLDLGLPIGLEPDISAFVATREISfgRGDMIILHTDGVTEAESGTGEL 736
Cdd:COG2208 239 VYDLDSGELTYsNAGHEPALILSADGEIEVEDLTALGLPIGLLPDYQYEVASLQLE--PGDLLVLYTDGVTEARNSDGEF 316
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 16264180 737 FGIERLCESARCRYGSSAEDVKSGIIEDLMAHIGTQKIHDDITLVVMRHR 786
Cdd:COG2208 317 FGLERLLKILGRLLGQPAEEILEAILESLEELQGDQIQDDDITLLVLKVK 366
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms] ...
418-534 3.84e-11

Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 65.06  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 418 FAAQA-----GISEATNRILIYQVLALLVSLFFVIAAVFA----ISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEV 488
Cdd:COG3850 127 FVAQIdqfvlALQRFAERKTILLVLVQLAGMLLILLLVVFtiywLRRRVVRPLNQLTSAAQRIGRRQFDQRPTDTGRNEL 206
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 16264180 489 GDAGAAFNRMAEEISFHTENLEQLVEDRTKEIEEANLQISAL---NQQL 534
Cdd:COG3850 207 GLLGRAFNQMSGELKKLYADLEQRVEEKTRDLEQKNQRLSFLyqsSRRL 255
Tar COG0840
Methyl-accepting chemotaxis protein [Cell motility, Signal transduction mechanisms];
401-545 1.15e-09

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


Pssm-ID: 223910 [Multi-domain]  Cd Length: 408  Bit Score: 59.62  E-value: 1.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 401 AMLLGIAVPEREIYASLFAAQAGISEATNRILIYQVLALLVSLFFVIAAVFAISKRITGGISALANAAKRIEAKDYSVRV 480
Cdd:COG0840  28 KLIDELGKLLLSLNLILDDAASAEAAALKAVLKFLLISLLVAIIVVLVLAILLLRAILEPISDLLEVVERIAAGDLTKRI 107
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16264180 481 DIPTRDEVGDAGAAFNRMAEEIsfhtENLEQLVEDRTKEIEEANLQISALNQQLRSENLRLGAEL 545
Cdd:COG0840 108 DESSNDEFGQLAKSFNEMILNL----RQIIDAVQDNAEALSGASEEIAASATELSARADQQAESL 168
PRK10600 PRK10600
nitrate/nitrite sensor protein NarX; Provisional
432-536 1.05e-07

nitrate/nitrite sensor protein NarX; Provisional


Pssm-ID: 182581 [Multi-domain]  Cd Length: 569  Bit Score: 53.91  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180  432 LIYQVLALLvSLFFVIAAVFAISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEISFHTENLEQ 511
Cdd:PRK10600 125 LVHRVFAVF-MALLLVFTIIWLRRRLLQPWRQLLSMANAVSHRDFTQRANISGRDEMAMLGTALNNMSAELAESYAVLEQ 203
                         90       100
                 ....*....|....*....|....*...
gi 16264180  512 LVEDRTKEIEEANLQISAL---NQQLRS 536
Cdd:PRK10600 204 RVQEKTAGLEQKNQILSFLwqaNRRLHS 231
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
435-530 1.22e-06

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 50.62  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180  435 QVLALLVSLFFVIAAVFAISKRITGGISALANAAKRIEAKDYS-VRVDIPTRDEVGDAGAAFNRMAEEISFHTENLEQLV 513
Cdd:PRK10935 154 SLLGLILILTLVFFTVRFTRRQVVAPLNQLVTASQQIEKGQFDhIPLDTTLPNELGLLAKAFNQMSSELHKLYRSLEASV 233
                         90
                 ....*....|....*..
gi 16264180  514 EDRTKEIEEANLQISAL 530
Cdd:PRK10935 234 EEKTRKLTQANRSLEVL 250
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms];
433-511 4.32e-06

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 48.58  E-value: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 433 IYQVLALLVSLFFVIAAV--FAISKRITGGISALANAAKRIEAKDYSVRVDIPTRDEVGDAGAAFNRMAEEISFHTENLE 510
Cdd:COG5002  28 INNILISGTLIALIITALlgILLARTITKPITDMRKQAVDMARGNYSRKVKVYGTDEIGELADSFNDLTKRVQEAQANTE 107

                .
gi 16264180 511 Q 511
Cdd:COG5002 108 Q 108
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
433-521 6.34e-06

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 48.23  E-value: 6.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180 433 IYQVLALLVSLFFVIAAVF---AISKRITGGISALANAAKRIEAKDYSVRVDIPTRDE-VGDAGAAFNRMAEEISFHTEN 508
Cdd:COG5000 278 AFALLYLSTALLVLLAAIWtaiAFARRIVRPIRKLIEAADEVADGDLDVQVPVRRVDEdVGRLSKAFNKMTEQLSSQQEA 357
                        90
                ....*....|....*.
gi 16264180 509 LEQ---LVEDRTKEIE 521
Cdd:COG5000 358 LERakdALEQRRRFLE 373
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
579-784 3.01e-04

stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs. [Cellular processes, Sporulation and germination]


Pssm-ID: 274328 [Multi-domain]  Cd Length: 764  Bit Score: 42.76  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   579 EVGGDYYDV--LQDGKrLKIGIGDVTGHG----LESGVLMLMVQSVARAlqemgEMEPAQFLNRVNRAIyknLVRTRTNK 652
Cdd:TIGR02865 565 LVSGDSYSFgkLSAGK-YAVAISDGMGSGpeaaQESSACVRLLEKFLES-----GFDREVAIKTVNSIL---SLRSTDEK 635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   653 H--LSLAFLDydgarlTLSGQHEELIV------IRDLERVERIDTLDLglPIGLEPDISAFVATREIsfGRGDMIILHTD 724
Cdd:TIGR02865 636 FstLDLSVID------LYTGQAEFVKVgavpsfIKRGAKVEVIRSSNL--PIGILDEVDVELVRKKL--KNGDLIVMVSD 705
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16264180   725 GVTEAESgtgELFGIERLCesarCRYGSSAEDVKSGII-EDLMAH---IGTQKIHDDITLVVMR 784
Cdd:TIGR02865 706 GVLEGEK---EVEGKVLWL----VRKLKETNTNDPEEIaEYLLEKakeLRSGKIKDDMTVIVAK 762
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
420-529 6.06e-04

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 42.07  E-value: 6.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   420 AQAGISEATNRILIYQVLALLVSLFFVIAAVFAISKRITGGISALAN----AAKRIEAKDYSVRVDIPTRDE---VGDAG 492
Cdd:TIGR02956 315 TEAAVSDLLMTLSVAQFGLLITGMLGLVILVFIMWRVVYRSVILRLNqhtqALLRLALGDLDISLDARGDDElahMGRAI 394
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16264180   493 AAFNRMA--------------EEISFHTENLEQLVEDRTKEIEEANLQISA 529
Cdd:TIGR02956 395 EAFRDTAahnlklqaderqvaQELQEHKESLEQLVAQRTQELAETNERLNA 445
PRK15347 PRK15347
two component system sensor kinase SsrA; Provisional
417-523 2.51e-03

two component system sensor kinase SsrA; Provisional


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.01  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180  417 LFAAQAGISEATNRILIYQVLALLVSLFFVIAAVFAISKRITGgiSALANAAKRIEA---KDYSVRVDIPTRDEVGDAGA 493
Cdd:PRK15347 280 TLYPRRNLANEALKPALQQLPFALLILVLLTSVLFLLLRRYLA--KPLWRFVDIINKtgpAALEPRLPENRLDELGSIAK 357
                         90       100       110
                 ....*....|....*....|....*....|
gi 16264180  494 AFNRMAEEISFHTENLEQLVEDRTKEIEEA 523
Cdd:PRK15347 358 AYNQLLDTLNEQYDTLENKVAERTQALAEA 387
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
378-512 5.49e-03

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 38.96  E-value: 5.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16264180   378 PYLVVLKQLQPTNLWASGPvRREAMLLGIAVP---EREIYASLFAAQA--GISEATNRIL--IYQVLALLVSLFFVIAAV 450
Cdd:TIGR03785 347 SHIIKALQGQPASTWRLSP-DSKAVILSAAYPiwiDTEVLGAVIAEQTtnGIRTLRNSALekLFNVILAIMSIGTLALFG 425
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16264180   451 FA--ISKRITGgISALANAAKRIEAKdysVRVDIP---TRDEVGDAGAAFNRMAEEISFHTENLEQL 512
Cdd:TIGR03785 426 FAswISWRIRR-LSDDAEAAIDSQGR---ISGAIPasrSRDEIGDLSRSFAQMVARLRQYTHYLENM 488
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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