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Conserved domains on  [gi|1370481357|ref|XP_024307833|]
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biotin--protein ligase isoform X4 [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 ...
410-590 1.92e-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: 1.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 488
Cdd:cd16442     1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 567
Cdd:cd16442    76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
                         170       180
                  ....*....|....*....|...
gi 1370481357 568 KAELKPLRADYLIARVVTVLEKL 590
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 ...
145-333 1.02e-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: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 145 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 191
Cdd:pfam09825  38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 192 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 240
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 241 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 314
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
                         250       260
                  ....*....|....*....|..
gi 1370481357 315 GLSC---DMKQVPALTPLYLLS 333
Cdd:pfam09825 256 GLKVneeEETTVPSLTPLHLSS 277
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
612-659 1.18e-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: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370481357 612 HSGQQVHLGSAEGPKV-SIVGLDDSGFLQVHQEGGEvvtvHPDGNSFDM 659
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 ...
410-590 1.92e-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: 1.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 488
Cdd:cd16442     1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 567
Cdd:cd16442    76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
                         170       180
                  ....*....|....*....|...
gi 1370481357 568 KAELKPLRADYLIARVVTVLEKL 590
Cdd:cd16442   151 KEVDRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
414-546 6.71e-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: 139.88  E-value: 6.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 414 FAEVTPTTMRLLDGLmFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVV 493
Cdd:pfam03099   1 LGERIKSTNTYLEEL-NSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370481357 494 EAVRS-IPEYQDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 546
Cdd:pfam03099  80 EALGLyKPGISGIPCFVKWPNDLYVNG-RKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
410-651 1.00e-36

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: 137.61  E-value: 1.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEVtPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVGCAlstLLISIPLRSQLG-QRIPFVQHLM 488
Cdd:COG0340     1 RIEVFDEV-DSTNDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKG---LYFSLLLRPDLPpARLPLLSLAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAVRsipEYQDINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNS--------NPTICINDL 559
Cdd:COG0340    76 GLAVAEALR---ELTGVDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQPpfdpeeldQPATSLKEE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 560 ITeynkqhkaelKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKV-SIVGLDDSGFL 638
Cdd:COG0340   152 TG----------KEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEgIAVGIDEDGAL 221
                         250
                  ....*....|...
gi 1370481357 639 QVHQEGGEVVTVH 651
Cdd:COG0340   222 LLETADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
410-645 4.76e-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: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEVTPTTMRLLDglMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLG-QRIPFVQHLM 488
Cdd:TIGR00121   1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAvrsIPEYQDiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTICINDLITEYNKQH 567
Cdd:TIGR00121  75 GIAIAEV---LKELGD-QVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 568 KAELKplRADyLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHL----GSAEGPKVSIvglDDSGFLQVHQE 643
Cdd:TIGR00121 150 GIDLD--RGE-LIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLLEDG 223

                  ..
gi 1370481357 644 GG 645
Cdd:TIGR00121 224 GG 225
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
407-646 1.38e-20

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 93.31  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 407 QLGKVILFAEVTPTTMRLLDGLmfqTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCalsTLLISIPLRSQLGQRipfvqH 486
Cdd:PRK11886   76 PPGRVTVLPVIDSTNQYLLDRI---AELKSGDLCLAEYQTAGRGRRGRQWFSPFGG---NLYLSLYWRLNQGPA-----Q 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 487 LMS------VAVVEAVRSIpeyQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTICI 556
Cdd:PRK11886  145 AMGlslvvgIAIAEALRRL---GAIDVGLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEELI 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 557 N----DLITeynkqhkaELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIV-G 631
Cdd:PRK11886  219 DqpwsDLQE--------AGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIArG 290
                         250
                  ....*....|....*
gi 1370481357 632 LDDSGFLQVHQEGGE 646
Cdd:PRK11886  291 IDEQGALLLEDDGVE 305
BPL_N pfam09825
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ...
145-333 1.02e-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: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 145 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 191
Cdd:pfam09825  38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 192 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 240
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 241 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 314
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
                         250       260
                  ....*....|....*....|..
gi 1370481357 315 GLSC---DMKQVPALTPLYLLS 333
Cdd:pfam09825 256 GLKVneeEETTVPSLTPLHLSS 277
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
612-659 1.18e-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: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370481357 612 HSGQQVHLGSAEGPKV-SIVGLDDSGFLQVHQEGGEvvtvHPDGNSFDM 659
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 ...
410-590 1.92e-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: 1.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 488
Cdd:cd16442     1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 567
Cdd:cd16442    76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
                         170       180
                  ....*....|....*....|...
gi 1370481357 568 KAELKPLRADYLIARVVTVLEKL 590
Cdd:cd16442   151 KEVDRNELLEELLAALENRLELF 173
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
414-546 6.71e-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: 139.88  E-value: 6.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 414 FAEVTPTTMRLLDGLmFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVV 493
Cdd:pfam03099   1 LGERIKSTNTYLEEL-NSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370481357 494 EAVRS-IPEYQDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 546
Cdd:pfam03099  80 EALGLyKPGISGIPCFVKWPNDLYVNG-RKLAGILQRSTRGGTLHHGVIGLGVN 132
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
410-651 1.00e-36

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: 137.61  E-value: 1.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEVtPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVGCAlstLLISIPLRSQLG-QRIPFVQHLM 488
Cdd:COG0340     1 RIEVFDEV-DSTNDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKG---LYFSLLLRPDLPpARLPLLSLAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAVRsipEYQDINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNS--------NPTICINDL 559
Cdd:COG0340    76 GLAVAEALR---ELTGVDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQPpfdpeeldQPATSLKEE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 560 ITeynkqhkaelKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKV-SIVGLDDSGFL 638
Cdd:COG0340   152 TG----------KEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEgIAVGIDEDGAL 221
                         250
                  ....*....|...
gi 1370481357 639 QVHQEGGEVVTVH 651
Cdd:COG0340   222 LLETADGEIRAVA 234
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
410-645 4.76e-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: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEVTPTTMRLLDglMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLG-QRIPFVQHLM 488
Cdd:TIGR00121   1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 489 SVAVVEAvrsIPEYQDiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTICINDLITEYNKQH 567
Cdd:TIGR00121  75 GIAIAEV---LKELGD-QVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 568 KAELKplRADyLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHL----GSAEGPKVSIvglDDSGFLQVHQE 643
Cdd:TIGR00121 150 GIDLD--RGE-LIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLLEDG 223

                  ..
gi 1370481357 644 GG 645
Cdd:TIGR00121 224 GG 225
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
407-646 1.38e-20

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


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 93.31  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 407 QLGKVILFAEVTPTTMRLLDGLmfqTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCalsTLLISIPLRSQLGQRipfvqH 486
Cdd:PRK11886   76 PPGRVTVLPVIDSTNQYLLDRI---AELKSGDLCLAEYQTAGRGRRGRQWFSPFGG---NLYLSLYWRLNQGPA-----Q 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 487 LMS------VAVVEAVRSIpeyQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTICI 556
Cdd:PRK11886  145 AMGlslvvgIAIAEALRRL---GAIDVGLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEELI 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 557 N----DLITeynkqhkaELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIV-G 631
Cdd:PRK11886  219 DqpwsDLQE--------AGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIArG 290
                         250
                  ....*....|....*
gi 1370481357 632 LDDSGFLQVHQEGGE 646
Cdd:PRK11886  291 IDEQGALLLEDDGVE 305
PRK08330 PRK08330
biotin--protein ligase; Provisional
410-650 4.64e-15

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 75.17  E-value: 4.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEVTPTT---MRLLDGLmfqtpqEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLGQR-IPFVQ 485
Cdd:PRK08330    4 NIIYFDEVDSTNeyaKRIAPDE------EEGTVIVADRQTAGHGRKGRAWASPEG----GLWMSVILKPKVSPEhLPKLV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 486 HLMSVAVVEAVRSIpeyqDINLRVKWPNDIYYsDLMKIGGVLVNstlmGETFYILIGCGFNVTNSNPticinDLITEYNK 565
Cdd:PRK08330   74 FLGALAVVDTLREF----GIEGKIKWPNDVLV-NYKKIAGVLVE----GKGDFVVLGIGLNVNNEIP-----DELRETAT 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 566 QHKAEL-KPLRADYLIARVVTVLEKLIKEFQdKGPNSVLPLYYRYWVHSGQQVHLGS-----AEGPKVSIvglDDSGFLQ 639
Cdd:PRK08330  140 SMKEVLgREVPLIEVFKRLVENLDRWYKLFL-EGPGEILEEVKGRSMILGKRVKIIGdgeilVEGIAEDI---DEFGALI 215
                         250
                  ....*....|.
gi 1370481357 640 VHQEGGEVVTV 650
Cdd:PRK08330  216 LRLDDGTVKKV 226
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
440-547 6.67e-12

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 66.04  E-value: 6.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 440 VIAARQTEGKGRGGNVWLSPVGCALSTLliSIPLRSQLGQRIPFVQHLMSVAVVEAVRSIPEYQDINlrVKWPNDIYYsD 519
Cdd:PTZ00276   36 VLAESQTAGRGTGGRTWTSPKGNMYFTL--CIPQKGVPPELVPVLPLITGLACRAAIMEVLHGAAVH--TKWPNDIIY-A 110
                          90       100
                  ....*....|....*....|....*...
gi 1370481357 520 LMKIGGVLVNSTlmGEtfYILIGCGFNV 547
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 ...
145-333 1.02e-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: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 145 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 191
Cdd:pfam09825  38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 192 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 240
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 241 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 314
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
                         250       260
                  ....*....|....*....|..
gi 1370481357 315 GLSC---DMKQVPALTPLYLLS 333
Cdd:pfam09825 256 GLKVneeEETTVPSLTPLHLSS 277
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
438-547 2.60e-07

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 52.86  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 438 LIVIAARQTEGKGRGGNVWLSPVGCALsTLLISIPLRSQLGQrIPFVQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYY 517
Cdd:PRK06955   66 IVRVAYEQTAGRGRQGRPWFAQPGNAL-LFSVACVLPRPVAA-LAGLSLAVGVALAEALAALPAALGQRIALKWPNDLLI 143
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370481357 518 SDlMKIGGVLVNSTLMG-ETFYILIGCGFNV 547
Cdd:PRK06955  144 AG-RKLAGILIETVWATpDATAVVIGIGLNV 173
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
438-594 1.03e-05

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 47.89  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 438 LIVIAARQTEGKG------RGGNVWLSPVGCALSTLLIsIPLRSQLgQRIPFVQHLMSVAVVEAVrsipEYQDINLRVKW 511
Cdd:PTZ00275   51 IIVSCNEQTNGIGtrdtkkNQDRIWLSEKGNLFTTFVF-LWNRNDI-EKVKYLAQTCTVAISKTL----EYFHLVTQIKW 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 512 PNDIYYsDLMKIGGVLVN-------STLMGETFYILIGCGFNVTNSNPTiciNDLITEYNKQHKAELKPLRADYLIARVV 584
Cdd:PTZ00275  125 INDVLV-NYKKIAGCLVHlyylddfPNLNSRYVCVMVGIGINVTLEDKH---NLLNNNYTSIKKELQRDFNTPKSIPSVE 200
                         170
                  ....*....|
gi 1370481357 585 TVLEKLIKEF 594
Cdd:PTZ00275  201 QVTEKLIINL 210
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
612-659 1.18e-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: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370481357 612 HSGQQVHLGSAEGPKV-SIVGLDDSGFLQVHQEGGEvvtvHPDGNSFDM 659
Cdd:pfam02237   1 TLGREVRVLLGDGIVEgIAVGIDDDGALLLETDDGT----IRDINSGEV 45
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
410-551 2.16e-04

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 43.02  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILFAEVTPTTMRLLDGLMFQTPQEMGLIViAARQTEGKGRGGNVWLSpvgcALSTLLISIPLR-SQLGQRIPfvqhLM 488
Cdd:PRK08477    2 EIRVFESLDSTQTYLIEKIKNGELKAPFAIV-AKEQTAGIGSRGNSWEG----KKGNLFFSFALKeSDLPKDLP----LQ 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370481357 489 SVAVVEAV--RSIPEYQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGEtfYILIGCGFNVTNSN 551
Cdd:PRK08477   73 SSSIYFGFllKEVLKELGSKVWLKWPNDLYLDDK-KIGGVITN--KIKN--FIVCGIGLNLKFSP 132
PRK05935 PRK05935
biotin--protein ligase; Provisional
410-546 1.18e-03

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 40.57  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370481357 410 KVILF--AEVTPTTMRLLDGLMFQTPQemGLIVIAAR-QTEGKGRGGNVWLSPVGCALSTLLISIplrSQLGQRIPFVQH 486
Cdd:PRK05935    2 KVIYYeiAETPSTNTTAKEGMHLWDPY--ALTVISTReQTAGKGKFGKSWHSSDQDLLASFCFFI---TVLNIDVSLLFR 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370481357 487 LMSVAVVEAVRS--IPeyqdiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 546
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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