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Conserved domains on  [gi|16130159|ref|NP_416726|]
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acetyl-CoA:acetoacetyl-CoA transferase subunit beta [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

sugar phosphate isomerase family( domain architecture ID 368)

sugar phosphate isomerase family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SugarP_isomerase super family cl00339
SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate ...
2-205 8.87e-117

SugarP_isomerase: Sugar Phosphate Isomerase family; includes type A ribose 5-phosphate isomerase (RPI_A), glucosamine-6-phosphate (GlcN6P) deaminase, and 6-phosphogluconolactonase (6PGL). RPI catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate, the first step of the non-oxidative branch of the pentose phosphate pathway. GlcN6P deaminase catalyzes the reversible conversion of GlcN6P to D-fructose-6-phosphate (Fru6P) and ammonium, the last step of the metabolic pathway of N-acetyl-D-glucosamine-6-phosphate. 6PGL converts 6-phosphoglucono-1,5-lactone to 6-phosphogluconate, the second step of the oxidative phase of the pentose phosphate pathway.


The actual alignment was detected with superfamily member TIGR02428:

Pssm-ID: 469729  Cd Length: 207  Bit Score: 330.79  E-value: 8.87e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     2 DAKQRIARRVAQELRDGDIVNLGIGLPTMVANYLPEGIHITLQSENGFLGLGPVTT---AHPDLVNAGGQPCGVLPGAAM 78
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEpgeEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159    79 FDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVVPGKMVPGMGGAMDLVTGSRKVIIAMEHCAKDGSAKILRRCTMPL 158
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAKRVIVAMEHTTKDGESKILKECTLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 16130159   159 TAQHAVHMLVTELAVFRFIDGKMWLTEIADGCDLATVRAKTEARFEV 205
Cdd:TIGR02428 161 TGAKCVDRIVTELAVFEVTDGGLILRELAPGVTVEELQAKTEADLII 207
 
Name Accession Description Interval E-value
pcaJ_scoB_fam TIGR02428
3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the ...
2-205 8.87e-117

3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the B subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The A subunit represents a different clade in pfam01144.


Pssm-ID: 188219  Cd Length: 207  Bit Score: 330.79  E-value: 8.87e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     2 DAKQRIARRVAQELRDGDIVNLGIGLPTMVANYLPEGIHITLQSENGFLGLGPVTT---AHPDLVNAGGQPCGVLPGAAM 78
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEpgeEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159    79 FDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVVPGKMVPGMGGAMDLVTGSRKVIIAMEHCAKDGSAKILRRCTMPL 158
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAKRVIVAMEHTTKDGESKILKECTLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 16130159   159 TAQHAVHMLVTELAVFRFIDGKMWLTEIADGCDLATVRAKTEARFEV 205
Cdd:TIGR02428 161 TGAKCVDRIVTELAVFEVTDGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
3-209 1.10e-87

Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];


Pssm-ID: 441660  Cd Length: 235  Bit Score: 258.17  E-value: 1.10e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159   3 AKQRIARRVAQELRDGDIVNLGIGLPTMVANYLP--EGIHITLQSENGFLGLGPV----TTAHPDLVNAGGQpcgvlpga 76
Cdd:COG2057   4 TRELMAVRAARELRDGEVVNLGIGLPTLAANLAPltHAPDVTLQSENGLLGPGPAplpgSVGDPDLINAGKQ-------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159  77 aMFDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVV-----PGKMVPGMGGAMDLVTGSRKVIIAMEHCAKdgsaKIL 151
Cdd:COG2057  76 -FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAKRVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130159 152 RRCTMpLTAQ---HAVHMLVTELAVFRFIDGK-MWLTEIADGCDLATVRAKTEARFEVAADL 209
Cdd:COG2057 151 EKCDL-LTGPgvvDGPRRVITDLAVFDFDPEKgLVLRELHPGVTVEEVQENTGFELIVADDV 211
CoA_trans pfam01144
Coenzyme A transferase;
4-180 3.66e-46

