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Conserved domains on  [gi|222151975|ref|YP_002561135|]
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sigma B regulation protein RsbU [Macrococcus caseolyticus JCSC5402]

Graphical summary

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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 ...
145-333 1.30e-58

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: 189.42  E-value: 1.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  145 DGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQL-PSDGLKRLNRVVEKNVNQNMFVTMFYGLYEEVNNKFYYASAG 223
Cdd:pfam07228   2 DGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLdPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  224 HEPGHIYRSKTDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVSEIRKLDGGFINTNELLSLIGKYKDLHP 303
Cdd:pfam07228  82 HPPPLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLSP 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 222151975  304 QDIVQIVYEELLKIGDPKKKDDLTILIIKR 333
Cdd:pfam07228 162 EELLDALLEDLLRLGGGELEDDITLLVLRV 191
RsbU_N super family cl07333
Phosphoserine phosphatase RsbU, N-terminal domain; RsbU is a phosphoserine phosphatase which ...
10-83 1.49e-13

Phosphoserine phosphatase RsbU, N-terminal domain; RsbU is a phosphoserine phosphatase which acts as a positive regulator of the general stress-response factor of gram positive organisms, sigma-B. The phosphatase activity of RsbU is stimulated by association with the RsbT kinase. Deletions in the N terminal domain are deleterious to the activity of RsbU.


The actual alignment was detected with superfamily member pfam08673:

Pssm-ID: 254966  Cd Length: 77  Bit Score: 64.98  E-value: 1.49e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222151975   10 RYIDILETYITTRDEKALEPLQALSFEAIELDISPEEIVMLHKDLINEKSYSGIEQ-QYGMDVLTEMIIGFGFTY 83
Cdd:pfam08673   3 QYKRLLDEYLASQDEQSLYKAEKFSRELIEKDISPEEIVSIHKSYLEELNPDLPEDvLDSFDFLLEVMVGYGLAY 77
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
9-335 3.19e-73

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


:

Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 233.06  E-value: 3.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   9 SRYIDILETYIT----TRDEKALEPLQALS-FEAIELDISPEEIVMLHK----DLINEKSYSGIEQQYGMDVLTEMIIGF 79
Cdd:COG2208   28 GLYAQISAEPLTemffLQTEKGLRQAELLYeINDILERFLPVEVLLGVSgklrALSEEIKHWRGGLPLVAELLVEINRAV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  80 GFTYRDYKALVKVMEAHDKEMDVAASLQSTMLKTKVPHLDKIEIGAISVPAHRVNGDYFNLIDHKDGTMSFAVADVIGKG 159
Cdd:COG2208  108 GLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKRLRIGIGDVSGKG 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975 160 IPAALAMSMIKFGMDSYGHSQL--PSDGLKRLNRVVEKNVNQNMFVTMFYGLYEEVNNKFYYASAGHEPGHIYRSKTDS- 236
Cdd:COG2208  188 VPAALLMLMPKLALRLLLESGPldPADVLETLNRVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIe 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975 237 FEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVSEIRKLDGGFINTNELLSLIGKYKDLHPQDIVQIVYEELLK 316
Cdd:COG2208  268 VEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQPAEEILEAILESLEE 347
                        330       340
                 ....*....|....*....|
gi 222151975 317 -IGDPKKKDDLTILIIKRIK 335
Cdd:COG2208  348 lQGDQIQDDDITLLVLKVKK 367
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
145-333 1.30e-58

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: 189.42  E-value: 1.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  145 DGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQL-PSDGLKRLNRVVEKNVNQNMFVTMFYGLYEEVNNKFYYASAG 223
Cdd:pfam07228   2 DGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLdPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  224 HEPGHIYRSKTDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVSEIRKLDGGFINTNELLSLIGKYKDLHP 303
Cdd:pfam07228  82 HPPPLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLSP 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 222151975  304 QDIVQIVYEELLKIGDPKKKDDLTILIIKR 333
Cdd:pfam07228 162 EELLDALLEDLLRLGGGELEDDITLLVLRV 191
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
118-315 2.86e-53

