NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446636283|ref|WP_000713629|]
View 

MULTISPECIES: radical SAM/SPASM domain-containing protein [Bacillus]

Protein Classification

radical SAM/SPASM domain-containing protein( domain architecture ID 15182439)

radical SAM protein containing an additional [4Fe-4S]-binding SPASM domain; radical SAM protein generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfers a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Gene Ontology:  GO:0003824|GO:0051539|GO:1904047
PubMed:  18307109|17936058|11222759|25477505
SCOP:  3000308

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SPASM_rSAM cd21122
Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; ...
 217-287 2.47e-39

Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


:

Pssm-ID: 410613 [Multi-domain]  Cd Length: 71  Bit Score: 132.35  E-value: 2.47e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446636283 217 GFCHGLRNQAGILANGTVIPCCLDGEGIINLGNINNDSFSNIIEGERATNIVDGFSKRVAVEELCRKCGYR 287
Cdd:cd21122    1 GYCYGLRTQIGILSNGTVVPCCLDADGVINLGNIKEQSLKEILSSPRAKAIIEGFKKGEAIEELCQRCGYR 71
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 8-112 1.96e-28

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


:

Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 106.91  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   8 YLEITSVCNLACSFCP--PTERQKQFISVEDFAKRLDQIKPH-TDYIYLHVkGEPLLHPKIDQLLDLSHEKGFKVNITTN 84
Cdd:COG0535    3 QIELTNRCNLRCKHCYadAGPKRPGELSTEEAKRILDELAELgVKVVGLTG-GEPLLRPDLFELVEYAKELGIRVNLSTN 81

                         90       100
                 ....*....|....*....|....*...
gi 446636283  85 GTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:COG0535   82 GTLLTEELAERLAEAGLDHVTISLDGVD 109
 
Name Accession Description Interval E-value
SPASM_rSAM cd21122
Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; ...
 217-287 2.47e-39

Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410613 [Multi-domain]  Cd Length: 71  Bit Score: 132.35  E-value: 2.47e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446636283 217 GFCHGLRNQAGILANGTVIPCCLDGEGIINLGNINNDSFSNIIEGERATNIVDGFSKRVAVEELCRKCGYR 287
Cdd:cd21122    1 GYCYGLRTQIGILSNGTVVPCCLDADGVINLGNIKEQSLKEILSSPRAKAIIEGFKKGEAIEELCQRCGYR 71
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 8-112 1.96e-28

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 106.91  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   8 YLEITSVCNLACSFCP--PTERQKQFISVEDFAKRLDQIKPH-TDYIYLHVkGEPLLHPKIDQLLDLSHEKGFKVNITTN 84
Cdd:COG0535    3 QIELTNRCNLRCKHCYadAGPKRPGELSTEEAKRILDELAELgVKVVGLTG-GEPLLRPDLFELVEYAKELGIRVNLSTN 81

                         90       100
                 ....*....|....*....|....*...
gi 446636283  85 GTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:COG0535   82 GTLLTEELAERLAEAGLDHVTISLDGVD 109
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 5-287 1.14e-15

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 76.18  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   5 KKFYLEITSVCNLACSFC---PPTERQKQFISVEDFAKRLDQIKPHT-DYIYLHVK---GEPLLHPK-IDQLLDL----- 71
Cdd:COG0641    1 KALVLKPTSRCNLRCSYCyysEGDEGSRRRMSEETAEKAIDFLIESSgPGKELTITffgGEPLLNFDfIKEIVEYarkya 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  72 SHEKGFKVNITTNGTLINKRRHRLLNKpalRQMNFSLhSFDGHPGSQDK-------EGYVRSILSFIREATsQSDLIVSL 144
Cdd:COG0641   81 KKGKKIRFSIQTNGTLLDDEWIDFLKE---NGFSVGI-SLDGPKEIHDRnrvtkngKGSFDRVMRNIKLLK-EHGVEVNI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283 145 RLwNLTQDNKTNAEiqknRDLLSIIENEF--------------GLSYQIEEKltpGKGIKIAERVFINQD------YEFQ 204
Cdd:COG0641  156 RC-TVTRENLDDPE----ELYDFLKELGFrsiqfnpvveegeaDYSLTPEDY---GEFLIELFDEWLERDggkifvREFD 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283 205 WpALHEEEDDGKGFCHG-LRNQAGILANGTVIPC-CLDGEGIINLGNINNDSFSNIIEGERATNIVDgfSKRVAVEELCR 282
Cdd:COG0641  228 I-LLAGLLPPCSSPCVGaGGNYLVVDPDGDIYPCdEFVGDPEFRLGNVFDGSLAELLDSPKLRAFGR--EKNVLLDEECR 304


                 ....*
gi 446636283 283 KCGYR 287
Cdd:COG0641  305 SCPYL 309
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 219-285 1.10e-11

Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur cluster binding domain in many radical SAM domain, pfam04055 proteins. The domain occurs in a number of proteins that modify a protein to become an active enzyme, or a peptide to become a ribosomal natural product. The domain is named SPASM because it occurs in the maturases of Subilitosin, PQQ, Anaerobic Sulfatases, and Mycofactocin.


Pssm-ID: 433020 [Multi-domain]  Cd Length: 66  Bit Score: 59.03  E-value: 1.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446636283  219 CHGLRNQAGILANGTVIPCCLDG-EGIINLGNINNDSFSNIIEGERATNIvdGFSKRVAVEELCRKCG 285
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCFDDDfVGPIVLGNIREQSLAEIWNSPKYREF--RKLGKFALIELCRDCP 66
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 9-112 3.29e-11

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 61.58  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   9 LEITSVCNLACSFCP----PTERQKQFISVEDFAKRLDQIKPHTDYIYLHVKGEPLLHPKIDQLLDLSHE--KGFKVNIT 82
Cdd:cd01335    1 LELTRGCNLNCGFCSnpasKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKelPGFEISIE 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 446636283  83 TNGTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:cd01335   81 TNGTLLTEELLKELKELGLDGVGVSLDSGD 110
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 11-112 9.97e-10

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 56.38  E-value: 9.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   11 ITSVCNLACSFCP----PTERQKQFISVEDFAKRLDQIKPH-TDYIYLHVkGEPLLHPKIDQLLDLSHEK----GFKVNI 81
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLgVEVVILGG-GEPLLLPDLVELLERLLKLelaeGIRITL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446636283   82 TTNGTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAGLDRVSIGLESGD 110
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 2-114 2.02e-09

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 57.66  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   2 KKFKKFYLEIT--SVCNLACSFCPP-------------------TERQKQFISVEDFAKRLDQIKPHTDYIYLhVKGEPL 60
Cdd:NF033640 105 DDVNPRYLDLRfgNLCNLKCRMCGPhsssswakeakklggpklgDKKKISWFEDEEFWKWLEELLPSLKEIYF-AGGEPL 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  61 LHPKIDQLLDLSHEKGFKVNIT----TNGTLINKRRHRLLNKpaLRQM-NFSLH-SFDGH 114
Cdd:NF033640 184 LIKEHYKLLEKLVEKGRAKNIElrynTNLTVLPDKLKDLLDL--WKKFkSVSISaSIDGV 241
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 7-287 5.39e-07

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 50.22  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283    7 FYLeiTSVCNLACSFC---PPTERQKQ---FISVEDFAKRLDQIKPHTDYIYLHVKGEPLLHPKIDQLLDLSHEKGFKVN 80
Cdd:TIGR04251   8 FYL--TEGCNLKCRHCwidPKYQGEGEqhpSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGENNLQLS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   81 ITTNGTLINKRRHRLLNKPALRQMNFSLHSFDG--HPGSQDKEGYVRSILSFIR---EATSQSDLIVS------------ 143
Cdd:TIGR04251  86 VETNGLLCTPQTARDLASCETPFVSVSLDGVDAatHDWMRGVKGAFDKAVRGIHnlvEAGIHPQIIMTvtrrnvgqmeqi 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  144 LRL----------WNLTQDNKTNAEIQKNRDLLSiIENEFGLSYQIEEKLTPGKGIKIaervFINQDYEFQWPA-LHEEE 212
Cdd:TIGR04251 166 VRLaeslgaesvkFNHVQPTSRGSKMHENGETLS-IGELVALGEWMERTLIPSTALRI----DFGHPPAFRPLGrMFGEK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446636283  213 DDGKGFChGLRNQAGILANGTVIPCCLdGEGIINL--GNINNDSFSNIIEGERATN-IVDGFSKRvaVEELCRKCGYR 287
Cdd:TIGR04251 241 PGGCGLC-GIFGILGVLSDGSYALCGI-GESIPELvfGNAGSDRLDSVWSENPVLNeIRNGMPGR--LEGVCGECLMK 314
spiroSPASM TIGR04321
spiro-SPASM protein; This three-domain protein is restricted to the spirochetes and widely ...
 7-85 2.46e-06

spiro-SPASM protein; This three-domain protein is restricted to the spirochetes and widely distributed (excepting Borrelia). It has a conserved C-terminal SPASM domain, a 4Fe-4S binding domain shared by a number of peptide-modifying and heme-modifying radical SAM proteins. It has a central radical SAM domain, although half the members have lost the signature 4Fe-4S-binding Cys residues, fail to register with the radical SAM domain definition of pfam04055, and must be considered pseudo-SAM proteins. PSI-BLAST shows a relationship between the N-terminal domain and various predicted glycosyltransferases (e.g. Bacillus subtilis SpsF) and cytidyltransferases. In some Treponema species, this protein appears to split into two tandem genes.


Pssm-ID: 275125 [Multi-domain]  Cd Length: 508  Bit Score: 48.47  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283    7 FYLEITSVCNLACSFCP-----PTERQKQFISVEDFAKRLDQIKPHTD--YIYLHVKGEPLLHPKIDQLLD-LSHEKGFK 78
Cdd:TIGR04321 233 YEIQIYRGCPLACSYCPypkfpDASTEKKFMDPEVFKSLLDKIAEFSEdaVISLSGWGEPLLHPDFAEIVEeVLSYPNLS 312


                  ....*..
gi 446636283   79 VNITTNG 85
Cdd:TIGR04321 313 LLIETSG 319
 
Name Accession Description Interval E-value
SPASM_rSAM cd21122
Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; ...
 217-287 2.47e-39

Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410613 [Multi-domain]  Cd Length: 71  Bit Score: 132.35  E-value: 2.47e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446636283 217 GFCHGLRNQAGILANGTVIPCCLDGEGIINLGNINNDSFSNIIEGERATNIVDGFSKRVAVEELCRKCGYR 287
Cdd:cd21122    1 GYCYGLRTQIGILSNGTVVPCCLDADGVINLGNIKEQSLKEILSSPRAKAIIEGFKKGEAIEELCQRCGYR 71
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 8-112 1.96e-28

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 106.91  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   8 YLEITSVCNLACSFCP--PTERQKQFISVEDFAKRLDQIKPH-TDYIYLHVkGEPLLHPKIDQLLDLSHEKGFKVNITTN 84
Cdd:COG0535    3 QIELTNRCNLRCKHCYadAGPKRPGELSTEEAKRILDELAELgVKVVGLTG-GEPLLRPDLFELVEYAKELGIRVNLSTN 81

                         90       100
                 ....*....|....*....|....*...
gi 446636283  85 GTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:COG0535   82 GTLLTEELAERLAEAGLDHVTISLDGVD 109
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 5-287 1.14e-15

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 76.18  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   5 KKFYLEITSVCNLACSFC---PPTERQKQFISVEDFAKRLDQIKPHT-DYIYLHVK---GEPLLHPK-IDQLLDL----- 71
Cdd:COG0641    1 KALVLKPTSRCNLRCSYCyysEGDEGSRRRMSEETAEKAIDFLIESSgPGKELTITffgGEPLLNFDfIKEIVEYarkya 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  72 SHEKGFKVNITTNGTLINKRRHRLLNKpalRQMNFSLhSFDGHPGSQDK-------EGYVRSILSFIREATsQSDLIVSL 144
Cdd:COG0641   81 KKGKKIRFSIQTNGTLLDDEWIDFLKE---NGFSVGI-SLDGPKEIHDRnrvtkngKGSFDRVMRNIKLLK-EHGVEVNI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283 145 RLwNLTQDNKTNAEiqknRDLLSIIENEF--------------GLSYQIEEKltpGKGIKIAERVFINQD------YEFQ 204
Cdd:COG0641  156 RC-TVTRENLDDPE----ELYDFLKELGFrsiqfnpvveegeaDYSLTPEDY---GEFLIELFDEWLERDggkifvREFD 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283 205 WpALHEEEDDGKGFCHG-LRNQAGILANGTVIPC-CLDGEGIINLGNINNDSFSNIIEGERATNIVDgfSKRVAVEELCR 282
Cdd:COG0641  228 I-LLAGLLPPCSSPCVGaGGNYLVVDPDGDIYPCdEFVGDPEFRLGNVFDGSLAELLDSPKLRAFGR--EKNVLLDEECR 304


                 ....*
gi 446636283 283 KCGYR 287
Cdd:COG0641  305 SCPYL 309
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 219-285 1.10e-11

Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur cluster binding domain in many radical SAM domain, pfam04055 proteins. The domain occurs in a number of proteins that modify a protein to become an active enzyme, or a peptide to become a ribosomal natural product. The domain is named SPASM because it occurs in the maturases of Subilitosin, PQQ, Anaerobic Sulfatases, and Mycofactocin.


Pssm-ID: 433020 [Multi-domain]  Cd Length: 66  Bit Score: 59.03  E-value: 1.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446636283  219 CHGLRNQAGILANGTVIPCCLDG-EGIINLGNINNDSFSNIIEGERATNIvdGFSKRVAVEELCRKCG 285
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCFDDDfVGPIVLGNIREQSLAEIWNSPKYREF--RKLGKFALIELCRDCP 66
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 9-112 3.29e-11

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 61.58  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   9 LEITSVCNLACSFCP----PTERQKQFISVEDFAKRLDQIKPHTDYIYLHVKGEPLLHPKIDQLLDLSHE--KGFKVNIT 82
Cdd:cd01335    1 LELTRGCNLNCGFCSnpasKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKelPGFEISIE 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 446636283  83 TNGTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:cd01335   81 TNGTLLTEELLKELKELGLDGVGVSLDSGD 110
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 15-87 2.80e-10

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 58.61  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  15 CNLACSFC--PPT--ERQKQFISVEDFAKRLDQIKPHtdyiylHVK---GEPLLHPKIDQLLDLSHEKGFKVNITTNGTL 87
Cdd:COG0602   30 CNLRCSWCdtKYAwdGEGGKRMSAEEILEEVAALGAR------HVVitgGEPLLQDDLAELLEALKDAGYEVALETNGTL 103
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
 218-284 2.93e-10

Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named SPASM after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. SPASM occurs as an additional C-terminal domain in many peptide-modifying enzymes of the radical S-adenosylmethionine (SAM) superfamily. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster.


Pssm-ID: 410609 [Multi-domain]  Cd Length: 65  Bit Score: 55.12  E-value: 2.93e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446636283 218 FCHGLRNQAGILANGTVIPCCLDGEGIINLGNINNDSFSNIIEGERATNIVDGFSKRvaVEELCRKC 284
Cdd:cd21109    1 PCPAPWTSLYITPDGDVYPCCFDVNEELKLGNIREQSLKEIWNSEKYREFRKLLLDG--KIKLCKNC 65
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 11-112 9.97e-10

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 56.38  E-value: 9.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   11 ITSVCNLACSFCP----PTERQKQFISVEDFAKRLDQIKPH-TDYIYLHVkGEPLLHPKIDQLLDLSHEK----GFKVNI 81
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLgVEVVILGG-GEPLLLPDLVELLERLLKLelaeGIRITL 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 446636283   82 TTNGTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAGLDRVSIGLESGD 110
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 2-114 2.02e-09

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 57.66  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   2 KKFKKFYLEIT--SVCNLACSFCPP-------------------TERQKQFISVEDFAKRLDQIKPHTDYIYLhVKGEPL 60
Cdd:NF033640 105 DDVNPRYLDLRfgNLCNLKCRMCGPhsssswakeakklggpklgDKKKISWFEDEEFWKWLEELLPSLKEIYF-AGGEPL 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  61 LHPKIDQLLDLSHEKGFKVNIT----TNGTLINKRRHRLLNKpaLRQM-NFSLH-SFDGH 114
Cdd:NF033640 184 LIKEHYKLLEKLVEKGRAKNIElrynTNLTVLPDKLKDLLDL--WKKFkSVSISaSIDGV 241
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 14-97 2.47e-07

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 50.58  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  14 VCNLACSFC------PPTERQKQFISVED-------FAKRLDQIKPHTDYIYLHVKGEPLLHPKIDQLLDLSHEK-GFKV 79
Cdd:COG0731   33 TCNFDCVYCqrgrttDLTRERREFDDPEEileelieFLRKLPEEAREPDHITFSGSGEPTLYPNLGELIEEIKKLrGIKT 112

                         90       100
                 ....*....|....*....|
gi 446636283  80 NITTNGTLINKR--RHRLLN 97
Cdd:COG0731  113 ALLTNGSLLHRPevREELLK 132
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 11-112 3.88e-07

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 50.44  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  11 ITSVCNLACSFCPPTE-----RQKQFISVEDFAkRLDQIkphtdYIYLHVK------GEPLLHPKIDQLL-DLSHEKGFK 78
Cdd:COG2896   20 VTDRCNFRCTYCMPEEgyqflPKEELLSFEEIE-RLVRA-----FVELGVRkirltgGEPLLRKDLPELIaRLAALPGIE 93

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446636283  79 -VNITTNGTLINKRRHRLlnKPA-LRQMNFSLHSFD 112
Cdd:COG2896   94 dLALTTNGSLLARYAEAL--KAAgLDRVNVSLDSLD 127
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 7-287 5.39e-07

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 50.22  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283    7 FYLeiTSVCNLACSFC---PPTERQKQ---FISVEDFAKRLDQIKPHTDYIYLHVKGEPLLHPKIDQLLDLSHEKGFKVN 80
Cdd:TIGR04251   8 FYL--TEGCNLKCRHCwidPKYQGEGEqhpSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGENNLQLS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283   81 ITTNGTLINKRRHRLLNKPALRQMNFSLHSFDG--HPGSQDKEGYVRSILSFIR---EATSQSDLIVS------------ 143
Cdd:TIGR04251  86 VETNGLLCTPQTARDLASCETPFVSVSLDGVDAatHDWMRGVKGAFDKAVRGIHnlvEAGIHPQIIMTvtrrnvgqmeqi 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  144 LRL----------WNLTQDNKTNAEIQKNRDLLSiIENEFGLSYQIEEKLTPGKGIKIaervFINQDYEFQWPA-LHEEE 212
Cdd:TIGR04251 166 VRLaeslgaesvkFNHVQPTSRGSKMHENGETLS-IGELVALGEWMERTLIPSTALRI----DFGHPPAFRPLGrMFGEK 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446636283  213 DDGKGFChGLRNQAGILANGTVIPCCLdGEGIINL--GNINNDSFSNIIEGERATN-IVDGFSKRvaVEELCRKCGYR 287
Cdd:TIGR04251 241 PGGCGLC-GIFGILGVLSDGSYALCGI-GESIPELvfGNAGSDRLDSVWSENPVLNeIRNGMPGR--LEGVCGECLMK 314
spiroSPASM TIGR04321
spiro-SPASM protein; This three-domain protein is restricted to the spirochetes and widely ...
 7-85 2.46e-06

spiro-SPASM protein; This three-domain protein is restricted to the spirochetes and widely distributed (excepting Borrelia). It has a conserved C-terminal SPASM domain, a 4Fe-4S binding domain shared by a number of peptide-modifying and heme-modifying radical SAM proteins. It has a central radical SAM domain, although half the members have lost the signature 4Fe-4S-binding Cys residues, fail to register with the radical SAM domain definition of pfam04055, and must be considered pseudo-SAM proteins. PSI-BLAST shows a relationship between the N-terminal domain and various predicted glycosyltransferases (e.g. Bacillus subtilis SpsF) and cytidyltransferases. In some Treponema species, this protein appears to split into two tandem genes.


Pssm-ID: 275125 [Multi-domain]  Cd Length: 508  Bit Score: 48.47  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283    7 FYLEITSVCNLACSFCP-----PTERQKQFISVEDFAKRLDQIKPHTD--YIYLHVKGEPLLHPKIDQLLD-LSHEKGFK 78
Cdd:TIGR04321 233 YEIQIYRGCPLACSYCPypkfpDASTEKKFMDPEVFKSLLDKIAEFSEdaVISLSGWGEPLLHPDFAEIVEeVLSYPNLS 312


                  ....*..
gi 446636283   79 VNITTNG 85
Cdd:TIGR04321 313 LLIETSG 319
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 11-96 8.00e-06

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 45.95  E-value: 8.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  11 ITSV----CNLACSFC-------PPTERQKQFISVEDFAKRLDQIKPHTD--------YiylhvkGEPLLHPK--IDqLL 69
Cdd:COG1180   23 RLSVftqgCNLRCPYChnpeisqGRPDAAGRELSPEELVEEALKDRGFLDscggvtfsG------GEPTLQPEflLD-LA 95

                         90       100
                 ....*....|....*....|....*..
gi 446636283  70 DLSHEKGFKVNITTNGTLINKRRHRLL 96
Cdd:COG1180   96 KLAKELGLHTALDTNGYIPEEALEELL 122
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
 11-112 1.41e-05

Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only];


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 45.67  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  11 ITSVCNLACSFCPPTE------RQKQFISVEDF----AKRLDQIKphTDYIYLHV--KGEPLLHPKIDQLLD-LSHEKGF 77
Cdd:COG2100   42 PTTGCNLNCIFCSVDAgphsrtRQAEYIVDPEYlvewFEKVARFK--GKGVEAHIdgVGEPLLYPYIVELVKgLKEIKGV 119

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446636283  78 K-VNITTNGTLINKRRHRLLNKPALRQMNFSLHSFD 112
Cdd:COG2100  120 KvVSMQTNGTLLSEKLIDELEEAGLDRINLSIDTLD 155
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
 15-92 2.22e-05

Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only];


Pssm-ID: 444038  Cd Length: 261  Bit Score: 44.98  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446636283  15 CNLACSFC------PPTERQKQFISVEDFAKRLDQIKPHTDYIYLHVKG-EPLLHPK-IDQLLDLSHEKGFKVNITTNGT 86
Cdd:COG5014   50 CNLRCGFCwswrfrDFPLTIGKFYSPEEVAERLIEIARERGYRQVRLSGgEPTIGFEhLLKVLELFSERGLTFILETNGI 129


                 ....*.
gi 446636283  87 LINKRR 92
Cdd:COG5014  130 LIGYDR 135
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 12-86 2.96e-05

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 43.89  E-value: 2.96e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446636283   12 TSVCNLACSFC----PPTERQKQFISVEDFAKRLDQIKPHTDYIYLhVKGEPLLHPKIDQLLDLSHEKGFKVNITTNGT 86
Cdd:TIGR02495  23 LQGCNLKCPYChnplLIPRRGSGEIEVEELLEFLRRRRGLLDGVVI-TGGEPTLQAGLPDFLREVRELGFEVKLDTNGS 100
SPASM_rSAM cd21126
Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; ...
 219-285 6.77e-04

Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410617 [Multi-domain]  Cd Length: 70  Bit Score: 37.45  E-value: 6.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446636283 219 CHGLRNQAGILANGTVIPCCLDGEGIINLGNINNDSFSNIIEGERATNIVDGFSKRVAVEELCRKCG 285
Cdd:cd21126    3 CWRMWHSCVITWDGKVVPCCFDKDASHKLGDLKTQSFKELWCGKKYQQFRKQLLKSRSEIEICKNCT 69
SPASM_rSAM cd21127
Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; ...
 228-285 7.23e-03

Iron-sulfur cluster-binding SPASM domain of an uncharacterized group of radical SAM proteins; Members of this group are radical S-adenosylmethionine (SAM) enzymes with a SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSME, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. Radical SAM enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. This group appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410618 [Multi-domain]  Cd Length: 83  Bit Score: 35.13  E-value: 7.23e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446636283 228 ILANGTVIPCCLDGEGIINLGNINNDSFSNIIEGERATNI-VDGFSKRVAVEELCRKCG 285
Cdd:cd21127   12 INSDGTVSPCFLDWQRKLIIGDVNKESLKEIWNSDKLNELrILHLKGKRKSNPVCSNCG 70
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH