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Conserved domains on  [gi|2241059500|ref|XP_002522994|]
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biotin--protein ligase 1, chloroplastic isoform X3 [Ricinus communis]

Protein Classification

biotin--[acetyl-CoA-carboxylase] ligase( domain architecture ID 11612782)

biotin--[acetyl-CoA-carboxylase] ligase catalyzes the formation of biotinyl-5'-AMP from biotin and ATP, and the succeeding biotinylation of the biotin carboxyl carrier protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 76-249 1.20e-36

biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.


:

Pssm-ID: 319741 [Multi-domain]  Cd Length: 173  Bit Score: 128.92  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHN-FYELPIGTVCVADTQSKGRG-WLEAWESPLG-----SLLFTFKVEMVDVGaanKLQFVISLA 148
Cdd:cd16442     2 LIVLDEIDSTNDEAKELaRSGAPEGTVVVAEEQTAGRGrRGRKWESPKGkglyfSLLLRPDVPPAEAP---LLTLLAAVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 149 VTEAIKDVCqknglpVLDVKIKWPAYLYLNGQRVGGILCNSTY-KSKKFNISAGIGLNVDNEKPTTCLNAVLRELSPAAs 227
Cdd:cd16442    79 VAEALEKLG------GIPVQIKWPNDILVNGKKLAGILTEASAeGEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGK- 151

                         170       180
                  ....*....|....*....|..
gi 2241059500 228 QLRREEILAAFFNKFESLYDLL 249
Cdd:cd16442   152 EVDRNELLEELLAALENRLELF 173
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 76-249 1.20e-36

biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.


Pssm-ID: 319741 [Multi-domain]  Cd Length: 173  Bit Score: 128.92  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHN-FYELPIGTVCVADTQSKGRG-WLEAWESPLG-----SLLFTFKVEMVDVGaanKLQFVISLA 148
Cdd:cd16442     2 LIVLDEIDSTNDEAKELaRSGAPEGTVVVAEEQTAGRGrRGRKWESPKGkglyfSLLLRPDVPPAEAP---LLTLLAAVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 149 VTEAIKDVCqknglpVLDVKIKWPAYLYLNGQRVGGILCNSTY-KSKKFNISAGIGLNVDNEKPTTCLNAVLRELSPAAs 227
Cdd:cd16442    79 VAEALEKLG------GIPVQIKWPNDILVNGKKLAGILTEASAeGEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGK- 151

                         170       180
                  ....*....|....*....|..
gi 2241059500 228 QLRREEILAAFFNKFESLYDLL 249
Cdd:cd16442   152 EVDRNELLEELLAALENRLELF 173
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 76-268 4.19e-30

Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440109 [Multi-domain]  Cd Length: 241  Bit Score: 113.73  E-value: 4.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHNFYE-LPIGTVCVADTQSKGRGWLE-AWESPLG-----SLLFTFKVEMVDVGaanKLQFVISLA 148
Cdd:COG0340     2 IEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGrSWVSPPGkglyfSLLLRPDLPPARLP---LLSLAAGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 149 VTEAIKDVCQknglpvLDVKIKWPAYLYLNGQRVGGILC-NSTYKSKKFNISAGIGLNVDNEK--------PTTCLNAVL 219
Cdd:COG0340    79 VAEALRELTG------VDVGLKWPNDILLNGKKLAGILIeASGEGDGIDWVVIGIGINVNQPPfdpeeldqPATSLKEET 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2241059500 220 RElspaasQLRREEILAAFFNKFESLYDLLINQGLQSLEElfdrAWHRR 268
Cdd:COG0340   153 GK------EVDREELLAALLEELEELYDRFLEEGFAPILE----EWRAR 191
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 78-205 1.64e-22

Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. 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. Each organizm probably has only one BPL. 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) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.


Pssm-ID: 427135  Cd Length: 132  Bit Score: 90.58  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  78 WSPRLTSTQDFV-SHNFYELPIGTVCVADTQSKGRGWLEA-WESPLGSLLFTFKVEMVDVGAANK----LQFVISLAVTE 151
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNvWHSPKGCLTYSLLLSKEHPNVDPSvlefYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2241059500 152 AIKDvcQKNGLPVLDVKIKWPAYLYLNGQRVGGILCNSTYKSKKFNISAGIGLN 205
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 76-254 4.05e-22

birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]


