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Conserved domains on  [gi|494652191|ref|WP_007410135|]
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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];
3-225 1.45e-125

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


:

Pssm-ID: 441394  Cd Length: 226  Bit Score: 354.39  E-value: 1.45e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   3 KGKVMDSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDdwGLGLLLANRQIKKMVASY--- 79
Cdd:COG1788    1 MDKVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvgg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191  80 VGENKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAW 159
Cdd:COG1788   79 VGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEGKETREIDGEEYVLEPALRADVALIHAQ 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494652191 160 KADPLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLL--GGIHEKRI 225
Cdd:COG1788  159 KADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEvpGGARDKRI 226
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
3-225 1.45e-125

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 354.39  E-value: 1.45e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   3 KGKVMDSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDdwGLGLLLANRQIKKMVASY--- 79
Cdd:COG1788    1 MDKVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvgg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191  80 VGENKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAW 159
Cdd:COG1788   79 VGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEGKETREIDGEEYVLEPALRADVALIHAQ 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494652191 160 KADPLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLL--GGIHEKRI 225
Cdd:COG1788  159 KADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEvpGGARDKRI 226
CoA_trans pfam01144
Coenzyme A transferase;
13-215 5.64e-85

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 251.45  E-value: 5.64e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   13 AAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVddWGLGLLLANRQIKKMVASYVGE--NKTFERQF 90
Cdd:pfam01144   8 VAKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaNPEFGRQY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   91 LSGELEVELVPQGTLAERIRAGGAGIP--AFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAWKADPLGNLM 168
Cdd:pfam01144  86 FSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKKRVPGFGGAMYLLEPALRADVALIKASKADGEGNLV 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 494652191  169 FRKTARNFN-PLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHV 215
Cdd:pfam01144 166 FRTTAPNFNgPAVAAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAV 213
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
5-217 1.26e-84

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: 250.84  E-value: 1.26e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191    5 KVMDSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDDWGLGLLLANRQIKKMVASY--VGE 82
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   83 NKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAWKAD 162
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEGKETREFDGKGYVLEYPLPADFALIKAHKAD 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 494652191  163 PLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLL 217
Cdd:TIGR02429 164 RWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVVE 218
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
3-219 5.99e-83

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 246.59  E-value: 5.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   3 KGKVMdSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDDWGLGLLLANRQIKKMVASYVGE 82
Cdd:PRK09920   2 KTKLM-TLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191  83 NKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAWKAD 162
Cdd:PRK09920  81 NPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRAD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494652191 163 PLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLLGG 219
Cdd:PRK09920 161 TLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQ 217
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
11-215 5.27e-81

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: 241.34  E-value: 5.27e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191    11 QDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGvddWGLGLLLANRQIKKMVASYVGENKTFERQF 90
Cdd:smart00882   3 AEAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191    91 LSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHK----TFDGRTYLLEKGITGNAAIVKAWKADPLGN 166
Cdd:smart00882  80 FDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEGGkvrpFGMGGAYLLVPAIRPDVALIRAHTADEFGN 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 494652191   167 LMFRKTARNFN-PLAAMAGKVTIAEAEEIVDAGELDPDQIH--TPGIFVQHV 215
Cdd:smart00882 160 LVYEKEATSCGlPLTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAV 211
 
Name Accession Description Interval E-value
AtoD COG1788
Acyl CoA:acetate/3-ketoacid CoA transferase, alpha subunit [Lipid transport and metabolism];
3-225 1.45e-125

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


Pssm-ID: 441394  Cd Length: 226  Bit Score: 354.39  E-value: 1.45e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   3 KGKVMDSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDdwGLGLLLANRQIKKMVASY--- 79
Cdd:COG1788    1 MDKVVISLAEAVADVKDGMTIAIGGFGLCGIPMALIDELIRQGVKDLTLISNNAGVD--GLGLLIGAGQVKKVIASYvgg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191  80 VGENKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAW 159
Cdd:COG1788   79 VGLNPEFRRAVEAGELEVELVPQGTLAERLRAGGAGLPFFPTRTGLGTDVAEGKETREIDGEEYVLEPALRADVALIHAQ 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 494652191 160 KADPLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLL--GGIHEKRI 225
Cdd:COG1788  159 KADRAGNLVYRGTARNFNPLMAMAAKRVIVEVEEIVEVGELDPDAVVTPGIFVDAVVEvpGGARDKRI 226
CoA_trans pfam01144
Coenzyme A transferase;
13-215 5.64e-85

Coenzyme A transferase;


Pssm-ID: 395909 [Multi-domain]  Cd Length: 216  Bit Score: 251.45  E-value: 5.64e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   13 AAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVddWGLGLLLANRQIKKMVASYVGE--NKTFERQF 90
Cdd:pfam01144   8 VAKEIKDGMTVNVGGFGLIGIPETLIAALARSGVKDLTVISNEAGV--LGLGPLLLNGSVKKVIASYGGEtaNPEFGRQY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   91 LSGELEVELVPQGTLAERIRAGGAGIP--AFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAWKADPLGNLM 168
Cdd:pfam01144  86 FSGELEFELWPQGGLADRLRAGGAGIPfeGFLTNTGIGTYVAPKKRVPGFGGAMYLLEPALRADVALIKASKADGEGNLV 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 494652191  169 FRKTARNFN-PLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHV 215
Cdd:pfam01144 166 FRTTAPNFNgPAVAAAAKVTILEVEEIVEKGELLPLTVHTPGVLVDAV 213
pcaI_scoA_fam TIGR02429
3-oxoacid CoA-transferase, A subunit; Various members of this family are characterized as the ...
5-217 1.26e-84

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: 250.84  E-value: 1.26e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191    5 KVMDSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDDWGLGLLLANRQIKKMVASY--VGE 82
Cdd:TIGR02429   4 KTIESAAEAVSVIPDGATIMIGGFGTAGQPFELIDALIDTGAKDLTIVSNNAGNGEIGLAALLKAGQVRKLICSFprQSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   83 NKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAWKAD 162
Cdd:TIGR02429  84 SYVFDELYRAGKIELELVPQGTLAERIRAAGAGLGAFFTPTGYGTLLAEGKETREFDGKGYVLEYPLPADFALIKAHKAD 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 494652191  163 PLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLL 217
Cdd:TIGR02429 164 RWGNLTYRKAARNFGPIMAMAAKTTIAQVSQVVELGELDPEDVITPGIFVQRVVE 218
PRK09920 PRK09920
acetyl-CoA:acetoacetyl-CoA transferase subunit alpha; Provisional
3-219 5.99e-83

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


Pssm-ID: 182146 [Multi-domain]  Cd Length: 219  Bit Score: 246.59  E-value: 5.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   3 KGKVMdSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGVDDWGLGLLLANRQIKKMVASYVGE 82
Cdd:PRK09920   2 KTKLM-TLQDATGFFRDGMTIMVGGFMGIGTPSRLVEALLESGVRDLTLIANDTAFVDTGIGPLIVNGRVKKVIASHIGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191  83 NKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHKTFDGRTYLLEKGITGNAAIVKAWKAD 162
Cdd:PRK09920  81 NPETGRRMISGEMDVELVPQGTLIEQIRCGGAGLGGFLTPTGVGTVVEEGKQTLTLDGKTWLLERPLRADLALIRAHRAD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 494652191 163 PLGNLMFRKTARNFNPLAAMAGKVTIAEAEEIVDAGELDPDQIHTPGIFVQHVLLGG 219
Cdd:PRK09920 161 TLGNLTYQLSARNFNPLIALAADITLVEPDELVETGELQPDHIVTPGAVIDHIIVSQ 217
CoA_trans smart00882
Coenzyme A transferase; Coenzyme A (CoA) transferases belong to an evolutionary conserved ...
11-215 5.27e-81

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: 241.34  E-value: 5.27e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191    11 QDAAALIKDGDTLIAGGFGLCGIPEQLILAIRDSGVKNLTVVSNNCGvddWGLGLLLANRQIKKMVASYVGENKTFERQF 90
Cdd:smart00882   3 AEAAREIKDGDTVALGGFGGLPTPAALILALIRQGPKDLTLISENGG---LGLGLLAGEGDVKKIIAGHVGLTPLLGRLY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191    91 LSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSVAEGKEHK----TFDGRTYLLEKGITGNAAIVKAWKADPLGN 166
Cdd:smart00882  80 FDGEIESFLLPQGGLADRLRAGAAGVPGFGTLAGLGTDVDPRYEGGkvrpFGMGGAYLLVPAIRPDVALIRAHTADEFGN 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 494652191   167 LMFRKTARNFN-PLAAMAGKVTIAEAEEIVDAGELDPDQIH--TPGIFVQHV 215
Cdd:smart00882 160 LVYEKEATSCGlPLTAAAAKKVIVQVEEIVDLGVLDPDPVRllIPGVLVDAV 211
YdiF COG4670
Acyl CoA:acetate/3-ketoacid CoA transferase [Lipid transport and metabolism];
4-215 2.95e-28

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


Pssm-ID: 443707 [Multi-domain]  Cd Length: 511  Bit Score: 111.36  E-value: 2.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191   4 GKVMdSYQDAAALIKDGDTLIAGGFGLCGIPEQLILAI----RDSGV-KNLTVVSnNCGVDDW---GLGLLLANRQIKKM 75
Cdd:COG4670    1 SKII-SAEEAAALIKDGDTVATSGFVGAGVPEELLKALeerfLETGHpRDLTLIH-AAGQGDGkgrGLDHLAHEGLVKRV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191  76 VASYVGENKTFERQFLSGELEVELVPQGTLAERIRAGGAGIPAFYTPAGVGTSV-------------AEGK-EHKTFDGR 141
Cdd:COG4670   79 IGGHWGLSPKLQKLAVENKIEAYNLPQGVISHLFREIAAGRPGVLTKVGLGTFVdprleggklnertTEDLvELVEIDGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494652191 142 TYLLEKGITGNAAIVKAWKADPLGNLMFRKTARNFNPLA-AMA-----GKVtIAEAEEIVDAGELDPDQIHTPGIFVQHV 215
Cdd:COG4670  159 EYLFYKAFPIDVALIRGTTADEDGNLSMEHEALTLEVLAiAQAaknsgGIV-IAQVERIVKRGSLHPKDVKVPGILVDYV 237
 
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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