|
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 338753397 467 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 545
Cdd:cd16442 1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 624
Cdd:cd16442 76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
|
170 180
....*....|....*....|...
gi 338753397 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 338753397 202 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 248
Cdd:pfam09825 38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 249 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 297
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 298 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 371
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
|
250 260
....*....|....*....|..
gi 338753397 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 338753397 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 338753397 467 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 545
Cdd:cd16442 1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 624
Cdd:cd16442 76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
|
170 180
....*....|....*....|...
gi 338753397 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 338753397 471 FAEVTPTTMRLLDGLmFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVV 550
Cdd:pfam03099 1 LGERIKSTNTYLEEL-NSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 338753397 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 338753397 467 KVILFAEVtPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVGCAlstLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:COG0340 1 RIEVFDEV-DSTNDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKG---LYFSLLLRPDLPpARLPLLSLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAVRsipEYQDINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNS--------NPTICINDL 616
Cdd:COG0340 76 GLAVAEALR---ELTGVDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQPpfdpeeldQPATSLKEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 617 ITeynkqhkaelKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKV-SIVGLDDSGFL 695
Cdd:COG0340 152 TG----------KEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEgIAVGIDEDGAL 221
|
250
....*....|...
gi 338753397 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 338753397 467 KVILFAEVTPTTMRLLDglMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:TIGR00121 1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAvrsIPEYQDiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTICINDLITEYNKQH 624
Cdd:TIGR00121 75 GIAIAEV---LKELGD-QVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 625 KAELKplRADyLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHL----GSAEGPKVSIvglDDSGFLQVHQE 700
Cdd:TIGR00121 150 GIDLD--RGE-LIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLLEDG 223
|
..
gi 338753397 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 338753397 464 QLGKVILFAEVTPTTMRLLDGLmfqTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCalsTLLISIPLRSQLGQRipfvqH 543
Cdd:PRK11886 76 PPGRVTVLPVIDSTNQYLLDRI---AELKSGDLCLAEYQTAGRGRRGRQWFSPFGG---NLYLSLYWRLNQGPA-----Q 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 544 LMS------VAVVEAVRSIpeyQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTICI 613
Cdd:PRK11886 145 AMGlslvvgIAIAEALRRL---GAIDVGLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEELI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 614 N----DLITeynkqhkaELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIV-G 688
Cdd:PRK11886 219 DqpwsDLQE--------AGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIArG 290
|
250
....*....|....*
gi 338753397 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 338753397 202 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 248
Cdd:pfam09825 38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 249 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 297
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 298 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 371
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
|
250 260
....*....|....*....|..
gi 338753397 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 338753397 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 338753397 467 KVILFAEvTPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVG-CALSTLLISIPLRSQlgqRIPFVQHLM 545
Cdd:cd16442 1 KLIVLDE-IDSTNDEAKELARSGAPE-GTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPPA---EAPLLTLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAVRSIPeyqDINLRVKWPNDIYYSDlMKIGGVLVNSTLMGET-FYILIGCGFNVTNSNPTICINDlITEYNKQH 624
Cdd:cd16442 76 AVAVAEALEKLG---GIPVQIKWPNDILVNG-KKLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-TSLATSLG 150
|
170 180
....*....|....*....|...
gi 338753397 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 338753397 471 FAEVTPTTMRLLDGLmFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCALSTLLISIPLRSQLGQRIPFVQHLMSVAVV 550
Cdd:pfam03099 1 LGERIKSTNTYLEEL-NSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAVL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 338753397 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 338753397 467 KVILFAEVtPTTMRLLDGLMFQTPQEmGLIVIAARQTEGKGRGGNVWLSPVGCAlstLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:COG0340 1 RIEVFDEV-DSTNDEAKELAREGAPE-GTVVVAEEQTAGRGRRGRSWVSPPGKG---LYFSLLLRPDLPpARLPLLSLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAVRsipEYQDINLRVKWPNDIYYSDLmKIGGVLV-NSTLMGETFYILIGCGFNVTNS--------NPTICINDL 616
Cdd:COG0340 76 GLAVAEALR---ELTGVDVGLKWPNDILLNGK-KLAGILIeASGEGDGIDWVVIGIGINVNQPpfdpeeldQPATSLKEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 617 ITeynkqhkaelKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKV-SIVGLDDSGFL 695
Cdd:COG0340 152 TG----------KEVDREELLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEgIAVGIDEDGAL 221
|
250
....*....|...
gi 338753397 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 338753397 467 KVILFAEVTPTTMRLLDglMFQTPQEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLG-QRIPFVQHLM 545
Cdd:TIGR00121 1 EVIVLDVIDSTNQYALE--LAKEGKLKGDLVVAEYQTAGRGRRGRKWLSPEG----GLYFSLILRPDLPkSPAPGLTLVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 546 SVAVVEAvrsIPEYQDiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETF-YILIGCGFNVTNSNPTICINDLITEYNKQH 624
Cdd:TIGR00121 75 GIAIAEV---LKELGD-QVQVKWPNDILLKD-KKLGGILTELTGKENRAdYVVIGIGINVQNRKPAESLREQAISLSEEA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 625 KAELKplRADyLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHL----GSAEGPKVSIvglDDSGFLQVHQE 700
Cdd:TIGR00121 150 GIDLD--RGE-LIEGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLttgnGEIEGIARGI---DKDGALLLEDG 223
|
..
gi 338753397 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 338753397 464 QLGKVILFAEVTPTTMRLLDGLmfqTPQEMGLIVIAARQTEGKGRGGNVWLSPVGCalsTLLISIPLRSQLGQRipfvqH 543
Cdd:PRK11886 76 PPGRVTVLPVIDSTNQYLLDRI---AELKSGDLCLAEYQTAGRGRRGRQWFSPFGG---NLYLSLYWRLNQGPA-----Q 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 544 LMS------VAVVEAVRSIpeyQDINLRVKWPNDIYYSDLmKIGGVLVNstLMGET---FYILIGCGFNVT-NSNPTICI 613
Cdd:PRK11886 145 AMGlslvvgIAIAEALRRL---GAIDVGLKWPNDIYLNDR-KLAGILVE--LSGETgdaAHVVIGIGINVAmPDFPEELI 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 614 N----DLITeynkqhkaELKPLRADYLIARVVTVLEKLIKEFQDKGPNSVLPLYYRYWVHSGQQVHLGSAEGPKVSIV-G 688
Cdd:PRK11886 219 DqpwsDLQE--------AGPTIDRNQLAAELIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIArG 290
|
250
....*....|....*
gi 338753397 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 338753397 467 KVILFAEVTPTT---MRLLDGLmfqtpqEMGLIVIAARQTEGKGRGGNVWLSPVGcalsTLLISIPLRSQLGQR-IPFVQ 542
Cdd:PRK08330 4 NIIYFDEVDSTNeyaKRIAPDE------EEGTVIVADRQTAGHGRKGRAWASPEG----GLWMSVILKPKVSPEhLPKLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 543 HLMSVAVVEAVRSIpeyqDINLRVKWPNDIYYsDLMKIGGVLVNstlmGETFYILIGCGFNVTNSNPticinDLITEYNK 622
Cdd:PRK08330 74 FLGALAVVDTLREF----GIEGKIKWPNDVLV-NYKKIAGVLVE----GKGDFVVLGIGLNVNNEIP-----DELRETAT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 623 QHKAEL-KPLRADYLIARVVTVLEKLIKEFQdKGPNSVLPLYYRYWVHSGQQVHLGS-----AEGPKVSIvglDDSGFLQ 696
Cdd:PRK08330 140 SMKEVLgREVPLIEVFKRLVENLDRWYKLFL-EGPGEILEEVKGRSMILGKRVKIIGdgeilVEGIAEDI---DEFGALI 215
|
250
....*....|.
gi 338753397 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 338753397 497 VIAARQTEGKGRGGNVWLSPVGCALSTLliSIPLRSQLGQRIPFVQHLMSVAVVEAVRSIPEYQDINlrVKWPNDIYYsD 576
Cdd:PTZ00276 36 VLAESQTAGRGTGGRTWTSPKGNMYFTL--CIPQKGVPPELVPVLPLITGLACRAAIMEVLHGAAVH--TKWPNDIIY-A 110
|
90 100
....*....|....*....|....*...
gi 338753397 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 338753397 202 EDSALRDPWTDNCLLLVIatresiP--EDL----------YQKFMAYLSQGGKVLGL-------SS-------------- 248
Cdd:pfam09825 38 AKVLLKEPWTSKCALLVF------PggADLpycrelngegNRRIKQFVRRGGAYLGFcaggyygSArcefevgdpklevv 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 249 -----SF--------TFGGFQVTS-KGAlhKTVQNLVFSKADQSEVKL-----------------SVLssgCRYQEgPVR 297
Cdd:pfam09825 112 gprelAFfpgtcrgpAFPGFVYNSeAGA--RAAKLKVNTSPVPDEFKSyyngggvfvdadkyanvEVL---ARYTE-DLD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 298 LSPGrlqghlenEDKDRMIVHVPFGTrgGEAVLCQVHLELPPSSNIVQTPEDFNL------LKSSNFRRYEVLREILTTL 371
Cdd:pfam09825 186 VDGG--------DGGPAAVVYCKVGK--GKALLTGPHPEFAPSNLKPQEADGPGYdkvvdeLAADEKARLEFLRACLTKL 255
|
250 260
....*....|....*....|..
gi 338753397 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 338753397 495 LIVIAARQTEGKGRGGNVWLSPVGCALsTLLISIPLRSQLGQrIPFVQHLMSVAVVEAVRSIPEYQDINLRVKWPNDIYY 574
Cdd:PRK06955 66 IVRVAYEQTAGRGRQGRPWFAQPGNAL-LFSVACVLPRPVAA-LAGLSLAVGVALAEALAALPAALGQRIALKWPNDLLI 143
|
90 100 110
....*....|....*....|....*....|.
gi 338753397 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 338753397 495 LIVIAARQTEGKG------RGGNVWLSPVGCALSTLLIsIPLRSQLgQRIPFVQHLMSVAVVEAVrsipEYQDINLRVKW 568
Cdd:PTZ00275 51 IIVSCNEQTNGIGtrdtkkNQDRIWLSEKGNLFTTFVF-LWNRNDI-EKVKYLAQTCTVAISKTL----EYFHLVTQIKW 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338753397 569 PNDIYYsDLMKIGGVLVN-------STLMGETFYILIGCGFNVTNSNPTiciNDLITEYNKQHKAELKPLRADYLIARVV 641
Cdd:PTZ00275 125 INDVLV-NYKKIAGCLVHlyylddfPNLNSRYVCVMVGIGINVTLEDKH---NLLNNNYTSIKKELQRDFNTPKSIPSVE 200
|
170
....*....|
gi 338753397 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 338753397 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 338753397 467 KVILFAEVTPTTMRLLDGLMFQTPQEMGLIViAARQTEGKGRGGNVWLSpVGCALsTLLISIPLrSQLGQRIPfvqhLMS 546
Cdd:PRK08477 2 EIRVFESLDSTQTYLIEKIKNGELKAPFAIV-AKEQTAGIGSRGNSWEG-KKGNL-FFSFALKE-SDLPKDLP----LQS 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338753397 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 338753397 467 KVILF--AEVTPTTMRLLDGLMFQTPQemGLIVIAAR-QTEGKGRGGNVWLSPVGCALSTLLISIplrSQLGQRIPFVQH 543
Cdd:PRK05935 2 KVIYYeiAETPSTNTTAKEGMHLWDPY--ALTVISTReQTAGKGKFGKSWHSSDQDLLASFCFFI---TVLNIDVSLLFR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 338753397 544 LMSVAVVEAVRS--IPeyqdiNLRVKWPNDIYYSDlMKIGGVLVNSTLMGETFYILIGCGFN 603
Cdd:PRK05935 77 LGTEAVMRLGEDlgIT-----EAVIKWPNDVLVHG-EKLCGVLCETIPVKGGLGVILGIGVN 132
|
|
| |