Pssm-ID: 272917 [Multi-domain]  Cd Length: 237  Bit Score: 92.47  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHNFYEL-PIGTVCVADTQSKGRG-WLEAWESPLGSLLFTFKVEM-VDVGAANKLQFVISLAVTEA 152
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGrRGRKWLSPEGGLYFSLILRPdLPKSPAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 153 IKDVcqknglpVLDVKIKWPAYLYLNGQRVGGILCNST-YKSKKFNISAGIGLNVDNEKPTTCL-NAVLRELSPAASQLR 230
Cdd:TIGR00121  82 LKEL-------GDQVQVKWPNDILLKDKKLGGILTELTgKENRADYVVIGIGINVQNRKPAESLrEQAISLSEEAGIDLD 154

                         170       180
                  ....*....|....*....|....
gi 2241059500 231 REEILAAFFNKFESLYDLLINQGL 254
Cdd:TIGR00121 155 RGELIEGFLRNFEENLEWFEQEGI 178
PRK08330 PRK08330
biotin--protein ligase; Provisional
 73-263 1.26e-18

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 82.87  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  73 GRLLIWSPRLTSTQDFVSHNFYELPIGTVCVADTQSKGRGWLE-AWESPLG----SLLFTFKVEMVDVgaaNKLQFVISL 147
Cdd:PRK08330    2 GRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGrAWASPEGglwmSVILKPKVSPEHL---PKLVFLGAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 148 AVTEAIKDVCqknglpvLDVKIKWPAYLYLNGQRVGGILCnstyKSKKFNISAGIGLNVDNEKPttclnavlRELSPAAS 227
Cdd:PRK08330   79 AVVDTLREFG-------IEGKIKWPNDVLVNYKKIAGVLV----EGKGDFVVLGIGLNVNNEIP--------DELRETAT 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2241059500 228 QLRRE--------EILAAFFNKFESLYDLLINQGLQSLEELFDR 263
Cdd:PRK08330  140 SMKEVlgrevpliEVFKRLVENLDRWYKLFLEGPGEILEEVKGR 183
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 76-249 1.20e-36

biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. 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.


Pssm-ID: 319741 [Multi-domain]  Cd Length: 173  Bit Score: 128.92  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHN-FYELPIGTVCVADTQSKGRG-WLEAWESPLG-----SLLFTFKVEMVDVGaanKLQFVISLA 148
Cdd:cd16442     2 LIVLDEIDSTNDEAKELaRSGAPEGTVVVAEEQTAGRGrRGRKWESPKGkglyfSLLLRPDVPPAEAP---LLTLLAAVA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 149 VTEAIKDVCqknglpVLDVKIKWPAYLYLNGQRVGGILCNSTY-KSKKFNISAGIGLNVDNEKPTTCLNAVLRELSPAAs 227
Cdd:cd16442    79 VAEALEKLG------GIPVQIKWPNDILVNGKKLAGILTEASAeGEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGK- 151

                         170       180
                  ....*....|....*....|..
gi 2241059500 228 QLRREEILAAFFNKFESLYDLL 249
Cdd:cd16442   152 EVDRNELLEELLAALENRLELF 173
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 76-268 4.19e-30

Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA carboxylase) ligase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440109 [Multi-domain]  Cd Length: 241  Bit Score: 113.73  E-value: 4.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHNFYE-LPIGTVCVADTQSKGRGWLE-AWESPLG-----SLLFTFKVEMVDVGaanKLQFVISLA 148
Cdd:COG0340     2 IEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGrSWVSPPGkglyfSLLLRPDLPPARLP---LLSLAAGLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 149 VTEAIKDVCQknglpvLDVKIKWPAYLYLNGQRVGGILC-NSTYKSKKFNISAGIGLNVDNEK--------PTTCLNAVL 219
Cdd:COG0340    79 VAEALRELTG------VDVGLKWPNDILLNGKKLAGILIeASGEGDGIDWVVIGIGINVNQPPfdpeeldqPATSLKEET 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2241059500 220 RElspaasQLRREEILAAFFNKFESLYDLLINQGLQSLEElfdrAWHRR 268
Cdd:COG0340   153 GK------EVDREELLAALLEELEELYDRFLEEGFAPILE----EWRAR 191
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 78-205 1.64e-22

Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, lipoate-protein ligase A and B. 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. Each organizm probably has only one BPL. 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) catalyzes the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes. The unusual biosynthesis pathway of lipoic acid is mechanistically intertwined with attachment of the cofactor.


Pssm-ID: 427135  Cd Length: 132  Bit Score: 90.58  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  78 WSPRLTSTQDFV-SHNFYELPIGTVCVADTQSKGRGWLEA-WESPLGSLLFTFKVEMVDVGAANK----LQFVISLAVTE 151
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNvWHSPKGCLTYSLLLSKEHPNVDPSvlefYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2241059500 152 AIKDvcQKNGLPVLDVKIKWPAYLYLNGQRVGGILCNSTYKSKKFNISAGIGLN 205
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 76-254 4.05e-22

birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the biotin--acetyl-CoA-carboxylase ligase region of biotin--acetyl-CoA-carboxylase ligase. In Escherichia coli and some other species, this enzyme is part of a bifunction protein BirA that includes a small, N-terminal biotin operon repressor domain. Proteins identified by this model should not be called bifunctional unless they are also identified by birA_repr_reg (TIGR00122). The protein name suggests that this enzyme transfers biotin only to acetyl-CoA-carboxylase but it also transfers the biotin moiety to other proteins. The apparent orthologs among the eukaryotes are larger proteins that contain a single copy of this domain. [Protein fate, Protein modification and repair]


Pssm-ID: 272917 [Multi-domain]  Cd Length: 237  Bit Score: 92.47  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  76 LIWSPRLTSTQDFVSHNFYEL-PIGTVCVADTQSKGRG-WLEAWESPLGSLLFTFKVEM-VDVGAANKLQFVISLAVTEA 152
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGrRGRKWLSPEGGLYFSLILRPdLPKSPAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 153 IKDVcqknglpVLDVKIKWPAYLYLNGQRVGGILCNST-YKSKKFNISAGIGLNVDNEKPTTCL-NAVLRELSPAASQLR 230
Cdd:TIGR00121  82 LKEL-------GDQVQVKWPNDILLKDKKLGGILTELTgKENRADYVVIGIGINVQNRKPAESLrEQAISLSEEAGIDLD 154

                         170       180
                  ....*....|....*....|....
gi 2241059500 231 REEILAAFFNKFESLYDLLINQGL 254
Cdd:TIGR00121 155 RGELIEGFLRNFEENLEWFEQEGI 178
PRK08330 PRK08330
biotin--protein ligase; Provisional
 73-263 1.26e-18

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 82.87  E-value: 1.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  73 GRLLIWSPRLTSTQDFVSHNFYELPIGTVCVADTQSKGRGWLE-AWESPLG----SLLFTFKVEMVDVgaaNKLQFVISL 147
Cdd:PRK08330    2 GRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGrAWASPEGglwmSVILKPKVSPEHL---PKLVFLGAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 148 AVTEAIKDVCqknglpvLDVKIKWPAYLYLNGQRVGGILCnstyKSKKFNISAGIGLNVDNEKPttclnavlRELSPAAS 227
Cdd:PRK08330   79 AVVDTLREFG-------IEGKIKWPNDVLVNYKKIAGVLV----EGKGDFVVLGIGLNVNNEIP--------DELRETAT 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2241059500 228 QLRRE--------EILAAFFNKFESLYDLLINQGLQSLEELFDR 263
Cdd:PRK08330  140 SMKEVlgrevpliEVFKRLVENLDRWYKLFLEGPGEILEEVKGR 183
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
41-257 8.63e-16

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 76.36  E-value: 8.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  41 ITLLLESEISipekensfdQQLFFNNLSTNrfgrlliwsPRLTSTQDFVSHNFYELPIGTVCVADTQSKGRGWLE-AWES 119
Cdd:PRK11886   63 LDLLDPERIS---------SQLPPGRVTVL---------PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGrQWFS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 120 PLG-----SLLFTFKVEMvdvGAANKLQFVISLAVTEAIKDvcqkngLPVLDVKIKWPAYLYLNGQRVGGIL-------- 186
Cdd:PRK11886  125 PFGgnlylSLYWRLNQGP---AQAMGLSLVVGIAIAEALRR------LGAIDVGLKWPNDIYLNDRKLAGILvelsgetg 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 187 --CnstykskkfNISAGIGLNV---DN-----EKPTTclnavlrELSPAASQLRREEILAAFFNKFESLYDLLINQGLQS 256
Cdd:PRK11886  196 daA---------HVVIGIGINVampDFpeeliDQPWS-------DLQEAGPTIDRNQLAAELIKQLRAALELFEQEGLAP 259


                  .
gi 2241059500 257 L 257
Cdd:PRK11886  260 F 260
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 103-268 3.35e-07

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 50.25  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 103 VADTQSKGRGWLE-AWESPLGSLLFTFKVEmvDVGAANKLQFVISLAVTEAikdvCQKNGLPVLD---VKIKWPAYLYLN 178
Cdd:PTZ00276   37 LAESQTAGRGTGGrTWTSPKGNMYFTLCIP--QKGVPPELVPVLPLITGLA----CRAAIMEVLHgaaVHTKWPNDIIYA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 179 GQRVGGILCNSTYKSkkfnISAGIGLNV-------DNEKPTTCLNAVLRELSPAA--SQLRREEILAAFFnkfeslyDLL 249
Cdd:PTZ00276  111 GKKIGGSLIESEGEY----LIIGIGMNIevappvtDAGRESTMVNEIAEDLGVKSvtPQDLAEAVWKHFF-------DIC 179

                         170       180
                  ....*....|....*....|....*..
gi 2241059500 250 INQGL--QSLEELFDRAW------HRR 268
Cdd:PTZ00276  180 SDPELtrEILIESFDAAMdkslklHKR 206
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
103-243 5.13e-07

biotin--[acetyl-CoA-carboxylase] ligase;


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 49.57  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 103 VADTQSKG---RGwlEAWESPLGSLLFTFKVEMVDVGAANKLQfVISLAVTEAIKDVCQKNGLPVLdvkIKWPAYLYLNG 179
Cdd:PRK08477   32 VAKEQTAGigsRG--NSWEGKKGNLFFSFALKESDLPKDLPLQ-SSSIYFGFLLKEVLKELGSKVW---LKWPNDLYLDD 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2241059500 180 QRVGGILCNstyKSKKFnISAGIGLNVDN-EKPTTCLNavlrelspaaSQLRREEILAAFFNKFE 243
Cdd:PRK08477  106 KKIGGVITN---KIKNF-IVCGIGLNLKFsPKNFACLD----------IEISDDLLLEGFLQKIE 156
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
96-271 1.22e-06

biotin--[acetyl-CoA-carboxylase] ligase;


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 49.01  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500  96 LPIGTVCVADTQSKGRGWL-EAWESPLGSLLfTFKVEMV---DVGAANKLQFVISLAVTEAIKDVCQKNGLpvlDVKIKW 171
Cdd:PRK06955   62 LPAPIVRVAYEQTAGRGRQgRPWFAQPGNAL-LFSVACVlprPVAALAGLSLAVGVALAEALAALPAALGQ---RIALKW 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 172 PAYLYLNGQRVGGILCNSTYKSKkfNISA---GIGLNVDNEKPTTCLNAVL--------RELSPAASQLRRE-----EIL 235
Cdd:PRK06955  138 PNDLLIAGRKLAGILIETVWATP--DATAvviGIGLNVRRADAVAAEVDALrareaalaRGLPPVALAAACAganltDTL 215

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2241059500 236 AAFFNKFESLYDLLINQGLQSleelFDRAWHRRPSY 271
Cdd:PRK06955  216 AAALNALAPALQAFGADGLAP----FAARWHALHAY 247
PRK05935 PRK05935
biotin--protein ligase; Provisional
 100-268 1.57e-06

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 47.50  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 100 TVCVADTQSKGRGWL-EAWESPLGSLL--FTFKVEMVDVGAAnkLQFVISlavTEAIKDVCQKNGLPvlDVKIKWPAYLY 176
Cdd:PRK05935   31 TVISTREQTAGKGKFgKSWHSSDQDLLasFCFFITVLNIDVS--LLFRLG---TEAVMRLGEDLGIT--EAVIKWPNDVL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 177 LNGQRVGGILCNSTYKSKKFNISAGIGLNVDnekptTCLNAVLRELSPAASQlrreEILAAFFNKFESLYDLLINQGLQS 256
Cdd:PRK05935  104 VHGEKLCGVLCETIPVKGGLGVILGIGVNGN-----TTKDELLGIDQPATSL----QELLGHPIDLEEQRERLIKHIKHV 174

                         170
                  ....*....|..
gi 2241059500 257 LEELFDRAWHRR 268
Cdd:PRK05935  175 LIQTLPKLLARE 186
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
100-244 6.89e-06

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 47.40  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 100 TVCVADTQSKGRGWL-EAWESPLGS-LLFTFKvemvdvGAANKLQFVI-SLAVTEAIkdVCQKN-GLPVLDVKIKWPAYL 175
Cdd:PRK13325  111 TICVTHLQSKGRGRQgRKWSHRLGEcLMFSFG------WVFDRPQYELgSLSPVAAV--ACRRAlSRLGLKTQIKWPNDL 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2241059500 176 YLNGQRVGGILCNSTYKSKKFNISAGIGLNV----------------------DNEKPTTCLNAVLRELSPAASQLrREE 233
Cdd:PRK13325  183 VVGRDKLGGILIETVRTGGKTVAVVGIGINFvlpkevenaasvqslfqtasrrGNADAAVLLETLLAELDAVLLQY-ARD 261

                         170
                  ....*....|.
gi 2241059500 234 ILAAFFNKFES 244
Cdd:PRK13325  262 GFAPFVAEYQA 272
 
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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