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Conserved domains on  [gi|154199605|ref|NP_011943|]
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type 2C protein phosphatase PTC7 [Saccharomyces cerevisiae S288C]

Protein Classification

PP2C family serine/threonine-protein phosphatase( domain architecture ID 10646350)

PP2C family protein-serine/threonine phosphatase catalyzes the dephosphorylation of phosphoserine and phosphothreonine residues of specific protein substrates; similar to Bacillus subtilis phosphoserine phosphatase RsbX that is a negative regulator of sigma-B activity

CATH:  3.60.40.10
EC:  3.1.3.-
Gene Ontology:  GO:0004722
PubMed:  8819174|2549856
SCOP:  3000909

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
71-302 1.11e-29

Sigma factor PP2C-like phosphatases;


:

Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 112.44  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605    71 DRDDLIYQKLKDSIRSptGEDNYFVTSNNVHDIFAGVADGVGgwaeHGYDSSAISRELCKKMDEISTALAENSSketllT 150
Cdd:smart00331   1 DDGGLIAQYYEDATQV--GGDFYDVVKLPEGRLLIAIADVMG----KGLAAALAMSMARSALRTLLSEGISLSQ-----I 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605   151 PKKIIGAAYAKIRDEKvvkvgGTTAIVAHF-PSNGKLEVANLGDSWCGVFR-DSKLVFQTKFQTvgfnapYQLSIIPEEM 228
Cdd:smart00331  70 LERLNRAIYENGEDGM-----FATLFLALYdFAGGTLSYANAGHSPPYLLRaDGGLVEDLDDLG------APLGLEPDVE 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154199605   229 LkeaerrgskyilntprdaDEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNaarTNDELQLLSQKFVDNV 302
Cdd:smart00331 139 V------------------DVRELTLEPGDLLLLYTDGLTEARNPERLEELLEEL---LGSPPAEIAQRILEEL 191
 
Name Accession Description Interval E-value
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
71-302 1.11e-29

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 112.44  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605    71 DRDDLIYQKLKDSIRSptGEDNYFVTSNNVHDIFAGVADGVGgwaeHGYDSSAISRELCKKMDEISTALAENSSketllT 150
Cdd:smart00331   1 DDGGLIAQYYEDATQV--GGDFYDVVKLPEGRLLIAIADVMG----KGLAAALAMSMARSALRTLLSEGISLSQ-----I 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605   151 PKKIIGAAYAKIRDEKvvkvgGTTAIVAHF-PSNGKLEVANLGDSWCGVFR-DSKLVFQTKFQTvgfnapYQLSIIPEEM 228
Cdd:smart00331  70 LERLNRAIYENGEDGM-----FATLFLALYdFAGGTLSYANAGHSPPYLLRaDGGLVEDLDDLG------APLGLEPDVE 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154199605   229 LkeaerrgskyilntprdaDEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNaarTNDELQLLSQKFVDNV 302
Cdd:smart00331 139 V------------------DVRELTLEPGDLLLLYTDGLTEARNPERLEELLEEL---LGSPPAEIAQRILEEL 191
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
87-342 1.36e-28

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 [Multi-domain]  Cd Length: 254  Bit Score: 111.26  E-value: 1.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  87 PTGEDNYFVTSNNVHD--IFAGVADGVGGWAEHGYDSSAISRELCKKMDEISTaLAENSSKETLLTPKKIIGAAYA-KIR 163
Cdd:cd00143   13 KTNEDAVVIKPNLNNEdgGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLT-LSEEDIEEALRKAFLRADEEILeEAQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 164 DEKVVKVGGTTAIVAHFpSNGKLEVANLGDSWCGVFRDSKLVFQTK----FQTVGFNAPYQLSIIPE-----EMLKEAER 234
Cdd:cd00143   92 DEPDDARSGTTAVVALI-RGNKLYVANVGDSRAVLCRNGEAVQLTKdhkpVNEEERERIEKAGGRVSngrvpGVLAVTRA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 235 RGSK----YILNTPrdaDEYSFQLKKKD-IIILATDGVTDNIATDDIELFLKDNAARTNdeLQLLSQKFVDNVVslskdp 309
Cdd:cd00143  171 LGDFdlkpGVSAEP---DVTVVKLTEDDdFLILASDGLWDVLSNQEAVDIVRSELAKED--LQEAAQELVDLAL------ 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 154199605 310 nypsvfaqeiskltgknySGGKEDDITVVVVRV 342
Cdd:cd00143  240 ------------------RRGSHDNITVVVVRL 254
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
90-343 3.75e-16

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 440396 [Multi-domain]  Cd Length: 247  Bit Score: 76.79  E-value: 3.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  90 EDNYFVTSNNVHDIFAgVADGVGGwAEHGydssAI-SRELCKKMDEISTALAENSSKETLLTPKKIIGAAYAKIRDEKVV 168
Cdd:COG0631   17 EDAFLVALDPGGGLFV-VADGMGG-HAAG----EVaSRLAVETLAELFQEALAPDPEDLEEALREAIRAANRAILELAQE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 169 KVG----GTTAIVAHFpSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVGfNAPYQLSIIPEEmlkEAERRGSKYIL--- 241
Cdd:COG0631   91 DPElagmGTTLVAALI-AGGRLYIAHVGDSRAYLLRDGELEQLTRDHSLV-QELVDAGRITPE---EARTHPQRNVLtra 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 242 ---NTPRDADEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNAArtndelqllSQKFVDNVVSLSKDpnypsvfaqe 318
Cdd:COG0631  166 lgtDDDVEPDISPLELEPGDRLLLCSDGLTDMVSDEEIAEILASAGD---------PQEAAEALIELALE---------- 226
                        250       260
                 ....*....|....*....|....*
gi 154199605 319 iskltgknysGGKEDDITVVVVRVD 343
Cdd:COG0631  227 ----------AGGPDNITVVLVRVE 241
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
101-343 1.49e-15

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: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 73.83  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  101 HDIFAGVADGVGgwaeHGYDSSAISRELCkkmDEISTALAENSSKETLLtpKKIIGAAYAKIRDEKVVkvggtTAIVAHF 180
Cdd:pfam07228   3 GRLALVIGDVMG----HGLPAALLMGLLR---TALRALAAEGLDPAEVL--KRLNRLLQRNLEEDMFA-----TAVLAVY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  181 -PSNGKLEVANLGDSWCGVFRDSKlvfQTKFQTVGFNAPyqLSIIPEEmlkeaerrgskyilntprDADEYSFQLKKKDI 259
Cdd:pfam07228  69 dPETGTLEYANAGHPPPLLLRPDG---GVVELLESPGLP--LGILPDA------------------PYEVVELELEPGDT 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  260 IILATDGVTDNIATDDiELFLKDNAARTNDELQLLS-QKFVDNVVslskdpnypsvfaQEISKLTGknysGGKEDDITVV 338
Cdd:pfam07228 126 LLLYTDGLTEARDPDG-ELFGLERLLALLAERHGLPpEELLDALL-------------EALLRLGG----GELEDDITLL 187

                  ....*
gi 154199605  339 VVRVD 343
Cdd:pfam07228 188 VLRVR 192
 
Name Accession Description Interval E-value
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
71-302 1.11e-29

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624 [Multi-domain]  Cd Length: 193  Bit Score: 112.44  E-value: 1.11e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605    71 DRDDLIYQKLKDSIRSptGEDNYFVTSNNVHDIFAGVADGVGgwaeHGYDSSAISRELCKKMDEISTALAENSSketllT 150
Cdd:smart00331   1 DDGGLIAQYYEDATQV--GGDFYDVVKLPEGRLLIAIADVMG----KGLAAALAMSMARSALRTLLSEGISLSQ-----I 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605   151 PKKIIGAAYAKIRDEKvvkvgGTTAIVAHF-PSNGKLEVANLGDSWCGVFR-DSKLVFQTKFQTvgfnapYQLSIIPEEM 228
Cdd:smart00331  70 LERLNRAIYENGEDGM-----FATLFLALYdFAGGTLSYANAGHSPPYLLRaDGGLVEDLDDLG------APLGLEPDVE 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154199605   229 LkeaerrgskyilntprdaDEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNaarTNDELQLLSQKFVDNV 302
Cdd:smart00331 139 V------------------DVRELTLEPGDLLLLYTDGLTEARNPERLEELLEEL---LGSPPAEIAQRILEEL 191
PP2Cc cd00143
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
87-342 1.36e-28

