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Conserved domains on  [gi|30693409|ref|NP_850957|]
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holocarboxylase synthetase 2 [Arabidopsis thaliana]

Protein Classification

lipoate--protein ligase family protein( domain architecture ID 11612795)

lipoate--protein ligase family protein, similar to Staphylococcus aureus lipoate--protein ligase 1 and Saccharomyces cerevisiae octanoyltransferase

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 ...
 75-250 8.40e-45

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: 150.88  E-value: 8.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  75 FLIWSPYLSSTHDVVSHNFSEI-PVGSVCVSDIQLKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 151
Cdd:cd16442   1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409 152 EAVKDVCDKkglsynDVKIKWPNDLYLNGLKIGGILCTSTYR-SRKFLVSVGVGLNVDNEQPTTCLNAVLKDVCPPSNlL 230
Cdd:cd16442  81 EALEKLGGI------PVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                       170       180
                ....*....|....*....|
gi 30693409 231 KREEILGAFFKKFENFFDLF 250
Cdd:cd16442 154 DRNELLEELLAALENRLELF 173
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 268-323 1.39e-04

Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.


:

Pssm-ID: 426672 [Multi-domain]  Cd Length: 48  Bit Score: 38.98  E-value: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30693409   268 HSGQRVIAEEknEDQVVqnVVTIQGLTSSGYLLAIGDDNVmyelHPDGNSFDFFKG 323
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 75-250 8.40e-45

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: 150.88  E-value: 8.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  75 FLIWSPYLSSTHDVVSHNFSEI-PVGSVCVSDIQLKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 151
Cdd:cd16442   1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409 152 EAVKDVCDKkglsynDVKIKWPNDLYLNGLKIGGILCTSTYR-SRKFLVSVGVGLNVDNEQPTTCLNAVLKDVCPPSNlL 230
Cdd:cd16442  81 EALEKLGGI------PVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                       170       180
                ....*....|....*....|
gi 30693409 231 KREEILGAFFKKFENFFDLF 250
Cdd:cd16442 154 DRNELLEELLAALENRLELF 173
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 82-300 2.90e-39

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: 138.77  E-value: 2.90e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  82 LSSTHDVVSHNFSE-IPVGSVCVSDIQLKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVTEAVKDVC 158
Cdd:COG0340   8 VDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPpARLPLLSLAAGLAVAEALRELT 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409 159 DKkglsynDVKIKWPNDLYLNGLKIGGILC--TSTYRSRKFLVsVGVGLNVDN--------EQPTTCLNAVLKDvcPPSn 228
Cdd:COG0340  88 GV------DVGLKWPNDILLNGKKLAGILIeaSGEGDGIDWVV-IGIGINVNQppfdpeelDQPATSLKEETGK--EVD- 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30693409 229 llkREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRVIAEEKNEDQvvqnVVTIQGLTSSGYLL 300
Cdd:COG0340 158 ---REELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETL----EGIAVGIDEDGALL 222
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 78-206 1.23e-38

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: 133.34  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409    78 WSPYLSSTHDVV-SHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTLEME----DGRVVPLIQYVVSLAVTE 152
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30693409   153 AVKDvcDKKGLSYNDVKIKWPNDLYLNGLKIGGILCTSTYRSRKFLVSVGVGLN 206
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 76-304 2.32e-27

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: 107.10  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409    76 LIWSPYLSSTHDVVSHNFSEI-PVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTLEMEDGRV-VPLIQYVVSLAVTEA 153
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   154 VKDVCDkkglsynDVKIKWPNDLYLNGLKIGGILCTSTYR-SRKFLVSVGVGLNVDN--------EQPTTCLNAVLKDVc 224
Cdd:TIGR00121  82 LKELGD-------QVQVKWPNDILLKDKKLGGILTELTGKeNRADYVVIGIGINVQNrkpaeslrEQAISLSEEAGIDL- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   225 ppsnllKREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRViaEEKNEDQVVQNVVtiQGLTSSGYLLAIGD 304
Cdd:TIGR00121 154 ------DRGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREV--SLTTGNGEIEGIA--RGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
80-300 2.95e-23

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 97.94  E-value: 2.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   80 PYLSSTHDVVSHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGC-LMYSFTLEMEDGrVVPLIQY--VVSLAVTEAVKD 156
Cdd:PRK11886  84 PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQG-PAQAMGLslVVGIAIAEALRR 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  157 vcdkkgLSYNDVKIKWPNDLYLNGLKIGGILctsTYRSRKF-----LVsVGVGLNV---DN-----EQPTTCLNAVLKDV 223
Cdd:PRK11886 163 ------LGAIDVGLKWPNDIYLNDRKLAGIL---VELSGETgdaahVV-IGIGINVampDFpeeliDQPWSDLQEAGPTI 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30693409  224 cppsnllKREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRVIAEEknEDQVVQNVVtiQGLTSSGYLL 300
Cdd:PRK11886 233 -------DRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLII--GDKEISGIA--RGIDEQGALL 298
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 268-323 1.39e-04

Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.


