|
Name |
Accession |
Description |
Interval |
E-value |
| BPL_N |
pfam09825 |
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ... |
12-281 |
8.99e-160 |
|
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: 464.69 E-value: 8.99e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 12 LNVLIYAGPGVTPESQRQCTESLKRLVGSKYAVAYITSNILKTEPWASTCALLVFPGGADLPFCRELNGTGNRAIIDYVR 91
Cdd:pfam09825 1 MNVLVYSGPGTTPESVRHTLETLRRLLSPYYAVIPVSAKVLLKEPWTSKCALLVFPGGADLPYCRELNGEGNRRIKQFVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 92 NGGAYLGFCAGGYYGSAVCWFGLEDPAQDVKGQRELAFFPGTCAGPAFKGFEYHREVGARAAKLTVRKEafsgaqAPPDV 171
Cdd:pfam09825 81 RGGAYLGFCAGGYYGSARCEFEVGDPKLEVVGPRELAFFPGTCRGPAFPGFVYNSEAGARAAKLKVNTS------PVPDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 172 FKSYYNGGGVFVDVEKFAsnGVEVLAEYADDIDVKSGE-KRAAVVFCKAGHGKAILTGPHPEFAGASLKPQ-ASIPGYDK 249
Cdd:pfam09825 155 FKSYYNGGGVFVDADKYA--NVEVLARYTEDLDVDGGDgGPAAVVYCKVGKGKALLTGPHPEFAPSNLKPQeADGPGYDK 232
|
250 260 270
....*....|....*....|....*....|..
gi 336270156 250 LIEEVTADETARLEFLAACLNKLGLSLPSKDA 281
Cdd:pfam09825 233 VVDELAADEKARLEFLRACLTKLGLKVNEEEE 264
|
|
| COG4285 |
COG4285 |
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1) ... |
1-240 |
6.73e-49 |
|
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1)-like domain [General function prediction only];
Pssm-ID: 443426 [Multi-domain] Cd Length: 221 Bit Score: 172.15 E-value: 6.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 1 MATAPktdQRVLNVLIYAGPGVTPESqRQCTESLKRLVGSKYAVAYITSNILKTEPWASTCaLLVFPGGADLPFCRELNG 80
Cdd:COG4285 1 MKARP---TPRPRVLVYRGPGASDDC-VEALVRALKQLNLGFKVRYVTAEDITAGTLANAD-LLIQPGGGDLPYYKALGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 81 TGNRAIIDYVRNGGAYLGFCAGGYYGSAVCWFGLEDPAQDVKGQRelaFFPGTCAGPAFKGFEYHREVGARAAKLTvrke 160
Cdd:COG4285 76 EGNAAIREFVENGGGYLGICAGAYLASKYVGFGLGTDARVVGNRE---FFPGVAVGPLGRPGADVSLTESTAVLVR---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 161 afsgaqAPPDVFKSYYNGGGVFVDVEKFAsnGVEVLAEYADdidvksgeKRAAVVFCKAGHGKAILTGPHPEfAGASLKP 240
Cdd:COG4285 149 ------WRGDTLTIYYQGGPYFEPAPDGP--GYTVLATYAD--------GSPAIVSGTYGKGRVVLSGPHPE-ATPGLEE 211
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
422-663 |
2.09e-40 |
|
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: 148.78 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 422 ETVTSTNTLLASnpHLMARLESGFTFTATRQVAGRGRGTNVWVSPPG-CLIMSTVInHPAsvMGMRPLAFINYLAAVAIV 500
Cdd:COG0340 6 DEVDSTNDEAKE--LAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLL-RPD--LPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 501 EAIKGydstdsiYQKLDVKIKWPNDIYVRDpsKpdepayvKVGGIL--ANCSYSSPNYqIIVGIGINTNNAE-------- 570
Cdd:COG0340 81 EALRE-------LTGVDVGLKWPNDILLNG--K-------KLAGILieASGEGDGIDW-VVIGIGINVNQPPfdpeeldq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 571 PTTSLDALLKwtasklggdkpppQPFHIERLVARIVTWLEILYDHFLSKGFSdELEALYYKHWLHTNQIVTLQDEDG-VK 649
Cdd:COG0340 144 PATSLKEETG-------------KEVDREELLAALLEELEELYDRFLEEGFA-PILEEWRARLATLGRRVRVETGGEtLE 209
|
250
....*....|....
gi 336270156 650 ARVLGITKDQGLLV 663
Cdd:COG0340 210 GIAVGIDEDGALLL 223
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
422-612 |
1.38e-37 |
|
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: 138.55 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 422 ETVTSTNTLLASnpHLMARLESGFTFTATRQVAGRGRGTNVWVSPPG-CLIMSTVINHPASVmgmRPLAFINYLAAVAIV 500
Cdd:cd16442 6 DEIDSTNDEAKE--LARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPP---AEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 501 EAIKGYdstdsiyQKLDVKIKWPNDIYVRDpsKpdepayvKVGGILANCSYSSPN-YQIIVGIGINTNNAEPTTSLDAll 579
Cdd:cd16442 81 EALEKL-------GGIPVQIKWPNDILVNG--K-------KLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-- 142
|
170 180 190
....*....|....*....|....*....|...
gi 336270156 580 kwTASKLGGDKPPPQPFHIERLVARIVTWLEIL 612
Cdd:cd16442 143 --TSLATSLGKEVDRNELLEELLAALENRLELF 173
|
|
| GATase1_ScBLP_like |
cd03144 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ... |
13-106 |
2.15e-37 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP); Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP). Biotin-apoprotein ligase modifies proteins by covalently attaching biotin. ScBLP is known to biotinylate acety-CoA carboxylase and pyruvate carboxylase. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, the Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in a typical GATase1 domain is conserved.
Pssm-ID: 153238 Cd Length: 114 Bit Score: 135.46 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 13 NVLIYAGPGVTPESQRQCTESLKRLvgskYAVAYITSNILKTEPWASTCALLVFPGGADLPFCRELNGTGNRAIIDYVRN 92
Cdd:cd03144 1 NVLVYNGPGASPGSLKHLAELLRLY----LAVSTVTADELAVGPWESKTALLVVPGGADLPYCRALNGKGNRRIRNFVRN 76
|
90
....*....|....
gi 336270156 93 GGAYLGFCAGGYYG 106
Cdd:cd03144 77 GGNYLGICAGAYLA 90
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
420-565 |
9.18e-26 |
|
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: 103.29 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 420 YGETVTSTNTLLasNPHLMARLESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVINHPASVMGMRPLAFINYLAAVAI 499
Cdd:pfam03099 1 LGERIKSTNTYL--EELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336270156 500 VEAIKGYdstDSIYQKLDVKIKWPNDIYVrdpskpdepAYVKVGGILANCSYSSPNYQIIVGIGIN 565
Cdd:pfam03099 79 LEALGLY---KPGISGIPCFVKWPNDLYV---------NGRKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
415-666 |
1.16e-24 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 105.64 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 415 GNHVMYGETVTSTNTLLASNphlMARLESGFTFTATRQVAGRGRGTNVWVSPPGC-LIMSTVINHPAsvmGMRPLAFINY 493
Cdd:PRK11886 77 PGRVTVLPVIDSTNQYLLDR---IAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQ---GPAQAMGLSL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 494 LAAVAIVEAIKGYDStdsiyqkLDVKIKWPNDIYVRDpskpdepayVKVGGILA--------NCsysspnyQIIVGIGIN 565
Cdd:PRK11886 151 VVGIAIAEALRRLGA-------IDVGLKWPNDIYLND---------RKLAGILVelsgetgdAA-------HVVIGIGIN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 566 TNNAEPTTSL-DAllKWTAskLGGDKPPpqpfhIER--LVARIVTWLEILYDHFLSKGFSDELEaLYYKHWLHTNQIVTL 642
Cdd:PRK11886 208 VAMPDFPEELiDQ--PWSD--LQEAGPT-----IDRnqLAAELIKQLRAALELFEQEGLAPFLE-RWKKLDLFLGREVKL 277
|
250 260
....*....|....*....|....*
gi 336270156 643 QDEDG-VKARVLGITKDQGLLVAEE 666
Cdd:PRK11886 278 IIGDKeISGIARGIDEQGALLLEDD 302
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
417-663 |
1.49e-23 |
|
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: 100.17 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 417 HVMYGETVTSTNTLLASNPHLMArlESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVINHPasvMGMRPLAFINYLAA 496
Cdd:TIGR00121 1 EVIVLDVIDSTNQYALELAKEGK--LKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPD---LPKSPAPGLTLVAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 497 VAIVEAIKGYDStdsiyqklDVKIKWPNDIYVRDPskpdepayvKVGGILANcSYSSPNY--QIIVGIGINTNNAEPTTS 574
Cdd:TIGR00121 76 IAIAEVLKELGD--------QVQVKWPNDILLKDK---------KLGGILTE-LTGKENRadYVVIGIGINVQNRKPAES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 575 LDALLKWTASKLGGDkpppqpfhIER--LVARIVTWLEILYDHFLSKGFsDELEALYYKHWLHTNQIVTLQDEDGV-KAR 651
Cdd:TIGR00121 138 LREQAISLSEEAGID--------LDRgeLIEGFLRNFEENLEWFEQEGI-DEILSKWEKLSAHIGREVSLTTGNGEiEGI 208
|
250
....*....|..
gi 336270156 652 VLGITKDQGLLV 663
Cdd:TIGR00121 209 ARGIDKDGALLL 220
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BPL_N |
pfam09825 |
Biotin-protein ligase, N terminal; The function of this structural domain is unknown. It is ... |
12-281 |
8.99e-160 |
|
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: 464.69 E-value: 8.99e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 12 LNVLIYAGPGVTPESQRQCTESLKRLVGSKYAVAYITSNILKTEPWASTCALLVFPGGADLPFCRELNGTGNRAIIDYVR 91
Cdd:pfam09825 1 MNVLVYSGPGTTPESVRHTLETLRRLLSPYYAVIPVSAKVLLKEPWTSKCALLVFPGGADLPYCRELNGEGNRRIKQFVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 92 NGGAYLGFCAGGYYGSAVCWFGLEDPAQDVKGQRELAFFPGTCAGPAFKGFEYHREVGARAAKLTVRKEafsgaqAPPDV 171
Cdd:pfam09825 81 RGGAYLGFCAGGYYGSARCEFEVGDPKLEVVGPRELAFFPGTCRGPAFPGFVYNSEAGARAAKLKVNTS------PVPDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 172 FKSYYNGGGVFVDVEKFAsnGVEVLAEYADDIDVKSGE-KRAAVVFCKAGHGKAILTGPHPEFAGASLKPQ-ASIPGYDK 249
Cdd:pfam09825 155 FKSYYNGGGVFVDADKYA--NVEVLARYTEDLDVDGGDgGPAAVVYCKVGKGKALLTGPHPEFAPSNLKPQeADGPGYDK 232
|
250 260 270
....*....|....*....|....*....|..
gi 336270156 250 LIEEVTADETARLEFLAACLNKLGLSLPSKDA 281
Cdd:pfam09825 233 VVDELAADEKARLEFLRACLTKLGLKVNEEEE 264
|
|
| COG4285 |
COG4285 |
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1) ... |
1-240 |
6.73e-49 |
|
Uncharacterized conserved protein, conains N-terminal glutamine amidotransferase (GATase1)-like domain [General function prediction only];
Pssm-ID: 443426 [Multi-domain] Cd Length: 221 Bit Score: 172.15 E-value: 6.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 1 MATAPktdQRVLNVLIYAGPGVTPESqRQCTESLKRLVGSKYAVAYITSNILKTEPWASTCaLLVFPGGADLPFCRELNG 80
Cdd:COG4285 1 MKARP---TPRPRVLVYRGPGASDDC-VEALVRALKQLNLGFKVRYVTAEDITAGTLANAD-LLIQPGGGDLPYYKALGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 81 TGNRAIIDYVRNGGAYLGFCAGGYYGSAVCWFGLEDPAQDVKGQRelaFFPGTCAGPAFKGFEYHREVGARAAKLTvrke 160
Cdd:COG4285 76 EGNAAIREFVENGGGYLGICAGAYLASKYVGFGLGTDARVVGNRE---FFPGVAVGPLGRPGADVSLTESTAVLVR---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 161 afsgaqAPPDVFKSYYNGGGVFVDVEKFAsnGVEVLAEYADdidvksgeKRAAVVFCKAGHGKAILTGPHPEfAGASLKP 240
Cdd:COG4285 149 ------WRGDTLTIYYQGGPYFEPAPDGP--GYTVLATYAD--------GSPAIVSGTYGKGRVVLSGPHPE-ATPGLEE 211
|
|
| BirA2 |
COG0340 |
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ... |
422-663 |
2.09e-40 |
|
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: 148.78 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 422 ETVTSTNTLLASnpHLMARLESGFTFTATRQVAGRGRGTNVWVSPPG-CLIMSTVInHPAsvMGMRPLAFINYLAAVAIV 500
Cdd:COG0340 6 DEVDSTNDEAKE--LAREGAPEGTVVVAEEQTAGRGRRGRSWVSPPGkGLYFSLLL-RPD--LPPARLPLLSLAAGLAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 501 EAIKGydstdsiYQKLDVKIKWPNDIYVRDpsKpdepayvKVGGIL--ANCSYSSPNYqIIVGIGINTNNAE-------- 570
Cdd:COG0340 81 EALRE-------LTGVDVGLKWPNDILLNG--K-------KLAGILieASGEGDGIDW-VVIGIGINVNQPPfdpeeldq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 571 PTTSLDALLKwtasklggdkpppQPFHIERLVARIVTWLEILYDHFLSKGFSdELEALYYKHWLHTNQIVTLQDEDG-VK 649
Cdd:COG0340 144 PATSLKEETG-------------KEVDREELLAALLEELEELYDRFLEEGFA-PILEEWRARLATLGRRVRVETGGEtLE 209
|
250
....*....|....
gi 336270156 650 ARVLGITKDQGLLV 663
Cdd:COG0340 210 GIAVGIDEDGALLL 223
|
|
| BPL |
cd16442 |
biotin protein ligase; Biotin protein ligase (EC 6.3.4.15) catalyzes the synthesis of an ... |
422-612 |
1.38e-37 |
|
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: 138.55 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 422 ETVTSTNTLLASnpHLMARLESGFTFTATRQVAGRGRGTNVWVSPPG-CLIMSTVINHPASVmgmRPLAFINYLAAVAIV 500
Cdd:cd16442 6 DEIDSTNDEAKE--LARSGAPEGTVVVAEEQTAGRGRRGRKWESPKGkGLYFSLLLRPDVPP---AEAPLLTLLAAVAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 501 EAIKGYdstdsiyQKLDVKIKWPNDIYVRDpsKpdepayvKVGGILANCSYSSPN-YQIIVGIGINTNNAEPTTSLDAll 579
Cdd:cd16442 81 EALEKL-------GGIPVQIKWPNDILVNG--K-------KLAGILTEASAEGEGvAAVVIGIGINVNNTPPPEPLPD-- 142
|
170 180 190
....*....|....*....|....*....|...
gi 336270156 580 kwTASKLGGDKPPPQPFHIERLVARIVTWLEIL 612
Cdd:cd16442 143 --TSLATSLGKEVDRNELLEELLAALENRLELF 173
|
|
| GATase1_ScBLP_like |
cd03144 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ... |
13-106 |
2.15e-37 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP); Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Saccharomyces cerevisiae biotin-apoprotein ligase (ScBLP). Biotin-apoprotein ligase modifies proteins by covalently attaching biotin. ScBLP is known to biotinylate acety-CoA carboxylase and pyruvate carboxylase. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, the Cys residue found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow in a typical GATase1 domain is conserved.
Pssm-ID: 153238 Cd Length: 114 Bit Score: 135.46 E-value: 2.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 13 NVLIYAGPGVTPESQRQCTESLKRLvgskYAVAYITSNILKTEPWASTCALLVFPGGADLPFCRELNGTGNRAIIDYVRN 92
Cdd:cd03144 1 NVLVYNGPGASPGSLKHLAELLRLY----LAVSTVTADELAVGPWESKTALLVVPGGADLPYCRALNGKGNRRIRNFVRN 76
|
90
....*....|....
gi 336270156 93 GGAYLGFCAGGYYG 106
Cdd:cd03144 77 GGNYLGICAGAYLA 90
|
|
| BPL_LplA_LipB |
pfam03099 |
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ... |
420-565 |
9.18e-26 |
|
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: 103.29 E-value: 9.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 420 YGETVTSTNTLLasNPHLMARLESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVINHPASVMGMRPLAFINYLAAVAI 499
Cdd:pfam03099 1 LGERIKSTNTYL--EELNSSELESGGVVVVRRQTGGRGRGGNVWHSPKGCLTYSLLLSKEHPNVDPSVLEFYVLELVLAV 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336270156 500 VEAIKGYdstDSIYQKLDVKIKWPNDIYVrdpskpdepAYVKVGGILANCSYSSPNYQIIVGIGIN 565
Cdd:pfam03099 79 LEALGLY---KPGISGIPCFVKWPNDLYV---------NGRKLAGILQRSTRGGTLHHGVIGLGVN 132
|
|
| PRK11886 |
PRK11886 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA; |
415-666 |
1.16e-24 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
Pssm-ID: 237010 [Multi-domain] Cd Length: 319 Bit Score: 105.64 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 415 GNHVMYGETVTSTNTLLASNphlMARLESGFTFTATRQVAGRGRGTNVWVSPPGC-LIMSTVINHPAsvmGMRPLAFINY 493
Cdd:PRK11886 77 PGRVTVLPVIDSTNQYLLDR---IAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGnLYLSLYWRLNQ---GPAQAMGLSL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 494 LAAVAIVEAIKGYDStdsiyqkLDVKIKWPNDIYVRDpskpdepayVKVGGILA--------NCsysspnyQIIVGIGIN 565
Cdd:PRK11886 151 VVGIAIAEALRRLGA-------IDVGLKWPNDIYLND---------RKLAGILVelsgetgdAA-------HVVIGIGIN 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 566 TNNAEPTTSL-DAllKWTAskLGGDKPPpqpfhIER--LVARIVTWLEILYDHFLSKGFSDELEaLYYKHWLHTNQIVTL 642
Cdd:PRK11886 208 VAMPDFPEELiDQ--PWSD--LQEAGPT-----IDRnqLAAELIKQLRAALELFEQEGLAPFLE-RWKKLDLFLGREVKL 277
|
250 260
....*....|....*....|....*
gi 336270156 643 QDEDG-VKARVLGITKDQGLLVAEE 666
Cdd:PRK11886 278 IIGDKeISGIARGIDEQGALLLEDD 302
|
|
| birA_ligase |
TIGR00121 |
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ... |
417-663 |
1.49e-23 |
|
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: 100.17 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 417 HVMYGETVTSTNTLLASNPHLMArlESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVINHPasvMGMRPLAFINYLAA 496
Cdd:TIGR00121 1 EVIVLDVIDSTNQYALELAKEGK--LKGDLVVAEYQTAGRGRRGRKWLSPEGGLYFSLILRPD---LPKSPAPGLTLVAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 497 VAIVEAIKGYDStdsiyqklDVKIKWPNDIYVRDPskpdepayvKVGGILANcSYSSPNY--QIIVGIGINTNNAEPTTS 574
Cdd:TIGR00121 76 IAIAEVLKELGD--------QVQVKWPNDILLKDK---------KLGGILTE-LTGKENRadYVVIGIGINVQNRKPAES 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 575 LDALLKWTASKLGGDkpppqpfhIER--LVARIVTWLEILYDHFLSKGFsDELEALYYKHWLHTNQIVTLQDEDGV-KAR 651
Cdd:TIGR00121 138 LREQAISLSEEAGID--------LDRgeLIEGFLRNFEENLEWFEQEGI-DEILSKWEKLSAHIGREVSLTTGNGEiEGI 208
|
250
....*....|..
gi 336270156 652 VLGITKDQGLLV 663
Cdd:TIGR00121 209 ARGIDKDGALLL 220
|
|
| PRK08330 |
PRK08330 |
biotin--protein ligase; Provisional |
415-671 |
5.42e-21 |
|
biotin--protein ligase; Provisional
Pssm-ID: 169384 [Multi-domain] Cd Length: 236 Bit Score: 92.89 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 415 GNHVMYGETVTSTN---TLLASNphlmarLESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVINHPASVMGMRPLAFi 491
Cdd:PRK08330 2 GRNIIYFDEVDSTNeyaKRIAPD------EEEGTVIVADRQTAGHGRKGRAWASPEGGLWMSVILKPKVSPEHLPKLVF- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 492 nyLAAVAIVEAIKGYDstdsiyqkLDVKIKWPNDIYVRdpskpdepaYVKVGGILANCSysspNYQIIVGIGINTNNAEP 571
Cdd:PRK08330 75 --LGALAVVDTLREFG--------IEGKIKWPNDVLVN---------YKKIAGVLVEGK----GDFVVLGIGLNVNNEIP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 572 ttslDALLKWTAS---KLGGDKPPPQPFHierlvaRIVTWLEILYDHFLsKGFSDELEALYYKhwlhtNQIVtlqdedGV 648
Cdd:PRK08330 132 ----DELRETATSmkeVLGREVPLIEVFK------RLVENLDRWYKLFL-EGPGEILEEVKGR-----SMIL------GK 189
|
250 260
....*....|....*....|...
gi 336270156 649 KARVLGITKDQGLLVAEEVMEDG 671
Cdd:PRK08330 190 RVKIIGDGEILVEGIAEDIDEFG 212
|
|
| PTZ00276 |
PTZ00276 |
biotin/lipoate protein ligase; Provisional |
427-594 |
1.06e-10 |
|
biotin/lipoate protein ligase; Provisional
Pssm-ID: 140302 [Multi-domain] Cd Length: 245 Bit Score: 62.58 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 427 TNTLLASNPHLMARLESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVI---NHPASVMGMRPLafINYLAA-VAIVEA 502
Cdd:PTZ00276 16 TSTMDVARTMLAAAGGKPFAVLAESQTAGRGTGGRTWTSPKGNMYFTLCIpqkGVPPELVPVLPL--ITGLACrAAIMEV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 503 IKGYdstdsiyqklDVKIKWPNDIYVrdpskpdepAYVKVGGILANCSYSSpnyqIIVGIGIN-------TNNAEPTTSL 575
Cdd:PTZ00276 94 LHGA----------AVHTKWPNDIIY---------AGKKIGGSLIESEGEY----LIIGIGMNievappvTDAGRESTMV 150
|
170
....*....|....*....
gi 336270156 576 DALlkwtASKLGGDKPPPQ 594
Cdd:PTZ00276 151 NEI----AEDLGVKSVTPQ 165
|
|
| PRK06955 |
PRK06955 |
biotin--[acetyl-CoA-carboxylase] ligase; |
422-621 |
2.68e-08 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 235896 [Multi-domain] Cd Length: 300 Bit Score: 56.33 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 422 ETVTSTNTLLASN----PHLMARLESGFTFTATRQVAGRGRGTNVWVSPPGCLIMSTVinhpASVMGMRP--LAFINYLA 495
Cdd:PRK06955 39 EETGSTNADLMARlkalPRSADALPAPIVRVAYEQTAGRGRQGRPWFAQPGNALLFSV----ACVLPRPVaaLAGLSLAV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 496 AVAIVEAIKGYDSTdsiyQKLDVKIKWPNDIYVrdpskpdepAYVKVGGILANCSYSSPNYQ-IIVGIGINTNNAEPTTS 574
Cdd:PRK06955 115 GVALAEALAALPAA----LGQRIALKWPNDLLI---------AGRKLAGILIETVWATPDATaVVIGIGLNVRRADAVAA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 336270156 575 LDALLKWTASKLGGDKPP-------PQPfHIERLVARIVTWLEILYDHFLSKGF 621
Cdd:PRK06955 182 EVDALRAREAALARGLPPvalaaacAGA-NLTDTLAAALNALAPALQAFGADGL 234
|
|
| PRK08477 |
PRK08477 |
biotin--[acetyl-CoA-carboxylase] ligase; |
417-576 |
2.95e-06 |
|
biotin--[acetyl-CoA-carboxylase] ligase;
Pssm-ID: 236273 [Multi-domain] Cd Length: 211 Bit Score: 48.80 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 417 HVMYGETVTSTNTllasnpHLMARLESG-----FTFTATRQVAGRG-RGtNVWVSPPGCLIMSTVINH---PASVmgmrP 487
Cdd:PRK08477 2 EIRVFESLDSTQT------YLIEKIKNGelkapFAIVAKEQTAGIGsRG-NSWEGKKGNLFFSFALKEsdlPKDL----P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 488 LAFInylaavaiveaikgydstdSIY---------QKLDVKI--KWPNDIYVRDPskpdepayvKVGGILANCSysspNY 556
Cdd:PRK08477 71 LQSS-------------------SIYfgfllkevlKELGSKVwlKWPNDLYLDDK---------KIGGVITNKI----KN 118
|
170 180
....*....|....*....|.
gi 336270156 557 QIIVGIGINTNNA-EPTTSLD 576
Cdd:PRK08477 119 FIVCGIGLNLKFSpKNFACLD 139
|
|
| PRK05935 |
PRK05935 |
biotin--protein ligase; Provisional |
426-579 |
9.93e-06 |
|
biotin--protein ligase; Provisional
Pssm-ID: 235649 [Multi-domain] Cd Length: 190 Bit Score: 47.12 E-value: 9.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 426 STNTLLASNPHLMARleSGFTFTATR-QVAGRGRGTNVWVSPPGCLIMS-----TVINHPASVMgMRplafinyLAAVAI 499
Cdd:PRK05935 13 STNTTAKEGMHLWDP--YALTVISTReQTAGKGKFGKSWHSSDQDLLASfcffiTVLNIDVSLL-FR-------LGTEAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 500 VEAIKGYDSTDSiyqkldvKIKWPNDIYVRDPskpdepayvKVGGILANCSYSSPNYQIIVGIGINTNNA--------EP 571
Cdd:PRK05935 83 MRLGEDLGITEA-------VIKWPNDVLVHGE---------KLCGVLCETIPVKGGLGVILGIGVNGNTTkdellgidQP 146
|
....*...
gi 336270156 572 TTSLDALL 579
Cdd:PRK05935 147 ATSLQELL 154
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
14-105 |
1.21e-04 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 41.42 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 14 VLIYAGPGVTPESQRQCTESLKRLvGSKYAVAYITSNILKTEPWASTCALLVFPGGADLPFCRELNGTGNRAIIDYVRNG 93
Cdd:cd03128 1 VAVLLFGGSEELELASPLDALREA-GAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAAAG 79
|
90
....*....|..
gi 336270156 94 GAYLGFCAGGYY 105
Cdd:cd03128 80 KPVLGICLGAQL 91
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
14-105 |
1.81e-04 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 41.82 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 14 VLIYAGPGVTPESQRQCTESLKRLvGSKYAVAYITSNILKTEPWASTCALLVFPGGADLPFCRELNGTGNRAIIDYVRNG 93
Cdd:cd01653 1 VAVLLFPGFEELELASPLDALREA-GAEVDVVSPDGGPVESDVDLDDYDGLILPGGPGTPDDLARDEALLALLREAAAAG 79
|
90
....*....|..
gi 336270156 94 GAYLGFCAGGYY 105
Cdd:cd01653 80 KPILGICLGAQL 91
|
|
| PRK13325 |
PRK13325 |
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase; |
452-648 |
4.67e-03 |
|
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
Pssm-ID: 183976 [Multi-domain] Cd Length: 592 Bit Score: 40.46 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 452 QVAGRGRGTNVWVSPPG-CLIMST--VINHPASVMGMrplafINYLAAVAIVEAIKGYDstdsiyqkLDVKIKWPNDIYV 528
Cdd:PRK13325 118 QSKGRGRQGRKWSHRLGeCLMFSFgwVFDRPQYELGS-----LSPVAAVACRRALSRLG--------LKTQIKWPNDLVV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336270156 529 -RDpskpdepayvKVGGILANCSYSSPNYQIIVGIGIN---TNNAEPTTSLDALLKwTASKLGGdkpPPQPFHIERLVAR 604
Cdd:PRK13325 185 gRD----------KLGGILIETVRTGGKTVAVVGIGINfvlPKEVENAASVQSLFQ-TASRRGN---ADAAVLLETLLAE 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 336270156 605 IVTWLEilydHFLSKGFSDELEALYYKHWLHTNQIVTLQDEDGV 648
Cdd:PRK13325 251 LDAVLL----QYARDGFAPFVAEYQAANRDHGKAVLLLRDGETV 290
|
|
| |
