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Conserved domains on  [gi|2579494854|ref|WP_310731941|]
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MULTISPECIES: glycine radical domain-containing protein [Rubrivivax]

Protein Classification

glycyl radical enzyme family protein( domain architecture ID 1562547)

glycyl radical enzyme family protein such as ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL), which have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical.

CATH:  3.20.70.20
PubMed:  10574800
SCOP:  3001069

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RNR_PFL super family cl38938
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and ...
 1-151 3.99e-106

Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL) are believed to have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical.


The actual alignment was detected with superfamily member cd01678:

Pssm-ID: 476821 [Multi-domain]  Cd Length: 738  Bit Score: 318.54  E-value: 3.99e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   1 MSVLTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQ 80
Cdd:cd01678   588 QSVLTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDKKGALASLASVAKLPYRDANDGISNTFSIVPNALGKTDEE 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2579494854  81 RVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:cd01678   668 RIDNLVGILDGYFTKGGHHLNVNVLNRETLLDAMEHPEKYPQLTIRVSGYAVNFVKLTREQQLDVISRTFH 738
 
Name Accession Description Interval E-value
PFL1 cd01678
Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, ...
 1-151 3.99e-106

Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.


Pssm-ID: 153087 [Multi-domain]  Cd Length: 738  Bit Score: 318.54  E-value: 3.99e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   1 MSVLTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQ 80
Cdd:cd01678   588 QSVLTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDKKGALASLASVAKLPYRDANDGISNTFSIVPNALGKTDEE 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2579494854  81 RVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:cd01678   668 RIDNLVGILDGYFTKGGHHLNVNVLNRETLLDAMEHPEKYPQLTIRVSGYAVNFVKLTREQQLDVISRTFH 738
PflD COG1882
Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of ...
 1-151 2.66e-98

Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 441486 [Multi-domain]  Cd Length: 789  Bit Score: 299.38  E-value: 2.66e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   1 MSVLTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGq 80
Cdd:COG1882   639 LSILTITSNVPYGKKTGATPDGRKAGEPLADGASPMHGRDKNGPTAVLKSVAKLPYEKATDGILLNQKFSPSALGGEEG- 717

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2579494854  81 rVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:COG1882   718 -IENLVSLLRTYFDLGGHHIQFNVVDRETLLDAQKHPEKYPDLTVRVAGYSAYFVELSKEQQDDIIARTEH 787
Gly_radical pfam01228
Glycine radical;
29-135 2.97e-55

Glycine radical;


Pssm-ID: 426140 [Multi-domain]  Cd Length: 106  Bit Score: 168.89  E-value: 2.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854  29 FAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQRVDNLVNLIDGYFgSGGHHVNVNVFDRA 108
Cdd:pfam01228   1 VAPGISPSHGADFEGPTAVLNSVGKIDYEVELDGISLNQKFLPAVLGYYDEEGYANLNTLIDTYF-EGGHHLQFNVVDRE 79

                          90       100
                  ....*....|....*....|....*..
gi 2579494854 109 TLLHAMEHPELYPQLTIRVSGYAVNFI 135
Cdd:pfam01228  80 TLPDAQKHPEKYPDLTVRVSGYSANFV 106
rad_fix_GrcA3 NF038360
autonomous glycyl radical cofactor GrcA3; This small protein, like GrcA and GrcA2, is a ...
 80-151 4.31e-43

autonomous glycyl radical cofactor GrcA3; This small protein, like GrcA and GrcA2, is a lineage-specific small protein related to the glycyl radical active site-containing C-terminal region of pyruvate formate-lyase (PFL, also called formate C-acetyltransferase) from similar species. Because PFL is prone to damage and inactivation, this protein is made as a spare part that fills in for the portion of the protein that was damaged and lost. The distinct families we now call GrcA, GrcA2, and GrcA3 all have the surprising property of being much more closely related to some full length PFL than to members of the other GrcA-series families.


Pssm-ID: 439653 [Multi-domain]  Cd Length: 78  Bit Score: 137.18  E-value: 4.31e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2579494854  80 QRVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:NF038360    4 AQIDNLVSLLDGYAEKGGHHLNVNVFNRETLLDAQAHPEKYPQLTVRVSGYAVNFNKLTKEQQDEVISRTFH 75
PRK11127 PRK11127
autonomous glycyl radical cofactor GrcA; Provisional
 58-151 2.36e-38

autonomous glycyl radical cofactor GrcA; Provisional


Pssm-ID: 182983 [Multi-domain]  Cd Length: 127  Bit Score: 126.88  E-value: 2.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854  58 CSQDGISYTFTIVPSALGPDEGQRVDnlVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKL 137
Cdd:PRK11127   33 VAKAGYAEDQVVAVSKLGEIEYREVP--VEVKPEVRVEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSL 110

                          90
                  ....*....|....
gi 2579494854 138 TREQQLDVISRTFH 151
Cdd:PRK11127  111 TPEQQRDVIARTFT 124
choline_CutC TIGR04394
choline trimethylamine-lyase; Members of this family, homologs to pyruvate formate-lyases and ...
 4-149 3.36e-25

choline trimethylamine-lyase; Members of this family, homologs to pyruvate formate-lyases and benzylsuccinate synthases, are glycine radical enzymes that appear to act as choline TMA-lyase, that is, to perform a C-N bond cleavage turning choline into trimethylamine (TMA) plus acetaldehyde. The gene symbol is cutC, for choline utilization. The activase, CutD, is a radical SAM enzyme. [Energy metabolism, Amino acids and amines]


Pssm-ID: 275187 [Multi-domain]  Cd Length: 789  Bit Score: 100.26  E-value: 3.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   4 LTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQrvD 83
Cdd:TIGR04394 641 LSISNNTPFGQLTGASANGRLAWTPLSDGISPTQGADFKGPTAIIKSVSKMANDSMNIGMVHNFKLMSGLLDTPEGE--N 718

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2579494854  84 NLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRT 149
Cdd:TIGR04394 719 GLITLLRTASILGNGEMQFNYLDNETLLDAQQHPEKYRDLVVRVAGYSAFFVELCKDVQDEIISRT 784
 
Name Accession Description Interval E-value
PFL1 cd01678
Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, ...
 1-151 3.99e-106

Pyruvate formate lyase 1; Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. The PFL mechanism involves an unusual radical cleavage of pyruvate in which two cysteines and one glycine form radicals that are required for catalysis. PFL has a ten-stranded alpha/beta barrel domain that is structurally similar to those of all three ribonucleotide reductase (RNR) classes as well as benzylsuccinate synthase and B12-independent glycerol dehydratase.


Pssm-ID: 153087 [Multi-domain]  Cd Length: 738  Bit Score: 318.54  E-value: 3.99e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   1 MSVLTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQ 80
Cdd:cd01678   588 QSVLTITSNVVYGKKTGNTPDGRRAGEPFAPGANPMHGRDKKGALASLASVAKLPYRDANDGISNTFSIVPNALGKTDEE 667

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2579494854  81 RVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:cd01678   668 RIDNLVGILDGYFTKGGHHLNVNVLNRETLLDAMEHPEKYPQLTIRVSGYAVNFVKLTREQQLDVISRTFH 738
PflD COG1882
Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of ...
 1-151 2.66e-98

Pyruvate-formate lyase [Energy production and conversion]; Pyruvate-formate lyase is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 441486 [Multi-domain]  Cd Length: 789  Bit Score: 299.38  E-value: 2.66e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   1 MSVLTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGq 80
Cdd:COG1882   639 LSILTITSNVPYGKKTGATPDGRKAGEPLADGASPMHGRDKNGPTAVLKSVAKLPYEKATDGILLNQKFSPSALGGEEG- 717

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2579494854  81 rVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:COG1882   718 -IENLVSLLRTYFDLGGHHIQFNVVDRETLLDAQKHPEKYPDLTVRVAGYSAYFVELSKEQQDDIIARTEH 787
Gly_radical pfam01228
Glycine radical;
29-135 2.97e-55

Glycine radical;


Pssm-ID: 426140 [Multi-domain]  Cd Length: 106  Bit Score: 168.89  E-value: 2.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854  29 FAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQRVDNLVNLIDGYFgSGGHHVNVNVFDRA 108
Cdd:pfam01228   1 VAPGISPSHGADFEGPTAVLNSVGKIDYEVELDGISLNQKFLPAVLGYYDEEGYANLNTLIDTYF-EGGHHLQFNVVDRE 79

                          90       100
                  ....*....|....*....|....*..
gi 2579494854 109 TLLHAMEHPELYPQLTIRVSGYAVNFI 135
Cdd:pfam01228  80 TLPDAQKHPEKYPDLTVRVSGYSANFV 106
rad_fix_GrcA3 NF038360
autonomous glycyl radical cofactor GrcA3; This small protein, like GrcA and GrcA2, is a ...
 80-151 4.31e-43

autonomous glycyl radical cofactor GrcA3; This small protein, like GrcA and GrcA2, is a lineage-specific small protein related to the glycyl radical active site-containing C-terminal region of pyruvate formate-lyase (PFL, also called formate C-acetyltransferase) from similar species. Because PFL is prone to damage and inactivation, this protein is made as a spare part that fills in for the portion of the protein that was damaged and lost. The distinct families we now call GrcA, GrcA2, and GrcA3 all have the surprising property of being much more closely related to some full length PFL than to members of the other GrcA-series families.


Pssm-ID: 439653 [Multi-domain]  Cd Length: 78  Bit Score: 137.18  E-value: 4.31e-43
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2579494854  80 QRVDNLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:NF038360    4 AQIDNLVSLLDGYAEKGGHHLNVNVFNRETLLDAQAHPEKYPQLTVRVSGYAVNFNKLTKEQQDEVISRTFH 75
PFL2_DhaB_BssA cd01677
Pyruvate formate lyase 2 and related enzymes; This family includes pyruvate formate lyase 2 ...
 4-149 5.56e-39

Pyruvate formate lyase 2 and related enzymes; This family includes pyruvate formate lyase 2 (PFL2), B12-independent glycerol dehydratase (DhaB) and the alpha subunit of benzylsuccinate synthase (BssA), all of which have a highly conserved ten-stranded alpha/beta barrel domain, which is similar to those of PFL1 (pyruvate formate lyase 1) and RNR (ribonucleotide reductase). Pyruvate formate lyase catalyzes a key step in anaerobic glycolysis, the conversion of pyruvate and CoenzymeA to formate and acetylCoA. DhaB catalyzes the first step in the conversion of glycerol to 1,3-propanediol while BssA catalyzes the first step in the anaerobic mineralization of both toluene and m-xylene.


Pssm-ID: 153086 [Multi-domain]  Cd Length: 781  Bit Score: 139.72  E-value: 5.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   4 LTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQRvd 83
Cdd:cd01677   637 YSVSANVPFGSVTGATPDGRLAGTPLSDGVSPSQGTDKKGPTAVIKSVSKLDHFNISGGTLLNQKFSPSTLEGEEGLK-- 714

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2579494854  84 NLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRT 149
Cdd:cd01677   715 KLAALIRTYFDLGGHHIQFNVVSAETLRDAQKHPEKYRDLIVRVAGYSAYFVELSKEVQDEIIART 780
PRK11127 PRK11127
autonomous glycyl radical cofactor GrcA; Provisional
 58-151 2.36e-38

autonomous glycyl radical cofactor GrcA; Provisional


Pssm-ID: 182983 [Multi-domain]  Cd Length: 127  Bit Score: 126.88  E-value: 2.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854  58 CSQDGISYTFTIVPSALGPDEGQRVDnlVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKL 137
Cdd:PRK11127   33 VAKAGYAEDQVVAVSKLGEIEYREVP--VEVKPEVRVEGGQHLNVNVLRRETLEDAVKHPEKYPQLTIRVSGYAVRFNSL 110

                          90
                  ....*....|....
gi 2579494854 138 TREQQLDVISRTFH 151
Cdd:PRK11127  111 TPEQQRDVIARTFT 124
pflD PRK09983
putative formate acetyltransferase 2; Provisional
 5-151 2.20e-26

putative formate acetyltransferase 2; Provisional


Pssm-ID: 182181 [Multi-domain]  Cd Length: 765  Bit Score: 103.75  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   5 TITSNVVYGKKTGNTPDGRKAGEPFAPGA-NPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQRvd 83
Cdd:PRK09983  618 TVSAHVPLGSVVGATPDGRFAGEQLADGGlSPMLGQDAQGPTAVLKSVSKLDNTLLSNGTLLNVKFTPATLEGEAGLR-- 695

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2579494854  84 NLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRTFH 151
Cdd:PRK09983  696 KLADFLRAFTQLKLQHIQFNVVNADTLREAQQRPQDYAGLVVRVAGYSAFFVELSKEIQDDIIRRTAH 763
choline_CutC TIGR04394
choline trimethylamine-lyase; Members of this family, homologs to pyruvate formate-lyases and ...
 4-149 3.36e-25

choline trimethylamine-lyase; Members of this family, homologs to pyruvate formate-lyases and benzylsuccinate synthases, are glycine radical enzymes that appear to act as choline TMA-lyase, that is, to perform a C-N bond cleavage turning choline into trimethylamine (TMA) plus acetaldehyde. The gene symbol is cutC, for choline utilization. The activase, CutD, is a radical SAM enzyme. [Energy metabolism, Amino acids and amines]


Pssm-ID: 275187 [Multi-domain]  Cd Length: 789  Bit Score: 100.26  E-value: 3.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854   4 LTITSNVVYGKKTGNTPDGRKAGEPFAPGANPMHGRDYKGAVASMASVAKLPYSCSQDGISYTFTIVPSALGPDEGQrvD 83
Cdd:TIGR04394 641 LSISNNTPFGQLTGASANGRLAWTPLSDGISPTQGADFKGPTAIIKSVSKMANDSMNIGMVHNFKLMSGLLDTPEGE--N 718

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2579494854  84 NLVNLIDGYFGSGGHHVNVNVFDRATLLHAMEHPELYPQLTIRVSGYAVNFIKLTREQQLDVISRT 149
Cdd:TIGR04394 719 GLITLLRTASILGNGEMQFNYLDNETLLDAQQHPEKYRDLVVRVAGYSAFFVELCKDVQDEIISRT 784
RNR_PFL cd00576
Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and ...
 24-104 2.24e-11

Ribonucleotide reductase and Pyruvate formate lyase; Ribonucleotide reductase (RNR) and pyruvate formate lyase (PFL) are believed to have diverged from a common ancestor. They have a structurally similar ten-stranded alpha-beta barrel domain that hosts the active site, and are radical enzymes. RNRs are found in all organisms and provide the only mechanism by which nucleotides are converted to deoxynucleotides. RNRs are separated into three classes based on their metallocofactor usage. Class I RNRs use a diiron-tyrosyl radical while Class II RNRs use coenzyme B12 (adenosylcobalamin, AdoCbl). Class III RNRs use an FeS cluster and S-adenosylmethionine to generate a glycyl radical. PFL, an essential enzyme in anaerobic bacteria, catalyzes the conversion of pyruvate and CoA to acteylCoA and formate in a mechanism that uses a glycyl radical.


Pssm-ID: 153083 [Multi-domain]  Cd Length: 401  Bit Score: 60.24  E-value: 2.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2579494854  24 KAGEPFAPGANPMHGRDY------KGAVASMASVAKLPYScSQDGISYTFTIVPSALgpdegqRVDNLVNLIDGYFGSGG 97
Cdd:cd00576   322 SSGAPATNGVSPSRG*IAivlngdIGPEESLASVAILQFY-ADNGISDTITIPDSAT------NLDQLLAVIDGAAAIKT 394


                  ....*..
gi 2579494854  98 HHVNVNV 104
Cdd:cd00576   395 THVRVNP 401
 
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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