NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|160878298|ref|YP_001557266|]
View 

protein serine/threonine phosphatase [Lachnoclostridium phytofermentans ISDg]

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
339-521 4.03e-28

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: 110.46  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  339 DSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEPAIKLINSVLVLRTENCMSSTVDLCVVNLCAGTCEFVKI 418
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  419 GAATTFIKRDH--FVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDKEGY---FINFIKNIPFKS 493
Cdd:pfam07228  81 GHPPPLLLRPDggVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGlerLLALLAERHGLS 160
                         170       180
                  ....*....|....*....|....*...
gi 160878298  494 PQEIANAILSAALEKHGYVPADDMTVLV 521
Cdd:pfam07228 161 PEELLDALLEDLLRLGGGELEDDITLLV 188
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
60-525 2.06e-102

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: 327.03  E-value: 2.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   60 DNGESYVkDEFQNTARKKLEGISGSIHKLASSF-DYMASPKTVLNTEDMQLVLEDISTNLCKNCKKCGVCWERNFNQSYQ 138
Cdd:TIGR02865 299 DLQEDYM-RKVREIAAEKLEEFSEVFRELSNTFvEALASNEKLTMKRKSSYLLENLAERVCQSCNMKHRCWKREFDYTYS 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  139 ATWNLLETAKGKGNVTvDDMPDMLRLQCIQVPEFVEEANRNLSMARLKMVWHNRIVESREAVAGQLGEIARIVKDFSGNL 218
Cdd:TIGR02865 378 AMEELIENLEEKKDPN-SKLPDEFERKCIKRKELINTTEDILNNYIINEMWRKRLEEGRRLVAEQLKGVAESVEDIAKEI 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  219 CDTGEVIELKRRKINQKLRVHRIKVQRVLMFERENRGM--ELHLRARCKNGRCLttKEAAILIGNALERRFVPREDSRNV 296
Cdd:TIGR02865 457 NLEIVFHQLLEEKIIRALNKNGIPYEDVLAYNTEGGNIdvELTIAACGGRGECE--KKIAPIISEVTGELMCVKDERCSI 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  297 IGREYDDYVFCEDANFKVLTGVSRASKKKGELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGF 376
Cdd:TIGR02865 535 DPKGRCHLTFEETPKYHVSTGVARAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGF 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  377 REEPAIKLINSVLVLRTENCMSSTVDLCVVNLCAGTCEFVKIGAATTFIKRDHFVETISSNSMPAGILNRVDYDTKSKKL 456
Cdd:TIGR02865 615 DREVAIKTVNSILSLRSTDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKL 694
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  457 YDGDYVIMVSDGVIDCVEE-EDKEGYFINFIKNIPFKSPQEIANAILSAALEKHGYVPADDMTVLVTGIW 525
Cdd:TIGR02865 695 KNGDLIVMVSDGVLEGEKEvEGKVLWLVRKLKETNTNDPEEIAEYLLEKAKELRSGKIKDDMTVIVAKVY 764
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
339-521 4.03e-28

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: 110.46  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  339 DSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEPAIKLINSVLVLRTENCMSSTVDLCVVNLCAGTCEFVKI 418
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  419 GAATTFIKRDH--FVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDKEGY---FINFIKNIPFKS 493
Cdd:pfam07228  81 GHPPPLLLRPDggVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGlerLLALLAERHGLS 160
                         170       180
                  ....*....|....*....|....*...
gi 160878298  494 PQEIANAILSAALEKHGYVPADDMTVLV 521
Cdd:pfam07228 161 PEELLDALLEDLLRLGGGELEDDITLLV 188
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
327-507 7.62e-24

