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Conserved domains on  [gi|528501102|ref|XP_005157453|]
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putative lipoyltransferase 2, mitochondrial isoform X1 [Danio rerio]

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] ...
11-213 5.09e-99

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: 285.92  E-value: 5.09e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  11 VHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPyppaeEQRLKALGADFCRTNRGGLITFHGP 90
Cdd:cd16444    3 RDLGLIPYEEAWELQKRLVAERIAG--ETPDTLWLLEHPPVYTLGRRGKP-----ENLLNNGGIPVVRTDRGGQVTYHGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  91 GQLVCYPILNLGCFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDM 169
Cdd:cd16444   76 GQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGaPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528501102 170 SWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQF 213
Cdd:cd16444  156 SPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
11-213 5.09e-99

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: 285.92  E-value: 5.09e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  11 VHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPyppaeEQRLKALGADFCRTNRGGLITFHGP 90
Cdd:cd16444    3 RDLGLIPYEEAWELQKRLVAERIAG--ETPDTLWLLEHPPVYTLGRRGKP-----ENLLNNGGIPVVRTDRGGQVTYHGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  91 GQLVCYPILNLGCFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDM 169
Cdd:cd16444   76 GQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGaPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528501102 170 SWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQF 213
Cdd:cd16444  156 SPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
5-218 5.55e-91

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: 266.20  E-value: 5.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102   5 KAAVKAVHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPyppaeEQRLKALGADFCRTNRGGL 84
Cdd:COG0321    1 NRPLIIRDLGLVDYEEAWAAQRRLTAARVAG--DTPDELWLLEHPPVYTLGRSGKP-----EHLLAPGGIPVVQTDRGGQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  85 ITFHGPGQLVCYPILNLGCFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLAL 163
Cdd:COG0321   74 ITYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGaPGVWVDGRKIAAIGLRVRRGVTYHGFAL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528501102 164 NCNTDMSWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQFNCTLT 218
Cdd:COG0321  154 NVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELV 208
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
4-218 9.16e-55

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 174.78  E-value: 9.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102   4 TKAAVKAVHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPYP-PAEeqrlkalGADFCRTNRG 82
Cdd:PRK14345   8 STMPIEVRRLGLVDYQEAWDLQRELADARVAG--EGPDTLLLLEHPAVYTAGKRTEPHErPTD-------GTPVVDVDRG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  83 GLITFHGPGQLVCYPILNLGcFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWV------GDNKICAIGIHCGRY 155
Cdd:PRK14345  79 GKITWHGPGQLVGYPIIKLA-EPLDVVDYVRRLEEALIAVCADLGLNAGRVDGrSGVWVpadggrPDRKIAAIGIRVSRG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528501102 156 ITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQFNCTLT 218
Cdd:PRK14345 158 VTMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDGRLP 220
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
43-214 1.37e-51

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: 164.97  E-value: 1.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102   43 LLLCEHEPVYTIGLRQAP--------YPPAEeqrlkalgadFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCE 114
Cdd:TIGR00214  15 IMLVEHYPVYTQGQAGKTehllfdpdIPPAE----------VVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVTQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  115 LERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQELE 193
Cdd:TIGR00214  85 LEQTVIITLAELGIEGEPIADaTGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLNQFLP 164
                         170       180
                  ....*....|....*....|.
gi 528501102  194 RdVPPEEAIPELLEAFTEQFN 214
Cdd:TIGR00214 165 G-ATVENVAPLLIKAFAELLG 184
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
11-213 5.09e-99

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: 285.92  E-value: 5.09e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  11 VHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPyppaeEQRLKALGADFCRTNRGGLITFHGP 90
Cdd:cd16444    3 RDLGLIPYEEAWELQKRLVAERIAG--ETPDTLWLLEHPPVYTLGRRGKP-----ENLLNNGGIPVVRTDRGGQVTYHGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  91 GQLVCYPILNLGCFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDM 169
Cdd:cd16444   76 GQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRRPGaPGVWVGDRKIASIGIRVRRGVTYHGLALNVNTDL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 528501102 170 SWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQF 213
Cdd:cd16444  156 SPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
5-218 5.55e-91

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: 266.20  E-value: 5.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102   5 KAAVKAVHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPyppaeEQRLKALGADFCRTNRGGL 84
Cdd:COG0321    1 NRPLIIRDLGLVDYEEAWAAQRRLTAARVAG--DTPDELWLLEHPPVYTLGRSGKP-----EHLLAPGGIPVVQTDRGGQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  85 ITFHGPGQLVCYPILNLGCFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLAL 163
Cdd:COG0321   74 ITYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERRPGaPGVWVDGRKIAAIGLRVRRGVTYHGFAL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 528501102 164 NCNTDMSWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQFNCTLT 218
Cdd:COG0321  154 NVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELV 208
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
4-218 9.16e-55

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 174.78  E-value: 9.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102   4 TKAAVKAVHLGRISYHSALKIQQQHIQQHLDSssNIPNTLLLCEHEPVYTIGLRQAPYP-PAEeqrlkalGADFCRTNRG 82
Cdd:PRK14345   8 STMPIEVRRLGLVDYQEAWDLQRELADARVAG--EGPDTLLLLEHPAVYTAGKRTEPHErPTD-------GTPVVDVDRG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  83 GLITFHGPGQLVCYPILNLGcFKKSVRWYVCELERTVIKMCGKFGIKASTSPD-TGVWV------GDNKICAIGIHCGRY 155
Cdd:PRK14345  79 GKITWHGPGQLVGYPIIKLA-EPLDVVDYVRRLEEALIAVCADLGLNAGRVDGrSGVWVpadggrPDRKIAAIGIRVSRG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528501102 156 ITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQELERDVPPEEAIPELLEAFTEQFNCTLT 218
Cdd:PRK14345 158 VTMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAALCDALDGRLP 220
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
43-214 1.37e-51

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: 164.97  E-value: 1.37e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102   43 LLLCEHEPVYTIGLRQAP--------YPPAEeqrlkalgadFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCE 114
Cdd:TIGR00214  15 IMLVEHYPVYTQGQAGKTehllfdpdIPPAE----------VVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVTQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  115 LERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQELE 193
Cdd:TIGR00214  85 LEQTVIITLAELGIEGEPIADaTGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLNQFLP 164
                         170       180
                  ....*....|....*....|.
gi 528501102  194 RdVPPEEAIPELLEAFTEQFN 214
Cdd:TIGR00214 165 G-ATVENVAPLLIKAFAELLG 184
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
41-200 2.82e-50

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 162.89  E-value: 2.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  41 NTLLLCEHEPVYTIGL--RQAPYPPAEEQrLKALGADFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCELERT 118
Cdd:PRK14348  39 NRIIFCEHPHVYTLGRsgKENNMLLGEEQ-LKTIGATLYHIDRGGDITYHGPGQLVCYPILNLEEFGLGLKEYVHLLEEA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 119 VIKMCGKFGIKAST-SPDTGVWV-GDN----KICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQEL 192
Cdd:PRK14348 118 VIRVCASYGVVAGRlEKATGVWLeGDTsrarKICAIGVRSSHYVTMHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQEL 197

                 ....*...
gi 528501102 193 ERDVPPEE 200
Cdd:PRK14348 198 GHSIDMAE 205
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
40-214 3.78e-43

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 144.83  E-value: 3.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  40 PNTLLLCEHEPVYTIGlRQAPY-----PPAEEQrlkalgADFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCE 114
Cdd:PRK14344  50 PQAVWLLEHQLCYTLG-RGASEdnllfSLNNPP------ADVFRIDRGGEVTHHMPGQLVTYLVLDLRRFNKDLNWYLRQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 115 LERTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQELe 193
Cdd:PRK14344 123 LEQVLIDVLADLGIDGERLDGlTGVWIGNKKVASIGIGCRRWITQHGFSLNVDCDLEGFNKIVPCGLEGCQVGRLSDWI- 201
                        170       180
                 ....*....|....*....|.
gi 528501102 194 RDVPPEEAIPELLEAFTEQFN 214
Cdd:PRK14344 202 PGLNIKEVKPLLKKSLQERFG 222
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
45-213 7.15e-40