Pssm-ID: 426672 [Multi-domain]  Cd Length: 48  Bit Score: 38.98  E-value: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30693409   268 HSGQRVIAEEknEDQVVqnVVTIQGLTSSGYLLAIGDDNVmyelHPDGNSFDFFKG 323
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
 75-250 8.40e-45

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: 150.88  E-value: 8.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  75 FLIWSPYLSSTHDVVSHNFSEI-PVGSVCVSDIQLKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVT 151
Cdd:cd16442   1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPpAEAPLLTLLAAVAVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409 152 EAVKDVCDKkglsynDVKIKWPNDLYLNGLKIGGILCTSTYR-SRKFLVSVGVGLNVDNEQPTTCLNAVLKDVCPPSNlL 230
Cdd:cd16442  81 EALEKLGGI------PVQIKWPNDILVNGKKLAGILTEASAEgEGVAAVVIGIGINVNNTPPPEPLPDTSLATSLGKE-V 153

                       170       180
                ....*....|....*....|
gi 30693409 231 KREEILGAFFKKFENFFDLF 250
Cdd:cd16442 154 DRNELLEELLAALENRLELF 173
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 82-300 2.90e-39

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: 138.77  E-value: 2.90e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  82 LSSTHDVVSHNFSE-IPVGSVCVSDIQLKGRGRTKNVWESPKG-CLMYSFTLEMEDG-RVVPLIQYVVSLAVTEAVKDVC 158
Cdd:COG0340   8 VDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLLRPDLPpARLPLLSLAAGLAVAEALRELT 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409 159 DKkglsynDVKIKWPNDLYLNGLKIGGILC--TSTYRSRKFLVsVGVGLNVDN--------EQPTTCLNAVLKDvcPPSn 228
Cdd:COG0340  88 GV------DVGLKWPNDILLNGKKLAGILIeaSGEGDGIDWVV-IGIGINVNQppfdpeelDQPATSLKEETGK--EVD- 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30693409 229 llkREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRVIAEEKNEDQvvqnVVTIQGLTSSGYLL 300
Cdd:COG0340 158 ---REELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETL----EGIAVGIDEDGALL 222
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 78-206 1.23e-38

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: 133.34  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409    78 WSPYLSSTHDVV-SHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTLEME----DGRVVPLIQYVVSLAVTE 152
Cdd:pfam03099   1 LGERIKSTNTYLeELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEhpnvDPSVLEFYVLELVLAVLE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 30693409   153 AVKDvcDKKGLSYNDVKIKWPNDLYLNGLKIGGILCTSTYRSRKFLVSVGVGLN 206
Cdd:pfam03099  81 ALGL--YKPGISGIPCFVKWPNDLYVNGRKLAGILQRSTRGGTLHHGVIGLGVN 132
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 76-304 2.32e-27

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: 107.10  E-value: 2.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409    76 LIWSPYLSSTHDVVSHNFSEI-PVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTLEMEDGRV-VPLIQYVVSLAVTEA 153
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGkLKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPDLPKSpAPGLTLVAGIAIAEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   154 VKDVCDkkglsynDVKIKWPNDLYLNGLKIGGILCTSTYR-SRKFLVSVGVGLNVDN--------EQPTTCLNAVLKDVc 224
Cdd:TIGR00121  82 LKELGD-------QVQVKWPNDILLKDKKLGGILTELTGKeNRADYVVIGIGINVQNrkpaeslrEQAISLSEEAGIDL- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   225 ppsnllKREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRViaEEKNEDQVVQNVVtiQGLTSSGYLLAIGD 304
Cdd:TIGR00121 154 ------DRGELIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREV--SLTTGNGEIEGIA--RGIDKDGALLLEDG 223
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
80-300 2.95e-23

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 97.94  E-value: 2.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   80 PYLSSTHDVVSHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGC-LMYSFTLEMEDGrVVPLIQY--VVSLAVTEAVKD 156
Cdd:PRK11886  84 PVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQG-PAQAMGLslVVGIAIAEALRR 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  157 vcdkkgLSYNDVKIKWPNDLYLNGLKIGGILctsTYRSRKF-----LVsVGVGLNV---DN-----EQPTTCLNAVLKDV 223
Cdd:PRK11886 163 ------LGAIDVGLKWPNDIYLNDRKLAGIL---VELSGETgdaahVV-IGIGINVampDFpeeliDQPWSDLQEAGPTI 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30693409  224 cppsnllKREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRVIAEEknEDQVVQNVVtiQGLTSSGYLL 300
Cdd:PRK11886 233 -------DRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLII--GDKEISGIA--RGIDEQGALL 298
PRK08330 PRK08330
biotin--protein ligase; Provisional
 73-306 1.33e-18

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 83.26  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   73 GRFLIWSPYLSSTHDVVSHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTL----EMEDgrvVPLIQYVVSL 148
Cdd:PRK08330   2 GRNIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILkpkvSPEH---LPKLVFLGAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  149 AVTEAVKDVcdkkGLsynDVKIKWPNDLYLNGLKIGGILCtstyRSRKFLVSVGVGLNVDNEQP------TTCLNAVLKD 222
Cdd:PRK08330  79 AVVDTLREF----GI---EGKIKWPNDVLVNYKKIAGVLV----EGKGDFVVLGIGLNVNNEIPdelretATSMKEVLGR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  223 VCPPSNLLKReeilgaFFKKFENFFDLFMEQGFKSLEELYYRTWLhSGQRVIAEEKNEDQVVQNVVTIQgltSSGYLLAI 302
Cdd:PRK08330 148 EVPLIEVFKR------LVENLDRWYKLFLEGPGEILEEVKGRSMI-LGKRVKIIGDGEILVEGIAEDID---EFGALILR 217


                 ....
gi 30693409  303 GDDN 306
Cdd:PRK08330 218 LDDG 221
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 103-256 3.63e-14

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 71.05  E-value: 3.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  103 VSDIQLKGRGRTKNVWESPKGCLMYSFTL--EMEDGRVVPLIQYVVSLAVTEAVKDVCDKKGLSyndvkIKWPNDLYLNG 180
Cdd:PTZ00276  37 LAESQTAGRGTGGRTWTSPKGNMYFTLCIpqKGVPPELVPVLPLITGLACRAAIMEVLHGAAVH-----TKWPNDIIYAG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  181 LKIGGILCTStyrSRKFLVsVGVGLNV-------DNEQPTTCLNAVLKDV----CPPSNLLKreeilgAFFKkfeNFFDL 249
Cdd:PTZ00276 112 KKIGGSLIES---EGEYLI-IGIGMNIevappvtDAGRESTMVNEIAEDLgvksVTPQDLAE------AVWK---HFFDI 178


                 ....*..
gi 30693409  250 FMEQGFK 256
Cdd:PTZ00276 179 CSDPELT 185
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
103-246 4.26e-13

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 67.29  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  103 VSDIQLKGRGRTKNVWESPKGCLMYSFTLEMED-GRVVPLIQyvVSLAVTEAVKDVCDKKGlsyNDVKIKWPNDLYLNGL 181
Cdd:PRK08477  32 VAKEQTAGIGSRGNSWEGKKGNLFFSFALKESDlPKDLPLQS--SSIYFGFLLKEVLKELG---SKVWLKWPNDLYLDDK 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30693409  182 KIGGILcTSTYRSrkFLVsVGVGLNVDN-EQPTTCLNAVlkdvcppsnlLKREEILGAFFKKFENF 246
Cdd:PRK08477 107 KIGGVI-TNKIKN--FIV-CGIGLNLKFsPKNFACLDIE----------ISDDLLLEGFLQKIEKK 158
BirA COG1654
Biotin operon repressor [Transcription];
67-293 1.62e-10

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 61.16  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  67 ISTHRFGRFLIWSPYLSSTHDVV-SHNFSEIPVGSVCVSDIQLKGRGRTKNVWESPKGCLMYSFTLEmedgRVVPLIQYV 145
Cdd:COG1654  75 LSTKRLGREILYVISSTSTNLLAlELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLL----RPPIAPALL 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409 146 VSLAVTEAVKDVCDKKGLSYNDVKIKWPNDLYLNGLKIGGILCTSTYRSRKFLVSVGVGLNVDN----EQPTTCLNAVLK 221
Cdd:COG1654 151 SLLLLAAAVAVAAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNsnpeEEPQELAELATS 230

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30693409 222 DVCPPSNLLKREEILGAFFKKFENFFDLFMEQGFKSLEELYYRTWLHSGQRVIAEEKNEDQVVQNVVTIQGL 293
Cdd:COG1654 231 LLLILRLRLLRLLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLG 302
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
100-206 9.72e-10

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


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 59.72  E-value: 9.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  100 SVCVSDIQLKGRGRTKNVWESPKG-CLMYSFTL-----EMEDGRVVPliqyVVSLAVTEAVkdvcdkkGLSYNDVKIKWP 173
Cdd:PRK13325 111 TICVTHLQSKGRGRQGRKWSHRLGeCLMFSFGWvfdrpQYELGSLSP----VAAVACRRAL-------SRLGLKTQIKWP 179

                         90       100       110
                 ....*....|....*....|....*....|...
gi 30693409  174 NDLYLNGLKIGGILCTSTYRSRKFLVSVGVGLN 206
Cdd:PRK13325 180 NDLVVGRDKLGGILIETVRTGGKTVAVVGIGIN 212
PRK05935 PRK05935
biotin--protein ligase; Provisional
 107-243 1.32e-08

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 54.05  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  107 QLKGRGRTKNVWESPKGCLMYSFTLEMEDGRVVpliqyvVSLAV---TEAVKDVCDKKGLSynDVKIKWPNDLYLNGLKI 183
Cdd:PRK05935  38 QTAGKGKFGKSWHSSDQDLLASFCFFITVLNID------VSLLFrlgTEAVMRLGEDLGIT--EAVIKWPNDVLVHGEKL 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30693409  184 GGILCtSTYRSRKFL-VSVGVGLN--------VDNEQPTTCLNAVLKDVCPPSNLLKR--EEILGAFFKKF 243
Cdd:PRK05935 110 CGVLC-ETIPVKGGLgVILGIGVNgnttkdelLGIDQPATSLQELLGHPIDLEEQRERliKHIKHVLIQTL 179
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
96-207 9.13e-06

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 46.70  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409   96 IPVGSVCVSDIQLKGRGRTKNVWES-PKGCLMYSFTLemedgrVVPL-------IQYVVSLAVTEAVKDVCDKKGLSynd 167
Cdd:PRK06955  62 LPAPIVRVAYEQTAGRGRQGRPWFAqPGNALLFSVAC------VLPRpvaalagLSLAVGVALAEALAALPAALGQR--- 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 30693409  168 VKIKWPNDLYLNGLKIGGILCTSTYRS--RKFLVsVGVGLNV 207
Cdd:PRK06955 133 IALKWPNDLLIAGRKLAGILIETVWATpdATAVV-IGIGLNV 173
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 268-323 1.39e-04

Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It is found to the C terminus of the biotin protein ligase catalytic domain pfam01317.


Pssm-ID: 426672 [Multi-domain]  Cd Length: 48  Bit Score: 38.98  E-value: 1.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 30693409   268 HSGQRVIAEEknEDQVVqnVVTIQGLTSSGYLLAIGDDNVmyelHPDGNSFDFFKG 323
Cdd:pfam02237   1 TLGREVRVLL--GDGIV--EGIAVGIDDDGALLLETDDGT----IRDINSGEVSLR 48
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 117-312 2.48e-04

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 42.12  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  117 VWESPKGCLMYSFTLEMEDGrvvpLIQYVVSLAVTEAVkdVCDKKGLSYNDV-KIKWPNDLYLNGLKIGGILCTSTY--- 192
Cdd:PTZ00275  74 IWLSEKGNLFTTFVFLWNRN----DIEKVKYLAQTCTV--AISKTLEYFHLVtQIKWINDVLVNYKKIAGCLVHLYYldd 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30693409  193 ----RSRKFLVSVGVGLNVD--------NEQPTTCLNAVLKDVCPPSNLLKREEILGAFFKKFENFFDLFMEQGFKSLEE 260
Cdd:PTZ00275 148 fpnlNSRYVCVMVGIGINVTledkhnllNNNYTSIKKELQRDFNTPKSIPSVEQVTEKLIINLKAVINKLRKEGFSSFLD 227

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30693409  261 LYYRTWLHSGQRVIAEEKNEDQVVQnvvtIQGLTSSGYLLAIGDDNVMYELH 312
Cdd:PTZ00275 228 YITPRLLYKDKKVLIDQDNELIVGY----LQGLLHDGSLLLLREKNKLVRVN 275
 
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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