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 175.61  E-value: 2.86e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   118 LDKIEIGAISVPAHRVNGDYFNLIDHKDGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQL-PSDGLKRLNRVVEKN 196
Cdd:smart00331   1 DDGGLIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGIsLSQILERLNRAIYEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   197 VNQNMFVTMFYGLYEEVNNKFYYASAGHEPGHIYRSKTDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVS 276
Cdd:smart00331  81 GEDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLT 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 222151975   277 EIRKLDggfintnELLSLIGKYKDLHPQDIVQIVYEELL 315
Cdd:smart00331 161 EARNPE-------RLEELLEELLGSPPAEIAQRILEELL 192
RsbU_N pfam08673
Phosphoserine phosphatase RsbU, N-terminal domain; RsbU is a phosphoserine phosphatase which ...
10-83 1.49e-13

Phosphoserine phosphatase RsbU, N-terminal domain; RsbU is a phosphoserine phosphatase which acts as a positive regulator of the general stress-response factor of gram positive organisms, sigma-B. The phosphatase activity of RsbU is stimulated by association with the RsbT kinase. Deletions in the N terminal domain are deleterious to the activity of RsbU.


Pssm-ID: 254966  Cd Length: 77  Bit Score: 64.98  E-value: 1.49e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222151975   10 RYIDILETYITTRDEKALEPLQALSFEAIELDISPEEIVMLHKDLINEKSYSGIEQ-QYGMDVLTEMIIGFGFTY 83
Cdd:pfam08673   3 QYKRLLDEYLASQDEQSLYKAEKFSRELIEKDISPEEIVSIHKSYLEELNPDLPEDvLDSFDFLLEVMVGYGLAY 77
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
9-335 3.19e-73

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 233.06  E-value: 3.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   9 SRYIDILETYIT----TRDEKALEPLQALS-FEAIELDISPEEIVMLHK----DLINEKSYSGIEQQYGMDVLTEMIIGF 79
Cdd:COG2208   28 GLYAQISAEPLTemffLQTEKGLRQAELLYeINDILERFLPVEVLLGVSgklrALSEEIKHWRGGLPLVAELLVEINRAV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  80 GFTYRDYKALVKVMEAHDKEMDVAASLQSTMLKTKVPHLDKIEIGAISVPAHRVNGDYFNLIDHKDGTMSFAVADVIGKG 159
Cdd:COG2208  108 GLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKRLRIGIGDVSGKG 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975 160 IPAALAMSMIKFGMDSYGHSQL--PSDGLKRLNRVVEKNVNQNMFVTMFYGLYEEVNNKFYYASAGHEPGHIYRSKTDS- 236
Cdd:COG2208  188 VPAALLMLMPKLALRLLLESGPldPADVLETLNRVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIe 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975 237 FEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVSEIRKLDGGFINTNELLSLIGKYKDLHPQDIVQIVYEELLK 316
Cdd:COG2208  268 VEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQPAEEILEAILESLEE 347
                        330       340
                 ....*....|....*....|
gi 222151975 317 -IGDPKKKDDLTILIIKRIK 335
Cdd:COG2208  348 lQGDQIQDDDITLLVLKVKK 367
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
132-332 4.80e-07

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: 50.08  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  132 RVNGDYFNLIDHKDGTMSFAVADVIGKGIPAA--------LAMSMIKFGMDsyghsqlPSDGLKRLNRVVEKNVNQNMFV 203
Cdd:TIGR02865 565 LVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAqessacvrLLEKFLESGFD-------REVAIKTVNSILSLRSTDEKFS 637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  204 T---MFYGLYEEvNNKFYyaSAGHEPGHIYRSktDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVseirk 280
Cdd:TIGR02865 638 TldlSVIDLYTG-QAEFV--KVGAVPSFIKRG--AKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGV----- 707
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 222151975  281 LDGGFINTNELLSLIGKYK---DLHPQDIVQIVYEELLKIGDPKKKDDLTILIIK 332
Cdd:TIGR02865 708 LEGEKEVEGKVLWLVRKLKetnTNDPEEIAEYLLEKAKELRSGKIKDDMTVIVAK 762
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
145-333 1.30e-58

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: 189.42  E-value: 1.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  145 DGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQL-PSDGLKRLNRVVEKNVNQNMFVTMFYGLYEEVNNKFYYASAG 223
Cdd:pfam07228   2 DGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLdPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  224 HEPGHIYRSKTDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVSEIRKLDGGFINTNELLSLIGKYKDLHP 303
Cdd:pfam07228  82 HPPPLLLRPDGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHGLSP 161
                         170       180       190
                  ....*....|....*....|....*....|
gi 222151975  304 QDIVQIVYEELLKIGDPKKKDDLTILIIKR 333
Cdd:pfam07228 162 EELLDALLEDLLRLGGGELEDDITLLVLRV 191
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
118-315 2.86e-53

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 175.61  E-value: 2.86e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   118 LDKIEIGAISVPAHRVNGDYFNLIDHKDGTMSFAVADVIGKGIPAALAMSMIKFGMDSYGHSQL-PSDGLKRLNRVVEKN 196
Cdd:smart00331   1 DDGGLIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGIsLSQILERLNRAIYEN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   197 VNQNMFVTMFYGLYEEVNNKFYYASAGHEPGHIYRSKTDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVS 276
Cdd:smart00331  81 GEDGMFATLFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLT 160
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 222151975   277 EIRKLDggfintnELLSLIGKYKDLHPQDIVQIVYEELL 315
Cdd:smart00331 161 EARNPE-------RLEELLEELLGSPPAEIAQRILEELL 192
RsbU_N pfam08673
Phosphoserine phosphatase RsbU, N-terminal domain; RsbU is a phosphoserine phosphatase which ...
10-83 1.49e-13

Phosphoserine phosphatase RsbU, N-terminal domain; RsbU is a phosphoserine phosphatase which acts as a positive regulator of the general stress-response factor of gram positive organisms, sigma-B. The phosphatase activity of RsbU is stimulated by association with the RsbT kinase. Deletions in the N terminal domain are deleterious to the activity of RsbU.


Pssm-ID: 254966  Cd Length: 77  Bit Score: 64.98  E-value: 1.49e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 222151975   10 RYIDILETYITTRDEKALEPLQALSFEAIELDISPEEIVMLHKDLINEKSYSGIEQ-QYGMDVLTEMIIGFGFTY 83
Cdd:pfam08673   3 QYKRLLDEYLASQDEQSLYKAEKFSRELIEKDISPEEIVSIHKSYLEELNPDLPEDvLDSFDFLLEVMVGYGLAY 77
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
9-335 3.19e-73

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 233.06  E-value: 3.19e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975   9 SRYIDILETYIT----TRDEKALEPLQALS-FEAIELDISPEEIVMLHK----DLINEKSYSGIEQQYGMDVLTEMIIGF 79
Cdd:COG2208   28 GLYAQISAEPLTemffLQTEKGLRQAELLYeINDILERFLPVEVLLGVSgklrALSEEIKHWRGGLPLVAELLVEINRAV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  80 GFTYRDYKALVKVMEAHDKEMDVAASLQSTMLKTKVPHLDKIEIGAISVPAHRVNGDYFNLIDHKDGTMSFAVADVIGKG 159
Cdd:COG2208  108 GLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKRLRIGIGDVSGKG 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975 160 IPAALAMSMIKFGMDSYGHSQL--PSDGLKRLNRVVEKNVNQNMFVTMFYGLYEEVNNKFYYASAGHEPGHIYRSKTDS- 236
Cdd:COG2208  188 VPAALLMLMPKLALRLLLESGPldPADVLETLNRVLKQNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIe 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975 237 FEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVSEIRKLDGGFINTNELLSLIGKYKDLHPQDIVQIVYEELLK 316
Cdd:COG2208  268 VEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQPAEEILEAILESLEE 347
                        330       340
                 ....*....|....*....|
gi 222151975 317 -IGDPKKKDDLTILIIKRIK 335
Cdd:COG2208  348 lQGDQIQDDDITLLVLKVKK 367
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
132-332 4.80e-07

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: 50.08  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  132 RVNGDYFNLIDHKDGTMSFAVADVIGKGIPAA--------LAMSMIKFGMDsyghsqlPSDGLKRLNRVVEKNVNQNMFV 203
Cdd:TIGR02865 565 LVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAqessacvrLLEKFLESGFD-------REVAIKTVNSILSLRSTDEKFS 637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 222151975  204 T---MFYGLYEEvNNKFYyaSAGHEPGHIYRSktDSFEELSARGLVLGIHPSTRYDQEEIDIEIGDMVIVFTDGVseirk 280
Cdd:TIGR02865 638 TldlSVIDLYTG-QAEFV--KVGAVPSFIKRG--AKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGV----- 707
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 222151975  281 LDGGFINTNELLSLIGKYK---DLHPQDIVQIVYEELLKIGDPKKKDDLTILIIK 332
Cdd:TIGR02865 708 LEGEKEVEGKVLWLVRKLKetnTNDPEEIAEYLLEKAKELRSGKIKDDMTVIVAK 762
 
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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