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Conserved domains on  [gi|161507727|ref|YP_001577688|]
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protein serine-threonine phosphatase [Lactobacillus helveticus DPC 4571]

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List of domain hits

Name Accession Description Interval E-value
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
5-240 6.97e-59

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: 189.46  E-value: 6.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   5 AYASSIGKVRKSNQDFVQVFENR--EGVTLAIVCDGMGGHQGGDVASTMAVTHLGHNFGMTDFTDANIARKWLDVQLNSE 82
Cdd:cd00143    3 AGVSDKGGDRKTNEDAVVIKPNLnnEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLSEEDIEEALRKAFLRA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  83 NEIILKTADKFPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNELVKmGQITKE----QAKHH 158
Cdd:cd00143   83 DEEILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEER-ERIEKAggrvSNGRV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 159 PQKNIITQALGVSS-----TIDPEIKEIKLDEND-IILLCTDGLTNSLSDPQIQQILAT--KELSLKERCNKLISESNRL 230
Cdd:cd00143  162 PGVLAVTRALGDFDlkpgvSAEPDVTVVKLTEDDdFLILASDGLWDVLSNQEAVDIVRSelAKEDLQEAAQELVDLALRR 241
                        250
                 ....*....|
gi 161507727 231 GGGDNITVCL 240
Cdd:cd00143  242 GSHDNITVVV 251
 
Name Accession Description Interval E-value
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
5-240 6.97e-59

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: 189.46  E-value: 6.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   5 AYASSIGKVRKSNQDFVQVFENR--EGVTLAIVCDGMGGHQGGDVASTMAVTHLGHNFGMTDFTDANIARKWLDVQLNSE 82
Cdd:cd00143    3 AGVSDKGGDRKTNEDAVVIKPNLnnEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLSEEDIEEALRKAFLRA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  83 NEIILKTADKFPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNELVKmGQITKE----QAKHH 158
Cdd:cd00143   83 DEEILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEER-ERIEKAggrvSNGRV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 159 PQKNIITQALGVSS-----TIDPEIKEIKLDEND-IILLCTDGLTNSLSDPQIQQILAT--KELSLKERCNKLISESNRL 230
Cdd:cd00143  162 PGVLAVTRALGDFDlkpgvSAEPDVTVVKLTEDDdFLILASDGLWDVLSNQEAVDIVRSelAKEDLQEAAQELVDLALRR 241
                        250
                 ....*....|
gi 161507727 231 GGGDNITVCL 240
Cdd:cd00143  242 GSHDNITVVV 251
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
1-240 2.27e-80

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 244.96  E-value: 2.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   1 MIETAYASSIGKVRKSNQDFVQVFENR--EGVTLAIVCDGMGGHQGGDVASTMAVTHLGHNFGMTDFTDAN-IARKWLDV 77
Cdd:COG0631    7 SLKVAGLSDVGTVRKHNEDAFLIKPNEngNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNeSLEELLKE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  78 QLNSENEIILKTADKFPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNELVKMGQITKEQAKH 157
Cdd:COG0631   87 AILKANEAIAEEGQLNEDVRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNRLEQRGIITPEEARS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 158 HPQKNIITQALGVSSTIDPEIKEIKLDENDIILLCTDGLTNSLSDPQIQQILaTKELSLKERCNKLISESNRLGGGDNIT 237
Cdd:COG0631  167 HPRRNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDIL-KNSETPQEAADKLIELALEGGGPDNIT 245

                 ...
gi 161507727 238 VCL 240
Cdd:COG0631  246 VVL 248
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
8-240 2.12e-38

