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Conserved domains on  [gi|1836505311|ref|XP_033833232|]
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putative lipoyltransferase 2, mitochondrial [Periophthalmus magnuspinnatus]

Protein Classification

lipoyl(octanoyl) transferase( domain architecture ID 11612812)

lipoyl(octanoyl) transferase (LipB/LIPT2) catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-209 6.28e-87

lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives.


:

Pssm-ID: 319743  Cd Length: 199  Bit Score: 255.88  E-value: 6.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   7 EVVRLGLVSYSEAMRVQRFYVDRVKSRPSSAwTLLLCEHSPVYTIGIRTsqypdRDLDLLRTKGAEVHKTNRGGLITFHG 86
Cdd:cd16444     1 IVRDLGLIPYEEAWELQKRLVAERIAGETPD-TLWLLEHPPVYTLGRRG-----KPENLLNNGGIPVVRTDRGGQVTYHG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  87 PGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVD 165
Cdd:cd16444    75 PGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPgAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1836505311 166 LSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNF 209
Cdd:cd16444   155 LSPFNRINPCGIkGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-209 6.28e-87

lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives.


Pssm-ID: 319743  Cd Length: 199  Bit Score: 255.88  E-value: 6.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   7 EVVRLGLVSYSEAMRVQRFYVDRVKSRPSSAwTLLLCEHSPVYTIGIRTsqypdRDLDLLRTKGAEVHKTNRGGLITFHG 86
Cdd:cd16444     1 IVRDLGLIPYEEAWELQKRLVAERIAGETPD-TLWLLEHPPVYTLGRRG-----KPENLLNNGGIPVVRTDRGGQVTYHG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  87 PGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVD 165
Cdd:cd16444    75 PGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPgAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1836505311 166 LSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNF 209
Cdd:cd16444   155 LSPFNRINPCGIkGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 3-217 1.44e-86

Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440090  Cd Length: 211  Bit Score: 255.42  E-value: 1.44e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   3 RPVLEVVRLGLVSYSEAMRVQRFYVDRVKSRPSSAwTLLLCEHSPVYTIGIRTsqypdRDLDLLRTKGAEVHKTNRGGLI 82
Cdd:COG0321     1 NRPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTPD-ELWLLEHPPVYTLGRSG-----KPEHLLAPGGIPVVQTDRGGQI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  83 TFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALN 161
Cdd:COG0321    75 TYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPgAPGVWVDGRKIAAIGLRVRRGVTYHGFALN 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1836505311 162 CDVDLSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNFNCDLHDAA 217
Cdd:COG0321   155 VNPDLSPFSRIVPCGIaDLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVELS 211
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-213 4.23e-60

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 189.04  E-value: 4.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   1 MSRPVLEVVRLGLVSYSEAMRVQRFYVDRV--KSRPSsawTLLLCEHSPVYTIGIRTsQYPDRDLDllrtkGAEVHKTNR 78
Cdd:PRK14345    7 SSTMPIEVRRLGLVDYQEAWDLQRELADARvaGEGPD---TLLLLEHPAVYTAGKRT-EPHERPTD-----GTPVVDVDR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  79 GGLITFHGPGQLVCYPILHLGLlKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIR------DHKVCAIGIHCSR 151
Cdd:PRK14345   78 GGKITWHGPGQLVGYPIIKLAE-PLDVVDYVRRLEEALIAVCADLGLNAGRVDgRSGVWVPadggrpDRKIAAIGIRVSR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836505311 152 YVTSHGLALNCDVDLSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNFNCDL 213
Cdd:PRK14345  157 GVTMHGFALNCDNDLAAFDAIVPCGIsDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDGRL 219
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 40-202 4.43e-43

lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as alpha-ketoacid dehydrogenases. Involved in activation and re-activation (following denaturation) of lipoyl-protein ligases (calcium ion-dependant process). [Protein fate, Protein modification and repair]


Pssm-ID: 272964  Cd Length: 184  Bit Score: 143.78  E-value: 4.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  40 LLLCEHSPVYTIG-IRTSQYPDRDLDLLRtkgAEVHKTNRGGLITFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVD 118
Cdd:TIGR00214  15 IMLVEHYPVYTQGqAGKTEHLLFDPDIPP---AEVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVTQLEQTVII 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311 119 VCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVDLSWFSHIAPCGL-DKGVTSLSRemQRRICVEE 196
Cdd:TIGR00214  92 TLAELGIEGEPIAdATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYaGREMGSLNQ--FLPGATVE 169


                  ....*.
gi 1836505311 197 SVHPLL 202
Cdd:TIGR00214 170 NVAPLL 175
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
 7-209 6.28e-87

lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives.


Pssm-ID: 319743  Cd Length: 199  Bit Score: 255.88  E-value: 6.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   7 EVVRLGLVSYSEAMRVQRFYVDRVKSRPSSAwTLLLCEHSPVYTIGIRTsqypdRDLDLLRTKGAEVHKTNRGGLITFHG 86
Cdd:cd16444     1 IVRDLGLIPYEEAWELQKRLVAERIAGETPD-TLWLLEHPPVYTLGRRG-----KPENLLNNGGIPVVRTDRGGQVTYHG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  87 PGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVD 165
Cdd:cd16444    75 PGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPgAPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTD 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1836505311 166 LSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNF 209
Cdd:cd16444   155 LSPFNRINPCGIkGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
 3-217 1.44e-86

Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440090  Cd Length: 211  Bit Score: 255.42  E-value: 1.44e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   3 RPVLEVVRLGLVSYSEAMRVQRFYVDRVKSRPSSAwTLLLCEHSPVYTIGIRTsqypdRDLDLLRTKGAEVHKTNRGGLI 82
Cdd:COG0321     1 NRPLIIRDLGLVDYEEAWAAQRRLTAARVAGDTPD-ELWLLEHPPVYTLGRSG-----KPEHLLAPGGIPVVQTDRGGQI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  83 TFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALN 161
Cdd:COG0321    75 TYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPgAPGVWVDGRKIAAIGLRVRRGVTYHGFALN 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1836505311 162 CDVDLSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNFNCDLHDAA 217
Cdd:COG0321   155 VNPDLSPFSRIVPCGIaDLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVELS 211
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-213 4.23e-60

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 189.04  E-value: 4.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   1 MSRPVLEVVRLGLVSYSEAMRVQRFYVDRV--KSRPSsawTLLLCEHSPVYTIGIRTsQYPDRDLDllrtkGAEVHKTNR 78
Cdd:PRK14345    7 SSTMPIEVRRLGLVDYQEAWDLQRELADARvaGEGPD---TLLLLEHPAVYTAGKRT-EPHERPTD-----GTPVVDVDR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  79 GGLITFHGPGQLVCYPILHLGLlKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIR------DHKVCAIGIHCSR 151
Cdd:PRK14345   78 GGKITWHGPGQLVGYPIIKLAE-PLDVVDYVRRLEEALIAVCADLGLNAGRVDgRSGVWVPadggrpDRKIAAIGIRVSR 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1836505311 152 YVTSHGLALNCDVDLSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSFSRNFNCDL 213
Cdd:PRK14345  157 GVTMHGFALNCDNDLAAFDAIVPCGIsDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDGRL 219
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
13-196 2.05e-47

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 156.34  E-value: 2.05e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  13 LVSYSEAMRVQRFYVD---RVKSRPSSAWT-LLLCEHSPVYTIGiRTSQYPDRDL--DLLRTKGAEVHKTNRGGLITFHG 86
Cdd:PRK14348   10 LIPYSEAWSRQTEWFDalvHAKQNGESYENrIIFCEHPHVYTLG-RSGKENNMLLgeEQLKTIGATLYHIDRGGDITYHG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  87 PGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANT-SPLTGVWI-----RDHKVCAIGIHCSRYVTSHGLAL 160
Cdd:PRK14348   89 PGQLVCYPILNLEEFGLGLKEYVHLLEEAVIRVCASYGVVAGRlEKATGVWLegdtsRARKICAIGVRSSHYVTMHGLAL 168

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1836505311 161 NCDVDLSWFSHIAPCG-LDKGVTSLSREMQRRICVEE 196
Cdd:PRK14348  169 NVNTDLRYFSYIHPCGfIDKGVTSLQQELGHSIDMAE 205
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
13-179 7.26e-45

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 149.45  E-value: 7.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  13 LVSYSEAMRVQRFYVDRVKSRPSSAWTLLLCEHSPVYTIGiRTSQYPDRDLDLLRTKgAEVHKTNRGGLITFHGPGQLVC 92
Cdd:PRK14344   26 IVPFEDAWKWQKEWQQALIEDPSNPQAVWLLEHQLCYTLG-RGASEDNLLFSLNNPP-ADVFRIDRGGEVTHHMPGQLVT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  93 YPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVDLSWFSH 171
Cdd:PRK14344  104 YLVLDLRRFNKDLNWYLRQLEQVLIDVLADLGIDGERLDgLTGVWIGNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNK 183


                  ....*...
gi 1836505311 172 IAPCGLDK 179
Cdd:PRK14344  184 IVPCGLEG 191
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
 40-202 4.43e-43

lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the lipoyl-protein ligase activity required for lipoylation of enzymes such as alpha-ketoacid dehydrogenases. Involved in activation and re-activation (following denaturation) of lipoyl-protein ligases (calcium ion-dependant process). [Protein fate, Protein modification and repair]


Pssm-ID: 272964  Cd Length: 184  Bit Score: 143.78  E-value: 4.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  40 LLLCEHSPVYTIG-IRTSQYPDRDLDLLRtkgAEVHKTNRGGLITFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVD 118
Cdd:TIGR00214  15 IMLVEHYPVYTQGqAGKTEHLLFDPDIPP---AEVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVTQLEQTVII 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311 119 VCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVDLSWFSHIAPCGL-DKGVTSLSRemQRRICVEE 196
Cdd:TIGR00214  92 TLAELGIEGEPIAdATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYaGREMGSLNQ--FLPGATVE 169


                  ....*.
gi 1836505311 197 SVHPLL 202
Cdd:TIGR00214 170 NVAPLL 175
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
2-184 4.30e-38

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 131.96  E-value: 4.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   2 SRPVLEVVRLGLVSYSEAMRV--QRFYVDRVKSRPSSAWtllLCEHSPVYTIGirTSQYPDrdlDLLRTKGAEVHKTNRG 79
Cdd:PRK14341    1 APPVEWRISDGLVPYPEALAFmeARVAAIAAGTADELVW---LLEHPPLYTAG--TSAKAE---DLLDPDRFPVYETGRG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  80 GLITFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDH--------KVCAIGIHCS 150
Cdd:PRK14341   73 GQYTYHGPGQRVAYVMLDLKRRRRDVRAFVAALEEWIIATLAAFNIRGERREdRVGVWVRRPdkgsgaedKIAAIGVRLR 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1836505311 151 RYVTSHGLALNCDVDLSWFSHIAPCGL-DKGVTSL 184
Cdd:PRK14341  153 RWVSFHGISINVEPDLSHFSGIVPCGIsEHGVTSL 187
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
 8-205 6.94e-36

biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). Biotin is covalently attached at the active site of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. Biotin protein ligase (BPL) is the enzyme responsible for attaching biotin to a specific lysine at the active site of biotin enzymes. Biotin attachment is a two step reaction that results in the formation of an amide linkage between the carboxyl group of biotin and the epsilon-amino group of the modified lysine. Lipoate-protein ligase A (LplA) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.


Pssm-ID: 319740  Cd Length: 198  Bit Score: 125.73  E-value: 6.94e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   8 VVRLGLVSYSEAMRVQR-FYVDRVKSRPSsawTLLLCEHSPVYTIGIRTSQYPDRDLDLLRTKGAEVHKTNRGGLITFHG 86
Cdd:cd16435     2 VEVLDSVDYESAWAAQEkSLRENVSNQSS---TLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  87 PGQLVCYPILHLGlLKKGIRWYVGQLERTVVDVCGQFGLRANTSPL-TGVWIRDHKVCAIGIHCSRYVTSHGLALNCDVD 165
Cdd:cd16435    79 PGQLVFSPVIGPN-VEFMISKFNLIIEEGIRDAIADFGQSAEVKWGrNDLWIDNRKVCGIAVRVVKEAIFHGIALNLNQD 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1836505311 166 LSWFSHIAPCGL-DKGVTSLSREMQRRICVEESVHPLLHSF 205
Cdd:cd16435   158 LENFTEIIPCGYkPERVTSLSLELGRKVTVEQVLERVLAAF 198
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
1-176 3.40e-33

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 119.22  E-value: 3.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   1 MSRPVLEVVRLGLVSY---SEAMrvQRFYVDRVKSRPSSAWtllLCEHSPVYTIGIrtsqyPDRDLDLLRTKGAEVHKTN 77
Cdd:PRK14342    1 MMQNKLIVRQLGLQPYepvWQAM--QEFTDTRDEETPDEIW---LVEHPPVFTQGQ-----AGKPEHILNPGDIPVVQSD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  78 RGGLITFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGLRANTSP-LTGVWIRDHKVCAIGIHCSRYVTSH 156
Cdd:PRK14342   71 RGGQVTYHGPGQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIEAHAKPdAPGVYVDGKKIASLGLRIRRGCSFH 150

                         170       180
                  ....*....|....*....|
gi 1836505311 157 GLALNCDVDLSWFSHIAPCG 176
Cdd:PRK14342  151 GLALNVNMDLSPFLRINPCG 170
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
6-176 1.30e-29

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 110.23  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   6 LEVVRLGLVSYS---EAMrvQRFYVDRVKSRPSSAWtllLCEHSPVYTIGIrtsqyPDRDLDLLRTKGAEVHKTNRGGLI 82
Cdd:PRK14346    3 MDRRMLGRVDYLatvQAM--QAFTAERTPETPDELW---ICEHPPVYTQGL-----AGKADHVLNPGDIPVVATNRGGQV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  83 TFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGL---RANTSPltGVWIR-----DH-------------- 140
Cdd:PRK14346   73 TYHGPGQVVAYPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVtghRVAGAP--GIYVRlddpfSHaalpqrpqkrggga 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1836505311 141 ---------KVCAIGIHCSRYVTSHGLALNCDVDLSWFSHIAPCG 176
Cdd:PRK14346  151 pqppfrglgKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCG 195
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
13-186 1.53e-28

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 106.94  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  13 LVSYSEAMRVQRFYVDRVKSrPSSAWTLLLCEHSPVYTIGIRTSQYpdrdlDLLRTKGAEVHKTNRGGLITFHGPGQLVC 92
Cdd:PRK14347   10 FADYQVTLKLMEDYVNKVIS-DHEPEIVYLVEHSEVYTAGTNYKQE-----ELLNYGDIPVIYTGRGGKFTFHGPGQRVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  93 YPILHLGL--LKKGIRWYVGQLERTVVDVCGQFGLRAN-TSPLTGVWIRDH-----KVCAIGIHCSRYVTSHGLALNCDV 164
Cdd:PRK14347   84 YPILNLASpnRHKDLKLYIKMLEEWIINSLNYFGIKAYiIKDKVGIWVKVRkdefaKIAAIGVRVRKWVTYHGVAINIST 163

                         170       180
                  ....*....|....*....|...
gi 1836505311 165 DLSWFSHIAPCGLDKG-VTSLSR 186
Cdd:PRK14347  164 DLSKFSGIIPCGLENSlVTSLNQ 186
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
4-176 4.47e-28

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 106.41  E-value: 4.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311   4 PVLEVVRLGLVSYS---EAMRVqrFYVDRVKSRPSSAWtllLCEHSPVYTIGirtsQYPDRDLDLLRTKGAEVHKTNRGG 80
Cdd:PRK14343   13 LPVTVRWRGREPYEacfDAMRA--FTDARTADTPDEIW---LVEHPPVYTLG----QAGDPAHLLVADSGIPLVKVDRGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  81 LITFHGPGQLVCYPILHLGLLKKGIRWYVGQLERTVVDVCGQFGL---RANTSPltGVWIRDH-----KVCAIGIHCSRY 152
Cdd:PRK14343   84 QITYHGPGQVVAYLLLDLRRRKLMVRELVTRIEQAVIDTLAAYNLaseRKAGAP--GIYVASGphqgaKIAALGLKIRNG 161

                         170       180
                  ....*....|....*....|....
gi 1836505311 153 VTSHGLALNCDVDLSWFSHIAPCG 176
Cdd:PRK14343  162 CSYHGLSLNVKMDLRPFLAINPCG 185
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
18-182 1.43e-24

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 96.96  E-value: 1.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  18 EAMRVqrFYVDRVKSRPSSAWtllLCEHSPVYTIGirTSQYPDRdldLLRTKGAEVHKTNRGGLITFHGPGQLVCYPILH 97
Cdd:PRK14349   16 DAMKA--FTAARGPGTADEIW---LCEHAPVYTLG--QAGRPEH---LLNPGLIPVVHCDRGGQVTYHGPGQVLAYTLFD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836505311  98 LGLLKKGIRWYVGQLERTVVDVCGQFGL----RANTSPltGVWIRD-----HKVCAIGIHCSRYVTSHGLALNCDVDLSW 168
Cdd:PRK14349   86 LRRAGLYVREYVDMLEQATLATLRELGLeqacRKPGAP--GIYVPQpggelAKIAALGVKVRNGYAYHGLALNIDMDLSP 163

                         170
                  ....*....|....
gi 1836505311 169 FSHIAPCGLDKGVT 182
Cdd:PRK14349  164 FLGINPCGYEGLRT 177
 
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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