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Conserved domains on  [gi|53803111|ref|YP_115148|]
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HAMP domain-containing protein [Methylococcus capsulatus str. Bath]

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List of domain hits

Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
196-255 1.19e-03

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


:

Pssm-ID: 100122  Cd Length: 48  Bit Score: 37.23  E-value: 1.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 196 LSRPLIRLTRSVRALARGNyddaahlLETELPQRmghaaPTDEIGILAGSFVQMAGEIRR 255
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGD-------LDVRLPVT-----GRDEIGELARAFNQMAERLRE 48
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
344-535 2.33e-54

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: 254114  Cd Length: 192  Bit Score: 183.65  E-value: 2.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   344 DGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDVGMFVTVFLATLDVETGRLVYSYG 423
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   424 GHNRPVLLGRDGSVEMLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAMNGESELFGDSRLLAALRGRTRED 503
Cdd:pfam07228  81 GHPPPLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLS 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 53803111   504 ASELVDAVISRVRAHAGtAEQSDDITLIAVRR 535
Cdd:pfam07228 161 PEELLDALLEDLLRLGG-GELEDDITLLVLRV 191
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
256-535 3.91e-53

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


:

Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 185.68  E-value: 3.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 256 SHEQLEEYNRTLEDKVRVrteELVEAYRKQKELENEILQESLRLARDIQMGMMSTAFPRFakgSPVDLYAMVDPAREVGG 335
Cdd:COG2208  90 RGGLPLVAELLVEINRAV---GLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLF---PGIDIEAILVPASEVGG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 336 DFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHG-SPREILQAVNPELCRENDVGMFVTVFLATLDVE 414
Cdd:COG2208 164 DYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPlDPADVLETLNRVLKQNLEEDMFVTLFLGVYDLD 243
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 415 TGRLVYSYGGHNrPVLLGRDGSVE--MLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAMNGESELFGDSRL 492
Cdd:COG2208 244 SGELTYSNAGHE-PALILSADGEIevEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERL 322
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 53803111 493 LAALRGRTREDASELVDAVISRVRAHAGTAEQSDDITLIAVRR 535
Cdd:COG2208 323 LKILGRLLGQPAEEILEAILESLEELQGDQIQDDDITLLVLKV 365
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
196-255 1.19e-03

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


Pssm-ID: 100122  Cd Length: 48  Bit Score: 37.23  E-value: 1.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 196 LSRPLIRLTRSVRALARGNyddaahlLETELPQRmghaaPTDEIGILAGSFVQMAGEIRR 255
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGD-------LDVRLPVT-----GRDEIGELARAFNQMAERLRE 48
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
344-535 2.33e-54

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: 254114  Cd Length: 192  Bit Score: 183.65  E-value: 2.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   344 DGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDVGMFVTVFLATLDVETGRLVYSYG 423
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   424 GHNRPVLLGRDGSVEMLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAMNGESELFGDSRLLAALRGRTRED 503
Cdd:pfam07228  81 GHPPPLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLS 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 53803111   504 ASELVDAVISRVRAHAGtAEQSDDITLIAVRR 535
Cdd:pfam07228 161 PEELLDALLEDLLRLGG-GELEDDITLLVLRV 191
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
321-512 3.54e-38

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 139.02  E-value: 3.54e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111    321 VDLYAMVDPAREVGGDFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDV 400
Cdd:smart00331   4 GLIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGED 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111    401 GMFVTVFLATLDVETGRLVYSYGGHNRPVLLGRDGSVEMLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAM 480
Cdd:smart00331  84 GMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEAR 163
                          170       180       190
                   ....*....|....*....|....*....|..
gi 53803111    481 NGEselfgdsRLLAALRGRTREDASELVDAVI 512
Cdd:smart00331 164 NPE-------RLEELLEELLGSPPAEIAQRIL 188
HAMP pfam00672
HAMP domain;
176-255 5.74e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 44.14  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   176 GIAGIFIVIGSGIVVLVSNALSRPLIRLTRSVRALARGNYDDAAHLletelpqrmghaAPTDEIGILAGSFVQMAGEIRR 255
Cdd:pfam00672   3 LVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPV------------SGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
196-256 2.78e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 36.07  E-value: 2.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53803111    196 LSRPLIRLTRSVRALARGNyddaahlLETELPQRmghaaPTDEIGILAGSFVQMAGEIRRS 256
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGD-------LTVRLPVD-----GRDEIGELARAFNEMADRLEET 51
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
180-261 7.44e-03

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 35.04  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 180 IFIVIGSGIVVLVSNALSRPLIRLTRSVRALARGNYDdaahlleTELPQRMghaapTDEIGILAGSFVQMAGEIRRSHEQ 259
Cdd:COG2770  14 ALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLS-------AEIPQPM-----LDEIGELAKAFNRMRDSLQRALSA 81

                ..
gi 53803111 260 LE 261
Cdd:COG2770  82 LE 83
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
256-535 3.91e-53

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 185.68  E-value: 3.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 256 SHEQLEEYNRTLEDKVRVrteELVEAYRKQKELENEILQESLRLARDIQMGMMSTAFPRFakgSPVDLYAMVDPAREVGG 335
Cdd:COG2208  90 RGGLPLVAELLVEINRAV---GLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLF---PGIDIEAILVPASEVGG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 336 DFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHG-SPREILQAVNPELCRENDVGMFVTVFLATLDVE 414
Cdd:COG2208 164 DYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPlDPADVLETLNRVLKQNLEEDMFVTLFLGVYDLD 243
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 415 TGRLVYSYGGHNrPVLLGRDGSVE--MLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAMNGESELFGDSRL 492
Cdd:COG2208 244 SGELTYSNAGHE-PALILSADGEIevEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERL 322
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 53803111 493 LAALRGRTREDASELVDAVISRVRAHAGTAEQSDDITLIAVRR 535
Cdd:COG2208 323 LKILGRLLGQPAEEILEAILESLEELQGDQIQDDDITLLVLKV 365
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
332-534 8.19e-13

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: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 69.72  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   332 EVGGDFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDVGMFVTVFLATL 411
Cdd:TIGR02865 565 LVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIKTVNSILSLRSTDEKFSTLDLSVI 644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   412 DVETGRL-VYSYGGhnRPVLLGRDGSVEMLTGDTaVALGVFDDIEFSEQERVLQPGAALVMYTDGVneaMNGESELFG-D 489
Cdd:TIGR02865 645 DLYTGQAeFVKVGA--VPSFIKRGAKVEVIRSSN-LPIGILDEVDVELVRKKLKNGDLIVMVSDGV---LEGEKEVEGkV 718
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 53803111   490 SRLLAALRGRTREDASELVDAVISRV-RAHAGTAEqsDDITLIAVR 534
Cdd:TIGR02865 719 LWLVRKLKETNTNDPEEIAEYLLEKAkELRSGKIK--DDMTVIVAK 762
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
167-307 1.87e-05

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 45.88  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 167 TRRVVLLGTGIAGIFIVIgsgIVVLVSNALSRPLIRLTRSVRALARGNYDdaahlletelpqRMGHAAPTDEIGILAGSF 246
Cdd:COG5002  28 INNILISGTLIALIITAL---LGILLARTITKPITDMRKQAVDMARGNYS------------RKVKVYGTDEIGELADSF 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53803111 247 VQMAGEIRRSHEQLEEYNRTLEDKVRVRTEELVEAYRKQK-ELENEILQESLRLARDIQMGM 307
Cdd:COG5002  93 NDLTKRVQEAQANTEQERRKLDSVLAYMTDGVIATDRRGKiILINKPALKMLGVSKEDALGR 154
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
178-283 1.66e-04

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 42.92  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111  178 AGIFIVIGSGIVVLVSNALSR-------PLIRLTRSVRALARGNYDDAAhlLETELPqrmghaaptDEIGILAGSFVQMA 250
Cdd:PRK10935 151 AAISLLGLILILTLVFFTVRFtrrqvvaPLNQLVTASQQIEKGQFDHIP--LDTTLP---------NELGLLAKAFNQMS 219
                         90       100       110
                 ....*....|....*....|....*....|...
gi 53803111  251 GEirrsheqLEEYNRTLEDKVRVRTEELVEAYR 283
Cdd:PRK10935 220 SE-------LHKLYRSLEASVEEKTRKLTQANR 245
 
Name Accession Description Interval E-value
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain. ...
196-255 1.19e-03

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


Pssm-ID: 100122  Cd Length: 48  Bit Score: 37.23  E-value: 1.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 196 LSRPLIRLTRSVRALARGNyddaahlLETELPQRmghaaPTDEIGILAGSFVQMAGEIRR 255
Cdd:cd06225   1 ILRPLRRLAEAAQRIAAGD-------LDVRLPVT-----GRDEIGELARAFNQMAERLRE 48
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
344-535 2.33e-54

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: 254114  Cd Length: 192  Bit Score: 183.65  E-value: 2.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   344 DGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDVGMFVTVFLATLDVETGRLVYSYG 423
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   424 GHNRPVLLGRDGSVEMLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAMNGESELFGDSRLLAALRGRTRED 503
Cdd:pfam07228  81 GHPPPLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLS 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 53803111   504 ASELVDAVISRVRAHAGtAEQSDDITLIAVRR 535
Cdd:pfam07228 161 PEELLDALLEDLLRLGG-GELEDDITLLVLRV 191
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
321-512 3.54e-38

