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Conserved domains on  [gi|446578407|ref|WP_000655753|]
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MULTISPECIES: bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA [Salmonella]

Protein Classification

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA( domain architecture ID 11485649)

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor, forming a BirA-biotinyl-5'-adenylate complex that can either transfer the biotinyl moiety to the BCCP subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon

CATH:  1.10.10.10
EC:  6.3.4.15
Gene Symbol:  birA
Gene Ontology:  GO:0005524|GO:0004077|GO:0003677|GO:0006355
PubMed:  3899863
SCOP:  4000146

Graphical summary

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List of domain hits

 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: 566.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   2 KDTTVPLTLISLLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDVDRIHSQLDSGNV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  82 AVLPVIDSTNQYLLDRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 162 RELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITLQEAGITLDRNMLAAK 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446578407 242 LIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQDGVIKPWMGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
 
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: 566.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   2 KDTTVPLTLISLLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDVDRIHSQLDSGNV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  82 AVLPVIDSTNQYLLDRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 162 RELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITLQEAGITLDRNMLAAK 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446578407 242 LIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQDGVIKPWMGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 81-317 2.18e-102

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: 300.09  E-value: 2.18e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   81 VAVLPVIDSTNQYLLDRIGELR-SGDACVAEYQQAGRGRRGRKWFSPFGAnLYLSMYWRLEQGPAAAIGLSLVIGIVMAE 159
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGKlKGDLVVAEYQTAGRGRRGRKWLSPEGG-LYFSLILRPDLPKSPAPGLTLVAGIAIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  160 VLRELGaDKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITLQEAGITLDRNMLA 239
Cdd:TIGR00121  81 VLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGELI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446578407  240 AKLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQDGVIKPWMGGEISLR 317
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 80-317 1.78e-96

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: 285.14  E-value: 1.78e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  80 NVAVLPVIDSTNQYLLDRIGE-LRSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 159 EVLRELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITL-QEAGITLDRNM 237
Cdd:COG0340   81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 238 LAAKLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQ-DGVIKPWMGGEISL 316
Cdd:COG0340  161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240


                 .
gi 446578407 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 3.14e-59

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: 187.47  E-value: 3.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  80 NVAVLPVIDSTNQYLLDRIGELR-SGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:cd16442    1 KLIVLDEIDSTNDEAKELARSGApEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 159 EVLRELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRrvEEDVINQGWITLQEAGITLDRNML 238
Cdd:cd16442   81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNT--PPPEPLPDTSLATSLGKEVDRNEL 158

                        170
                 ....*....|....*
gi 446578407 239 AAKLIYKLRAALELF 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 1.25e-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: 109.84  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   83 VLPVIDSTNQYLL-DRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGaNLYLSMYWRLEQG---PAAAIGLSLVIGIVMA 158
Cdd:pfam03099   1 LGERIKSTNTYLEeLNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446578407  159 EVL----RELGADKVRVKWPNDLYLLDRKLAGILVELTgKTGDAAQIVIGAGIN 208
Cdd:pfam03099  80 EALglykPGISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
HTH_metalloreg NF033788
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ...
 8-48 5.25e-04

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: 38.21  E-value: 5.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446578407   8 LTLISLLADGEFHSGEqLGERLGMSRAAINKHIQTLRDWGV 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: 566.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   2 KDTTVPLTLISLLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDVDRIHSQLDSGNV 81
Cdd:PRK11886   1 KTYTVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLDIFSVKGKGYRLAEPLDLLDPERISSQLPPGRV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  82 AVLPVIDSTNQYLLDRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMAEVL 161
Cdd:PRK11886  81 TVLPVIDSTNQYLLDRIAELKSGDLCLAEYQTAGRGRRGRQWFSPFGGNLYLSLYWRLNQGPAQAMGLSLVVGIAIAEAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 162 RELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITLQEAGITLDRNMLAAK 241
Cdd:PRK11886 161 RRLGAIDVGLKWPNDIYLNDRKLAGILVELSGETGDAAHVVIGIGINVAMPDFPEELIDQPWSDLQEAGPTIDRNQLAAE 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446578407 242 LIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQDGVIKPWMGGEISLRSAE 320
Cdd:PRK11886 241 LIKQLRAALELFEQEGLAPFLERWKKLDLFLGREVKLIIGDKEISGIARGIDEQGALLLEDDGVEKPFNGGEISLRSWE 319
birA_ligase TIGR00121
birA, biotin-[acetyl-CoA-carboxylase] ligase region; This model represents the ...
 81-317 2.18e-102

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: 300.09  E-value: 2.18e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   81 VAVLPVIDSTNQYLLDRIGELR-SGDACVAEYQQAGRGRRGRKWFSPFGAnLYLSMYWRLEQGPAAAIGLSLVIGIVMAE 159
Cdd:TIGR00121   2 VIVLDVIDSTNQYALELAKEGKlKGDLVVAEYQTAGRGRRGRKWLSPEGG-LYFSLILRPDLPKSPAPGLTLVAGIAIAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  160 VLRELGaDKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITLQEAGITLDRNMLA 239
Cdd:TIGR00121  81 VLKELG-DQVQVKWPNDILLKDKKLGGILTELTGKENRADYVVIGIGINVQNRKPAESLREQAISLSEEAGIDLDRGELI 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446578407  240 AKLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQDGVIKPWMGGEISLR 317
Cdd:TIGR00121 160 EGFLRNFEENLEWFEQEGIDEILSKWEKLSAHIGREVSLTTGNGEIEGIARGIDKDGALLLEDGGGIKKIISGEISLR 237
BirA2 COG0340
Biotin-(acetyl-CoA carboxylase) ligase [Coenzyme transport and metabolism]; Biotin-(acetyl-CoA ...
 80-317 1.78e-96

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: 285.14  E-value: 1.78e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  80 NVAVLPVIDSTNQYLLDRIGE-LRSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:COG0340    1 RIEVFDEVDSTNDEAKELAREgAPEGTVVVAEEQTAGRGRRGRSWVSPPGKGLYFSLLLRPDLPPARLPLLSLAAGLAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 159 EVLRELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITL-QEAGITLDRNM 237
Cdd:COG0340   81 EALRELTGVDVGLKWPNDILLNGKKLAGILIEASGEGDGIDWVVIGIGINVNQPPFDPEELDQPATSLkEETGKEVDREE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 238 LAAKLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQ-DGVIKPWMGGEISL 316
Cdd:COG0340  161 LLAALLEELEELYDRFLEEGFAPILEEWRARLATLGRRVRVETGGETLEGIAVGIDEDGALLLETaDGEIRAVAAGEVSL 240


                 .
gi 446578407 317 R 317
Cdd:COG0340  241 R 241
BirA COG1654
Biotin operon repressor [Transcription];
3-320 8.38e-80

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 245.67  E-value: 8.38e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   3 DTTVPLTLISLLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGYSLPEPIQLLDVDRIHSQLDSGNVA 82
Cdd:COG1654    2 MSSTRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESVPGKGYRLAEPPDLLDPEEIRAGLSTKRLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  83 --VLPVIDSTNQYLLDRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMAEV 160
Cdd:COG1654   82 reILYVISSTSTNLLALELAAQGGDAGTVVAAEQQRGGRGRRRRSWSSPGGGGLLYSLLLRPPIAPALLSLLLLAAAVAV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 161 LRELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRRVEEDVINQGWITLQEAGITLDRNMLAA 240
Cdd:COG1654  162 AAALAEGGGLVKWKKWPNDLLKKGKKILGILEEEGGDADGVVIVVGGGGNNNNSNPEEEPQELAELATSLLLILRLRLLR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 241 KLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLIIGDKEIFGISRGIDTQGALLLEQDGVIKPWMGGEISLRSAE 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 3.14e-59

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: 187.47  E-value: 3.14e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  80 NVAVLPVIDSTNQYLLDRIGELR-SGDACVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQGPAAAIGLSLVIGIVMA 158
Cdd:cd16442    1 KLIVLDEIDSTNDEAKELARSGApEGTVVVAEEQTAGRGRRGRKWESPKGKGLYFSLLLRPDVPPAEAPLLTLLAAVAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 159 EVLRELGADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINMAMRrvEEDVINQGWITLQEAGITLDRNML 238
Cdd:cd16442   81 EALEKLGGIPVQIKWPNDILVNGKKLAGILTEASAEGEGVAAVVIGIGINVNNT--PPPEPLPDTSLATSLGKEVDRNEL 158

                        170
                 ....*....|....*
gi 446578407 239 AAKLIYKLRAALELF 253
Cdd:cd16442  159 LEELLAALENRLELF 173
PRK06955 PRK06955
biotin--[acetyl-CoA-carboxylase] ligase;
67-320 2.38e-43

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


Pssm-ID: 235896 [Multi-domain]  Cd Length: 300  Bit Score: 150.70  E-value: 2.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  67 LDVDRIHSQLDSG----NVAVLPVIDSTNQYLLDRIGEL-RSGDAC------VAEYQQAGRGRRGRKWFSPFGANLYLSM 135
Cdd:PRK06955  17 IDRDRLDAHLAAAarawPLEIVEETGSTNADLMARLKALpRSADALpapivrVAYEQTAGRGRQGRPWFAQPGNALLFSV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 136 YWRLEQGPAAAIGLSLVIGIVMAEVLREL---GADKVRVKWPNDLYLLDRKLAGILVELTGKTGDAAQIVIGAGINM--- 209
Cdd:PRK06955  97 ACVLPRPVAALAGLSLAVGVALAEALAALpaaLGQRIALKWPNDLLIAGRKLAGILIETVWATPDATAVVIGIGLNVrra 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 210 AMRRVEEDVINQGWITL---------QEAGITLDRNMLAAKLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVKLII 280
Cdd:PRK06955 177 DAVAAEVDALRAREAALarglppvalAAACAGANLTDTLAAALNALAPALQAFGADGLAPFAARWHALHAYAGREVVLLE 256

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 446578407 281 GDKEIF-GISRGIDTQGALLLEQDGVIKPWMGGEISLRSAE 320
Cdd:PRK06955 257 DGAELArGVAHGIDETGQLLLDTPAGRQAIAAGDVSLREAD 297
BPL_LplA_LipB pfam03099
Biotin/lipoate A/B protein ligase family; This family includes biotin protein ligase, ...
 83-208 1.25e-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: 109.84  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407   83 VLPVIDSTNQYLL-DRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGaNLYLSMYWRLEQG---PAAAIGLSLVIGIVMA 158
Cdd:pfam03099   1 LGERIKSTNTYLEeLNSSELESGGVVVVRRQTGGRGRGGNVWHSPKG-CLTYSLLLSKEHPnvdPSVLEFYVLELVLAVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446578407  159 EVL----RELGADKVRVKWPNDLYLLDRKLAGILVELTgKTGDAAQIVIGAGIN 208
Cdd:pfam03099  80 EALglykPGISGIPCFVKWPNDLYVNGRKLAGILQRST-RGGTLHHGVIGLGVN 132
PRK08330 PRK08330
biotin--protein ligase; Provisional
 80-317 3.84e-23

biotin--protein ligase; Provisional


Pssm-ID: 169384 [Multi-domain]  Cd Length: 236  Bit Score: 95.58  E-value: 3.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  80 NVAVLPVIDSTNQYLLDRIGELRSGDACVAEYQQAGRGRRGRKWFSPFGAnLYLSMYWRLEQGPAAAIGLSLVIGIVMAE 159
Cdd:PRK08330   4 NIIYFDEVDSTNEYAKRIAPDEEEGTVIVADRQTAGHGRKGRAWASPEGG-LWMSVILKPKVSPEHLPKLVFLGALAVVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 160 VLRELGADKvRVKWPNDLYLLDRKLAGILVELTGKtgdaaQIVIGAGINMAmRRVEEDVINQGWITLQEAGITLDRNMLA 239
Cdd:PRK08330  83 TLREFGIEG-KIKWPNDVLVNYKKIAGVLVEGKGD-----FVVLGIGLNVN-NEIPDELRETATSMKEVLGREVPLIEVF 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 240 AKLIYKLRAALELFeQEGLSPYLSRWKKLDNFIDRPVKlIIGDKEIF--GISRGIDTQGALLLE-QDGVIKPWMGGEISL 316
Cdd:PRK08330 156 KRLVENLDRWYKLF-LEGPGEILEEVKGRSMILGKRVK-IIGDGEILveGIAEDIDEFGALILRlDDGTVKKVLYGDVSL 233


                 .
gi 446578407 317 R 317
Cdd:PRK08330 234 R 234
birA_repr_reg TIGR00122
BirA biotin operon repressor domain; This model represents the amino-terminal helix-turn-helix ...
 6-76 5.21e-23

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: 90.22  E-value: 5.21e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446578407    6 VPLTLISLLADGEFHsGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVpGKGYSLPEPIQLLDVDRIHSQL 76
Cdd:TIGR00122   1 MPLRLLALLADNPFS-GEKLGEALGMSRTAVNKHIQTLREWGVDVLTV-GKGYRLPPPIPLLNAKQIRGQL 69
PRK13325 PRK13325
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;
107-317 1.27e-21

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/type III pantothenate kinase;


Pssm-ID: 183976 [Multi-domain]  Cd Length: 592  Bit Score: 95.16  E-value: 1.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 107 CVAEYQQAGRGRRGRKWFSPFGANLYLSMYWRLEQgPAAAIG-LSLVIGIVMAEVLRELGADkVRVKWPNDLYLLDRKLA 185
Cdd:PRK13325 113 CVTHLQSKGRGRQGRKWSHRLGECLMFSFGWVFDR-PQYELGsLSPVAAVACRRALSRLGLK-TQIKWPNDLVVGRDKLG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 186 GILVElTGKTGDAAQIVIGAGINMAM-RRVEEDVINQGWITLQEAGITLDRNMLAAKLIYKLRAALELFEQEGLSPYLSR 264
Cdd:PRK13325 191 GILIE-TVRTGGKTVAVVGIGINFVLpKEVENAASVQSLFQTASRRGNADAAVLLETLLAELDAVLLQYARDGFAPFVAE 269

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446578407 265 WKKLDNFIDRPVkLIIGDKEIF--GISRGIDTQGALLLEQDGVIKPWMGGEISLR 317
Cdd:PRK13325 270 YQAANRDHGKAV-LLLRDGETVfeGTVKGVDGQGVLHLETAEGKQTVVSGEISLR 323
PRK08477 PRK08477
biotin--[acetyl-CoA-carboxylase] ligase;
87-272 1.88e-17

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


Pssm-ID: 236273 [Multi-domain]  Cd Length: 211  Bit Score: 79.23  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407  87 IDSTNQYLLDRI--GELRSGDACVAEYQQAGRGRRGRKWFSPFGaNLYLSMYWRLEQGP-----AAAiglSLVIGIVMAE 159
Cdd:PRK08477   9 LDSTQTYLIEKIknGELKAPFAIVAKEQTAGIGSRGNSWEGKKG-NLFFSFALKESDLPkdlplQSS---SIYFGFLLKE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 160 VLRELGAdKVRVKWPNDLYLLDRKLAGIlveLTGKTGDaaQIVIGAGINMAmrRVEEdvinqgwitlqEAGItLDRNMLA 239
Cdd:PRK08477  85 VLKELGS-KVWLKWPNDLYLDDKKIGGV---ITNKIKN--FIVCGIGLNLK--FSPK-----------NFAC-LDIEISD 144

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446578407 240 AKLIYKLRAALE--LFEQEGLSPYLSRWKKLDNFI 272
Cdd:PRK08477 145 DLLLEGFLQKIEkkILWKQIFSKYKLEFEKSKSFS 179
PTZ00276 PTZ00276
biotin/lipoate protein ligase; Provisional
 106-211 5.50e-13

biotin/lipoate protein ligase; Provisional


Pssm-ID: 140302 [Multi-domain]  Cd Length: 245  Bit Score: 67.58  E-value: 5.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 106 ACVAEYQQAGRGRRGRKWFSPFGaNLYLSM-YWRLEQGPAAAIGLSLVIGIV-MAEVLRELGADKVRVKWPNDLYLLDRK 183
Cdd:PTZ00276  35 AVLAESQTAGRGTGGRTWTSPKG-NMYFTLcIPQKGVPPELVPVLPLITGLAcRAAIMEVLHGAAVHTKWPNDIIYAGKK 113

                         90       100
                 ....*....|....*....|....*...
gi 446578407 184 LAGILVEltgktGDAAQIVIGAGINMAM 211
Cdd:PTZ00276 114 IGGSLIE-----SEGEYLIIGIGMNIEV 136
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 13-58 1.44e-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: 55.90  E-value: 1.44e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446578407   13 LLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGKGY 58
Cdd:pfam08279   7 LLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAEPGRGY 52
BPL_C pfam02237
Biotin protein ligase C terminal domain; The function of this structural domain is unknown. It ...
 271-317 7.14e-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: 53.62  E-value: 7.14e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446578407  271 FIDRPVKLIIGDKEIFGISRGIDTQGALLLEQ-DGVIKPWMGGEISLR 317
Cdd:pfam02237   1 TLGREVRVLLGDGIVEGIAVGIDDDGALLLETdDGTIRDINSGEVSLR 48
PRK05935 PRK05935
biotin--protein ligase; Provisional
 112-264 1.15e-07

biotin--protein ligase; Provisional


Pssm-ID: 235649 [Multi-domain]  Cd Length: 190  Bit Score: 50.97  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 112 QQAGRGRRGRKWFSPFGaNLYLSMYWRLEQgpaAAIGLSLVIGIVMAEVLR---ELGADKVRVKWPNDLYLLDRKLAGIL 188
Cdd:PRK05935  38 QTAGKGKFGKSWHSSDQ-DLLASFCFFITV---LNIDVSLLFRLGTEAVMRlgeDLGITEAVIKWPNDVLVHGEKLCGVL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 189 VE---LTGKTGdaaqIVIGAGINMAMRRVEEDVINQGWITLQE-AGITLDRNMLAAKLIYKLRAALelfeQEGLSPYLSR 264
Cdd:PRK05935 114 CEtipVKGGLG----VILGIGVNGNTTKDELLGIDQPATSLQElLGHPIDLEEQRERLIKHIKHVL----IQTLPKLLAR 185
YobV COG2378
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ...
 8-62 2.06e-05

Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];


Pssm-ID: 441945 [Multi-domain]  Cd Length: 314  Bit Score: 45.45  E-value: 2.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446578407   8 LTLISLLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWGVDVFTVPGK--GYSLPE 62
Cdd:COG2378    8 LALLQLLQSRRGVTAAELAERLEVSERTIYRDIDALRELGVPIEAERGRggGYRLRD 64
HTH_metalloreg NF033788
metalloregulator ArsR/SmtB family transcription factor; Transcriptional repressors that sense ...
 8-48 5.25e-04

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: 38.21  E-value: 5.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446578407   8 LTLISLLADGEFHSGEqLGERLGMSRAAINKHIQTLRDWGV 48
Cdd:NF033788  14 LRILELLAEGELCVCE-LAEALGLSQSAVSQHLKVLRDAGL 53
ArsR COG0640
DNA-binding transcriptional regulator, ArsR family [Transcription];
8-48 6.49e-04

DNA-binding transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 440405 [Multi-domain]  Cd Length: 92  Bit Score: 38.33  E-value: 6.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446578407   8 LTLISLLADGEFHSGEqLGERLGMSRAAINKHIQTLRDWGV 48
Cdd:COG0640   23 LRILRLLAEGELCVGE-LAEALGLSQSTVSHHLKVLREAGL 62
PTZ00275 PTZ00275
biotin-acetyl-CoA-carboxylase ligase; Provisional
 170-300 8.79e-04

biotin-acetyl-CoA-carboxylase ligase; Provisional


Pssm-ID: 185536 [Multi-domain]  Cd Length: 285  Bit Score: 40.19  E-value: 8.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446578407 170 RVKWPNDLYLLDRKLAGILVEL------TGKTGDAAQIVIGAGINMAMRRvEEDVINQGWITLQEAGI----------TL 233
Cdd:PTZ00275 121 QIKWINDVLVNYKKIAGCLVHLyylddfPNLNSRYVCVMVGIGINVTLED-KHNLLNNNYTSIKKELQrdfntpksipSV 199

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446578407 234 DRNMLaaKLIYKLRAALELFEQEGLSPYLSRWKKLDNFIDRPVkLIIGDKE-IFGISRGIDTQGALLL 300
Cdd:PTZ00275 200 EQVTE--KLIINLKAVINKLRKEGFSSFLDYITPRLLYKDKKV-LIDQDNElIVGYLQGLLHDGSLLL 264
GbsR COG1510
DNA-binding transcriptional regulator GbsR, MarR family [Transcription];
13-55 3.32e-03

DNA-binding transcriptional regulator GbsR, MarR family [Transcription];


Pssm-ID: 441119  Cd Length: 164  Bit Score: 37.61  E-value: 3.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446578407  13 LLADGEFHSGEQLGERLGMSRAAINKHIQTLRDWG-VDVFTVPG 55
Cdd:COG1510   36 LYLSDEPLTADELAEELGVSKSSVSTALRELEDWGlVRRVRKPG 79
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 10-69 6.28e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 34.97  E-value: 6.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446578407  10 LISLLADGEFHSGEqLGERLGMSRAAINKHIQTLRDWGV--DVFTVPGKGYSLPEPIQLLDV 69
Cdd:cd00090   12 ILRLLLEGPLTVSE-LAERLGLSQSTVSRHLKKLEEAGLveSRREGRRVYYSLTDAERLLAL 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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