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 98.57  E-value: 7.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   327 ELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEPAIKLINSVLVLRTENCMSSTVDLCVV 406
Cdd:smart00331  15 QVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGEDGMFATLFLALY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   407 NLCAGTCEFVKIGAATTFIKR--DHFVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDKEGYFIN 484
Cdd:smart00331  95 DFAGGTLSYANAGHSPPYLLRadGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARNPERLEELLEE 174
                          170       180
                   ....*....|....*....|...
gi 160878298   485 FIKNipfkSPQEIANAILSAALE 507
Cdd:smart00331 175 LLGS----PPAEIAQRILEELLE 193
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
329-521 9.21e-10

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 58.14  E-value: 9.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 329 NGDNFSFLYPDSQDVVMMLS--DGMGSGSEAYEESEMVIELLEQFLEAGFREEP----------AIKLINSVLVLRTEN- 395
Cdd:COG0631   23 NEDAFLIKPNENGNLLLLFAvaDGMGGHAAGEVASKLAVEALARLFDETNFNSLnesleellkeAILKANEAIAEEGQLn 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 396 ----CMSSTVDLCVVN------LCAGTCEFVKI--GAATTfIKRDH-FVETISSN---------SMP-AGILNR------ 446
Cdd:COG0631  103 edvrGMGTTLVLLLIRgnklyvANVGDSRAYLLrdGELKQ-LTEDHsLVNRLEQRgiitpeearSHPrRNALTRalgdfd 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160878298 447 -VDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDkegyFINFIKNipFKSPQEIANAILSAALEKHGYvpaDDMTVLV 521
Cdd:COG0631  182 lLEPDITELELEPGDFLLLCSDGLWDVVSDDE----IVDILKN--SETPQEAADKLIELALEGGGP---DNITVVL 248
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
458-521 3.05e-05

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 44.24  E-value: 3.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160878298 458 DGDYVIMVSDGVIDCVEEEDkegyFINFIKNIPFK-SPQEIANAILSAALEKHGyvpADDMTVLV 521
Cdd:cd00143  194 DDDFLILASDGLWDVLSNQE----AVDIVRSELAKeDLQEAAQELVDLALRRGS---HDNITVVV 251
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
60-525 2.06e-102

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: 327.03  E-value: 2.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   60 DNGESYVkDEFQNTARKKLEGISGSIHKLASSF-DYMASPKTVLNTEDMQLVLEDISTNLCKNCKKCGVCWERNFNQSYQ 138
Cdd:TIGR02865 299 DLQEDYM-RKVREIAAEKLEEFSEVFRELSNTFvEALASNEKLTMKRKSSYLLENLAERVCQSCNMKHRCWKREFDYTYS 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  139 ATWNLLETAKGKGNVTvDDMPDMLRLQCIQVPEFVEEANRNLSMARLKMVWHNRIVESREAVAGQLGEIARIVKDFSGNL 218
Cdd:TIGR02865 378 AMEELIENLEEKKDPN-SKLPDEFERKCIKRKELINTTEDILNNYIINEMWRKRLEEGRRLVAEQLKGVAESVEDIAKEI 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  219 CDTGEVIELKRRKINQKLRVHRIKVQRVLMFERENRGM--ELHLRARCKNGRCLttKEAAILIGNALERRFVPREDSRNV 296
Cdd:TIGR02865 457 NLEIVFHQLLEEKIIRALNKNGIPYEDVLAYNTEGGNIdvELTIAACGGRGECE--KKIAPIISEVTGELMCVKDERCSI 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  297 IGREYDDYVFCEDANFKVLTGVSRASKKKGELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGF 376
Cdd:TIGR02865 535 DPKGRCHLTFEETPKYHVSTGVARAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGF 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  377 REEPAIKLINSVLVLRTENCMSSTVDLCVVNLCAGTCEFVKIGAATTFIKRDHFVETISSNSMPAGILNRVDYDTKSKKL 456
Cdd:TIGR02865 615 DREVAIKTVNSILSLRSTDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKL 694
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  457 YDGDYVIMVSDGVIDCVEE-EDKEGYFINFIKNIPFKSPQEIANAILSAALEKHGYVPADDMTVLVTGIW 525
Cdd:TIGR02865 695 KNGDLIVMVSDGVLEGEKEvEGKVLWLVRKLKETNTNDPEEIAEYLLEKAKELRSGKIKDDMTVIVAKVY 764
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
327-521 7.19e-25