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 139.02  E-value: 3.54e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111    321 VDLYAMVDPAREVGGDFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDV 400
Cdd:smart00331   4 GLIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGED 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111    401 GMFVTVFLATLDVETGRLVYSYGGHNRPVLLGRDGSVEMLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAM 480
Cdd:smart00331  84 GMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEAR 163
                          170       180       190
                   ....*....|....*....|....*....|..
gi 53803111    481 NGEselfgdsRLLAALRGRTREDASELVDAVI 512
Cdd:smart00331 164 NPE-------RLEELLEELLGSPPAEIAQRIL 188
HAMP pfam00672
HAMP domain;
176-255 5.74e-06

HAMP domain;


Pssm-ID: 250044  Cd Length: 70  Bit Score: 44.14  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   176 GIAGIFIVIGSGIVVLVSNALSRPLIRLTRSVRALARGNYDDAAHLletelpqrmghaAPTDEIGILAGSFVQMAGEIRR 255
Cdd:pfam00672   3 LVLLIALLLLLLLAWLLARRLLRPLRRLAEAARRIASGDLDDRVPV------------SGPDEIGELARAFNQMADRLRE 70
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
196-256 2.78e-03

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


Pssm-ID: 197640  Cd Length: 53  Bit Score: 36.07  E-value: 2.78e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 53803111    196 LSRPLIRLTRSVRALARGNyddaahlLETELPQRmghaaPTDEIGILAGSFVQMAGEIRRS 256
Cdd:smart00304   3 LLRPLRRLAEAAQRIADGD-------LTVRLPVD-----GRDEIGELARAFNEMADRLEET 51
ResE COG2770
FOG: HAMP domain [Signal transduction mechanisms]
180-261 7.44e-03

FOG: HAMP domain [Signal transduction mechanisms]


Pssm-ID: 225359  Cd Length: 83  Bit Score: 35.04  E-value: 7.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 180 IFIVIGSGIVVLVSNALSRPLIRLTRSVRALARGNYDdaahlleTELPQRMghaapTDEIGILAGSFVQMAGEIRRSHEQ 259
Cdd:COG2770  14 ALVLILAVLLLAAARRVTRPLRRLADLAQNLALGDLS-------AEIPQPM-----LDEIGELAKAFNRMRDSLQRALSA 81

                ..
gi 53803111 260 LE 261
Cdd:COG2770  82 LE 83
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
256-535 3.91e-53

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 185.68  E-value: 3.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 256 SHEQLEEYNRTLEDKVRVrteELVEAYRKQKELENEILQESLRLARDIQMGMMSTAFPRFakgSPVDLYAMVDPAREVGG 335
Cdd:COG2208  90 RGGLPLVAELLVEINRAV---GLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLF---PGIDIEAILVPASEVGG 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 336 DFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHG-SPREILQAVNPELCRENDVGMFVTVFLATLDVE 414
Cdd:COG2208 164 DYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPlDPADVLETLNRVLKQNLEEDMFVTLFLGVYDLD 243
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 415 TGRLVYSYGGHNrPVLLGRDGSVE--MLTGDTAVALGVFDDIEFSEQERVLQPGAALVMYTDGVNEAMNGESELFGDSRL 492
Cdd:COG2208 244 SGELTYSNAGHE-PALILSADGEIevEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERL 322
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 53803111 493 LAALRGRTREDASELVDAVISRVRAHAGTAEQSDDITLIAVRR 535
Cdd:COG2208 323 LKILGRLLGQPAEEILEAILESLEELQGDQIQDDDITLLVLKV 365
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
332-534 8.19e-13

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: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 69.72  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   332 EVGGDFYDFLYLDGRTLLIAIGDVSGKGMAAALFMVKVKTMIRAVTSAHGSPREILQAVNPELCRENDVGMFVTVFLATL 411
Cdd:TIGR02865 565 LVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIKTVNSILSLRSTDEKFSTLDLSVI 644
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111   412 DVETGRL-VYSYGGhnRPVLLGRDGSVEMLTGDTaVALGVFDDIEFSEQERVLQPGAALVMYTDGVneaMNGESELFG-D 489
Cdd:TIGR02865 645 DLYTGQAeFVKVGA--VPSFIKRGAKVEVIRSSN-LPIGILDEVDVELVRKKLKNGDLIVMVSDGV---LEGEKEVEGkV 718
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 53803111   490 SRLLAALRGRTREDASELVDAVISRV-RAHAGTAEqsDDITLIAVR 534
Cdd:TIGR02865 719 LWLVRKLKETNTNDPEEIAEYLLEKAkELRSGKIK--DDMTVIVAK 762
VicK COG5002
Signal transduction histidine kinase [Signal transduction mechanisms]
167-307 1.87e-05