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: 135.97  E-value: 2.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727     8 SSIGKVRKSNQDFVQV-FENREGVTLAIVCDGMGGHQggdvASTMAVTHLGHNFGMTDFTDANIARKWLDVqLNsenEII 86
Cdd:smart00332  14 SSMQGVRKPMEDAHVItPDLSDSGGFFGVFDGHGGSE----AAKFLSKNLPEILAEELIKEKDELEDVEEA-LR---KAF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727    87 LKTADKF--PDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNElVKMGQITKEQAKHHPQKNI- 163
Cdd:smart00332  86 LSTDEEIleELEALSGSTAVVALISGNKLYVANVGDSRAVLCRNGKAVQLTEDHKPSNE-DERARIEAAGGFVINGRVNg 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   164 ---ITQALGVSS-----TIDPEIKEIKL-DENDIILLCTDGLTNSLSDPQIQQIL-ATKELSLKERCNKLISESNRLGGG 233
Cdd:smart00332 165 vlaLSRAIGDFFlkpyvSAEPDVTVVELtEKDDFLILASDGLWDVLSNQEVVDIVrKHLSKDPKEAAKRLIDLALARGSK 244

                   ....*..
gi 161507727   234 DNITVCL 240
Cdd:smart00332 245 DNITVVV 251
PP2C pfam00481
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
35-236 2.03e-22

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 249892  Cd Length: 253  Bit Score: 92.43  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   35 VCDGMGGHQGGDVASTMAVTHLGHNFgmtDFTDANIARKWLDVQLNSENEIILKTADKFPDLNgMGTTIVLAFAFKDNAL 114
Cdd:pfam00481  39 VFDGHGGSEAAKYAGKHLHTILALRR---SFLTLRKLEDALRESFLETDEELRSDAANHEDLS-SGSTAVVALIRGNKLY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  115 IAHLGDSRAY-SYSEGKFVQLTEDHSLVNELvKMGQITKEQAKHHPQkNIITQALGVSSTI--------------DPEIK 179
Cdd:pfam00481 115 VANVGDSRAVlCRNGGAIKQLTEDHKPSDED-ERRRIRAAGGFVSRN-GRVNGVLAVSRAFgdfdlkpgeqpvsaEPDIT 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161507727  180 EIKLDEND-IILLCTDGLTNSLSDPQIQQIL---ATKELSLKERCNKLISESNRLGGGDNI 236
Cdd:pfam00481 193 SHKITEDDeFLILACDGLWDVLSDQEVVDIVrsnLSDGGDPMEAAEKLVDEAIAYGSEDNI 253
PRK14559 PRK14559
putative protein serine/threonine phosphatase; Provisional
2-240 3.62e-34

putative protein serine/threonine phosphatase; Provisional


Pssm-ID: 237756 [Multi-domain]  Cd Length: 645  Bit Score: 129.41  E-value: 3.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   2 IETAYASSIGKVRKSNQDF------VQVFENREGVT-----LAIVCDGMGGHQGGDVASTMAVTHLGHNFGM---TDFTD 67
Cdd:PRK14559 375 LEDAGRTDVGRQRHHNEDYfgintrIQKLENPHGRIvqargLYILCDGMGGHAAGEVASALAVETLQQYFQQhwqDELPD 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  68 ANIARKwldvQLNSENEIILKTADK--FPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYS-EGKFVQLTEDHSLVNEL 144
Cdd:PRK14559 455 EETIRE----AIYLANEAIYDLNQQnaRSGSGRMGTTLVMALVQDTQVAVAHVGDSRLYRVTrKGGLEQLTVDHEVGQRE 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 145 VKMGqITKEQAKHHPQKNIITQALGV--SSTIDPEIKEIKLDENDIILLCTDGLT-NSLSDPQIQQILA---TKELSLKE 218
Cdd:PRK14559 531 IQRG-VEPQIAYARPDAYQLTQALGPrdNSAIQPDIQFLEIEEDTLLLLCSDGLSdNDLLETHWQTHLLpllSSSANLDQ 609
                        250       260
                 ....*....|....*....|..
gi 161507727 219 RCNKLISESNRLGGGDNITVCL 240
Cdd:PRK14559 610 GLNKLIDLANQYNGHDNITAIL 631
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
148-238 5.99e-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: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 39.29  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  148 GQITKEQAKHHPqkniitqaLGVSSTIDPEIKEIKLDENDIILLCTDGLTNSLSDPQ------IQQILATKELSLKERCN 221
Cdd:TIGR02865 667 AKVEVIRSSNLP--------IGILDEVDVELVRKKLKNGDLIVMVSDGVLEGEKEVEgkvlwlVRKLKETNTNDPEEIAE 738
                          90       100
                  ....*....|....*....|
gi 161507727  222 KLISESNRLGGG---DNITV 238
Cdd:TIGR02865 739 YLLEKAKELRSGkikDDMTV 758
 
Name Accession Description Interval E-value
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
5-240 6.97e-59

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: 189.46  E-value: 6.97e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   5 AYASSIGKVRKSNQDFVQVFENR--EGVTLAIVCDGMGGHQGGDVASTMAVTHLGHNFGMTDFTDANIARKWLDVQLNSE 82
Cdd:cd00143    3 AGVSDKGGDRKTNEDAVVIKPNLnnEDGGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLTLSEEDIEEALRKAFLRA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  83 NEIILKTADKFPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNELVKmGQITKE----QAKHH 158
Cdd:cd00143   83 DEEILEEAQDEPDDARSGTTAVVALIRGNKLYVANVGDSRAVLCRNGEAVQLTKDHKPVNEEER-ERIEKAggrvSNGRV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 159 PQKNIITQALGVSS-----TIDPEIKEIKLDEND-IILLCTDGLTNSLSDPQIQQILAT--KELSLKERCNKLISESNRL 230
Cdd:cd00143  162 PGVLAVTRALGDFDlkpgvSAEPDVTVVKLTEDDdFLILASDGLWDVLSNQEAVDIVRSelAKEDLQEAAQELVDLALRR 241
                        250
                 ....*....|
gi 161507727 231 GGGDNITVCL 240
Cdd:cd00143  242 GSHDNITVVV 251
PTC1 COG0631
Serine/threonine protein phosphatase [Signal transduction mechanisms]
1-240 2.27e-80

Serine/threonine protein phosphatase [Signal transduction mechanisms]


Pssm-ID: 223704  Cd Length: 262  Bit Score: 244.96  E-value: 2.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   1 MIETAYASSIGKVRKSNQDFVQVFENR--EGVTLAIVCDGMGGHQGGDVASTMAVTHLGHNFGMTDFTDAN-IARKWLDV 77
Cdd:COG0631    7 SLKVAGLSDVGTVRKHNEDAFLIKPNEngNLLLLFAVADGMGGHAAGEVASKLAVEALARLFDETNFNSLNeSLEELLKE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  78 QLNSENEIILKTADKFPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNELVKMGQITKEQAKH 157
Cdd:COG0631   87 AILKANEAIAEEGQLNEDVRGMGTTLVLLLIRGNKLYVANVGDSRAYLLRDGELKQLTEDHSLVNRLEQRGIITPEEARS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 158 HPQKNIITQALGVSSTIDPEIKEIKLDENDIILLCTDGLTNSLSDPQIQQILaTKELSLKERCNKLISESNRLGGGDNIT 237
Cdd:COG0631  167 HPRRNALTRALGDFDLLEPDITELELEPGDFLLLCSDGLWDVVSDDEIVDIL-KNSETPQEAADKLIELALEGGGPDNIT 245

                 ...
gi 161507727 238 VCL 240
Cdd:COG0631  246 VVL 248
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
8-240 2.12e-38