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 152.07  E-value: 3.66e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     4 KQRIARRVAQELRDGDIVNLG----IGLP-TMVANYLPEGI--HITLQSENGFLGLGPVTTAH---PDLVNAGGQPCGVL 73
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVkdLTVISNEAGVLGLGPLLLNGsvkKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159    74 PGAAMFDSAMSFAL-IRGGHIDACVLGGLQVDEEANLANWVV-----PGKMVPGMGGAMDLVTGS-RKVIIAMEHCAKDG 146
Cdd:pfam01144  81 FGRQYFSGELEFELwPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPAlRADVALIKASKADG 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 16130159   147 SAKILRRCTMPLTAQHAVHM--LVTELAVFRFIDGK 180
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAAaaKVTILEVEEIVEKG 196
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
7-183 1.76e-43

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 145.04  E-value: 1.76e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159      7 IARRVAQELRDGDIVNLGIGL--PTMVANYLPE----GIHITLQSENGFLGLGPVTTAH-PDLVNAGGQPCGVLPGAAMF 79
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFGglPTPAALILALirqgPKDLTLISENGGLGLGLLAGEGdVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     80 DSAM-SFALIRGGHIDACVLGGLQVDEEANLANW-------VVPGKMV-PGMGGAMDLVTGSRK-VIIAMEHCAK-DGSA 148
Cdd:smart00882  81 DGEIeSFLLPQGGLADRLRAGAAGVPGFGTLAGLgtdvdprYEGGKVRpFGMGGAYLLVPAIRPdVALIRAHTADeFGNL 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 16130159    149 ---KILRRCTMPLTAQHA-----VHMLVTELAVFRFIDGKMWL 183
Cdd:smart00882 161 vyeKEATSCGLPLTAAAAkkvivQVEEIVDLGVLDPDPVRLLI 203
 
Name Accession Description Interval E-value
pcaJ_scoB_fam TIGR02428
3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the ...
2-205 8.87e-117

3-oxoacid CoA-transferase, B subunit; Various members of this family are characterized as the B subunits of succinyl-CoA:3-ketoacid-CoA transferase (EC 2.8.3.5), beta-ketoadipate:succinyl-CoA transferase (EC 2.8.3.6), acetyl-CoA:acetoacetate CoA transferase (EC 2.8.3.8), and butyrate-acetoacetate CoA-transferase (EC 2.8.3.9). This represents a very distinct clade with strong sequence conservation within the larger family defined by pfam01144. The A subunit represents a different clade in pfam01144.


Pssm-ID: 188219  Cd Length: 207  Bit Score: 330.79  E-value: 8.87e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     2 DAKQRIARRVAQELRDGDIVNLGIGLPTMVANYLPEGIHITLQSENGFLGLGPVTT---AHPDLVNAGGQPCGVLPGAAM 78
Cdd:TIGR02428   1 WTRDQIAARAAQELKDGDYVNLGIGIPTLVANYLPEGIEVFLQSENGILGMGPAPEpgeEDPDLINAGKQPVTLLPGASY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159    79 FDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVVPGKMVPGMGGAMDLVTGSRKVIIAMEHCAKDGSAKILRRCTMPL 158
Cdd:TIGR02428  81 FDSADSFAMIRGGHVDVAVLGALQVSENGDLANWMIPGKLVPGMGGAMDLVAGAKRVIVAMEHTTKDGESKILKECTLPL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 16130159   159 TAQHAVHMLVTELAVFRFIDGKMWLTEIADGCDLATVRAKTEARFEV 205
Cdd:TIGR02428 161 TGAKCVDRIVTELAVFEVTDGGLILRELAPGVTVEELQAKTEADLII 207
AtoA COG2057
Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];
3-209 1.10e-87

Acyl-CoA:acetate/3-ketoacid CoA transferase, beta subunit [Lipid transport and metabolism];


Pssm-ID: 441660  Cd Length: 235  Bit Score: 258.17  E-value: 1.10e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159   3 AKQRIARRVAQELRDGDIVNLGIGLPTMVANYLP--EGIHITLQSENGFLGLGPV----TTAHPDLVNAGGQpcgvlpga 76
Cdd:COG2057   4 TRELMAVRAARELRDGEVVNLGIGLPTLAANLAPltHAPDVTLQSENGLLGPGPAplpgSVGDPDLINAGKQ-------- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159  77 aMFDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVV-----PGKMVPGMGGAMDLVTGSRKVIIAMEHCAKdgsaKIL 151
Cdd:COG2057  76 -FFDSADSFAMIRGGHIDVGFLGAAQVDRYGNLNNWMIgdydkPGKRLPGMGGAMDLAAGAKRVIVVMEHSKR----KFV 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130159 152 RRCTMpLTAQ---HAVHMLVTELAVFRFIDGK-MWLTEIADGCDLATVRAKTEARFEVAADL 209
Cdd:COG2057 151 EKCDL-LTGPgvvDGPRRVITDLAVFDFDPEKgLVLRELHPGVTVEEVQENTGFELIVADDV 211
CoA_trans pfam01144
Coenzyme A transferase;
4-180 3.66e-46

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 152.07  E-value: 3.66e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     4 KQRIARRVAQELRDGDIVNLG----IGLP-TMVANYLPEGI--HITLQSENGFLGLGPVTTAH---PDLVNAGGQPCGVL 73
Cdd:pfam01144   1 VESAAEAVAKEIKDGMTVNVGgfglIGIPeTLIAALARSGVkdLTVISNEAGVLGLGPLLLNGsvkKVIASYGGETANPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159    74 PGAAMFDSAMSFAL-IRGGHIDACVLGGLQVDEEANLANWVV-----PGKMVPGMGGAMDLVTGS-RKVIIAMEHCAKDG 146
Cdd:pfam01144  81 FGRQYFSGELEFELwPQGGLADRLRAGGAGIPFEGFLTNTGIgtyvaPKKRVPGFGGAMYLLEPAlRADVALIKASKADG 160
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 16130159   147 SAKILRRCTMPLTAQHAVHM--LVTELAVFRFIDGK 180
Cdd:pfam01144 161 EGNLVFRTTAPNFNGPAVAAaaKVTILEVEEIVEKG 196
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
7-183 1.76e-43

Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved family of enzymes catalyzing the reversible transfer of CoA from one carboxylic acid to another. They have been identified in many prokaryotes and in mammalian tissues. The bacterial enzymes are heterodimer of two subunits (A and B) of about 25 Kd each while eukaryotic SCOT consist of a single chain which is colinear with the two bacterial subunits.


Pssm-ID: 214882 [Multi-domain]  Cd Length: 212  Bit Score: 145.04  E-value: 1.76e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159      7 IARRVAQELRDGDIVNLGIGL--PTMVANYLPE----GIHITLQSENGFLGLGPVTTAH-PDLVNAGGQPCGVLPGAAMF 79
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFGglPTPAALILALirqgPKDLTLISENGGLGLGLLAGEGdVKKIIAGHVGLTPLLGRLYF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159     80 DSAM-SFALIRGGHIDACVLGGLQVDEEANLANW-------VVPGKMV-PGMGGAMDLVTGSRK-VIIAMEHCAK-DGSA 148
Cdd:smart00882  81 DGEIeSFLLPQGGLADRLRAGAAGVPGFGTLAGLgtdvdprYEGGKVRpFGMGGAYLLVPAIRPdVALIRAHTADeFGNL 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 16130159    149 ---KILRRCTMPLTAQHA-----VHMLVTELAVFRFIDGKMWL 183
Cdd:smart00882 161 vyeKEATSCGLPLTAAAAkkvivQVEEIVDLGVLDPDPVRLLI 203
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
1-209 1.68e-23

Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 97.49  E-value: 1.68e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159   1 MDAKQRIARRVAQELRDGDIVNLGIGLPTMVANYL-PEGIH--ITLQSENGFLGlGpvttahpdlVNAGGQPCGVLPGA- 76
Cdd:COG4670 273 LDERKVIARRAAMELRPGAVVNLGIGIPEGVAAVAaEEGISdlITLTVESGPIG-G---------VPAGGLDFGAAVNAe 342
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159  77 AMFDSAMSFALIRGGHIDACVLGGLQVDEEANlanwVVPGKM---VPGMGGAMDLVTGSRKVI-----------IAMEHC 142
Cdd:COG4670 343 AIIDQPDQFDFYDGGGLDIAFLGFAQVDRHGN----VNVSKFggrIAGCGGFINITQNAKKVVfcgtftagglkVEVEDG 418
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159 143 A----KDG--------------SAKILRRctmplTAQHAvhMLVTELAVFRFIDGKMWLTEIADGCDLAT-VRAKTEARF 203
Cdd:COG4670 419 KlrilQEGkikkfvkkveqitfSGKYARE-----RGQEV--LYVTERAVFELTPEGLELTEIAPGIDLERdILAQMEFRP 491

                ....*.
gi 16130159 204 EVAADL 209
Cdd:COG4670 492 IIADDL 497
GlpR COG1349
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ...
2-170 7.21e-05

DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];


Pssm-ID: 440960 [Multi-domain]  Cd Length: 254  Bit Score: 42.43  E-value: 7.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159   2 DAKQRIARRVAQELRDGDIVNLGIGLPTM-VANYLPEGIHITLqsengflglgpVTTA-----------HPDLVNAGGQp 69
Cdd:COG1349  77 EEKRAIARAAASLIEDGDTIFLDAGTTTLaLARALPDRRNLTV-----------VTNSlnianelaerpNIEVILLGGE- 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130159  70 cgVLPGAAMFDSAMSFALIRGGHIDACVLG--GLQVD--------EEANLANwvvpgkmvpgmggAMdlVTGSRKVIIAM 139
Cdd:COG1349 145 --LRPSSGSLVGPLAEEALRRFRADKAFLGasGIDAEgglttfdeEEAEVKR-------------AM--IEAARRVILLA 207
                       170       180       190
                ....*....|....*....|....*....|.
gi 16130159 140 EHcakdgsAKILRRCTMPLTAQHAVHMLVTE 170
Cdd:COG1349 208 DS------SKFGRRALARVAPLSEIDVLITD 232
DeoRC pfam00455
DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive ...
2-42 7.70e-04

DeoR C terminal sensor domain; The sensor domains of the DeoR are catalytically inactive versions of the ISOCOT fold, but retain the substrate binding site. DeorC senses diverse sugar derivatives such as deoxyribose nucleoside (DeoR), tagatose phosphate (LacR), galactosamine (AgaR), myo-inositol (Bacillus IolR) and L-ascorbate (UlaR). It can also bind L-ascorbate 6-phosphate, agrocinopines, sn-glycerol 3-phosphate, and sulfoquinovose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395365  Cd Length: 160  Bit Score: 38.65  E-value: 7.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 16130159     2 DAKQRIARRVAQELRDGDIVNLGIGLPTM-VANYLPEGIHIT 42
Cdd:pfam00455   4 EEKRRIAKAAASLIEDGDTIFLDAGTTTLeLARALPDRRNLT 45
AcetylCoA_hyd_C pfam13336
Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which ...
114-170 2.77e-03

Acetyl-CoA hydrolase/transferase C-terminal domain; This family contains several enzymes which take part in pathways involving acetyl-CoA. Acetyl-CoA hydrolase EC:3.1.2.1 catalyzes the formation of acetate from acetyl-CoA, CoA transferase (CAT1) EC:2.8.3.- produces succinyl-CoA, and acetate-CoA transferase EC:2.8.3.8 utilizes acyl-CoA and acetate to form acetyl-CoA.


Pssm-ID: 433126 [Multi-domain]  Cd Length: 154  Bit Score: 37.03  E-value: 2.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130159   114 VPGKMVPGMGGAMDLVTGSR-----KVIIAMEHCAKDGS-AKILRRCTMPL---TAQHAVHMLVTE 170
Cdd:pfam13336  55 IGGRQYSGVGGQLDFVRGAYlskggKSIIALPSTAKDGTiSRIVPMLSPGAhvtTTRHDVDYVVTE 120
 
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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