Signal transduction histidine kinase [Signal transduction mechanisms]


Pssm-ID: 227335 [Multi-domain]  Cd Length: 459  Bit Score: 45.88  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 167 TRRVVLLGTGIAGIFIVIgsgIVVLVSNALSRPLIRLTRSVRALARGNYDdaahlletelpqRMGHAAPTDEIGILAGSF 246
Cdd:COG5002  28 INNILISGTLIALIITAL---LGILLARTITKPITDMRKQAVDMARGNYS------------RKVKVYGTDEIGELADSF 92
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53803111 247 VQMAGEIRRSHEQLEEYNRTLEDKVRVRTEELVEAYRKQK-ELENEILQESLRLARDIQMGM 307
Cdd:COG5002  93 NDLTKRVQEAQANTEQERRKLDSVLAYMTDGVIATDRRGKiILINKPALKMLGVSKEDALGR 154
PRK10935 PRK10935
nitrate/nitrite sensor protein NarQ; Provisional
178-283 1.66e-04

nitrate/nitrite sensor protein NarQ; Provisional


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 42.92  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111  178 AGIFIVIGSGIVVLVSNALSR-------PLIRLTRSVRALARGNYDDAAhlLETELPqrmghaaptDEIGILAGSFVQMA 250
Cdd:PRK10935 151 AAISLLGLILILTLVFFTVRFtrrqvvaPLNQLVTASQQIEKGQFDHIP--LDTTLP---------NELGLLAKAFNQMS 219
                         90       100       110
                 ....*....|....*....|....*....|...
gi 53803111  251 GEirrsheqLEEYNRTLEDKVRVRTEELVEAYR 283
Cdd:PRK10935 220 SE-------LHKLYRSLEASVEEKTRKLTQANR 245
NtrY COG5000
Signal transduction histidine kinase involved in nitrogen fixation and metabolism regulation ...
154-281 6.60e-04

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


Pssm-ID: 227333 [Multi-domain]  Cd Length: 712  Bit Score: 40.91  E-value: 6.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 154 QEIANSRAEIEAATRrVVLLGTGIAGIFIVIGSGIvvLVSNALSRPLIRLTRSVRALARGNYDdaahlletelPQRMGHA 233
Cdd:COG5000 266 RELEAGRDGLQIAFA-LLYLSTALLVLLAAIWTAI--AFARRIVRPIRKLIEAADEVADGDLD----------VQVPVRR 332
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 53803111 234 APtDEIGILAGSFVQMAGEIRRSHEQLEEyNRTLEDKVRVRTEELVEA 281
Cdd:COG5000 333 VD-EDVGRLSKAFNKMTEQLSSQQEALER-AKDALEQRRRFLEAVLSG 378
NarQ COG3850
Signal transduction histidine kinase, nitrate/nitrite-specific [Signal transduction mechanisms]
162-283 3.60e-03

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


Pssm-ID: 226368 [Multi-domain]  Cd Length: 574  Bit Score: 38.48  E-value: 3.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111 162 EIEAATRRVVLLGT---GIAGIFIVIGSGIVV-LVSNALSRPLIRLTRSVRALARGNYDdaAHLLETElpqrmghaapTD 237
Cdd:COG3850 137 ALQRFAERKTILLVlvqLAGMLLILLLVVFTIyWLRRRVVRPLNQLTSAAQRIGRRQFD--QRPTDTG----------RN 204
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 53803111 238 EIGILAGSFVQMAGEirrsheqLEEYNRTLEDKVRVRTEELVEAYR 283
Cdd:COG3850 205 ELGLLGRAFNQMSGE-------LKKLYADLEQRVEEKTRDLEQKNQ 243
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
163-304 4.53e-03

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 38.29  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53803111  163 IEAATRRVVLLGTGIAGIFIVIGsgivVLVSNALSRPLIRLTRSVRALARGNyddaahllETELPQRMGHaaptdEIGIL 242
Cdd:PRK11100 177 IKRSERRILWAGALLLGIALLIG----AGVVWWLNRSIRRLTRYADAVTEGK--------PVPLPKLGSS-----ELREL 239
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53803111  243 AGSFVQMageirrsHEQLE--EYnrtLEDKVRVRTEEL---VEAYRKQKELeneiLQESL------RLARDIQ 304
Cdd:PRK11100 240 AQALESM-------RVKLEgkAY---VEQYVQTLTHELkspLAAIRGAAEL----LQEDPppedraRFTGNIL 298
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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