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Conserved domains on  [gi|46255045|ref|NP_000402|]
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biotin--protein ligase isoform 1 [Homo sapiens]

Protein Classification

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 ...
467-647 2.73e-40

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: 145.48  E-value: 2.73e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 467 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 545
Cdd:cd16442   1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 546 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 624
Cdd:cd16442  76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
                       170       180
                ....*....|....*....|...
gi 46255045 625 KAELKPLRADYLIARVVTVLEKL 647
Cdd:cd16442 151 KEVDRNELLEELLAALENRLELF 173
BPL_N super family cl48072
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ...
202-390 1.13e-08

Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.


The actual alignment was detected with superfamily member pfam09825:

Pssm-ID: 462915  Cd Length: 277  Bit Score: 56.76  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   202 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 248
Cdd:pfam09825  38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   249 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 297
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   298 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 371
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
                         250       260
                  ....*....|....*....|..
gi 46255045   372 GLSC---DMKQVPALTPLYLLS 390
Cdd:pfam09825 256 GLKVneeEETTVPSLTPLHLSS 277
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
669-716 1.20e-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: 40.14  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 46255045   669 HSGQQVHLGSAEGPKV-SIVGLDDSGFLQVHQEGGEvvtvHPDGNSFDM 716
Cdd:pfam02237   1 TLGREVRVLLGDGIVEgIAVGIDDDGALLLETDDGT----IRDINSGEV 45
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
467-647 2.73e-40

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: 145.48  E-value: 2.73e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 467 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 545
Cdd:cd16442   1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 546 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 624
Cdd:cd16442  76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
                       170       180
                ....*....|....*....|...
gi 46255045 625 KAELKPLRADYLIARVVTVLEKL 647
Cdd:cd16442 151 KEVDRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
471-603 5.68e-39

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: 140.66  E-value: 5.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   471 FAEVTPTTMRLLDGLmFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVV 550
Cdd:pfam03099   1 LGERIKSTNTYLEEL-NSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46255045   551 EAVRS-IPEYQDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 603
Cdd:pfam03099  80 EALGLyKPGISGIPCFVKWPNDLYVNG-RKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
467-708 8.26e-37

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: 138.38  E-value: 8.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 467 KVILFAEVtPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVGCAlstLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:COG0340   1 RIEVFDEV-DSTNDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKG---LYFSLLLRPDLPpARLPLLSLAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 546 SVAVVEAVRsipEYQDINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNS--------NPTICINDL 616
Cdd:COG0340  76 GLAVAEALR---ELTGVDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQPpfdpeeldQPATSLKEE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 617 ITeynkqhkaelKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKV-SIVGLDDSGFL 695
Cdd:COG0340 152 TG----------KEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEgIAVGIDEDGAL 221
                       250
                ....*....|...
gi 46255045 696 QVHQEGGEVVTVH 708
Cdd:COG0340 222 LLETADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
467-702 6.04e-26

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: 6.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   467 KVILFAEVTPTTMRLLDglMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:TIGR00121   1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   546 SVAVVEAvrsIPEYQDiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTICINDLITEYNKQH 624
Cdd:TIGR00121  75 GIAIAEV---LKELGD-QVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   625 KAELKplRADyLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHL----GSAEGPKVSIvglDDSGFLQVHQE 700
Cdd:TIGR00121 150 GIDLD--RGE-LIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLLEDG 223

                  ..
gi 46255045   701 GG 702
Cdd:TIGR00121 224 GG 225
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
464-703 1.68e-20

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 92.93  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  464 QLGKVILFAEVTPTTMRLLDGLmfqTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCalsTLLISIPLRSQLGQRipfvqH 543
Cdd:PRK11886  76 PPGRVTVLPVIDSTNQYLLDRI---AELKSGDLCLAEYQTAGRGRRGRQWFSPFGG---NLYLSLYWRLNQGPA-----Q 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  544 LMS------VAVVEAVRSIpeyQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTICI 613
Cdd:PRK11886 145 AMGlslvvgIAIAEALRRL---GAIDVGLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEELI 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  614 N----DLITeynkqhkaELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIV-G 688
Cdd:PRK11886 219 DqpwsDLQE--------AGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIArG 290
                        250
                 ....*....|....*
gi 46255045  689 LDDSGFLQVHQEGGE 703
Cdd:PRK11886 291 IDEQGALLLEDDGVE 305
BPL_N pfam09825
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ...
202-390 1.13e-08

Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.


Pssm-ID: 462915  Cd Length: 277  Bit Score: 56.76  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   202 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 248
Cdd:pfam09825  38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   249 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 297
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   298 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 371
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
                         250       260
                  ....*....|....*....|..
gi 46255045   372 GLSC---DMKQVPALTPLYLLS 390
Cdd:pfam09825 256 GLKVneeEETTVPSLTPLHLSS 277
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
669-716 1.20e-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: 40.14  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 46255045   669 HSGQQVHLGSAEGPKV-SIVGLDDSGFLQVHQEGGEvvtvHPDGNSFDM 716
Cdd:pfam02237   1 TLGREVRVLLGDGIVEgIAVGIDDDGALLLETDDGT----IRDINSGEV 45
 
Name Accession Description Interval E-value
BPL cd16442
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ...
467-647 2.73e-40

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: 145.48  E-value: 2.73e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 467 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 545
Cdd:cd16442   1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 546 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 624
Cdd:cd16442  76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
                       170       180
                ....*....|....*....|...
gi 46255045 625 KAELKPLRADYLIARVVTVLEKL 647
Cdd:cd16442 151 KEVDRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
471-603 5.68e-39

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: 140.66  E-value: 5.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   471 FAEVTPTTMRLLDGLmFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVV 550
Cdd:pfam03099   1 LGERIKSTNTYLEEL-NSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 46255045   551 EAVRS-IPEYQDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 603
Cdd:pfam03099  80 EALGLyKPGISGIPCFVKWPNDLYVNG-RKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
467-708 8.26e-37

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: 138.38  E-value: 8.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 467 KVILFAEVtPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVGCAlstLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:COG0340   1 RIEVFDEV-DSTNDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKG---LYFSLLLRPDLPpARLPLLSLAA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 546 SVAVVEAVRsipEYQDINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNS--------NPTICINDL 616
Cdd:COG0340  76 GLAVAEALR---ELTGVDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQPpfdpeeldQPATSLKEE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045 617 ITeynkqhkaelKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKV-SIVGLDDSGFL 695
Cdd:COG0340 152 TG----------KEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEgIAVGIDEDGAL 221
                       250
                ....*....|...
gi 46255045 696 QVHQEGGEVVTVH 708
Cdd:COG0340 222 LLETADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
467-702 6.04e-26

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: 6.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   467 KVILFAEVTPTTMRLLDglMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:TIGR00121   1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   546 SVAVVEAvrsIPEYQDiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTICINDLITEYNKQH 624
Cdd:TIGR00121  75 GIAIAEV---LKELGD-QVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   625 KAELKplRADyLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHL----GSAEGPKVSIvglDDSGFLQVHQE 700
Cdd:TIGR00121 150 GIDLD--RGE-LIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLLEDG 223

                  ..
gi 46255045   701 GG 702
Cdd:TIGR00121 224 GG 225
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
464-703 1.68e-20

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 92.93  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  464 QLGKVILFAEVTPTTMRLLDGLmfqTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCalsTLLISIPLRSQLGQRipfvqH 543
Cdd:PRK11886  76 PPGRVTVLPVIDSTNQYLLDRI---AELKSGDLCLAEYQTAGRGRRGRQWFSPFGG---NLYLSLYWRLNQGPA-----Q 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  544 LMS------VAVVEAVRSIpeyQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTICI 613
Cdd:PRK11886 145 AMGlslvvgIAIAEALRRL---GAIDVGLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEELI 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  614 N----DLITeynkqhkaELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIV-G 688
Cdd:PRK11886 219 DqpwsDLQE--------AGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIArG 290
                        250
                 ....*....|....*
gi 46255045  689 LDDSGFLQVHQEGGE 703
Cdd:PRK11886 291 IDEQGALLLEDDGVE 305
PRK08330 PRK08330
biotin--protein ligase; Provisional
467-707 5.31e-15

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 75.17  E-value: 5.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  467 KVILFAEVTPTT---MRLLDGLmfqtpqEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLGQR-IPFVQ 542
Cdd:PRK08330   4 NIIYFDEVDSTNeyaKRIAPDE------EEGTVIVADRQTAGHGRKGRAWASPEG----GLWMSVILKPKVSPEhLPKLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  543 HLMSVAVVEAVRSIpeyqDINLRVKWPNDIYYsDLMKIGGVLVNstlmGETFYILIGCGFNVTNSNPticinDLITEYNK 622
Cdd:PRK08330  74 FLGALAVVDTLREF----GIEGKIKWPNDVLV-NYKKIAGVLVE----GKGDFVVLGIGLNVNNEIP-----DELRETAT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  623 QHKAEL-KPLRADYLIARVVTVLEKLIKEFQdKGPNSVLPLYYRYWVHSGQQVHLGS-----AEGPKVSIvglDDSGFLQ 696
Cdd:PRK08330 140 SMKEVLgREVPLIEVFKRLVENLDRWYKLFL-EGPGEILEEVKGRSMILGKRVKIIGdgeilVEGIAEDI---DEFGALI 215
                        250
                 ....*....|.
gi 46255045  697 VHQEGGEVVTV 707
Cdd:PRK08330 216 LRLDDGTVKKV 226
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
497-604 7.42e-12

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 66.04  E-value: 7.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  497 VIAARQTEGKGRGGNVWLSPVGCALSTLliSIPLRSQLGQRIPFVQHLMSVAVVEAVRSIPEYQDINlrVKWPNDIYYsD 576
Cdd:PTZ00276  36 VLAESQTAGRGTGGRTWTSPKGNMYFTL--CIPQKGVPPELVPVLPLITGLACRAAIMEVLHGAAVH--TKWPNDIIY-A 110
                         90       100
                 ....*....|....*....|....*...
gi 46255045  577 LMKIGGVLVNSTlmGEtfYILIGCGFNV 604
Cdd:PTZ00276 111 GKKIGGSLIESE--GE--YLIIGIGMNI 134
BPL_N pfam09825
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ...
202-390 1.13e-08

Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is found to the N terminus of the biotin protein ligase (BPL) catalytic domain. This domain is essential in BPL activity.


Pssm-ID: 462915  Cd Length: 277  Bit Score: 56.76  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   202 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 248
Cdd:pfam09825  38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   249 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 297
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045   298 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 371
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
                         250       260
                  ....*....|....*....|..
gi 46255045   372 GLSC---DMKQVPALTPLYLLS 390
Cdd:pfam09825 256 GLKVneeEETTVPSLTPLHLSS 277
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
495-604 2.89e-07

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 52.86  E-value: 2.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  495 LIVIAARQTEGKGRGGNVWLSPVGCALsTLLISIPLRSQLGQrIPFVQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYY 574
Cdd:PRK06955  66 IVRVAYEQTAGRGRQGRPWFAQPGNAL-LFSVACVLPRPVAA-LAGLSLAVGVALAEALAALPAALGQRIALKWPNDLLI 143
                         90       100       110
                 ....*....|....*....|....*....|.
gi 46255045  575 SDlMKIGGVLVNSTLMG-ETFYILIGCGFNV 604
Cdd:PRK06955 144 AG-RKLAGILIETVWATpDATAVVIGIGLNV 173
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
495-651 1.31e-05

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 47.51  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  495 LIVIAARQTEGKG------RGGNVWLSPVGCALSTLLIsIPLRSQLgQRIPFVQHLMSVAVVEAVrsipEYQDINLRVKW 568
Cdd:PTZ00275  51 IIVSCNEQTNGIGtrdtkkNQDRIWLSEKGNLFTTFVF-LWNRNDI-EKVKYLAQTCTVAISKTL----EYFHLVTQIKW 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  569 PNDIYYsDLMKIGGVLVN-------STLMGETFYILIGCGFNVTNSNPTiciNDLITEYNKQHKAELKPLRADYLIARVV 641
Cdd:PTZ00275 125 INDVLV-NYKKIAGCLVHlyylddfPNLNSRYVCVMVGIGINVTLEDKH---NLLNNNYTSIKKELQRDFNTPKSIPSVE 200
                        170
                 ....*....|
gi 46255045  642 TVLEKLIKEF 651
Cdd:PTZ00275 201 QVTEKLIINL 210
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
669-716 1.20e-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: 40.14  E-value: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 46255045   669 HSGQQVHLGSAEGPKV-SIVGLDDSGFLQVHQEGGEvvtvHPDGNSFDM 716
Cdd:pfam02237   1 TLGREVRVLLGDGIVEgIAVGIDDDGALLLETDDGT----IRDINSGEV 45
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
467-608 2.86e-04

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 42.64  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  467 KVILFAEVTPTTMRLLDGLMFQTPQEMGLIViAARQTEGKGRGGNVWLSpVGCALsTLLISIPLrSQLGQRIPfvqhLMS 546
Cdd:PRK08477   2 EIRVFESLDSTQTYLIEKIKNGELKAPFAIV-AKEQTAGIGSRGNSWEG-KKGNL-FFSFALKE-SDLPKDLP----LQS 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46255045  547 VAVVEAV--RSIPEYQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGEtfYILIGCGFNVTNSN 608
Cdd:PRK08477  74 SSIYFGFllKEVLKELGSKVWLKWPNDLYLDDK-KIGGVITN--KIKN--FIVCGIGLNLKFSP 132
PRK05935 PRK05935
biotin--protein ligase; Provisional
467-603 1.35e-03

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 40.57  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46255045  467 KVILF--AEVTPTTMRLLDGLMFQTPQemGLIVIAAR-QTEGKGRGGNVWLSPVGCALSTLLISIplrSQLGQRIPFVQH 543
Cdd:PRK05935   2 KVIYYeiAETPSTNTTAKEGMHLWDPY--ALTVISTReQTAGKGKFGKSWHSSDQDLLASFCFFI---TVLNIDVSLLFR 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46255045  544 LMSVAVVEAVRS--IPeyqdiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 603
Cdd:PRK05935  77 LGTEAVMRLGEDlgIT-----EAVIKWPNDVLVHG-EKLCGVLCETIPVKGGLGVILGIGVN 132
 
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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