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: 135.97  E-value: 2.12e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727     8 SSIGKVRKSNQDFVQV-FENREGVTLAIVCDGMGGHQggdvASTMAVTHLGHNFGMTDFTDANIARKWLDVqLNsenEII 86
Cdd:smart00332  14 SSMQGVRKPMEDAHVItPDLSDSGGFFGVFDGHGGSE----AAKFLSKNLPEILAEELIKEKDELEDVEEA-LR---KAF 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727    87 LKTADKF--PDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYSEGKFVQLTEDHSLVNElVKMGQITKEQAKHHPQKNI- 163
Cdd:smart00332  86 LSTDEEIleELEALSGSTAVVALISGNKLYVANVGDSRAVLCRNGKAVQLTEDHKPSNE-DERARIEAAGGFVINGRVNg 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   164 ---ITQALGVSS-----TIDPEIKEIKL-DENDIILLCTDGLTNSLSDPQIQQIL-ATKELSLKERCNKLISESNRLGGG 233
Cdd:smart00332 165 vlaLSRAIGDFFlkpyvSAEPDVTVVELtEKDDFLILASDGLWDVLSNQEVVDIVrKHLSKDPKEAAKRLIDLALARGSK 244

                   ....*..
gi 161507727   234 DNITVCL 240
Cdd:smart00332 245 DNITVVV 251
PP2C pfam00481
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
35-236 2.03e-22

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 249892  Cd Length: 253  Bit Score: 92.43  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   35 VCDGMGGHQGGDVASTMAVTHLGHNFgmtDFTDANIARKWLDVQLNSENEIILKTADKFPDLNgMGTTIVLAFAFKDNAL 114
Cdd:pfam00481  39 VFDGHGGSEAAKYAGKHLHTILALRR---SFLTLRKLEDALRESFLETDEELRSDAANHEDLS-SGSTAVVALIRGNKLY 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  115 IAHLGDSRAY-SYSEGKFVQLTEDHSLVNELvKMGQITKEQAKHHPQkNIITQALGVSSTI--------------DPEIK 179
Cdd:pfam00481 115 VANVGDSRAVlCRNGGAIKQLTEDHKPSDED-ERRRIRAAGGFVSRN-GRVNGVLAVSRAFgdfdlkpgeqpvsaEPDIT 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 161507727  180 EIKLDEND-IILLCTDGLTNSLSDPQIQQIL---ATKELSLKERCNKLISESNRLGGGDNI 236
Cdd:pfam00481 193 SHKITEDDeFLILACDGLWDVLSDQEVVDIVrsnLSDGGDPMEAAEKLVDEAIAYGSEDNI 253
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
19-209 7.38e-17

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 75.08  E-value: 7.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727    19 DFVQVFENREGVTLAIVCDGMGGHQGGDVASTMAVTHLGHnfgmtdftdaniarkwlDVQLNSENEIILKTADKFPDLN- 97
Cdd:smart00331  19 DFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRT-----------------LLSEGISLSQILERLNRAIYENg 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727    98 --GMGTTIVLA-FAFK-DNALIAHLGDSRAYSY-SEGKFVQLTEDhslvnelvkmgqitkeqakhhpqkniITQALGVSS 172
Cdd:smart00331  82 edGMFATLFLAlYDFAgGTLSYANAGHSPPYLLrADGGLVEDLDD--------------------------LGAPLGLEP 135
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 161507727   173 TIDPEIKEIKLDENDIILLCTDGLTNSLSDPQIQQIL 209
Cdd:smart00331 136 DVEVDVRELTLEPGDLLLLYTDGLTEARNPERLEELL 172
PP2C_2 pfam13672
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
12-204 8.14e-16

Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.


Pssm-ID: 257978  Cd Length: 210  Bit Score: 72.34  E-value: 8.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   12 KVRKSNQDFVQVFENREGVtLAIVCDGMGGHQGGDVASTMAVTHLGHNF-----GMTDFTDANIARKWLDVQLNSENEII 86
Cdd:pfam13672   7 RRGLPCQDAFAYRVLSDGW-LIAVADGAGSAKYSDVGARLAVEAAVEALrelldSGELPELEALVRQILNDILALVRQEA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   87 LKTADKFPDLngmGTTIVLAFAFKDNALIAHLGDSR-AYSYSEGKFVQLTEDHS--LVNELVKmgqITKEQAKHHPQkni 163
Cdd:pfam13672  86 AAQGLEPRDY---ATTLLLAVITPGGIVFFQIGDGAiVVRDRDGELQLLSEPDSgeYANETTF---LTSPDALEEFR--- 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 161507727  164 itqalgvsstidpeIKEIKLDENDIILLCTDGLTNSLSDPQ 204
Cdd:pfam13672 157 --------------IRRLTLEPGDALALMTDGLSDSLVTEE 183
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
167-240 2.20e-06

