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Conserved domains on  [gi|1476721347|gb|RIE80797|]
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glutathionylspermidine synthase preATP-grasp family protein [Shigella dysenteriae]

Protein Classification

glutathionylspermidine synthase family protein( domain architecture ID 10002371)

glutathionylspermidine (GSP) synthase family protein, similar to Escherichia coli putative acid--amine ligase YjfC and the C-terminal domain of bifunctional glutathionylspermidine synthetase/amidase GspSA, which catalyzes the penultimate step of the biosynthesis-amide bond formation between spermidine and the glycine carboxylate of GSH

EC:  6.3.1.-
Gene Ontology:  GO:0005524|GO:0016874|GO:0046872
SCOP:  4000414

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gsp COG0754
Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism];
1-352 0e+00

Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism];


:

Pssm-ID: 440517  Cd Length: 383  Bit Score: 522.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347   1 MLRHNVPVRRDLDQIAANNGFDFHIIDNEIYWDESRAYRFTLRQIEEqIEKPTAELHQMCLEVVDRAVKDEEILTQLAIP 80
Cdd:COG0754     1 MRRITIPPRPDWRAKAEELGFVFHTLDGEPYWDESAYYVFSLAEIEE-LEEATNELHQMCLEAVDHVVKDERLLARLGIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  81 PLYWDVIAESWRARDPSLYGRMDFAWCGNAPVKLLEYNA---------------------------------IQERLISR 127
Cdd:COG0754    80 EALWPLIRESWERRDPSLYGRFDLAYDGRGPAKLLEYNAdtptslyeaavvqwlwledqglglppgadqfnsLHEALVER 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 128 FSELYSR---EPFYFCCCQDTDEDRSTVLYLQDCAQQAGQESRFIYIEDLGLGVGGVLTDLDDNVIQRAFKLYPLEWMMR 204
Cdd:COG0754   160 WKELAARlpgGPLHFACDEDSPEDRGTVAYLQDTAREAGLDTKFIYIEDIGWDEEGRFVDLDGRPIEFLFKLYPWEWMLR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 205 DDNGPLLRKRREQWVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEKpqiAAGESYVRKPIYSREGGNVTIFDGqN 284
Cdd:COG0754   240 EEFGLALLRAGVRWIEPAWKLILSNKAILPLLWELFPNHPNLLPAYFEPDP---GLLTGYVRKPLFGREGANISIVDP-G 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721347 285 NVVDHADGDYADEPMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYIAG 352
Cdd:COG0754   316 GELEETDGPYGEEGFIYQAYAPLPKFDGNYPVIGSWVVGDEAAGIGIREDDGLITDDLSRFVPHIILD 383
 
Name Accession Description Interval E-value
Gsp COG0754
Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism];
1-352 0e+00

Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism];


Pssm-ID: 440517  Cd Length: 383  Bit Score: 522.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347   1 MLRHNVPVRRDLDQIAANNGFDFHIIDNEIYWDESRAYRFTLRQIEEqIEKPTAELHQMCLEVVDRAVKDEEILTQLAIP 80
Cdd:COG0754     1 MRRITIPPRPDWRAKAEELGFVFHTLDGEPYWDESAYYVFSLAEIEE-LEEATNELHQMCLEAVDHVVKDERLLARLGIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  81 PLYWDVIAESWRARDPSLYGRMDFAWCGNAPVKLLEYNA---------------------------------IQERLISR 127
Cdd:COG0754    80 EALWPLIRESWERRDPSLYGRFDLAYDGRGPAKLLEYNAdtptslyeaavvqwlwledqglglppgadqfnsLHEALVER 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 128 FSELYSR---EPFYFCCCQDTDEDRSTVLYLQDCAQQAGQESRFIYIEDLGLGVGGVLTDLDDNVIQRAFKLYPLEWMMR 204
Cdd:COG0754   160 WKELAARlpgGPLHFACDEDSPEDRGTVAYLQDTAREAGLDTKFIYIEDIGWDEEGRFVDLDGRPIEFLFKLYPWEWMLR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 205 DDNGPLLRKRREQWVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEKpqiAAGESYVRKPIYSREGGNVTIFDGqN 284
Cdd:COG0754   240 EEFGLALLRAGVRWIEPAWKLILSNKAILPLLWELFPNHPNLLPAYFEPDP---GLLTGYVRKPLFGREGANISIVDP-G 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721347 285 NVVDHADGDYADEPMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYIAG 352
Cdd:COG0754   316 GELEETDGPYGEEGFIYQAYAPLPKFDGNYPVIGSWVVGDEAAGIGIREDDGLITDDLSRFVPHIILD 383
GSP_synth pfam03738
Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine ...
13-350 1.58e-175

Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine synthase enzymatic activity EC:6.3.1.8. This is the C-terminal region in bi-enzymes. Glutathionylspermidine (GSP) synthetases of Trypanosomatidae and Escherichia coli couple hydrolysis of ATP (to ADP and Pi) with formation of an amide bond between spermidine and the glycine carboxylate of glutathione (gamma-Glu-Cys-Gly). In the pathogenic trypanosomatids, this reaction is the penultimate step in the biosynthesis of the antioxidant metabolite, trypanothione (N1,N8-bis-(glutathionyl)spermidine), and is a target for drug design. This region, the pre-ATP grasp region, probably carries the substrate-binding site.


Pssm-ID: 427476  Cd Length: 371  Bit Score: 491.70  E-value: 1.58e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  13 DQIAANNGFDFHIIDNEIYWDESRAYRFTLRQIEEqIEKPTAELHQMCLEVVDRAVKDEEiLTQLAIPPLYWDVIAESWR 92
Cdd:pfam03738   2 RAKAEELGFTFHTGDGEPYWDEDAYYEFTLAEVEE-LEEATEELHDMCLEAVDHVVDNDL-LARLGIPPAAWPLIRESWE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  93 ARDPSLYGRMDFAWCGNAPVKLLEYNA------------------------------IQERLISRFSELYSRE--PFYFC 140
Cdd:pfam03738  80 RRDPSLYGRFDLAYDGRGPAKLLEYNAdtptslleaavvqwawlednlppeadqfnsIHEALVERWKELRTYGgpHLHFS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 141 CCQDTDEDRSTVLYLQDCAQQAGQESRFIYIEDLGLG-VGGVLTDLDDNVIQRAFKLYPLEWMMRDDNGPLLRKRRE--Q 217
Cdd:pfam03738 160 CVRDSGEDRGTVAYLQDTAAQAGLETAFLPIEDIGLDeEEGRFVDLDGRPIETLFKLYPWEWMVRDEFGPHLALALLetR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 218 WVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEkPQIAAGESYVRKPIYSREGGNVTIFDGQNNVVDHADGDYADE 297
Cdd:pfam03738 240 WLEPAWKMLLSNKALLPLLWELFPGHPNLLPAYFDED-PTPLLGRKYVRKPLFGREGANVRIVRDGGEVTAETDGPYGAE 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1476721347 298 PMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYI 350
Cdd:pfam03738 319 GYIYQEYAPLPKFDGNYPVIGSWVVGDEAAGLGIREDRGLITDNLSRFVPHII 371
PHA02117 PHA02117
glutathionylspermidine synthase domain-containing protein
1-352 1.27e-85

glutathionylspermidine synthase domain-containing protein


Pssm-ID: 177351  Cd Length: 397  Bit Score: 264.06  E-value: 1.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347   1 MLRHNVPVRRDLDQIAANNGFDFHIIDNEIYWDESRA----YRFTLRQIEEqIEKPTAELHQMCLEVVD------RAVKD 70
Cdd:PHA02117    1 MKRVSIEARKDWLPQLTSEGLLWTTTEEGPYWIEAMArppyYSFTQAEQDE-LEGAANELHAMCGHALDwmfsypSEASR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  71 EEILTQLAIPPLYWDVIAESWRARDPSLYGRMDFAWCGNAPVKLLEYNA-----------------------------IQ 121
Cdd:PHA02117   80 HPAFDMFNIPENARQMIKRSWTEDEWGLYGRFDLIMTPNGGPKMLEYNAdtptiliesaisqwnwlddahprrqqfneIH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 122 ERLISRFSEL--YSREPFYFCCCQDTD-EDRSTVLYLQDCAQQAGQESRFIYIEDLGLGVGG-VLTDLDDNVIQRAFKLY 197
Cdd:PHA02117  160 EALVNHWADMkkLNALNGCLNIVATGQvEDFVTIAYLAETATEAGAVVKFFDIQEIQLSDRGpFFVDGEDAPIDMCFKLY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 198 PLEWMMRDDNGPLLRKRREQWVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEKP--QIAAGES--YVRKPIYSRE 273
Cdd:PHA02117  240 PWEWMMEDEFSAEILVSQTRFIEPAWKMMLSNKGLLALLYERYPDCPWLVPAYVEDDFDreNLFTLENpkYVSKPLLSRE 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1476721347 274 GGNVTIFDgQNNVVDHADGDYADEPMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYIAG 352
Cdd:PHA02117  320 GNNIHIFE-YGGESEDTDGNYAEEPRVVQQLIEWGRFDGCYPMIGVWMVGSEAAGLCIREDDPRITGNNSRFIPHVVEN 397
 
Name Accession Description Interval E-value
Gsp COG0754
Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism];
1-352 0e+00

Glutathionylspermidine synthase, CHAP domain [Amino acid transport and metabolism];


Pssm-ID: 440517  Cd Length: 383  Bit Score: 522.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347   1 MLRHNVPVRRDLDQIAANNGFDFHIIDNEIYWDESRAYRFTLRQIEEqIEKPTAELHQMCLEVVDRAVKDEEILTQLAIP 80
Cdd:COG0754     1 MRRITIPPRPDWRAKAEELGFVFHTLDGEPYWDESAYYVFSLAEIEE-LEEATNELHQMCLEAVDHVVKDERLLARLGIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  81 PLYWDVIAESWRARDPSLYGRMDFAWCGNAPVKLLEYNA---------------------------------IQERLISR 127
Cdd:COG0754    80 EALWPLIRESWERRDPSLYGRFDLAYDGRGPAKLLEYNAdtptslyeaavvqwlwledqglglppgadqfnsLHEALVER 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 128 FSELYSR---EPFYFCCCQDTDEDRSTVLYLQDCAQQAGQESRFIYIEDLGLGVGGVLTDLDDNVIQRAFKLYPLEWMMR 204
Cdd:COG0754   160 WKELAARlpgGPLHFACDEDSPEDRGTVAYLQDTAREAGLDTKFIYIEDIGWDEEGRFVDLDGRPIEFLFKLYPWEWMLR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 205 DDNGPLLRKRREQWVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEKpqiAAGESYVRKPIYSREGGNVTIFDGqN 284
Cdd:COG0754   240 EEFGLALLRAGVRWIEPAWKLILSNKAILPLLWELFPNHPNLLPAYFEPDP---GLLTGYVRKPLFGREGANISIVDP-G 315
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476721347 285 NVVDHADGDYADEPMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYIAG 352
Cdd:COG0754   316 GELEETDGPYGEEGFIYQAYAPLPKFDGNYPVIGSWVVGDEAAGIGIREDDGLITDDLSRFVPHIILD 383
GSP_synth pfam03738
Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine ...
13-350 1.58e-175

Glutathionylspermidine synthase preATP-grasp; This region contains the Glutathionylspermidine synthase enzymatic activity EC:6.3.1.8. This is the C-terminal region in bi-enzymes. Glutathionylspermidine (GSP) synthetases of Trypanosomatidae and Escherichia coli couple hydrolysis of ATP (to ADP and Pi) with formation of an amide bond between spermidine and the glycine carboxylate of glutathione (gamma-Glu-Cys-Gly). In the pathogenic trypanosomatids, this reaction is the penultimate step in the biosynthesis of the antioxidant metabolite, trypanothione (N1,N8-bis-(glutathionyl)spermidine), and is a target for drug design. This region, the pre-ATP grasp region, probably carries the substrate-binding site.


Pssm-ID: 427476  Cd Length: 371  Bit Score: 491.70  E-value: 1.58e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  13 DQIAANNGFDFHIIDNEIYWDESRAYRFTLRQIEEqIEKPTAELHQMCLEVVDRAVKDEEiLTQLAIPPLYWDVIAESWR 92
Cdd:pfam03738   2 RAKAEELGFTFHTGDGEPYWDEDAYYEFTLAEVEE-LEEATEELHDMCLEAVDHVVDNDL-LARLGIPPAAWPLIRESWE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  93 ARDPSLYGRMDFAWCGNAPVKLLEYNA------------------------------IQERLISRFSELYSRE--PFYFC 140
Cdd:pfam03738  80 RRDPSLYGRFDLAYDGRGPAKLLEYNAdtptslleaavvqwawlednlppeadqfnsIHEALVERWKELRTYGgpHLHFS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 141 CCQDTDEDRSTVLYLQDCAQQAGQESRFIYIEDLGLG-VGGVLTDLDDNVIQRAFKLYPLEWMMRDDNGPLLRKRRE--Q 217
Cdd:pfam03738 160 CVRDSGEDRGTVAYLQDTAAQAGLETAFLPIEDIGLDeEEGRFVDLDGRPIETLFKLYPWEWMVRDEFGPHLALALLetR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 218 WVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEkPQIAAGESYVRKPIYSREGGNVTIFDGQNNVVDHADGDYADE 297
Cdd:pfam03738 240 WLEPAWKMLLSNKALLPLLWELFPGHPNLLPAYFDED-PTPLLGRKYVRKPLFGREGANVRIVRDGGEVTAETDGPYGAE 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1476721347 298 PMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYI 350
Cdd:pfam03738 319 GYIYQEYAPLPKFDGNYPVIGSWVVGDEAAGLGIREDRGLITDNLSRFVPHII 371
PHA02117 PHA02117
glutathionylspermidine synthase domain-containing protein
1-352 1.27e-85

glutathionylspermidine synthase domain-containing protein


Pssm-ID: 177351  Cd Length: 397  Bit Score: 264.06  E-value: 1.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347   1 MLRHNVPVRRDLDQIAANNGFDFHIIDNEIYWDESRA----YRFTLRQIEEqIEKPTAELHQMCLEVVD------RAVKD 70
Cdd:PHA02117    1 MKRVSIEARKDWLPQLTSEGLLWTTTEEGPYWIEAMArppyYSFTQAEQDE-LEGAANELHAMCGHALDwmfsypSEASR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  71 EEILTQLAIPPLYWDVIAESWRARDPSLYGRMDFAWCGNAPVKLLEYNA-----------------------------IQ 121
Cdd:PHA02117   80 HPAFDMFNIPENARQMIKRSWTEDEWGLYGRFDLIMTPNGGPKMLEYNAdtptiliesaisqwnwlddahprrqqfneIH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 122 ERLISRFSEL--YSREPFYFCCCQDTD-EDRSTVLYLQDCAQQAGQESRFIYIEDLGLGVGG-VLTDLDDNVIQRAFKLY 197
Cdd:PHA02117  160 EALVNHWADMkkLNALNGCLNIVATGQvEDFVTIAYLAETATEAGAVVKFFDIQEIQLSDRGpFFVDGEDAPIDMCFKLY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 198 PLEWMMRDDNGPLLRKRREQWVEPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEKP--QIAAGES--YVRKPIYSRE 273
Cdd:PHA02117  240 PWEWMMEDEFSAEILVSQTRFIEPAWKMMLSNKGLLALLYERYPDCPWLVPAYVEDDFDreNLFTLENpkYVSKPLLSRE 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1476721347 274 GGNVTIFDgQNNVVDHADGDYADEPMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVPHYIAG 352
Cdd:PHA02117  320 GNNIHIFE-YGGESEDTDGNYAEEPRVVQQLIEWGRFDGCYPMIGVWMVGSEAAGLCIREDDPRITGNNSRFIPHVVEN 397
PRK10507 PRK10507
bifunctional glutathionylspermidine amidase/glutathionylspermidine synthetase; Provisional
35-347 1.24e-40

bifunctional glutathionylspermidine amidase/glutathionylspermidine synthetase; Provisional


Pssm-ID: 182504 [Multi-domain]  Cd Length: 619  Bit Score: 150.59  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347  35 SRAYR-FTLRQIEEQ-IEKPTAELHQMCLEVVDRAVKDEEILTQLAIPPLYWDVIAESW-RARDPSLYGRMDFAWCGNAp 111
Cdd:PRK10507  247 QDPYHyFTITESAEQeLIKATNELHLMYLHATDKVLKDDNLLALFDIPKILWPRLRLSWqRRRHHMITGRMDFCMDERG- 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 112 VKLLEYNA-----------IQERLISR-------------FSEL-----YSREPFYFCCCQDTD-EDRSTVLYLQDCAQQ 161
Cdd:PRK10507  326 LKVYEYNAdsaschteaglILERWAEQgykgnghnpaeglINELagawkHSRARPFVHIMQDKDiEENYHAQFMQQALHQ 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 162 AGQESRFIY-IEDLGLGVGGVLTDLDDNVIQRAFKLYPLEWMM---RDD----------------NGP-----LLRKrrE 216
Cdd:PRK10507  406 AGFETKILRgLDELRWDAAGQLIDGDGRLVNCVWKTWAWETALdqiREVsdrefaavpirtghpqNEVrlidvLLRP--E 483
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476721347 217 QWV-EPLWKSILSNKGLMPLLWRFFPGHPNLLASWFEGEKPQIAAGesYVRKPIYSREGGNVTIFDGQNNVVDHADGDYA 295
Cdd:PRK10507  484 VLVfEPLWTVIPGNKAILPVLWSLFPHHRYLLDTDFTVNDELVKTG--YAVKPIAGRCGSNIDLVSHQEEVLDKTSGKFA 561
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1476721347 296 DEPMIYQAFQPLPRFGDSYTLIGSWIVDDEACGMGIREDNTLITKDTSRFVP 347
Cdd:PRK10507  562 EQKNIYQQLWCLPKVDGKYIQVCTFTVGGNYGGTCLRGDPSLVIKKESDIEP 613
 
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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