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 [Multi-domain]  Cd Length: 254  Bit Score: 111.26  E-value: 1.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  87 PTGEDNYFVTSNNVHD--IFAGVADGVGGWAEHGYDSSAISRELCKKMDEISTaLAENSSKETLLTPKKIIGAAYA-KIR 163
Cdd:cd00143   13 KTNEDAVVIKPNLNNEdgGLFGVFDGHGGHAAGEFASKLLVEELLEELEETLT-LSEEDIEEALRKAFLRADEEILeEAQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 164 DEKVVKVGGTTAIVAHFpSNGKLEVANLGDSWCGVFRDSKLVFQTK----FQTVGFNAPYQLSIIPE-----EMLKEAER 234
Cdd:cd00143   92 DEPDDARSGTTAVVALI-RGNKLYVANVGDSRAVLCRNGEAVQLTKdhkpVNEEERERIEKAGGRVSngrvpGVLAVTRA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 235 RGSK----YILNTPrdaDEYSFQLKKKD-IIILATDGVTDNIATDDIELFLKDNAARTNdeLQLLSQKFVDNVVslskdp 309
Cdd:cd00143  171 LGDFdlkpGVSAEP---DVTVVKLTEDDdFLILASDGLWDVLSNQEAVDIVRSELAKED--LQEAAQELVDLAL------ 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 154199605 310 nypsvfaqeiskltgknySGGKEDDITVVVVRV 342
Cdd:cd00143  240 ------------------RRGSHDNITVVVVRL 254
PP2Cc smart00332
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
88-340 3.86e-25

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 [Multi-domain]  Cd Length: 252  Bit Score: 101.68  E-value: 3.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605    88 TGEDNYFVTSNNVHDI-FAGVADGVGGwaehgydsSAISRELCKKMDEIStALAENSSKETLLTPKKIIGAAYAKIrDEK 166
Cdd:smart00332  22 PMEDAHVITPDLSDSGgFFGVFDGHGG--------SEAAKFLSKNLPEIL-AEELIKEKDELEDVEEALRKAFLST-DEE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605   167 VVKVG----GTTAIVAHFpSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVgfNAPYQLSIIPEEMLKEAERR------- 235
Cdd:smart00332  92 ILEELealsGSTAVVALI-SGNKLYVANVGDSRAVLCRNGKAVQLTEDHKP--SNEDERARIEAAGGFVINGRvngvlal 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605   236 --------GSKYILNTPRDADEYSfqLKKKDIIILATDGVTDNIATDDIELFLKDNaartndelqllsqkfvdnvvsLSK 307
Cdd:smart00332 169 sraigdffLKPYVSAEPDVTVVEL--TEKDDFLILASDGLWDVLSNQEVVDIVRKH---------------------LSK 225
                          250       260       270
                   ....*....|....*....|....*....|...
gi 154199605   308 DpnyPSVFAQEISKLTGKNysgGKEDDITVVVV 340
Cdd:smart00332 226 D---PKEAAKRLIDLALAR---GSKDNITVVVV 252
PTC1 COG0631
Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];
90-343 3.75e-16

Serine/threonine protein phosphatase PrpC [Signal transduction mechanisms];


Pssm-ID: 440396 [Multi-domain]  Cd Length: 247  Bit Score: 76.79  E-value: 3.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  90 EDNYFVTSNNVHDIFAgVADGVGGwAEHGydssAI-SRELCKKMDEISTALAENSSKETLLTPKKIIGAAYAKIRDEKVV 168
Cdd:COG0631   17 EDAFLVALDPGGGLFV-VADGMGG-HAAG----EVaSRLAVETLAELFQEALAPDPEDLEEALREAIRAANRAILELAQE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 169 KVG----GTTAIVAHFpSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVGfNAPYQLSIIPEEmlkEAERRGSKYIL--- 241
Cdd:COG0631   91 DPElagmGTTLVAALI-AGGRLYIAHVGDSRAYLLRDGELEQLTRDHSLV-QELVDAGRITPE---EARTHPQRNVLtra 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 242 ---NTPRDADEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNAArtndelqllSQKFVDNVVSLSKDpnypsvfaqe 318
Cdd:COG0631  166 lgtDDDVEPDISPLELEPGDRLLLCSDGLTDMVSDEEIAEILASAGD---------PQEAAEALIELALE---------- 226
                        250       260
                 ....*....|....*....|....*
gi 154199605 319 iskltgknysGGKEDDITVVVVRVD 343
Cdd:COG0631  227 ----------AGGPDNITVVLVRVE 241
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
101-343 1.49e-15

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: 462119 [Multi-domain]  Cd Length: 192  Bit Score: 73.83  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  101 HDIFAGVADGVGgwaeHGYDSSAISRELCkkmDEISTALAENSSKETLLtpKKIIGAAYAKIRDEKVVkvggtTAIVAHF 180
Cdd:pfam07228   3 GRLALVIGDVMG----HGLPAALLMGLLR---TALRALAAEGLDPAEVL--KRLNRLLQRNLEEDMFA-----TAVLAVY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  181 -PSNGKLEVANLGDSWCGVFRDSKlvfQTKFQTVGFNAPyqLSIIPEEmlkeaerrgskyilntprDADEYSFQLKKKDI 259
Cdd:pfam07228  69 dPETGTLEYANAGHPPPLLLRPDG---GVVELLESPGLP--LGILPDA------------------PYEVVELELEPGDT 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605  260 IILATDGVTDNIATDDiELFLKDNAARTNDELQLLS-QKFVDNVVslskdpnypsvfaQEISKLTGknysGGKEDDITVV 338
Cdd:pfam07228 126 LLLYTDGLTEARDPDG-ELFGLERLLALLAERHGLPpEELLDALL-------------EALLRLGG----GELEDDITLL 187

                  ....*
gi 154199605  339 VVRVD 343
Cdd:pfam07228 188 VLRVR 192
SpoIIE COG5817
Stage II sporulation protein SpoIIE/SpoIIH (serine phosphatase - sigma-F activation) [Cell ...
246-343 1.07e-06

Stage II sporulation protein SpoIIE/SpoIIH (serine phosphatase - sigma-F activation) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444519 [Multi-domain]  Cd Length: 803  Bit Score: 50.27  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 246 DADEYSFQLKKKDIIILATDGVTD-NIATDDIELFLKDnaartndelqLLSQKFVDNvvslskdpnyPSVFAQEISKLTG 324
Cdd:COG5817  721 EVDSVERQLKPGDLLIMVSDGILDaPRHVENKEEWLKR----------FLKEIDTDD----------PQELADLILEEAI 780
                         90
                 ....*....|....*....
gi 154199605 325 KNYSGGKEDDITVVVVRVD 343
Cdd:COG5817  781 RLSGGKIEDDMTVLVAKVE 799
PP2C pfam00481
Protein phosphatase 2C; Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine ...
99-194 4.96e-06

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


Pssm-ID: 395385  Cd Length: 252  Bit Score: 47.33  E-value: 4.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605   99 NVHDIFAGVADGVGGwaehgydssaisRELCKKMDE-ISTALAENSSKETLLTPKKIIGAAYAKIRDEKVVKV------G 171
Cdd:pfam00481  31 KDSWSFFAVFDGHGG------------SEAAKYCGKhLHTILALRRSFLEGEKLEDALRKSFLEDTDEVLRSAekedldS 98
                          90       100
                  ....*....|....*....|...
gi 154199605  172 GTTAIVAhFPSNGKLEVANLGDS 194
Cdd:pfam00481  99 GCTAVVA-LISGNKLYVANVGDS 120
RsbU COG2208
Phosphoserine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms, ...
248-343 1.81e-04

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


Pssm-ID: 441810 [Multi-domain]  Cd Length: 435  Bit Score: 43.13  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154199605 248 DEYSFQLKKKDIIILATDGVTDNIATDDIEL-------FLKDNAARTNDELqllsqkfVDNVVslskdpnypsvfaQEIS 320
Cdd:COG2208  356 EEHEIPLEPGDRLLLYTDGLTEARNGDGELFgeerlleLLAENADLPAEEL-------LDALL-------------EALE 415
                         90       100
                 ....*....|....*....|...
gi 154199605 321 KLTGKnysGGKEDDITVVVVRVD 343
Cdd:COG2208  416 EFRGG---GPQEDDITLLALRRR 435
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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