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 104.79  E-value: 7.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 327 ELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEP-AIKLINSVLVLRTENCMSSTVDLCV 405
Cdd:COG2208  160 EVGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPLDPAdVLETLNRVLKQNLEEDMFVTLFLGV 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 406 VNLCAGTCEFVKIGAATTFIKRDH---FVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCveeEDKEGYF 482
Cdd:COG2208  240 YDLDSGELTYSNAGHEPALILSADgeiEVEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEA---RNSDGEF 316
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 160878298 483 INFIKNIP------FKSPQEIANAILSAALEKHGYVPA-DDMTVLV 521
Cdd:COG2208  317 FGLERLLKilgrllGQPAEEILEAILESLEELQGDQIQdDDITLLV 362
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
339-521 4.03e-28

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: 110.46  E-value: 4.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  339 DSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEPAIKLINSVLVLRTENCMSSTVDLCVVNLCAGTCEFVKI 418
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  419 GAATTFIKRDH--FVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDKEGY---FINFIKNIPFKS 493
Cdd:pfam07228  81 GHPPPLLLRPDggVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGlerLLALLAERHGLS 160
                         170       180
                  ....*....|....*....|....*...
gi 160878298  494 PQEIANAILSAALEKHGYVPADDMTVLV 521
Cdd:pfam07228 161 PEELLDALLEDLLRLGGGELEDDITLLV 188
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
327-507 7.62e-24

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 98.57  E-value: 7.62e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   327 ELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEPAIKLINSVLVLRTENCMSSTVDLCVV 406
Cdd:smart00331  15 QVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGEDGMFATLFLALY 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   407 NLCAGTCEFVKIGAATTFIKR--DHFVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDKEGYFIN 484
Cdd:smart00331  95 DFAGGTLSYANAGHSPPYLLRadGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARNPERLEELLEE 174
                          170       180
                   ....*....|....*....|...
gi 160878298   485 FIKNipfkSPQEIANAILSAALE 507
Cdd:smart00331 175 LLGS----PPAEIAQRILEELLE 193
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
329-521 9.21e-10

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 58.14  E-value: 9.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 329 NGDNFSFLYPDSQDVVMMLS--DGMGSGSEAYEESEMVIELLEQFLEAGFREEP----------AIKLINSVLVLRTEN- 395
Cdd:COG0631   23 NEDAFLIKPNENGNLLLLFAvaDGMGGHAAGEVASKLAVEALARLFDETNFNSLnesleellkeAILKANEAIAEEGQLn 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 396 ----CMSSTVDLCVVN------LCAGTCEFVKI--GAATTfIKRDH-FVETISSN---------SMP-AGILNR------ 446
Cdd:COG0631  103 edvrGMGTTLVLLLIRgnklyvANVGDSRAYLLrdGELKQ-LTEDHsLVNRLEQRgiitpeearSHPrRNALTRalgdfd 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160878298 447 -VDYDTKSKKLYDGDYVIMVSDGVIDCVEEEDkegyFINFIKNipFKSPQEIANAILSAALEKHGYvpaDDMTVLV 521
Cdd:COG0631  182 lLEPDITELELEPGDFLLLCSDGLWDVVSDDE----IVDILKN--SETPQEAADKLIELALEGGGP---DNITVVL 248
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
450-521 2.80e-07

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 214625  Cd Length: 252  Bit Score: 50.45  E-value: 2.80e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 160878298   450 DTKSKKLY-DGDYVIMVSDGVIDCVEEEDkegyFINFIKNIPFKSPQEIANAILSAALEKHGYvpaDDMTVLV 521
Cdd:smart00332 186 DVTVVELTeKDDFLILASDGLWDVLSNQE----VVDIVRKHLSKDPKEAAKRLIDLALARGSK---DNITVVV 251
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
458-521 3.05e-05

Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.


