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Conserved domains on  [gi|15607833|ref|NP_215207|]
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mycofactocin radical SAM maturase MftC [Mycobacterium tuberculosis H37Rv]

Protein Classification

radical SAM/SPASM domain-containing protein( domain architecture ID 11499256)

radical SAM (S-adenosylmethionine) protein containing additional 4Fe4S-binding SPASM domain, similar to coenzyme PQQ synthesis protein E (PqqE) and anaerobic sulfatase-maturating enzyme (anSME)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
mycofact_rSAM TIGR03962
mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM ...
9-349 0e+00

mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM proteins from the Mycobacterium tuberculosis and many other Actinobacteria, as well as some deltaproteobacteria (e.g. Geobacter uraniireducens), firmicutes (Pelotomaculum thermopropionicum and Desulfotomaculum acetoxidans), and Chloroflexi (Thermomicrobium roseum DSM 5159 and Sphaerobacter thermophilus DSM 20745). They resemble several characterized radical SAM enzymes of peptide modification (PqqE, AlbA), and are always found next to the proposed target, TIGR03969, the putative mycofactocin precursor. [Unknown function, Enzymes of unknown specificity]


:

Pssm-ID: 188477 [Multi-domain]  Cd Length: 339  Bit Score: 701.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833     9 IEQFERGLDAPICLTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDY 88
Cdd:TIGR03962   1 VEQFRRGLDAPICLTWELTYACNLACVHCLSSSGKRDPRELTTAECKRLIDELAAMQVFYVNIGGGEPTVRPDFWELMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    89 ATAHHVGVKFSTNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITR 168
Cdd:TIGR03962  81 ATAHGVGVKFSTNGVRIDPEVADRLAATDYVDVQISLDGATAEVNDAVRGAGSFDLARRAMDNLAAAGFRGFKISVVLTR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   169 RNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQQVQLYDWLVSKGERVLTGDSFFHLAPLGQsgALAGL 248
Cdd:TIGR03962 161 RNFGQLDEFYALADRYGAQLRLTRLRPSGRGADVWDELHPTAAQQRQLYDWLVAHGERVLTGDSFFHLAALGQ--PLPGL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   249 NMCGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDGGFQNVWKNSSLFRELREPQSAGACGSCGHYDSCRGGCMAAKF 328
Cdd:TIGR03962 239 NMCGAGRVVCLIDPVGDVYACPFVIHEEFLAGNVREDGGFAGVWRTSPLFRRLREPQSGGACQSCSAYDSCRGGCMAAKF 318
                         330       340
                  ....*....|....*....|.
gi 15607833   329 FTGLPLDGPDPECVQGHSEPA 349
Cdd:TIGR03962 319 FTGLPLDGPDPECVFGHGTGA 339
 
Name Accession Description Interval E-value
mycofact_rSAM TIGR03962
mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM ...
9-349 0e+00

mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM proteins from the Mycobacterium tuberculosis and many other Actinobacteria, as well as some deltaproteobacteria (e.g. Geobacter uraniireducens), firmicutes (Pelotomaculum thermopropionicum and Desulfotomaculum acetoxidans), and Chloroflexi (Thermomicrobium roseum DSM 5159 and Sphaerobacter thermophilus DSM 20745). They resemble several characterized radical SAM enzymes of peptide modification (PqqE, AlbA), and are always found next to the proposed target, TIGR03969, the putative mycofactocin precursor. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188477 [Multi-domain]  Cd Length: 339  Bit Score: 701.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833     9 IEQFERGLDAPICLTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDY 88
Cdd:TIGR03962   1 VEQFRRGLDAPICLTWELTYACNLACVHCLSSSGKRDPRELTTAECKRLIDELAAMQVFYVNIGGGEPTVRPDFWELMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    89 ATAHHVGVKFSTNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITR 168
Cdd:TIGR03962  81 ATAHGVGVKFSTNGVRIDPEVADRLAATDYVDVQISLDGATAEVNDAVRGAGSFDLARRAMDNLAAAGFRGFKISVVLTR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   169 RNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQQVQLYDWLVSKGERVLTGDSFFHLAPLGQsgALAGL 248
Cdd:TIGR03962 161 RNFGQLDEFYALADRYGAQLRLTRLRPSGRGADVWDELHPTAAQQRQLYDWLVAHGERVLTGDSFFHLAALGQ--PLPGL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   249 NMCGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDGGFQNVWKNSSLFRELREPQSAGACGSCGHYDSCRGGCMAAKF 328
Cdd:TIGR03962 239 NMCGAGRVVCLIDPVGDVYACPFVIHEEFLAGNVREDGGFAGVWRTSPLFRRLREPQSGGACQSCSAYDSCRGGCMAAKF 318
                         330       340
                  ....*....|....*....|.
gi 15607833   329 FTGLPLDGPDPECVQGHSEPA 349
Cdd:TIGR03962 319 FTGLPLDGPDPECVFGHGTGA 339
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
22-165 4.45e-57

