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Conserved domains on  [gi|499404642|ref|WP_011092109|]
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NAD(P)-dependent oxidoreductase [Pectobacterium atrosepticum]

Protein Classification

NAD(P)-dependent oxidoreductase( domain architecture ID 11449905)

NAD(P)-dependent oxidoreductase similar to 3-hydroxyisobutyrate dehydrogenase, L-threonate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and glyoxylate/succinic semialdehyde reductase

CATH:  3.40.50.720
EC:  1.1.-.-
Gene Ontology:  GO:0050661|GO:0051287|GO:0016491
PubMed:  8749365
SCOP:  4000072

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
5-288 5.31e-48

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


:

Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 161.82  E-value: 5.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   5 VSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQLFtQEKQIVLICLKDAEAIRDVFQSED-VI 83
Cdd:COG2084    4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAA-AAADVVITMLPDDAAVEEVLLGEDgLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  84 HKLslyRP--LFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFAsAVNDIVSCLSDHY 161
Cdd:COG2084   83 AAL---RPgaVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFE-RARPVLEAMGKRI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642 162 VLMESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYMEVMLDRYLNPRETVSVPLSIRL 241
Cdd:COG2084  159 VHVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLML 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 499404642 242 KDLDLANTLFQRSAIHSEFFDTARQLYQSTADLSADPQDQTACFAYL 288
Cdd:COG2084  239 KDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
5-288 5.31e-48

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 161.82  E-value: 5.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   5 VSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQLFtQEKQIVLICLKDAEAIRDVFQSED-VI 83
Cdd:COG2084    4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAA-AAADVVITMLPDDAAVEEVLLGEDgLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  84 HKLslyRP--LFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFAsAVNDIVSCLSDHY 161
Cdd:COG2084   83 AAL---RPgaVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFE-RARPVLEAMGKRI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642 162 VLMESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYMEVMLDRYLNPRETVSVPLSIRL 241
Cdd:COG2084  159 VHVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLML 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 499404642 242 KDLDLANTLFQRSAIHSEFFDTARQLYQSTADLSADPQDQTACFAYL 288
Cdd:COG2084  239 KDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
4-149 3.71e-26

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 101.01  E-value: 3.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642    4 SVSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQlFTQEKQIVLICLKDAEAIRDVFQSEDVI 83
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAE-FVAGLDVVITMVPAGAAVDAVIFGEGLL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404642   84 HKLslyRP--LFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFASA 149
Cdd:pfam03446  80 PGL---KPgdIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERV 144
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
5-283 2.51e-19

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 85.84  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   5 VSLVGVGVLGKAISLRLLQRHFSLSVfNRTHSKTNDVAAEGAQAVPELHQLfTQEKQIVLICLKDAEAIRDVFQSEDVIH 84
Cdd:PRK15059   3 LGFIGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQV-TEASDIIFIMVPDTPQVEEVLFGENGCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  85 KLSLYRPLFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFASaVNDIVSCLSDHYVLM 164
Cdd:PRK15059  81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFER-VKPLFELLGKNITLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642 165 ESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYMEV----MLDRYLNPretvSVPLSIR 240
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVhgerMIKRTFNP----GFKIALH 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499404642 241 LKDLDLANTLFQRSAIHSEFFDTARQLYQSTADLSADPQDQTA 283
Cdd:PRK15059 236 QKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSA 278
 
Name Accession Description Interval E-value
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
5-288 5.31e-48

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 161.82  E-value: 5.31e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   5 VSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQLFtQEKQIVLICLKDAEAIRDVFQSED-VI 83
Cdd:COG2084    4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAA-AAADVVITMLPDDAAVEEVLLGEDgLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  84 HKLslyRP--LFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFAsAVNDIVSCLSDHY 161
Cdd:COG2084   83 AAL---RPgaVVVDMSTISPETARELAAAAAARGVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFE-RARPVLEAMGKRI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642 162 VLMESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYMEVMLDRYLNPRETVSVPLSIRL 241
Cdd:COG2084  159 VHVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLML 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 499404642 242 KDLDLANTLFQRSAIHSEFFDTARQLYQSTADLSADPQDQTACFAYL 288
Cdd:COG2084  239 KDLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
4-149 3.71e-26

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 101.01  E-value: 3.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642    4 SVSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQlFTQEKQIVLICLKDAEAIRDVFQSEDVI 83
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAE-FVAGLDVVITMVPAGAAVDAVIFGEGLL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499404642   84 HKLslyRP--LFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFASA 149
Cdd:pfam03446  80 PGL---KPgdIIIDGSTSSPEDARRRAKELKEKGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERV 144
PRK15059 PRK15059
2-hydroxy-3-oxopropionate reductase;
5-283 2.51e-19

2-hydroxy-3-oxopropionate reductase;


Pssm-ID: 185019 [Multi-domain]  Cd Length: 292  Bit Score: 85.84  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   5 VSLVGVGVLGKAISLRLLQRHFSLSVfNRTHSKTNDVAAEGAQAVPELHQLfTQEKQIVLICLKDAEAIRDVFQSEDVIH 84
Cdd:PRK15059   3 LGFIGLGIMGTPMAINLARAGHQLHV-TTIGPVADELLSLGAVSVETARQV-TEASDIIFIMVPDTPQVEEVLFGENGCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  85 KLSLYRPLFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFASaVNDIVSCLSDHYVLM 164
Cdd:PRK15059  81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDYLDAPVSGGEIGAREGTLSIMVGGDEAVFER-VKPLFELLGKNITLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642 165 ESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYMEV----MLDRYLNPretvSVPLSIR 240
Cdd:PRK15059 160 GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVhgerMIKRTFNP----GFKIALH 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499404642 241 LKDLDLANTLFQRSAIHSEFFDTARQLYQSTADLSADPQDQTA 283
Cdd:PRK15059 236 QKDLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSA 278
garR PRK11559
tartronate semialdehyde reductase; Provisional
1-250 8.62e-17

tartronate semialdehyde reductase; Provisional


Pssm-ID: 183197 [Multi-domain]  Cd Length: 296  Bit Score: 78.55  E-value: 8.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   1 MTHSVSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQLfTQEKQIVLICLKDAEAIRDVFQSE 80
Cdd:PRK11559   1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAV-AEQCDVIITMLPNSPHVKEVALGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  81 D-VIHKLslyRP--LFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFaSAVNDIVSCL 157
Cdd:PRK11559  80 NgIIEGA---KPgtVVIDMSSIAPLASREIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIF-DKYYDLMKAM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642 158 SDHYVLMESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYME----VMLDRYLNPretv 233
Cdd:PRK11559 156 AGSVVHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDakapMVMDRNFKP---- 231
                        250
                 ....*....|....*..
gi 499404642 234 SVPLSIRLKdlDLANTL 250
Cdd:PRK11559 232 GFRIDLHIK--DLANAL 246
NAD_binding_11 pfam14833
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ...
169-283 1.91e-07

NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.


Pssm-ID: 434252 [Multi-domain]  Cd Length: 122  Bit Score: 49.06  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  169 SAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYME-----VMLDRYLNPRetvsVPLSIRLKD 243
Cdd:pfam14833   2 AGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALEnkfpqRVLSRDFDPG----FALDLMLKD 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499404642  244 LDLANTLFQRSAIHSEFFDTARQLYQSTADLSADPQDQTA 283
Cdd:pfam14833  78 LGLALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSA 117
PRK15461 PRK15461
sulfolactaldehyde 3-reductase;
3-179 6.86e-07

sulfolactaldehyde 3-reductase;


Pssm-ID: 185358 [Multi-domain]  Cd Length: 296  Bit Score: 49.85  E-value: 6.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   3 HSVSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDVAAEGAQAVPELHQLfTQEKQIVLICLKDAEAIRDVFQSED- 81
Cdd:PRK15461   2 AAIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQA-AAGAEFVITMLPNGDLVRSVLFGENg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  82 VIHKLSlYRPLFLNISTIGPEESRWMETFFHQHGAHYVECPVSGGPEGARQGRLAAWVGPYADDFASAvNDIVSCLSDHY 161
Cdd:PRK15461  81 VCEGLS-RDALVIDMSTIHPLQTDKLIADMQAKGFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERA-TPILMAMGNEL 158
                        170
                 ....*....|....*...
gi 499404642 162 VLMESNHSAQTMKVINNY 179
Cdd:PRK15461 159 INAGGPGMGIRVKLINNY 176
PLN02858 PLN02858
fructose-bisphosphate aldolase
5-270 1.11e-05

fructose-bisphosphate aldolase


Pssm-ID: 215463 [Multi-domain]  Cd Length: 1378  Bit Score: 46.77  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642    5 VSLVGVGVLGKAISLRLLQRHFS----------LSVFNRTHSKTNDVAAEGAQAVPELHQLFTQEKQIVLICLKDAEAIR 74
Cdd:PLN02858  327 IGFIGLGAMGFGMASHLLKSNFSvcgydvykptLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDLGAVS 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   75 dVFQSEDVIHKLSLYRPLFL-NISTIGPEESRwmetffhqhGAHYVECPVSGGPEGARQGRLAAwVGPYADDFASAVNDI 153
Cdd:PLN02858  407 -ALPAGASIVLSSTVSPGFViQLERRLENEGR---------DIKLVDAPVSGGVKRAAMGTLTI-MASGTDEALKSAGSV 475
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  154 VSCLSDH-YVLMESNHSAQTMKVINNYCEAVHLLVAAEALLLAEAHGIAPDVLANALTLGRGRSTYMEVMLDRYLNPRET 232
Cdd:PLN02858  476 LSALSEKlYVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYT 555
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 499404642  233 VSVPLSIRLKDLDLANTLFQRSAIHSEFFDTARQLYQS 270
Cdd:PLN02858  556 PYSALDIFVKDLGIVSREGSSRKIPLHLSTVAHQLFLA 593
PTZ00142 PTZ00142
6-phosphogluconate dehydrogenase; Provisional
5-179 2.18e-05

6-phosphogluconate dehydrogenase; Provisional


Pssm-ID: 240287 [Multi-domain]  Cd Length: 470  Bit Score: 45.55  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642   5 VSLVGVGVLGKAISLRLLQRHFSLSVFNRTHSKTNDV---AAEGAQAVPELHQLftqeKQIVLICLKDAEAIRDVFQSED 81
Cdd:PTZ00142   4 IGLIGLAVMGQNLALNIASRGFKISVYNRTYEKTEEFvkkAKEGNTRVKGYHTL----EELVNSLKKPRKVILLIKAGEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499404642  82 VIHKLSLYRPLFLNISTI---GPEE---SRWMETFFHQHGAHYVECPVSGGPEGARQ-------GRLAAW--VGPYADDF 146
Cdd:PTZ00142  80 VDETIDNLLPLLEKGDIIidgGNEWylnTERRIKRCEEKGILYLGMGVSGGEEGARYgpslmpgGNKEAYdhVKDILEKC 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 499404642 147 ASAVNDIVSCL------SDHYVLMESN-----------HSAQTMKVINNY 179
Cdd:PTZ00142 160 SAKVGDSPCVTyvgpgsSGHYVKMVHNgieygdmqlisESYKLMKHILGM 209
 
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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