Pssm-ID: 238083  Cd Length: 254  Bit Score: 44.24  E-value: 3.05e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160878298 458 DGDYVIMVSDGVIDCVEEEDkegyFINFIKNIPFK-SPQEIANAILSAALEKHGyvpADDMTVLV 521
Cdd:cd00143  194 DDDFLILASDGLWDVLSNQE----AVDIVRSELAKeDLQEAAQELVDLALRRGS---HDNITVVV 251
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
60-525 2.06e-102

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: 327.03  E-value: 2.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298   60 DNGESYVkDEFQNTARKKLEGISGSIHKLASSF-DYMASPKTVLNTEDMQLVLEDISTNLCKNCKKCGVCWERNFNQSYQ 138
Cdd:TIGR02865 299 DLQEDYM-RKVREIAAEKLEEFSEVFRELSNTFvEALASNEKLTMKRKSSYLLENLAERVCQSCNMKHRCWKREFDYTYS 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  139 ATWNLLETAKGKGNVTvDDMPDMLRLQCIQVPEFVEEANRNLSMARLKMVWHNRIVESREAVAGQLGEIARIVKDFSGNL 218
Cdd:TIGR02865 378 AMEELIENLEEKKDPN-SKLPDEFERKCIKRKELINTTEDILNNYIINEMWRKRLEEGRRLVAEQLKGVAESVEDIAKEI 456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  219 CDTGEVIELKRRKINQKLRVHRIKVQRVLMFERENRGM--ELHLRARCKNGRCLttKEAAILIGNALERRFVPREDSRNV 296
Cdd:TIGR02865 457 NLEIVFHQLLEEKIIRALNKNGIPYEDVLAYNTEGGNIdvELTIAACGGRGECE--KKIAPIISEVTGELMCVKDERCSI 534
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  297 IGREYDDYVFCEDANFKVLTGVSRASKKKGELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGF 376
Cdd:TIGR02865 535 DPKGRCHLTFEETPKYHVSTGVARAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGF 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  377 REEPAIKLINSVLVLRTENCMSSTVDLCVVNLCAGTCEFVKIGAATTFIKRDHFVETISSNSMPAGILNRVDYDTKSKKL 456
Cdd:TIGR02865 615 DREVAIKTVNSILSLRSTDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKL 694
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298  457 YDGDYVIMVSDGVIDCVEE-EDKEGYFINFIKNIPFKSPQEIANAILSAALEKHGYVPADDMTVLVTGIW 525
Cdd:TIGR02865 695 KNGDLIVMVSDGVLEGEKEvEGKVLWLVRKLKETNTNDPEEIAEYLLEKAKELRSGKIKDDMTVIVAKVY 764
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
327-521 7.19e-25

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 104.79  E-value: 7.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 327 ELNGDNFSFLYPDSQDVVMMLSDGMGSGSEAYEESEMVIELLEQFLEAGFREEP-AIKLINSVLVLRTENCMSSTVDLCV 405
Cdd:COG2208  160 EVGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPKLALRLLLESGPLDPAdVLETLNRVLKQNLEEDMFVTLFLGV 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160878298 406 VNLCAGTCEFVKIGAATTFIKRDH---FVETISSNSMPAGILNRVDYDTKSKKLYDGDYVIMVSDGVIDCveeEDKEGYF 482
Cdd:COG2208  240 YDLDSGELTYSNAGHEPALILSADgeiEVEDLTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEA---RNSDGEF 316
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 160878298 483 INFIKNIP------FKSPQEIANAILSAALEKHGYVPA-DDMTVLV 521
Cdd:COG2208  317 FGLERLLKilgrllGQPAEEILEAILESLEELQGDQIQdDDITLLV 362
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH