NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|229577004|ref|NP_080286|]
View 

octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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] ...
7-220 1.78e-70

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: 213.89  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   7 RLVWLGRVHYSELLALQEHWLRRLQADPRPGTLsgtkagvlLVCE-PagPVYTGGLRGglTPEETtrLRALGAEVRATGR 85
Cdd:cd16444    1 IVRDLGLIPYEEAWELQKRLVAERIAGETPDTL--------WLLEhP--PVYTLGRRG--KPENL--LNNGGIPVVRTDR 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  86 GGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHITS 165
Cdd:cd16444   67 GGQVTYHGPGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRR--PGAPGVWVGDRKIASIGIRVRRGVTY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 229577004 166 HGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAFKETF 220
Cdd:cd16444  145 HGLALNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
7-220 1.78e-70

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: 213.89  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   7 RLVWLGRVHYSELLALQEHWLRRLQADPRPGTLsgtkagvlLVCE-PagPVYTGGLRGglTPEETtrLRALGAEVRATGR 85
Cdd:cd16444    1 IVRDLGLIPYEEAWELQKRLVAERIAGETPDTL--------WLLEhP--PVYTLGRRG--KPENL--LNNGGIPVVRTDR 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  86 GGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHITS 165
Cdd:cd16444   67 GGQVTYHGPGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRR--PGAPGVWVGDRKIASIGIRVRRGVTY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 229577004 166 HGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAFKETF 220
Cdd:cd16444  145 HGLALNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
6-226 1.25e-61

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: 191.86  E-value: 1.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   6 VRLVWLGRVHYSELLALQEHWLRRLQADPRPGTLsgtkagvlLVCE-PagPVYTGGLRGGltPEEttRLRALGAEVRATG 84
Cdd:COG0321    4 LIIRDLGLVDYEEAWAAQRRLTAARVAGDTPDEL--------WLLEhP--PVYTLGRSGK--PEH--LLAPGGIPVVQTD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  85 RGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHIT 164
Cdd:COG0321   70 RGGQITYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERR--PGAPGVWVDGRKIAAIGLRVRRGVT 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577004 165 SHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAFKETFKCTLIS 226
Cdd:COG0321  148 YHGFALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVE 209
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-216 1.35e-36

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 128.56  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   1 MSLPVVRLVWLGRVHYSELLALQehwlRRLqADPRpgtLSGTKAGVLLVCEPAgPVYTGGLRggLTPEEttrLRALGAEV 80
Cdd:PRK14345   7 SSTMPIEVRRLGLVDYQEAWDLQ----REL-ADAR---VAGEGPDTLLLLEHP-AVYTAGKR--TEPHE---RPTDGTPV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  81 RATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRtHVAALEACAVRLCELRGLQGAR--ARpppyTGVWL------GERKI 152
Cdd:PRK14345  73 VDVDRGGKITWHGPGQLVGYPIIKLAEPLDVVD-YVRRLEEALIAVCADLGLNAGRvdGR----SGVWVpadggrPDRKI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577004 153 CAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAF 216
Cdd:PRK14345 148 AAIGIRVSRGVTMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAAL 211
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
42-220 6.77e-33

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: 117.59  E-value: 6.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   42 TKAGVLLVCEPagPVYTGGlRGGLTPEETTRLRALGAEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEA 121
Cdd:TIGR00214  11 TLDEIMLVEHY--PVYTQG-QAGKTEHLLFDPDIPPAEVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVTQLEQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  122 CAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQR 201
Cdd:TIGR00214  88 TVIITLAELGIEGEPI--ADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLNQFLPG 165
                         170
                  ....*....|....*....
gi 229577004  202 lVTVDEVMPSFLVAFKETF 220
Cdd:TIGR00214 166 -ATVENVAPLLIKAFAELL 183
 
Name Accession Description Interval E-value
LipB cd16444
lipoyl/octanoyl transferase; Lipoate-protein ligase B is a octanoyl-[acyl carrier protein] ...
7-220 1.78e-70

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: 213.89  E-value: 1.78e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   7 RLVWLGRVHYSELLALQEHWLRRLQADPRPGTLsgtkagvlLVCE-PagPVYTGGLRGglTPEETtrLRALGAEVRATGR 85
Cdd:cd16444    1 IVRDLGLIPYEEAWELQKRLVAERIAGETPDTL--------WLLEhP--PVYTLGRRG--KPENL--LNNGGIPVVRTDR 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  86 GGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHITS 165
Cdd:cd16444   67 GGQVTYHGPGQLVGYPILDLRRRGLDVRRYVRALEEAVIRTLAEYGIEAGRR--PGAPGVWVGDRKIASIGIRVRRGVTY 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 229577004 166 HGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAFKETF 220
Cdd:cd16444  145 HGLALNVNTDLSPFNRINPCGIKGKGVTSLSDLGGREVDMEEVKQKLVEEFAKIF 199
LipB COG0321
Lipoate-protein ligase B [Coenzyme transport and metabolism]; Lipoate-protein ligase B is part ...
6-226 1.25e-61

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: 191.86  E-value: 1.25e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   6 VRLVWLGRVHYSELLALQEHWLRRLQADPRPGTLsgtkagvlLVCE-PagPVYTGGLRGGltPEEttRLRALGAEVRATG 84
Cdd:COG0321    4 LIIRDLGLVDYEEAWAAQRRLTAARVAGDTPDEL--------WLLEhP--PVYTLGRSGK--PEH--LLAPGGIPVVQTD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  85 RGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHIT 164
Cdd:COG0321   70 RGGQITYHGPGQLVGYPILDLRRRGLDVRAYVRRLEEAVIDTLAEYGIEAERR--PGAPGVWVDGRKIAAIGLRVRRGVT 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577004 165 SHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAFKETFKCTLIS 226
Cdd:COG0321  148 YHGFALNVNPDLSPFSRIVPCGIADLGVTSLSDELGRPVTMEEVAEALIRHFAEVFGYELVE 209
PRK14345 PRK14345
lipoyl(octanoyl) transferase LipB;
1-216 1.35e-36

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 184638  Cd Length: 234  Bit Score: 128.56  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   1 MSLPVVRLVWLGRVHYSELLALQehwlRRLqADPRpgtLSGTKAGVLLVCEPAgPVYTGGLRggLTPEEttrLRALGAEV 80
Cdd:PRK14345   7 SSTMPIEVRRLGLVDYQEAWDLQ----REL-ADAR---VAGEGPDTLLLLEHP-AVYTAGKR--TEPHE---RPTDGTPV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  81 RATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRtHVAALEACAVRLCELRGLQGAR--ARpppyTGVWL------GERKI 152
Cdd:PRK14345  73 VDVDRGGKITWHGPGQLVGYPIIKLAEPLDVVD-YVRRLEEALIAVCADLGLNAGRvdGR----SGVWVpadggrPDRKI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 229577004 153 CAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAF 216
Cdd:PRK14345 148 AAIGIRVSRGVTMHGFALNCDNDLAAFDAIVPCGISDAGVTTLSAELGRTVTVAEVVDPVAAAL 211
PRK14348 PRK14348
lipoyl(octanoyl) transferase LipB;
14-208 1.74e-34

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172824  Cd Length: 221  Bit Score: 122.83  E-value: 1.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  14 VHYSELLALQEHWLRRLQADPRPGTLSGTKagvLLVCEPAGpVYTGGLRGG----LTPEEttRLRALGAEVRATGRGGLA 89
Cdd:PRK14348  11 IPYSEAWSRQTEWFDALVHAKQNGESYENR---IIFCEHPH-VYTLGRSGKennmLLGEE--QLKTIGATLYHIDRGGDI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  90 TFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARARPPpyTGVWLG-----ERKICAIGVRCGRHIT 164
Cdd:PRK14348  85 TYHGPGQLVCYPILNLEEFGLGLKEYVHLLEEAVIRVCASYGVVAGRLEKA--TGVWLEgdtsrARKICAIGVRSSHYVT 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 229577004 165 SHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEV 208
Cdd:PRK14348 163 MHGLALNVNTDLRYFSYIHPCGFIDKGVTSLQQELGHSIDMAEV 206
lipB TIGR00214
lipoate-protein ligase B; Involved in lipoate biosynthesis as the main determinant of the ...
42-220 6.77e-33

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: 117.59  E-value: 6.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   42 TKAGVLLVCEPagPVYTGGlRGGLTPEETTRLRALGAEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEA 121
Cdd:TIGR00214  11 TLDEIMLVEHY--PVYTQG-QAGKTEHLLFDPDIPPAEVVQSERGGQVTYHGPGQQVMYVILDLKRFQLDVRWLVTQLEQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  122 CAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQR 201
Cdd:TIGR00214  88 TVIITLAELGIEGEPI--ADATGVWVEGKKVASLGIRVRRGCTFHGLALNINMDLSPFSHINPCGYAGREMGSLNQFLPG 165
                         170
                  ....*....|....*....
gi 229577004  202 lVTVDEVMPSFLVAFKETF 220
Cdd:TIGR00214 166 -ATVENVAPLLIKAFAELL 183
PRK14344 PRK14344
lipoyl(octanoyl) transferase LipB;
85-221 1.00e-24

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237683  Cd Length: 223  Bit Score: 97.06  E-value: 1.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  85 RGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHIT 164
Cdd:PRK14344  89 RGGEVTHHMPGQLVTYLVLDLRRFNKDLNWYLRQLEQVLIDVLADLGIDGERL--DGLTGVWIGNKKVASIGIGCRRWIT 166
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 229577004 165 SHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLvTVDEVMPSFLVAFKETFK 221
Cdd:PRK14344 167 QHGFSLNVDCDLEGFNKIVPCGLEGCQVGRLSDWIPGL-NIKEVKPLLKKSLQERFG 222
BPL_LplA_LipB cd16435
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ...
11-216 1.34e-23

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: 93.76  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  11 LGRVHYSELLALQEHWLRrlqadprpGTLSGTKAGVLLVCEPAgpVYTGGLRGGLTPE-ETTRLRALGAEVRATGRGGLA 89
Cdd:cd16435    5 LDSVDYESAWAAQEKSLR--------ENVSNQSSTLLLWEHPT--TVTLGRLDRELPHlELAKKIERGYELVVRNRGGRA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  90 TFHGPGQLLCHPVLDLRLLGLRLRtHVAALEACAVRLCELRGLQGARArpPPYTGVWLGERKICAIGVRCGRHITSHGLA 169
Cdd:cd16435   75 VSHDPGQLVFSPVIGPNVEFMISK-FNLIIEEGIRDAIADFGQSAEVK--WGRNDLWIDNRKVCGIAVRVVKEAIFHGIA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 229577004 170 LNCSTDLTWFEHIVPCGLVGTGVTSLSEALQRLVTVDEVMPSFLVAF 216
Cdd:cd16435  152 LNLNQDLENFTEIIPCGYKPERVTSLSLELGRKVTVEQVLERVLAAF 198
PRK14341 PRK14341
lipoyl(octanoyl) transferase LipB;
55-220 3.09e-23

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237680  Cd Length: 213  Bit Score: 93.05  E-value: 3.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  55 PVYTGGLRGglTPEETtrLRALGAEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQG 134
Cdd:PRK14341  45 PLYTAGTSA--KAEDL--LDPDRFPVYETGRGGQYTYHGPGQRVAYVMLDLKRRRRDVRAFVAALEEWIIATLAAFNIRG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004 135 ARArpPPYTGVWL--------GERKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLsEALQRLVTVD 206
Cdd:PRK14341 121 ERR--EDRVGVWVrrpdkgsgAEDKIAAIGVRLRRWVSFHGISINVEPDLSHFSGIVPCGISEHGVTSL-VDLGLPVTMD 197
                        170
                 ....*....|....
gi 229577004 207 EVMPSFLVAFKETF 220
Cdd:PRK14341 198 DVDAALKKAFEKVF 211
PRK14342 PRK14342
lipoyl(octanoyl) transferase LipB;
55-221 1.29e-20

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237681  Cd Length: 213  Bit Score: 86.09  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  55 PVYTGGLRGglTPEETtrLRALGAEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQg 134
Cdd:PRK14342  45 PVFTQGQAG--KPEHI--LNPGDIPVVQSDRGGQVTYHGPGQLVMYVLLDLKRLKLGVRQLVTAIEQTVINTLAEYGIE- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004 135 ARARP--PpytGVWLGERKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSEaLQRLVTVDEVMPSF 212
Cdd:PRK14342 120 AHAKPdaP---GVYVDGKKIASLGLRIRRGCSFHGLALNVNMDLSPFLRINPCGYAGLEMTQLSD-LGGPATVDEVAPRL 195

                 ....*....
gi 229577004 213 LVAFKETFK 221
Cdd:PRK14342 196 LAELLALLG 204
PRK14346 PRK14346
lipoyl(octanoyl) transferase LipB;
10-196 8.58e-20

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237684  Cd Length: 230  Bit Score: 84.42  E-value: 8.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  10 WLGRVHYSELL-ALQEHWLRRLQADPrpgtlsgtkaGVLLVCEPAgPVYTGGLRGgltpEETTRLRALGAEVRATGRGGL 88
Cdd:PRK14346   7 MLGRVDYLATVqAMQAFTAERTPETP----------DELWICEHP-PVYTQGLAG----KADHVLNPGDIPVVATNRGGQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  89 ATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARA---------------------RPPPYTGV-- 145
Cdd:PRK14346  72 VTYHGPGQVVAYPLIDLRRAGYFVKEYVYRIEEAVIRTLAHFGVTGHRVagapgiyvrlddpfshaalpqRPQKRGGGap 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 229577004 146 ---WLGERKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLS 196
Cdd:PRK14346 152 qppFRGLGKIAALGIKVSRHCTYHGVALNVAMDLEPFSRINPCGYAGLQTVDLS 205
PRK14347 PRK14347
lipoyl(octanoyl) transferase LipB;
83-197 3.38e-17

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172823  Cd Length: 209  Bit Score: 76.90  E-value: 3.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  83 TGRGGLATFHGPGQLLCHPVLDLRL--LGLRLRTHVAALEACAVRLCELRGLQGARARPPpyTGVWLGER-----KICAI 155
Cdd:PRK14347  67 TGRGGKFTFHGPGQRVIYPILNLASpnRHKDLKLYIKMLEEWIINSLNYFGIKAYIIKDK--VGIWVKVRkdefaKIAAI 144
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 229577004 156 GVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLSE 197
Cdd:PRK14347 145 GVRVRKWVTYHGVAINISTDLSKFSGIIPCGLENSLVTSLNQ 186
PRK14349 PRK14349
lipoyl(octanoyl) transferase LipB;
49-196 5.98e-13

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 172825  Cd Length: 220  Bit Score: 65.76  E-value: 5.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  49 VCEPAgPVYTGGLRGglTPEETtrLRALGAEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCE 128
Cdd:PRK14349  35 LCEHA-PVYTLGQAG--RPEHL--LNPGLIPVVHCDRGGQVTYHGPGQVLAYTLFDLRRAGLYVREYVDMLEQATLATLR 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 229577004 129 LRGLQGArARPPPYTGVWL----GE-RKICAIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGTGVTSLS 196
Cdd:PRK14349 110 ELGLEQA-CRKPGAPGIYVpqpgGElAKIAALGVKVRNGYAYHGLALNIDMDLSPFLGINPCGYEGLRTVDLA 181
PRK14343 PRK14343
lipoyl(octanoyl) transferase LipB;
2-215 6.11e-10

lipoyl(octanoyl) transferase LipB;


Pssm-ID: 237682  Cd Length: 235  Bit Score: 57.49  E-value: 6.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004   2 SLPVVRLVWLGRVHYSELLALQEHWLRRLQADprpgtlsgTKAGVLLVCEPagPVYTGGLRGG----LTPEEttrlralG 77
Cdd:PRK14343  11 AALPVTVRWRGREPYEACFDAMRAFTDARTAD--------TPDEIWLVEHP--PVYTLGQAGDpahlLVADS-------G 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 229577004  78 AEVRATGRGGLATFHGPGQLLCHPVLDLRLLGLRLRTHVAALEACAVRLCELRGLQGARARPPP--Y--TGVWLGErKIC 153
Cdd:PRK14343  74 IPLVKVDRGGQITYHGPGQVVAYLLLDLRRRKLMVRELVTRIEQAVIDTLAAYNLASERKAGAPgiYvaSGPHQGA-KIA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 229577004 154 AIGVRCGRHITSHGLALNCSTDLTWFEHIVPCGLVGtgvtslsealqrLVTVDevMPSFLVA 215
Cdd:PRK14343 153 ALGLKIRNGCSYHGLSLNVKMDLRPFLAINPCGYAG------------LETVD--MASLGVA 200
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH