|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
2-320 |
0e+00 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 557.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 2 KDYTVPLTLISILADAEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDEEQIARQIEHGRV 81
Cdd:PRK11886 1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 82 TVLPVIDSTNQYLLDRLSELQSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIAEVL 161
Cdd:PRK11886 81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 162 QSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISLQEAGISIDRNTLAAC 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504649994 242 LIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQDGMVKPWIGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
81-317 |
2.86e-98 |
|
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: 289.30 E-value: 2.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 81 VTVLPVIDSTNQYLLDRLSELQ-SGDACVAEYQQAGRGRRGRKWFSPFGsNLYLSMYWRLEQGPAAAIGLSLVIGIVIAE 159
Cdd:TIGR00121 2 VIVLDVIDSTNQYALELAKEGKlKGDLVVAEYQTAGRGRRGRKWLSPEG-GLYFSLILRPDLPKSPAPGLTLVAGIAIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 160 VLQSLGaDKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISLQEAGISIDRNTLA 239
Cdd:TIGR00121 81 VLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGELI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504649994 240 ACLIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQDGMVKPWIGGEISLR 317
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
80-317 |
7.06e-97 |
|
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: 285.91 E-value: 7.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 80 RVTVLPVIDSTNQYLLDRLSE-LQSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIA 158
Cdd:COG0340 1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 159 EVLQSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISL-QEAGISIDRNT 237
Cdd:COG0340 81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 238 LAACLIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQ-DGMVKPWIGGEISL 316
Cdd:COG0340 161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240
|
.
gi 504649994 317 R 317
Cdd:COG0340 241 R 241
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
80-253 |
2.16e-58 |
|
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: 185.54 E-value: 2.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 80 RVTVLPVIDSTNQYLLDRLSEL-QSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIA 158
Cdd:cd16442 1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 159 EVLQSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVvnQGWISLQEAGISIDRNTL 238
Cdd:cd16442 81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPL--PDTSLATSLGKEVDRNEL 158
|
170
....*....|....*
gi 504649994 239 AACLIKELRAGFKLF 253
Cdd:cd16442 159 LEELLAALENRLELF 173
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
83-208 |
2.67e-29 |
|
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: 109.07 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 83 VLPVIDSTNQYLL-DRLSELQSGDACVAEYQQAGRGRRGRKWFSPFGsNLYLSMYWRLEQG---PAAAIGLSLVIGIVIA 158
Cdd:pfam03099 1 LGERIKSTNTYLEeLNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504649994 159 EVLQS----LGADKVRVKWPNDLYLQDRKLSGILVELTgKTGDAAQIVSGAGIN 208
Cdd:pfam03099 80 EALGLykpgISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
|
|
| HTH_metalloreg |
NF033788 |
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ... |
8-48 |
7.30e-03 |
|
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense toxic heavy metals such as arsenic or cadmium, and are released from DNA so that resistance factors will be expressed, include ArsR, SmtB, ZiaR, CadC, CadX, KmtR, etc. However, some members of this family, including the sporulation delaying system autorepressor SdpR and its family (see NF033789), may lack metal-binding cites and instead regulate other cellular processes.
Pssm-ID: 411368 [Multi-domain] Cd Length: 76 Bit Score: 34.74 E-value: 7.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 504649994 8 LTLISILADAEFHSGEqLGERLGMSRAAINKHIQTLRDWGV 48
Cdd:NF033788 14 LRILELLAEGELCVCE-LAEALGLSQSAVSQHLKVLRDAGL 53
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
2-320 |
0e+00 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 557.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 2 KDYTVPLTLISILADAEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDEEQIARQIEHGRV 81
Cdd:PRK11886 1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 82 TVLPVIDSTNQYLLDRLSELQSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIAEVL 161
Cdd:PRK11886 81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 162 QSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISLQEAGISIDRNTLAAC 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504649994 242 LIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQDGMVKPWIGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
81-317 |
2.86e-98 |
|
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: 289.30 E-value: 2.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 81 VTVLPVIDSTNQYLLDRLSELQ-SGDACVAEYQQAGRGRRGRKWFSPFGsNLYLSMYWRLEQGPAAAIGLSLVIGIVIAE 159
Cdd:TIGR00121 2 VIVLDVIDSTNQYALELAKEGKlKGDLVVAEYQTAGRGRRGRKWLSPEG-GLYFSLILRPDLPKSPAPGLTLVAGIAIAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 160 VLQSLGaDKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISLQEAGISIDRNTLA 239
Cdd:TIGR00121 81 VLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGELI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504649994 240 ACLIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQDGMVKPWIGGEISLR 317
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
80-317 |
7.06e-97 |
|
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: 285.91 E-value: 7.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 80 RVTVLPVIDSTNQYLLDRLSE-LQSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIA 158
Cdd:COG0340 1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 159 EVLQSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISL-QEAGISIDRNT 237
Cdd:COG0340 81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 238 LAACLIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQ-DGMVKPWIGGEISL 316
Cdd:COG0340 161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240
|
.
gi 504649994 317 R 317
Cdd:COG0340 241 R 241
|
|
| BirA |
COG1654 |
Biotin operon repressor [Transcription]; |
3-320 |
2.45e-76 |
|
Biotin operon repressor [Transcription];
Pssm-ID: 441260 [Multi-domain] Cd Length: 324 Bit Score: 236.81 E-value: 2.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 3 DYTVPLTLISILADAEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDEEQIARQIEHGRV- 81
Cdd:COG1654 2 MSSTRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEEIRAGLSTKRLg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 82 -TVLPVIDSTNQYLLDRLSELQSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIAEV 160
Cdd:COG1654 82 rEILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 161 LQSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVVNQGWISLQEAGISIDRNTLAA 240
Cdd:COG1654 162 AAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 241 CLIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIFGISRGIDAQGALLLEQDGMVKPWIGGEISLRSAE 320
Cdd:COG1654 242 LLLLLLLLLLELLELLGFLEFFFLWERLDWELLRVLKLVVVVVEIGGGGGGGGALGGGLLGLLLLGGGGGGGEGSLSAVV 321
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
80-253 |
2.16e-58 |
|
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: 185.54 E-value: 2.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 80 RVTVLPVIDSTNQYLLDRLSEL-QSGDACVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIA 158
Cdd:cd16442 1 KLIVLDEIDSTNDEAKELARSGaPEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 159 EVLQSLGADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLMMRRVESDVvnQGWISLQEAGISIDRNTL 238
Cdd:cd16442 81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNTPPPEPL--PDTSLATSLGKEVDRNEL 158
|
170
....*....|....*
gi 504649994 239 AACLIKELRAGFKLF 253
Cdd:cd16442 159 LEELLAALENRLELF 173
|
|
| PRK06955 |
PRK06955 |
biotin--[acetyl-CoA-carboxylase] ligase; |
89-320 |
9.06e-41 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 235896 [Multi-domain] Cd Length: 300 Bit Score: 144.15 E-value: 9.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 89 STNQYLLDRLSELQSGDAC-------VAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQGPAAAIGLSLVIGIVIAEVL 161
Cdd:PRK06955 43 STNADLMARLKALPRSADAlpapivrVAYEQTAGRGRQGRPWFAQPGNALLFSVACVLPRPVAALAGLSLAVGVALAEAL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 162 QSL---GADKVRVKWPNDLYLQDRKLSGILVELTGKTGDAAQIVSGAGINLmmRRVESDVVNQGW--------------I 224
Cdd:PRK06955 123 AALpaaLGQRIALKWPNDLLIAGRKLAGILIETVWATPDATAVVIGIGLNV--RRADAVAAEVDAlrareaalarglppV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 225 SLQEAGISIDRNTLAACLIKELRAGFKLFENEGLAPYLTRWEKLDNFINRPVKLIIGDKEIF-GISRGIDAQGALLLEQD 303
Cdd:PRK06955 201 ALAAACAGANLTDTLAAALNALAPALQAFGADGLAPFAARWHALHAYAGREVVLLEDGAELArGVAHGIDETGQLLLDTP 280
|
250
....*....|....*..
gi 504649994 304 GMVKPWIGGEISLRSAE 320
Cdd:PRK06955 281 AGRQAIAAGDVSLREAD 297
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
83-208 |
2.67e-29 |
|
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: 109.07 E-value: 2.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 83 VLPVIDSTNQYLL-DRLSELQSGDACVAEYQQAGRGRRGRKWFSPFGsNLYLSMYWRLEQG---PAAAIGLSLVIGIVIA 158
Cdd:pfam03099 1 LGERIKSTNTYLEeLNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 504649994 159 EVLQS----LGADKVRVKWPNDLYLQDRKLSGILVELTgKTGDAAQIVSGAGIN 208
Cdd:pfam03099 80 EALGLykpgISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
|
|
| PRK08330 |
PRK08330 |
biotin--protein ligase; Provisional |
87-317 |
9.26e-25 |
|
biotin--protein ligase; Provisional
Pssm-ID: 169384 [Multi-domain] Cd Length: 236 Bit Score: 99.82 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 87 IDSTNQYLLDRLSELQSGDACVAEYQQAGRGRRGRKWFSPFGSnLYLSMYWRLEQGPAAAIGLSLVIGIVIAEVLQSLGA 166
Cdd:PRK08330 11 VDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGG-LWMSVILKPKVSPEHLPKLVFLGALAVVDTLREFGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 167 DKvRVKWPNDLYLQDRKLSGILVELTGKtgdaaQIVSGAGINlmmrrVESDVVNQGW---ISLQEA-GISIDRNTLAACL 242
Cdd:PRK08330 90 EG-KIKWPNDVLVNYKKIAGVLVEGKGD-----FVVLGIGLN-----VNNEIPDELRetaTSMKEVlGREVPLIEVFKRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504649994 243 IKELRAGFKLFENEGLAPYLTRWEKlDNFINRPVKlIIGDKEIF--GISRGIDAQGALLLE-QDGMVKPWIGGEISLR 317
Cdd:PRK08330 159 VENLDRWYKLFLEGPGEILEEVKGR-SMILGKRVK-IIGDGEILveGIAEDIDEFGALILRlDDGTVKKVLYGDVSLR 234
|
|
| birA_repr_reg |
TIGR00122 |
BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix ... |
6-72 |
9.61e-24 |
|
BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix repressor region of the biotin--acetyl-CoA-carboxylase ligase/biotin operon repressor bifunctional protein BirA. In many species, the biotin--acetyl-CoA-carboxylase ligase ortholog lacks this DNA-binding repressor region and therefore is not equivalent to the well-characterized BirA of E. coli. This model may recognize some other putative repressor proteins, such as DnrO of Streptomyces peucetius with scores below the noise cutoff but with significance shown by low E-value. [Regulatory functions, DNA interactions]
Pssm-ID: 272918 [Multi-domain] Cd Length: 69 Bit Score: 92.14 E-value: 9.61e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504649994 6 VPLTLISILADAEFHsGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVpGKGYSLPEPIQLLDEEQI 72
Cdd:TIGR00122 1 MPLRLLALLADNPFS-GEKLGEALGMSRTAVNKHIQTLREWGVDVLTV-GKGYRLPPPIPLLNAKQI 65
|
|
| PRK13325 |
PRK13325 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase; |
107-317 |
6.34e-23 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
Pssm-ID: 183976 [Multi-domain] Cd Length: 592 Bit Score: 99.01 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 107 CVAEYQQAGRGRRGRKWFSPFGSNLYLSMYWRLEQgPAAAIG-LSLVIGIVIAEVLQSLGADkVRVKWPNDLYLQDRKLS 185
Cdd:PRK13325 113 CVTHLQSKGRGRQGRKWSHRLGECLMFSFGWVFDR-PQYELGsLSPVAAVACRRALSRLGLK-TQIKWPNDLVVGRDKLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 186 GILVElTGKTGDAAQIVSGAGINLMM-RRVESDVVNQGWISLQEAGISIDRNTLAACLIKELRAGFKLFENEGLAPYLTR 264
Cdd:PRK13325 191 GILIE-TVRTGGKTVAVVGIGINFVLpKEVENAASVQSLFQTASRRGNADAAVLLETLLAELDAVLLQYARDGFAPFVAE 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504649994 265 WEKLDNFINRPVkLIIGDKEIF--GISRGIDAQGALLLEQDGMVKPWIGGEISLR 317
Cdd:PRK13325 270 YQAANRDHGKAV-LLLRDGETVfeGTVKGVDGQGVLHLETAEGKQTVVSGEISLR 323
|
|
| PRK08477 |
PRK08477 |
biotin--[acetyl-CoA-carboxylase] ligase; |
87-272 |
6.63e-18 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 236273 [Multi-domain] Cd Length: 211 Bit Score: 80.77 E-value: 6.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 87 IDSTNQYLLDRLS--ELQSGDACVAEYQQAGRGRRGRKWFSPfGSNLYLSMYWRLEQGP-----AAAiglSLVIGIVIAE 159
Cdd:PRK08477 9 LDSTQTYLIEKIKngELKAPFAIVAKEQTAGIGSRGNSWEGK-KGNLFFSFALKESDLPkdlplQSS---SIYFGFLLKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 160 VLQSLGAdKVRVKWPNDLYLQDRKLSGIlveLTGKTGDaaQIVSGAGINLmmrrvesDVVNQGWISLQeagISIDRNTLA 239
Cdd:PRK08477 85 VLKELGS-KVWLKWPNDLYLDDKKIGGV---ITNKIKN--FIVCGIGLNL-------KFSPKNFACLD---IEISDDLLL 148
|
170 180 190
....*....|....*....|....*....|...
gi 504649994 240 ACLIKELRAgfKLFENEGLAPYLTRWEKLDNFI 272
Cdd:PRK08477 149 EGFLQKIEK--KILWKQIFSKYKLEFEKSKSFS 179
|
|
| PTZ00276 |
PTZ00276 |
biotin/lipoate protein ligase; Provisional |
106-209 |
4.29e-12 |
|
biotin/lipoate protein ligase; Provisional
Pssm-ID: 140302 [Multi-domain] Cd Length: 245 Bit Score: 64.89 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 106 ACVAEYQQAGRGRRGRKWFSPFGsNLYLSM-YWRLEQGPAAAIGLSLVIGIVI-AEVLQSLGADKVRVKWPNDLYLQDRK 183
Cdd:PTZ00276 35 AVLAESQTAGRGTGGRTWTSPKG-NMYFTLcIPQKGVPPELVPVLPLITGLACrAAIMEVLHGAAVHTKWPNDIIYAGKK 113
|
90 100
....*....|....*....|....*.
gi 504649994 184 LSGILVEltgktGDAAQIVSGAGINL 209
Cdd:PTZ00276 114 IGGSLIE-----SEGEYLIIGIGMNI 134
|
|
| BPL_C |
pfam02237 |
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ... |
271-317 |
2.99e-10 |
|
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: 54.78 E-value: 2.99e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504649994 271 FINRPVKLIIGDKEIFGISRGIDAQGALLLEQ-DGMVKPWIGGEISLR 317
Cdd:pfam02237 1 TLGREVRVLLGDGIVEGIAVGIDDDGALLLETdDGTIRDINSGEVSLR 48
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
8-58 |
3.15e-10 |
|
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
Pssm-ID: 429896 [Multi-domain] Cd Length: 52 Bit Score: 54.75 E-value: 3.15e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 504649994 8 LTLISILADA-EFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGY 58
Cdd:pfam08279 1 LQILQLLLEArGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
|
|
| PRK05935 |
PRK05935 |
biotin--protein ligase; Provisional |
112-249 |
8.66e-09 |
|
biotin--protein ligase; Provisional
Pssm-ID: 235649 [Multi-domain] Cd Length: 190 Bit Score: 54.44 E-value: 8.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 112 QQAGRGRRGRKWFSPFGsNLYLSMYWRLEQgpaAAIGLSLVIGI---VIAEVLQSLGADKVRVKWPNDLYLQDRKLSGIL 188
Cdd:PRK05935 38 QTAGKGKFGKSWHSSDQ-DLLASFCFFITV---LNIDVSLLFRLgteAVMRLGEDLGITEAVIKWPNDVLVHGEKLCGVL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504649994 189 VE---LTGKTGdaaqIVSGAGINLMMRRVESDVVNQGWISLQE-AGISIDRNTLAACLIKELRAG 249
Cdd:PRK05935 114 CEtipVKGGLG----VILGIGVNGNTTKDELLGIDQPATSLQElLGHPIDLEEQRERLIKHIKHV 174
|
|
| YobV |
COG2378 |
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ... |
8-73 |
5.28e-06 |
|
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];
Pssm-ID: 441945 [Multi-domain] Cd Length: 314 Bit Score: 47.38 E-value: 5.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504649994 8 LTLISILADAEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGK--GYSLPE----PIQLLDEEQIA 73
Cdd:COG2378 8 LALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELGVPIEAERGRggGYRLRDgyrlPPLMLTEEEAL 79
|
|
| BPL_LplA_LipB |
cd16435 |
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), ... |
58-209 |
3.24e-04 |
|
biotin-lipoate ligase family; This family includes biotin protein ligase (BPL), lipoate-protein ligase A (LplA) and octanoyl-[acyl carrier protein]-protein acyltransferase (LipB). 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. 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) catalyses the formation of an amide linkage between lipoic acid and a specific lysine residue in lipoate dependent enzymes.
Pssm-ID: 319740 Cd Length: 198 Bit Score: 40.98 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504649994 58 YSLPEPIQLLDEEQIARQIEHGRVTVLPVIDSTNQYLLDRLS----ELQSGDACVAEYQQAGRGRRGRKWFSPFGSnlyL 133
Cdd:cd16435 6 DSVDYESAWAAQEKSLRENVSNQSSTLLLWEHPTTVTLGRLDrelpHLELAKKIERGYELVVRNRGGRAVSHDPGQ---L 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504649994 134 SMYWRLeqGPAAAIGLS---LVIGIVIAEVLQSLGADKVRVKWPNDLYLQDRKLSGILVELTgktgdAAQIVSGAGINL 209
Cdd:cd16435 83 VFSPVI--GPNVEFMISkfnLIIEEGIRDAIADFGQSAEVKWGRNDLWIDNRKVCGIAVRVV-----KEAIFHGIALNL 154
|
|
| GbsR |
COG1510 |
DNA-binding transcriptional regulator GbsR, MarR family [Transcription]; |
23-55 |
6.29e-03 |
|
DNA-binding transcriptional regulator GbsR, MarR family [Transcription];
Pssm-ID: 441119 Cd Length: 164 Bit Score: 36.84 E-value: 6.29e-03
10 20 30
....*....|....*....|....*....|....
gi 504649994 23 EQLGERLGMSRAAINKHIQTLRDWG-VDVFTVPG 55
Cdd:COG1510 46 DELAEELGVSKSSVSTALRELEDWGlVRRVRKPG 79
|
|
| HTH_metalloreg |
NF033788 |
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ... |
8-48 |
7.30e-03 |
|
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense toxic heavy metals such as arsenic or cadmium, and are released from DNA so that resistance factors will be expressed, include ArsR, SmtB, ZiaR, CadC, CadX, KmtR, etc. However, some members of this family, including the sporulation delaying system autorepressor SdpR and its family (see NF033789), may lack metal-binding cites and instead regulate other cellular processes.
Pssm-ID: 411368 [Multi-domain] Cd Length: 76 Bit Score: 34.74 E-value: 7.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 504649994 8 LTLISILADAEFHSGEqLGERLGMSRAAINKHIQTLRDWGV 48
Cdd:NF033788 14 LRILELLAEGELCVCE-LAEALGLSQSAVSQHLKVLRDAGL 53
|
|
| |