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: 183.95  E-value: 4.45e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  22 LTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFSTN 101
Cdd:COG0535   2 LQIELTNRCNLRCKHCYADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIRVNLSTN 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607833 102 GVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRG-TGSFDMAVRALQNLAAAGFaGVKISVV 165
Cdd:COG0535  82 GTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRGvPGAFDKVLEAIKLLKEAGI-PVGINTV 145
SPASM_MftC-like cd21123
Iron-sulfur cluster-binding SPASM domain of mycofactocin radical SAM maturase MftC and similar ...
249-342 8.38e-29

Iron-sulfur cluster-binding SPASM domain of mycofactocin radical SAM maturase MftC and similar proteins; This group is composed of Mycobacterium tuberculosis putative mycofactocin radical SAM maturase MftC and similar proteins. MftC is a radical S-adenosylmethionine (SAM) enzyme that may function to modify mycofactocin, a conserved polypeptide that might serve as an electron carrier. 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 that is similar to the second auxillary 4Fe-4S cluster (AuxII) of Clostridium perfringens anaerobic sulfatase-maturating enzyme (anSME).


Pssm-ID: 410614 [Multi-domain]  Cd Length: 91  Bit Score: 107.73  E-value: 8.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 249 NMCGAGRVVCLIDPVGDVYACPFaihDHFLAGNVLSDgGFQNVWKNSSLFRELREPQSA-GACGSCGHYDSCrGGCMAAK 327
Cdd:cd21123   2 GGCGAGRGIAFISPDGDVYPCGF---LPFSAGNVRED-SFKDIWENSELFKKLRDREFLkGKCGKCKYRNVC-GGCRARA 76
                        90
                ....*....|....*
gi 15607833 328 FFTGLPLDGPDPECV 342
Cdd:cd21123  77 YAYTGDPLGEDPGCI 91
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
26-177 2.75e-25

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: 100.29  E-value: 2.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    26 LTYACNLACVHCL--SSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVG----VKFS 99
Cdd:pfam04055   1 ITRGCNLRCTYCAfpSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegirITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607833   100 TNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKI-SVVITRRNVAQLDEF 177
Cdd:pfam04055  81 TNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDnIVGLPGETDEDLEET 159
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
13-177 3.71e-11

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: 64.21  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   13 ERGLDAPICLTWELTY--ACNLACVHC---LSSS-----------GKRDPGELSTRQCKDIIDELE----RMQVFYVNig 72
Cdd:NF033640 101 EDGSDDVNPRYLDLRFgnLCNLKCRMCgphSSSSwakeakklggpKLGDKKKISWFEDEEFWKWLEellpSLKEIYFA-- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   73 GGEPTVRPDFWELVDYAT----AHHVGVKFSTNGVRITPEVATRLaatDY------VDVQISLDGaTAEVNDAIRgTGS- 141
Cdd:NF033640 179 GGEPLLIKEHYKLLEKLVekgrAKNIELRYNTNLTVLPDKLKDLL---DLwkkfksVSISASIDG-VGERNEYIR-YGSk 253
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15607833  142 ---FDMAVRALQNLAAAgfAGVKISVVITRRNVAQLDEF 177
Cdd:NF033640 254 wdeIEKNLKKLKEECPN--VELRINPTVSALNVLHLPEL 290
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-212 1.12e-10

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 62.08  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    1 MTSPVPRLIEQFERgldapicltwELTY-------ACNLACVHCLSS---SGKRDPGELStrqckdiIDELERM-QVFyV 69
Cdd:PRK00164   1 PVPMTSQLIDRFGR----------KFTYlrisvtdRCNFRCTYCMPEgylPFLPKEELLS-------LEEIERLvRAF-V 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   70 NIG-------GGEPTVRPDFWELVDyATAHHVGVK---FSTNGVRItPEVATRLAATDYVDVQISLDGATAEVNDAIRGT 139
Cdd:PRK00164  63 ALGvrkvrltGGEPLLRKDLEDIIA-ALAALPGIRdlaLTTNGYLL-ARRAAALKDAGLDRVNVSLDSLDPERFKAITGR 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607833  140 GSFDMAVRALQNLAAAGFAGVKI-SVVITRRNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQ 212
Cdd:PRK00164 141 DRLDQVLAGIDAALAAGLTPVKVnAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAE 214
 
Name Accession Description Interval E-value
mycofact_rSAM TIGR03962
mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM ...
9-349 0e+00

mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM proteins from the Mycobacterium tuberculosis and many other Actinobacteria, as well as some deltaproteobacteria (e.g. Geobacter uraniireducens), firmicutes (Pelotomaculum thermopropionicum and Desulfotomaculum acetoxidans), and Chloroflexi (Thermomicrobium roseum DSM 5159 and Sphaerobacter thermophilus DSM 20745). They resemble several characterized radical SAM enzymes of peptide modification (PqqE, AlbA), and are always found next to the proposed target, TIGR03969, the putative mycofactocin precursor. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188477 [Multi-domain]  Cd Length: 339  Bit Score: 701.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833     9 IEQFERGLDAPICLTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDY 88
Cdd:TIGR03962   1 VEQFRRGLDAPICLTWELTYACNLACVHCLSSSGKRDPRELTTAECKRLIDELAAMQVFYVNIGGGEPTVRPDFWELMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    89 ATAHHVGVKFSTNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITR 168
Cdd:TIGR03962  81 ATAHGVGVKFSTNGVRIDPEVADRLAATDYVDVQISLDGATAEVNDAVRGAGSFDLARRAMDNLAAAGFRGFKISVVLTR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   169 RNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQQVQLYDWLVSKGERVLTGDSFFHLAPLGQsgALAGL 248
Cdd:TIGR03962 161 RNFGQLDEFYALADRYGAQLRLTRLRPSGRGADVWDELHPTAAQQRQLYDWLVAHGERVLTGDSFFHLAALGQ--PLPGL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   249 NMCGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDGGFQNVWKNSSLFRELREPQSAGACGSCGHYDSCRGGCMAAKF 328
Cdd:TIGR03962 239 NMCGAGRVVCLIDPVGDVYACPFVIHEEFLAGNVREDGGFAGVWRTSPLFRRLREPQSGGACQSCSAYDSCRGGCMAAKF 318
                         330       340
                  ....*....|....*....|.
gi 15607833   329 FTGLPLDGPDPECVQGHSEPA 349
Cdd:TIGR03962 319 FTGLPLDGPDPECVFGHGTGA 339
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
22-165 4.45e-57

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: 183.95  E-value: 4.45e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  22 LTWELTYACNLACVHCLSSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFSTN 101
Cdd:COG0535   2 LQIELTNRCNLRCKHCYADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIRVNLSTN 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15607833 102 GVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRG-TGSFDMAVRALQNLAAAGFaGVKISVV 165
Cdd:COG0535  82 GTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRGvPGAFDKVLEAIKLLKEAGI-PVGINTV 145
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
22-341 6.90e-42

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 150.14  E-value: 6.90e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  22 LTWELTYACNLACVHCLSSSGKRDPGE-LSTRQCKDIIDELERMQ--VFYVNIG--GGEPTVRPDF-WELVDYA---TAH 92
Cdd:COG0641   3 LVLKPTSRCNLRCSYCYYSEGDEGSRRrMSEETAEKAIDFLIESSgpGKELTITffGGEPLLNFDFiKEIVEYArkyAKK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  93 HVGVKFS--TNGVRITPEVATRLAATDyVDVQISLDGaTAEVNDAIR----GTGSFDMAVRALQNLAAAGFAgVKISVVI 166
Cdd:COG0641  83 GKKIRFSiqTNGTLLDDEWIDFLKENG-FSVGISLDG-PKEIHDRNRvtknGKGSFDRVMRNIKLLKEHGVE-VNIRCTV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 167 TRRNVAQLDEFATLASRYGAT-LRITRLRPSGrgtdvWADLHPTADQQVQLYD-----WLVSKGERVltgdSFFHLAPLG 240
Cdd:COG0641 160 TRENLDDPEELYDFLKELGFRsIQFNPVVEEG-----EADYSLTPEDYGEFLIelfdeWLERDGGKI----FVREFDILL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 241 QSGALAGLNMC-GAGRVVCLIDPVGDVYACP-FAIHDHFLAGNVLsDGGFQNVWKNSSL--FRELREPQSAGACGSCGHY 316
Cdd:COG0641 231 AGLLPPCSSPCvGAGGNYLVVDPDGDIYPCDeFVGDPEFRLGNVF-DGSLAELLDSPKLraFGREKNVLLDEECRSCPYL 309
                       330       340
                ....*....|....*....|....*.
gi 15607833 317 DSCRGGCMAAKF-FTGLPLDGPDPEC 341
Cdd:COG0641 310 PLCGGGCPANRYaETGDGFKPYSYYC 335
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
26-343 2.00e-31

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: 122.25  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    26 LTYACNLACVHC-----LSSSGKRDPGeLSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFST 100
Cdd:TIGR04251  10 LTEGCNLKCRHCwidpkYQGEGEQHPS-LDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGENNLQLSVET 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   101 NGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGT-GSFDMAVRALQNLAAAGFAGvKISVVITRRNVAQLDEFAT 179
Cdd:TIGR04251  89 NGLLCTPQTARDLASCETPFVSVSLDGVDAATHDWMRGVkGAFDKAVRGIHNLVEAGIHP-QIIMTVTRRNVGQMEQIVR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   180 LASRYGA-TLRITRLRPSGRGTdvwaDLHPTAD-----QQVQLYDWLvskgERVLTGDS-----FFH---LAPLGQSGAL 245
Cdd:TIGR04251 168 LAESLGAeSVKFNHVQPTSRGS----KMHENGEtlsigELVALGEWM----ERTLIPSTalridFGHppaFRPLGRMFGE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   246 AGlNMCGAGRVVCLIDPVGDVYACPFAIHDH---FLAGNVLSDgGFQNVWKNSSLFRELREP---QSAGACGSCGHYDSC 319
Cdd:TIGR04251 240 KP-GGCGLCGIFGILGVLSDGSYALCGIGESipeLVFGNAGSD-RLDSVWSENPVLNEIRNGmpgRLEGVCGECLMKEKC 317
                         330       340
                  ....*....|....*....|....
gi 15607833   320 RGGCMAAKFFTGLPLDGPDPECVQ 343
Cdd:TIGR04251 318 LGSCIAQNYYAKRHLWSPFWYCEE 341
SPASM_MftC-like cd21123
Iron-sulfur cluster-binding SPASM domain of mycofactocin radical SAM maturase MftC and similar ...
249-342 8.38e-29

Iron-sulfur cluster-binding SPASM domain of mycofactocin radical SAM maturase MftC and similar proteins; This group is composed of Mycobacterium tuberculosis putative mycofactocin radical SAM maturase MftC and similar proteins. MftC is a radical S-adenosylmethionine (SAM) enzyme that may function to modify mycofactocin, a conserved polypeptide that might serve as an electron carrier. 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 that is similar to the second auxillary 4Fe-4S cluster (AuxII) of Clostridium perfringens anaerobic sulfatase-maturating enzyme (anSME).


Pssm-ID: 410614 [Multi-domain]  Cd Length: 91  Bit Score: 107.73  E-value: 8.38e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 249 NMCGAGRVVCLIDPVGDVYACPFaihDHFLAGNVLSDgGFQNVWKNSSLFRELREPQSA-GACGSCGHYDSCrGGCMAAK 327
Cdd:cd21123   2 GGCGAGRGIAFISPDGDVYPCGF---LPFSAGNVRED-SFKDIWENSELFKKLRDREFLkGKCGKCKYRNVC-GGCRARA 76
                        90
                ....*....|....*
gi 15607833 328 FFTGLPLDGPDPECV 342
Cdd:cd21123  77 YAYTGDPLGEDPGCI 91
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
26-177 2.75e-25

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: 100.29  E-value: 2.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    26 LTYACNLACVHCL--SSSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVG----VKFS 99
Cdd:pfam04055   1 ITRGCNLRCTYCAfpSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegirITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15607833   100 TNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKI-SVVITRRNVAQLDEF 177
Cdd:pfam04055  81 TNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDnIVGLPGETDEDLEET 159
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
25-180 1.31e-22

SynChlorMet cassette radical SAM/SPASM protein ScmE; 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 closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 97.62  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    25 ELTYACNLACVHCLS-SSGKRDPGELSTRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYATAHHVGVKFSTNGV 103
Cdd:TIGR04250   8 DITGRCNLRCRYCSHfSSAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVKNRMRFSILSNGT 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15607833   104 RITPEVATRLAATDYVD-VQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAgVKISVVITRRNVAQLDEFATL 180
Cdd:TIGR04250  88 LITDAIASFLAATRRCDyVQVSIDGSTPGTHDRLRGTGSFLQAVEGIELLRKHAIP-VVVRVTIHRWNVDDLRPIAAL 164
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
24-218 2.87e-18

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: 82.38  E-value: 2.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  24 WELTYACNLACVHCLSSSGKRDPGELS--TRQCKDIIDELERMQVFYVNIGGGEPTVRPDFWELVDYA--TAHHVGVKFS 99
Cdd:cd01335   1 LELTRGCNLNCGFCSNPASKGRGPESPpeIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLkkELPGFEISIE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 100 TNGVRITPEVATRLAATDYVDVQISLDGATAEVNDAIRG-TGSFDMAVRALQNLAAAGFaGVKISVVITRRNVAQLDEFA 178
Cdd:cd01335  81 TNGTLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGsGESFKERLEALKELREAGL-GLSTTLLVGLGDEDEEDDLE 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15607833 179 TLA----SRYGATLRITRLRPSGRGTDVWADLHPTADQQVQLYD 218
Cdd:cd01335 160 ELEllaeFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIA 203
rSAM_more_4Fe4S TIGR04085
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ...
251-341 2.86e-17

radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding additional 4Fe4S clusters found in various radical SAM proteins C-terminal to the domain described by model pfam04055. Radical SAM enzymes with this domain tend to be involved in protein modification, including anaerobic sulfatase maturation proteins, a quinohemoprotein amine dehydrogenase biogenesis protein, the Pep1357-cyclizing radical SAM enzyme, and various bacteriocin biosynthesis proteins. The motif CxxCxxxxxCxxxC is nearly invariant for members of this family, although PqqE has a variant form. We name this domain SPASM for Subtilosin, PQQ, Anaerobic Sulfatase, and Mycofactocin.


Pssm-ID: 274968 [Multi-domain]  Cd Length: 93  Bit Score: 76.46  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   251 CGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLsDGGFQNVWKNSSL--FRELREPQSAGACGSCGHYDSCRGGCMA-AK 327
Cdd:TIGR04085   1 CGAGRNSLVVDPDGDVYPCDHFVYPEYKLGNIR-EDSLEEILNSSKQleFGRWKSPKLPEECRSCKYLPLCGGGCPAnRY 79
                          90
                  ....*....|....
gi 15607833   328 FFTGLPLDGPDPEC 341
Cdd:TIGR04085  80 LKTGDINGPKNPLC 93
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
26-189 1.44e-13

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: 70.86  E-value: 1.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  26 LTYACNLACVHCLSSSG---KRDPGELStrqckdiIDELER-MQVFyVNIG-------GGEPTVRPDFWELVDyATAHHV 94
Cdd:COG2896  20 VTDRCNFRCTYCMPEEGyqfLPKEELLS-------FEEIERlVRAF-VELGvrkirltGGEPLLRKDLPELIA-RLAALP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  95 GVK---FSTNGVRItPEVATRLAATDyVD-VQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITR-R 169
Cdd:COG2896  91 GIEdlaLTTNGSLL-ARYAEALKAAG-LDrVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVVMRgV 168
                       170       180
                ....*....|....*....|
gi 15607833 170 NVAQLDEFATLASRYGATLR 189
Cdd:COG2896 169 NDDEILDLLEFAKERGIDLR 188
rSAM_pep_methan TIGR04083
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ...
27-342 5.89e-13

putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are radical SAM enzymes, homologous to a variety of other peptide-modifying radical SAM, and found primarily in methanogenic archaea.


Pssm-ID: 274966 [Multi-domain]  Cd Length: 376  Bit Score: 69.37  E-value: 5.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    27 TYACNLACVHCLSSSGKRDPGELSTrqCKDIIDELERMQVFYVNIG--GGEPTVR-PDFW----ELVDYATAH-HVGVKF 98
Cdd:TIGR04083   7 TLGCPSKCKYCWSSEETSPVMSIDT--VKDIVEWLKDFRDDRVTFTfhGGEPLLAgADFYrqalPLLSEGLAHlKPEFAM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    99 STNGVRITPEVATRLAATDyVDVQISLDGATaEVNDAIRGTGSFDMAVRALQNLAAAGFAgVKISVVITRRNVAQLDEFA 178
Cdd:TIGR04083  85 QTNLWLMTPELAEIFAEYN-VPIGSSIDGPE-EINDYQRGEGYYQKTMKGYEIAKEHGLD-VRFICTFTSYSVKQKEEIF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   179 TLASRYGATLRITRLRPSGRGTDV--WAdLHPTADQQVqLYDWLvskgERVLTGDSFFHLAPLGQsgaLAGLNMCGAGRV 256
Cdd:TIGR04083 162 NFFLENGFTLKLHPALPSLRSDNPgeWA-LDPEEYGEL-LVYLL----DKYLENMDKIEVMNIND---LCRCVFTRRGTV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   257 VCLID---------PVGDVYAC-PFAIHDHFLAGNVLSDGGFQNV-----WKNSSLFRELREPqsagACGSCGHYDSCRG 321
Cdd:TIGR04083 233 CTFVDcmgttfavgPDGSIYPCyRFVGMPEYVMGNVRDRPTMEDLmesdaGKLMLAFKEYVDT----HCAKCSHIKYCRG 308
                         330       340
                  ....*....|....*....|....*
gi 15607833   322 GC----MAAkffTGLPLDGPDPECV 342
Cdd:TIGR04083 309 GCpynaIAP---TDGEIKGVDPHCI 330
SPASM_AlbA-like cd21125
Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis ...
251-341 1.25e-12

Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis protein AlbA and similar proteins; Bacillus subtilis antilisterial bacteriocin subtilosin biosynthesis protein AlbA is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the formation of three thioether bonds in the post-translational modification of a linear peptide into the cyclic peptide subtilosin A. The thioether bonds formed are between the sulfur of three cysteine residues and the alpha-carbons of two phenylalanines and one threonine to produce a rigid cyclic peptide. 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. AlbA appears to contain one auxillary Fe-S cluster, similar to the auxillary 4Fe-4S cluster in Bacillus circulans butirosin biosynthetic enzyme BtrN.


Pssm-ID: 410616 [Multi-domain]  Cd Length: 97  Bit Score: 63.28  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 251 CGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDGG---FQNvwKNSSLFRELREPQSAGaCGSCGHYDSCRGGCMAAK 327
Cdd:cd21125   3 CGAGWKSIVIDPDGEVYPCHLLHPTEFKLGNIFEDSLasiLKN--PVLEIWQTYDPRFSEH-CKKCPFYGICGGGCIAKS 79
                        90
                ....*....|....
gi 15607833 328 FFTGLPLDGPDPEC 341
Cdd:cd21125  80 LISYGRFDKPDPYC 93
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
13-177 3.71e-11

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: 64.21  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   13 ERGLDAPICLTWELTY--ACNLACVHC---LSSS-----------GKRDPGELSTRQCKDIIDELE----RMQVFYVNig 72
Cdd:NF033640 101 EDGSDDVNPRYLDLRFgnLCNLKCRMCgphSSSSwakeakklggpKLGDKKKISWFEDEEFWKWLEellpSLKEIYFA-- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   73 GGEPTVRPDFWELVDYAT----AHHVGVKFSTNGVRITPEVATRLaatDY------VDVQISLDGaTAEVNDAIRgTGS- 141
Cdd:NF033640 179 GGEPLLIKEHYKLLEKLVekgrAKNIELRYNTNLTVLPDKLKDLL---DLwkkfksVSISASIDG-VGERNEYIR-YGSk 253
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15607833  142 ---FDMAVRALQNLAAAgfAGVKISVVITRRNVAQLDEF 177
Cdd:NF033640 254 wdeIEKNLKKLKEECPN--VELRINPTVSALNVLHLPEL 290
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-212 1.12e-10

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 62.08  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833    1 MTSPVPRLIEQFERgldapicltwELTY-------ACNLACVHCLSS---SGKRDPGELStrqckdiIDELERM-QVFyV 69
Cdd:PRK00164   1 PVPMTSQLIDRFGR----------KFTYlrisvtdRCNFRCTYCMPEgylPFLPKEELLS-------LEEIERLvRAF-V 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   70 NIG-------GGEPTVRPDFWELVDyATAHHVGVK---FSTNGVRItPEVATRLAATDYVDVQISLDGATAEVNDAIRGT 139
Cdd:PRK00164  63 ALGvrkvrltGGEPLLRKDLEDIIA-ALAALPGIRdlaLTTNGYLL-ARRAAALKDAGLDRVNVSLDSLDPERFKAITGR 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15607833  140 GSFDMAVRALQNLAAAGFAGVKI-SVVITRRNVAQLDEFATLASRYGATLRITRLRPSGRGTDVWADLHPTADQ 212
Cdd:PRK00164 141 DRLDQVLAGIDAALAAGLTPVKVnAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAE 214
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
30-156 2.31e-09

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 57.69  E-value: 2.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  30 CNLACVHCLS---SSGKRDPGEL-STRQCKDIIDEL-ERMQVFYVNIGGGEPTVRPD-FWELVDYATAHhvGVKF--STN 101
Cdd:COG5014  50 CNLRCGFCWSwrfRDFPLTIGKFySPEEVAERLIEIaRERGYRQVRLSGGEPTIGFEhLLKVLELFSER--GLTFilETN 127
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607833 102 GVRIT--PEVATRLAATDYVDVQISLDGATAEVNDAIrgTGS----FDMAVRALQNLAAAG 156
Cdd:COG5014 128 GILIGydRELARELASFRNIVVRVSIKGCTPEEFSML--TGAdpefFELQLRALKNLVDAG 186
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
251-313 3.83e-09

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: 52.42  E-value: 3.83e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607833 251 CGAGRVVCLIDPVGDVYACPFAIHDHFLAGNVLSDgGFQNVWkNSSLFRELREPQSAG---ACGSC 313
Cdd:cd21109   2 CPAPWTSLYITPDGDVYPCCFDVNEELKLGNIREQ-SLKEIW-NSEKYREFRKLLLDGkikLCKNC 65
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
27-224 3.66e-08

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 53.65  E-value: 3.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  27 TYACNLACVHC----LSSSGKRDPGELSTrqCKDIIDELERMQVFYVNIGG-----GEPTVRPDF-WELVDYATAHHVGV 96
Cdd:COG1180  28 TQGCNLRCPYChnpeISQGRPDAAGRELS--PEELVEEALKDRGFLDSCGGvtfsgGEPTLQPEFlLDLAKLAKELGLHT 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  97 KFSTNGVrITPEVATRLAatDYVD-VQISLDGATAEVNDAIRGTGsfdmAVRALQNLAAAGFAGVKI---SVVITRRN-- 170
Cdd:COG1180 106 ALDTNGY-IPEEALEELL--PYLDaVNIDLKAFDDEFYRKLTGVS----LEPVLENLELLAESGVHVeirTLVIPGLNds 178
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15607833 171 VAQLDEFATLASRYGAT--LRITRLRPSGRgtdvWADLHPTADQQVQ-LYDWLVSKG 224
Cdd:COG1180 179 EEELEAIARFIAELGDVipVHLLPFHPLYK----LEDVPPPSPETLErAREIAREYG 231
SPASM_CteB-like cd21124
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ...
248-341 3.65e-07

Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar proteins; Clostridium thermocellum sactionine bond-forming enzyme CteB is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the formation of the requisite thioether bridge between a cysteine and the alpha-carbon of an opposing amino acid that is required in sactipeptide biosynthesis. 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 (RS) enzymes with a C-terminal SPASM domain contain at least one other iron-sulfur cluster. CteB contains two auxillary 4Fe-4S clusters in its SPASM domain; the auxillary cluster nearest the RS site, called AuxI, exhibits an open coordination site in the absence of peptide substrate, which is coordinated by a peptidyl-cysteine residue in the bound state.


Pssm-ID: 410615 [Multi-domain]  Cd Length: 96  Bit Score: 47.73  E-value: 3.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833 248 LNMCGAGRVVCLIDPVGDVYAC-PFAIHDHFLAGNVLSdgGFQNVwKNSSLFRELREPQSAGaCGSCGHYDSCRGGCMAA 326
Cdd:cd21124   1 LSGCGAGHEYFAVDPDGDIYPChRFVGMEEYRMGNVYD--GSSLM-ELQSEFWKRHVENKEE-CRECWARFYCGGGCPAN 76
                        90
                ....*....|....*.
gi 15607833 327 KF-FTGLPLDGPDPEC 341
Cdd:cd21124  77 SYaENGDIRTPYEPYC 92
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
29-132 8.45e-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: 49.80  E-value: 8.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833  29 ACNLACVHClsssgKRDPGELSTRQ------CKDIIDELERMQ---------VFYVNIGG-GEPTVRPDFWELVDYATAH 92
Cdd:COG0731  33 TCNFDCVYC-----QRGRTTDLTRErrefddPEEILEELIEFLrklpeearePDHITFSGsGEPTLYPNLGELIEEIKKL 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15607833  93 HvGVKFS--TNGVRIT-PEVATRLAATDYvdVQISLDGATAEV 132
Cdd:COG0731 108 R-GIKTAllTNGSLLHrPEVREELLKADQ--VYPSLDAADEET 147
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
26-195 8.84e-07

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 50.52  E-value: 8.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   26 LTYACNLACVHCLSSSG---KRDPGELSTrqckdiiDELERMQVFYVNIG-------GGEPTVRPDFWELVDYATA---- 91
Cdd:PLN02951  64 LTERCNLRCQYCMPEEGvelTPKSHLLSQ-------DEIVRLAGLFVAAGvdkirltGGEPTLRKDIEDICLQLSSlkgl 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607833   92 HHVGVkfSTNGVRITPEVaTRLAATDYVDVQISLDGATAEVNDAIRGTGSFDMAVRALQNLAAAGFAGVKISVVITR-RN 170
Cdd:PLN02951 137 KTLAM--TTNGITLSRKL-PRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRgFN 213
                        170       180
                 ....*....|....*....|....*
gi 15607833  171 VAQLDEFATLASRYGATLRITRLRP 195
Cdd:PLN02951 214 DDEICDFVELTRDKPINVRFIEFMP 238
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
251-315 1.43e-04

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: 39.77  E-value: 1.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15607833   251 CGAGRVVCLIDPVGDVYACPFA-IHDHFLAGNVlSDGGFQNVWkNSSLFRELREPQSAGACGSCGH 315
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCFDDdFVGPIVLGNI-REQSLAEIW-NSPKYREFRKLGKFALIELCRD 64
 
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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