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Conserved domains on  [gi|489323525|ref|WP_003230839|]
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MULTISPECIES: CoA transferase subunit A [Bacillus]

Protein Classification

CoA transferase subunit A( domain architecture ID 10004510)

CoA transferase subunit A is part of a complex that catalyzes the reversible transfer of CoA from one carboxylic acid to another

CATH:  3.40.1080.10
Gene Ontology:  GO:0008410
SCOP:  4001854

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
8-228 1.91e-82

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 244.99  E-value: 1.91e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   8 ISIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIgpLIVNQRVKTLIASH---IGSNP 84
Cdd:COG1788    6 ISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVDGLGL--LIGAGQVKKVIASYvggVGLNP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525  85 VAGKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQmVCEKKDIVTVAGKRYLIEEALTADFAFINAYIADE 164
Cdd:COG1788   84 EFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTD-VAEGKETREIDGEEYVLEPALRADVALIHAQKADR 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489323525 165 FGNLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSEGVKWKWAW 228
Cdd:COG1788  163 AGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGGARDKRI 226
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
8-228 1.91e-82

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 244.99  E-value: 1.91e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   8 ISIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIgpLIVNQRVKTLIASH---IGSNP 84
Cdd:COG1788    6 ISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVDGLGL--LIGAGQVKKVIASYvggVGLNP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525  85 VAGKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQmVCEKKDIVTVAGKRYLIEEALTADFAFINAYIADE 164
Cdd:COG1788   84 EFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTD-VAEGKETREIDGEEYVLEPALRADVALIHAQKADR 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489323525 165 FGNLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSEGVKWKWAW 228
Cdd:COG1788  163 AGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGGARDKRI 226
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
5-220 7.55e-77

acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 230.79  E-value: 7.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   5 QKAISIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIGPLIVNQRVKTLIASHIGSNP 84
Cdd:PRK09920   3 TKLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525  85 VAGKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIdNQMVCEKKDIVTVAGKRYLIEEALTADFAFINAYIADE 164
Cdd:PRK09920  83 ETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGV-GTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRADT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489323525 165 FGNLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSE 220
Cdd:PRK09920 162 LGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQ 217
CoA_trans pfam01144
Coenzyme A transferase;
9-219 9.57e-62

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 192.13  E-value: 9.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525    9 SIDTAIA-DVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFpdIGIGPLIVNQRVKTLIASHIGS--NPV 85
Cdd:pfam01144   3 SAAEAVAkEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaNPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   86 AGKQMTEGTLEVQFSPQGTLAERIRAGGA--GLGGILTDVGIDnQMVCEKKDIVTVAGKRYLIEEALTADFAFINAYIAD 163
Cdd:pfam01144  81 FGRQYFSGELEFELWPQGGLADRLRAGGAgiPFEGFLTNTGIG-TYVAPKKRVPGFGGAMYLLEPALRADVALIKASKAD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489323525  164 EFGNLTYDKTARNMN-PLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRS 219
Cdd:pfam01144 160 GEGNLVFRTTAPNFNgPAVAAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
9-221 2.08e-60

3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the A 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 B subunit represents a different clade in pfam01144, described by TIGR02428. The two are found in general as tandem genes and occasionally as a fusion.


Pssm-ID: 131482  Cd Length: 222  Bit Score: 189.20  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525    9 SIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIGPLIVNQRVKTLIASHIGSNP--VA 86
Cdd:TIGR02429   8 SAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFPRQSDsyVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   87 GKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQMVcEKKDIVTVAGKRYLIEEALTADFAFINAYIADEFG 166
Cdd:TIGR02429  88 DELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLA-EGKETREFDGKGYVLEYPLPADFALIKAHKADRWG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489323525  167 NLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSEG 221
Cdd:TIGR02429 167 NLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVVEVRD 221
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
9-217 2.87e-55

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: 175.47  E-value: 2.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525     9 SIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGfpdIGIGPLIVNQRVKTLIASHIGSNPVAGK 88
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525    89 QMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQMVCE---KKDIVTVAGKRYLIEEALTADFAFINAYIADEF 165
Cdd:smart00882  78 LYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRyegGKVRPFGMGGAYLLVPAIRPDVALIRAHTADEF 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489323525   166 GNLTYDKTARNMN-PLMAMAARRTFAEAERIVPMGEISEEMI--VTPGVFVEGVV 217
Cdd:smart00882 158 GNLVYEKEATSCGlPLTAAAAKKVIVQVEEIVDLGVLDPDPVrlLIPGVLVDAVV 212
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
8-228 1.91e-82

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 244.99  E-value: 1.91e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   8 ISIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIgpLIVNQRVKTLIASH---IGSNP 84
Cdd:COG1788    6 ISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVDGLGL--LIGAGQVKKVIASYvggVGLNP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525  85 VAGKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQmVCEKKDIVTVAGKRYLIEEALTADFAFINAYIADE 164
Cdd:COG1788   84 EFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTD-VAEGKETREIDGEEYVLEPALRADVALIHAQKADR 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489323525 165 FGNLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSEGVKWKWAW 228
Cdd:COG1788  163 AGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEVPGGARDKRI 226
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
5-220 7.55e-77

acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 230.79  E-value: 7.55e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   5 QKAISIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIGPLIVNQRVKTLIASHIGSNP 84
Cdd:PRK09920   3 TKLMTLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGTNP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525  85 VAGKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIdNQMVCEKKDIVTVAGKRYLIEEALTADFAFINAYIADE 164
Cdd:PRK09920  83 ETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGV-GTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRADT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489323525 165 FGNLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSE 220
Cdd:PRK09920 162 LGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQ 217
CoA_trans pfam01144
Coenzyme A transferase;
9-219 9.57e-62

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 192.13  E-value: 9.57e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525    9 SIDTAIA-DVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFpdIGIGPLIVNQRVKTLIASHIGS--NPV 85
Cdd:pfam01144   3 SAAEAVAkEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaNPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   86 AGKQMTEGTLEVQFSPQGTLAERIRAGGA--GLGGILTDVGIDnQMVCEKKDIVTVAGKRYLIEEALTADFAFINAYIAD 163
Cdd:pfam01144  81 FGRQYFSGELEFELWPQGGLADRLRAGGAgiPFEGFLTNTGIG-TYVAPKKRVPGFGGAMYLLEPALRADVALIKASKAD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 489323525  164 EFGNLTYDKTARNMN-PLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRS 219
Cdd:pfam01144 160 GEGNLVFRTTAPNFNgPAVAAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAVVEA 216
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
9-221 2.08e-60

3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the A 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 B subunit represents a different clade in pfam01144, described by TIGR02428. The two are found in general as tandem genes and occasionally as a fusion.


Pssm-ID: 131482  Cd Length: 222  Bit Score: 189.20  E-value: 2.08e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525    9 SIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGFPDIGIGPLIVNQRVKTLIASHIGSNP--VA 86
Cdd:TIGR02429   8 SAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFPRQSDsyVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   87 GKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQMVcEKKDIVTVAGKRYLIEEALTADFAFINAYIADEFG 166
Cdd:TIGR02429  88 DELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLA-EGKETREFDGKGYVLEYPLPADFALIKAHKADRWG 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489323525  167 NLTYDKTARNMNPLMAMAARRTFAEAERIVPMGEISEEMIVTPGVFVEGVVRSEG 221
Cdd:TIGR02429 167 NLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVVEVRD 221
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
9-217 2.87e-55

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: 175.47  E-value: 2.87e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525     9 SIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAILDSGVTDLTVICNDAGfpdIGIGPLIVNQRVKTLIASHIGSNPVAGK 88
Cdd:smart00882   1 SAAEAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525    89 QMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGIDNQMVCE---KKDIVTVAGKRYLIEEALTADFAFINAYIADEF 165
Cdd:smart00882  78 LYFDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRyegGKVRPFGMGGAYLLVPAIRPDVALIRAHTADEF 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 489323525   166 GNLTYDKTARNMN-PLMAMAARRTFAEAERIVPMGEISEEMI--VTPGVFVEGVV 217
Cdd:smart00882 158 GNLVYEKEATSCGlPLTAAAAKKVIVQVEEIVDLGVLDPDPVrlLIPGVLVDAVV 212
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
6-220 9.74e-24

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 98.65  E-value: 9.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525   6 KAISIDTAIADVRDGSVLMFGGFGGVGSPPSLIEAI----LDSGV-TDLTVI-CNDAG-FPDIGIGPLIVNQRVKTLIAS 78
Cdd:COG4670    2 KIISAEEAAALIKDGDTVATSGFVGAGVPEELLKALeerfLETGHpRDLTLIhAAGQGdGKGRGLDHLAHEGLVKRVIGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525  79 HIGSNPVAGKQMTEGTLEVQFSPQGTLAERIRAGGAGLGGILTDVGID------------NQmvCEKKDIV---TVAGKR 143
Cdd:COG4670   82 HWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGtfvdprleggklNE--RTTEDLVelvEIDGEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489323525 144 YLIEEALTADFAFINAYIADEFGNLTYDKTARNMNPL-MAMAARRT----FAEAERIVPMGEISEEMIVTPGVFVEGVVR 218
Cdd:COG4670  160 YLFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLaIAQAAKNSggivIAQVERIVKRGSLHPKDVKVPGILVDYVVV 239

                 ..
gi 489323525 219 SE 220
Cdd:COG4670  240 AP 241
 
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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