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: 45.74  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  167 ALGVSSTIDPEIKEIKLDENDIILLCTDGLTNSLS--------DPQIQQILATKELSLKERCNKLISESNRLGGG---DN 235
Cdd:pfam07228 104 PLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDpdgelfglERLLALLAERHGLSPEELLDALLEDLLRLGGGeleDD 183

                  ....*
gi 161507727  236 ITVCL 240
Cdd:pfam07228 184 ITLLV 188
PRK14559 PRK14559
putative protein serine/threonine phosphatase; Provisional
2-240 3.62e-34

putative protein serine/threonine phosphatase; Provisional


Pssm-ID: 237756 [Multi-domain]  Cd Length: 645  Bit Score: 129.41  E-value: 3.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727   2 IETAYASSIGKVRKSNQDF------VQVFENREGVT-----LAIVCDGMGGHQGGDVASTMAVTHLGHNFGM---TDFTD 67
Cdd:PRK14559 375 LEDAGRTDVGRQRHHNEDYfgintrIQKLENPHGRIvqargLYILCDGMGGHAAGEVASALAVETLQQYFQQhwqDELPD 454
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  68 ANIARKwldvQLNSENEIILKTADK--FPDLNGMGTTIVLAFAFKDNALIAHLGDSRAYSYS-EGKFVQLTEDHSLVNEL 144
Cdd:PRK14559 455 EETIRE----AIYLANEAIYDLNQQnaRSGSGRMGTTLVMALVQDTQVAVAHVGDSRLYRVTrKGGLEQLTVDHEVGQRE 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727 145 VKMGqITKEQAKHHPQKNIITQALGV--SSTIDPEIKEIKLDENDIILLCTDGLT-NSLSDPQIQQILA---TKELSLKE 218
Cdd:PRK14559 531 IQRG-VEPQIAYARPDAYQLTQALGPrdNSAIQPDIQFLEIEEDTLLLLCSDGLSdNDLLETHWQTHLLpllSSSANLDQ 609
                        250       260
                 ....*....|....*....|..
gi 161507727 219 RCNKLISESNRLGGGDNITVCL 240
Cdd:PRK14559 610 GLNKLIDLANQYNGHDNITAIL 631
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
148-238 5.99e-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: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 39.29  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161507727  148 GQITKEQAKHHPqkniitqaLGVSSTIDPEIKEIKLDENDIILLCTDGLTNSLSDPQ------IQQILATKELSLKERCN 221
Cdd:TIGR02865 667 AKVEVIRSSNLP--------IGILDEVDVELVRKKLKNGDLIVMVSDGVLEGEKEVEgkvlwlVRKLKETNTNDPEEIAE 738
                          90       100
                  ....*....|....*....|
gi 161507727  222 KLISESNRLGGG---DNITV 238
Cdd:TIGR02865 739 YLLEKAKELRSGkikDDMTV 758
6PF1K_euk TIGR02478
6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one ...
135-175 5.99e-04

6-phosphofructokinase, eukaryotic type; Members of this family are eukaryotic (with one exception) ATP-dependent 6-phosphofructokinases (EC 2.7.1.11) in which two tandem copies of the phosphofructokinase are found. Members are found, often including several isozymes, in animals and fungi and in the bacterium Propionibacterium acnes KPA171202 (a human skin commensal).


Pssm-ID: 233884 [Multi-domain]  Cd Length: 746  Bit Score: 39.24  E-value: 5.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 161507727  135 TEDHSLVNELVKMGQITKEQAKHHPQKNIItqalGVSSTID 175
Cdd:TIGR02478 115 EEWPSLLEELVDTGKITAEQAEEHRHLTIV----GLVGSID 151
 
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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