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 136.19  E-value: 7.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  45 LCEHEPVYTIGLRQAPYPPAEEQRLKALgadfcRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCELERTVIKMCG 124
Cdd:PRK14341  40 LLEHPPLYTAGTSAKAEDLLDPDRFPVY-----ETGRGGQYTYHGPGQRVAYVMLDLKRRRRDVRAFVAALEEWIIATLA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 125 KFGIKASTSPDT-GVWVGDN--------KICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLsQELERD 195
Cdd:PRK14341 115 AFNIRGERREDRvGVWVRRPdkgsgaedKIAAIGVRLRRWVSFHGISINVEPDLSHFSGIVPCGISEHGVTSL-VDLGLP 193
                        170
                 ....*....|....*...
gi 528501102 196 VPPEEAIPELLEAFTEQF 213
Cdd:PRK14341 194 VTMDDVDAALKKAFEKVF 211
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
37-209 7.92e-40

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: 135.36  E-value: 7.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  37 SNIPNTLLLCEHEPVYTIGLRQAPYPPAEEQRLKALGADFCRTNRGGLITFHGPGQLVCYPILNLGcFKKSVRWYVCELE 116
Cdd:cd16435   26 SNQSSTLLLWEHPTTVTLGRLDRELPHLELAKKIERGYELVVRNRGGRAVSHDPGQLVFSPVIGPN-VEFMISKFNLIIE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 117 RTVIKMCGKFGIKASTSPD-TGVWVGDNKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQELERD 195
Cdd:cd16435  105 EGIRDAIADFGQSAEVKWGrNDLWIDNRKVCGIAVRVVKEAIFHGIALNLNQDLENFTEIIPCGYKPERVTSLSLELGRK 184
                        170
                 ....*....|....
gi 528501102 196 VPPEEAIPELLEAF 209
Cdd:cd16435  185 VTVEQVLERVLAAF 198
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
36-214 1.22e-39

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 135.39  E-value: 1.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  36 SSNIPNTLLLCEHEPVYTIGlrQAPYPpaeEQRLKALGADFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCEL 115
Cdd:PRK14342  31 DEETPDEIWLVEHPPVFTQG--QAGKP---EHILNPGDIPVVQSDRGGQVTYHGPGQLVMYVLLDLKRLKLGVRQLVTAI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 116 ERTVIKMCGKFGIKASTSPDT-GVWVGDNKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLSQeLER 194
Cdd:PRK14342 106 EQTVINTLAEYGIEAHAKPDApGVYVDGKKIASLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGLEMTQLSD-LGG 184
                        170       180
                 ....*....|....*....|
gi 528501102 195 DVPPEEAIPELLEAFTEQFN 214
Cdd:PRK14342 185 PATVDEVAPRLLAELLALLG 204
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
36-190 8.50e-31

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 112.72  E-value: 8.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  36 SSNIPNTLLLCEHEPVYTIGLRQApyppaEEQRLKALGADFCRTNRGGLITFHGPGQLVCYPILNLGC--FKKSVRWYVC 113
Cdd:PRK14347  29 SDHEPEIVYLVEHSEVYTAGTNYK-----QEELLNYGDIPVIYTGRGGKFTFHGPGQRVIYPILNLASpnRHKDLKLYIK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 114 ELERTVIKMCGKFGIKASTSPD-TGVWVGDN-----KICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTS 187
Cdd:PRK14347 104 MLEEWIINSLNYFGIKAYIIKDkVGIWVKVRkdefaKIAAIGVRVRKWVTYHGVAINISTDLSKFSGIIPCGLENSLVTS 183

                 ...
gi 528501102 188 LSQ 190
Cdd:PRK14347 184 LNQ 186
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
12-189 9.15e-28

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 105.22  E-value: 9.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  12 HLGRISYHSALKIQQQHIQQHLDSSsniPNTLLLCEHEPVYTIGLrqapyPPAEEQRLKALGADFCRTNRGGLITFHGPG 91
Cdd:PRK14346   7 MLGRVDYLATVQAMQAFTAERTPET---PDELWICEHPPVYTQGL-----AGKADHVLNPGDIPVVATNRGGQVTYHGPG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  92 QLVCYPILNLGCFKKSVRWYVCELERTVIKMCGKFGI-----------------------------KASTSPDTGVWVGD 142
Cdd:PRK14346  79 QVVAYPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVtghrvagapgiyvrlddpfshaalpqrpqKRGGGAPQPPFRGL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 528501102 143 NKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLS 189
Cdd:PRK14346 159 GKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLS 205
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
40-189 1.31e-24

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 96.58  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  40 PNTLLLCEHEPVYTIGlrQAPYPpaeEQRLKALGADFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCELERTV 119
Cdd:PRK14349  30 ADEIWLCEHAPVYTLG--QAGRP---EHLLNPGLIPVVHCDRGGQVTYHGPGQVLAYTLFDLRRAGLYVREYVDMLEQAT 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528501102 120 IKMCGKFGI-KASTSPDT-GVWVGD-----NKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVGKGVTSLS 189
Cdd:PRK14349 105 LATLRELGLeQACRKPGApGIYVPQpggelAKIAALGVKVRNGYAYHGLALNIDMDLSPFLGINPCGYEGLRTVDLA 181
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
40-182 5.94e-22

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 89.85  E-value: 5.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  40 PNTLLLCEHEPVYTIGlrQAPYPpaeEQRLKA-LGADFCRTNRGGLITFHGPGQLVCYPILNLGCFKKSVRWYVCELERT 118
Cdd:PRK14343  44 PDEIWLVEHPPVYTLG--QAGDP---AHLLVAdSGIPLVKVDRGGQITYHGPGQVVAYLLLDLRRRKLMVRELVTRIEQA 118
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528501102 119 VIKMCGKFGIKASTSP-------DTGVWVGDnKICAIGIHCGRYITSHGLALNCNTDMSWFDNIVPCGIVG 182
Cdd:PRK14343 119 VIDTLAAYNLASERKAgapgiyvASGPHQGA-KIAALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAG 188
LplA COG0095
Lipoate-protein ligase A [Coenzyme transport and metabolism]; Lipoate-protein ligase A is part ...
39-214 1.18e-08

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


Pssm-ID: 439865  Cd Length: 246  Bit Score: 53.70  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102  39 IPNTLLLCEHEPVYTIGLRQAPYPPAEEQRLKALGADFCRTNRGGLITFHGPGQLvCY---------PILNLGCFKKSVR 109
Cdd:COG0095   29 DPPTLRLWRNPPTVVIGRFQNVLPEVNLEYVEEHGIPVVRRISGGGAVYHDPGNL-NYslilpeddvPLSIEESYRKLLE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 110 WyvcelertVIKMCGKFGIKASTSPDTGVWVGDNKICaiGI---HCGRYITSHG-LALNCNTD-MSWFDNIVPCGIVGKG 184
Cdd:COG0095  108 P--------ILEALRKLGVDAEFSGRNDIVVDGRKIS--GNaqrRRKGAVLHHGtLLVDGDLEkLAKVLRVPYEKLRDKG 177
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 528501102 185 -------VTSLSQELERDVPPEEAIPELLEAFTEQFN 214
Cdd:COG0095  178 iksvrsrVTNLSELLGTDITREEVKEALLEAFAEVLG 214
PRK08330 PRK08330
biotin--protein ligase; Provisional
119-207 1.53e-03

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 38.57  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528501102 119 VIKMCGKFGIKASTSPDTGVWVGDNKICAIGIHC-GRYITShGLALNCNtdmswfdNIVPCGIVgKGVTSLSQELERDVP 197
Cdd:PRK08330  80 VVDTLREFGIEGKIKWPNDVLVNYKKIAGVLVEGkGDFVVL-GIGLNVN-------NEIPDELR-ETATSMKEVLGREVP 150
                         90
                 ....*....|
gi 528501102 198 PEEAIPELLE 207
Cdd:PRK08330 151 LIEVFKRLVE 160
 
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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