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Conserved domains on  [gi|446503973|ref|WP_000581827|]
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MULTISPECIES: thioether cross-link-forming SCIFF peptide maturase [Bacillus]

Protein Classification

radical SAM/SPASM domain-containing protein( domain architecture ID 11499265)

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
rSAM_six_Cys TIGR03974
SCIFF radical SAM maturase; Members of this protein family are predicted radical SAM enzymes ...
2-453 0e+00

SCIFF radical SAM maturase; Members of this protein family are predicted radical SAM enzymes universally associated with Six Cysteines in Forty-Five protein, or SCIFF (family TIGR03973), a predicted ribosomal natural product precursor that is nearly universal in the class Clostridia. Similarity of this family to radical SAM maturases (PqqE and subtilosin A maturase) found in the vicinity of other peptide precursors suggests this protein is the SCIFF radical SAM maturase. [Cellular processes, Biosynthesis of natural products]


:

Pssm-ID: 274892 [Multi-domain]  Cd Length: 451  Bit Score: 796.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973    2 IHQYKLNGYNIVLDTYSGSVHVVDDLAYEIIMLYENTPMVEILSMMQEKYKYDFhvSEKEIRETIADIEELKRDGKLFTD 81
Cdd:TIGR03974   1 IHQYKNNGYNIVLDVNSGSVHVVDDVTYDVIALYEEGKDKETPEEIKEKLKGKY--SEEDIEEAYDEITELKEAGQLFTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973   82 DDYKDLSIDLIN-RPTYVKALCLNVAHTCNLSCEYCFASQGKYNGNRAIMSYEVGKRAIDFLLENSGNHQNLDVDFFGGE 160
Cdd:TIGR03974  79 DIYEDYIIDFKKmRKTVVKALCLHVAHDCNLACKYCFAEEGEYHGRRALMSFEVGKKALDFLIANSGSRRNLEVDFFGGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  161 PLMAWKTVKQIVAYARNKEKEYKKTFRFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIV 240
Cdd:TIGR03974 159 PLMNFDVVKDLVAYGRSIEKEHNKNFRFTLTTNGVLLNDEIIEFANKEMSNVVLSLDGRKEVNDRMRPTRNGKGSYDLIV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  241 PKFQEFVEKRGDKEYYVRGTYTHNNVDFTNDIYHIADLGFNKISMEPVICNPREPYALGEEDLLEIYNQYEILSKEMLNR 320
Cdd:TIGR03974 239 PKFQKLVESRGQKKYYVRGTFTHNNLDFSKDVLHLADLGFKQISVEPVVADPEEPYALTEEDLPIIFEEYEKLAKEMIKR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  321 EEKGSGFTFYHYMLDLSEGPCVQKRISGCGSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDGITKTEIQSQFKKSNCY 400
Cdd:TIGR03974 319 KKEGKGFNFFHFMIDLTGGPCVYKRLSGCGSGTEYLAVTPWGDLYPCHQFVGNEEFKMGNVFDGITNTDIRDEFKKCNVY 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446503973  401 SKTECQECWAQLYCSGGCPANTIHATGSLKGTHEFSCKIFRKRIECSMMVKVA 453
Cdd:TIGR03974 399 SKEKCKDCWARFYCSGGCAANSYNFTGDINDPYDLGCELQRKRIECAIMIKAA 451
 
Name Accession Description Interval E-value
rSAM_six_Cys TIGR03974
SCIFF radical SAM maturase; Members of this protein family are predicted radical SAM enzymes ...
2-453 0e+00

SCIFF radical SAM maturase; Members of this protein family are predicted radical SAM enzymes universally associated with Six Cysteines in Forty-Five protein, or SCIFF (family TIGR03973), a predicted ribosomal natural product precursor that is nearly universal in the class Clostridia. Similarity of this family to radical SAM maturases (PqqE and subtilosin A maturase) found in the vicinity of other peptide precursors suggests this protein is the SCIFF radical SAM maturase. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274892 [Multi-domain]  Cd Length: 451  Bit Score: 796.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973    2 IHQYKLNGYNIVLDTYSGSVHVVDDLAYEIIMLYENTPMVEILSMMQEKYKYDFhvSEKEIRETIADIEELKRDGKLFTD 81
Cdd:TIGR03974   1 IHQYKNNGYNIVLDVNSGSVHVVDDVTYDVIALYEEGKDKETPEEIKEKLKGKY--SEEDIEEAYDEITELKEAGQLFTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973   82 DDYKDLSIDLIN-RPTYVKALCLNVAHTCNLSCEYCFASQGKYNGNRAIMSYEVGKRAIDFLLENSGNHQNLDVDFFGGE 160
Cdd:TIGR03974  79 DIYEDYIIDFKKmRKTVVKALCLHVAHDCNLACKYCFAEEGEYHGRRALMSFEVGKKALDFLIANSGSRRNLEVDFFGGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  161 PLMAWKTVKQIVAYARNKEKEYKKTFRFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIV 240
Cdd:TIGR03974 159 PLMNFDVVKDLVAYGRSIEKEHNKNFRFTLTTNGVLLNDEIIEFANKEMSNVVLSLDGRKEVNDRMRPTRNGKGSYDLIV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  241 PKFQEFVEKRGDKEYYVRGTYTHNNVDFTNDIYHIADLGFNKISMEPVICNPREPYALGEEDLLEIYNQYEILSKEMLNR 320
Cdd:TIGR03974 239 PKFQKLVESRGQKKYYVRGTFTHNNLDFSKDVLHLADLGFKQISVEPVVADPEEPYALTEEDLPIIFEEYEKLAKEMIKR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  321 EEKGSGFTFYHYMLDLSEGPCVQKRISGCGSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDGITKTEIQSQFKKSNCY 400
Cdd:TIGR03974 319 KKEGKGFNFFHFMIDLTGGPCVYKRLSGCGSGTEYLAVTPWGDLYPCHQFVGNEEFKMGNVFDGITNTDIRDEFKKCNVY 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446503973  401 SKTECQECWAQLYCSGGCPANTIHATGSLKGTHEFSCKIFRKRIECSMMVKVA 453
Cdd:TIGR03974 399 SKEKCKDCWARFYCSGGCAANSYNFTGDINDPYDLGCELQRKRIECAIMIKAA 451
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
99-451 1.79e-121

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 358.53  E-value: 1.79e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  99 KALCLNVAHTCNLSCEYCFASQGKYNGNRaIMSYEVGKRAIDFLLENSGNHQNLDVDFFGGEPLMAWKTVKQIVAYARNK 178
Cdd:COG0641    1 KALVLKPTSRCNLRCSYCYYSEGDEGSRR-RMSEETAEKAIDFLIESSGPGKELTITFFGGEPLLNFDFIKEIVEYARKY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 179 EKeYKKTFRFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIVPKFQEFVEKrgDKEYYVR 258
Cdd:COG0641   80 AK-KGKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVMRNIKLLKEH--GVEVNIR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 259 GTYTHNNVDFTNDIY-HIADLGFNKISMEPVICNPREPYALGEEDLLEIYNQYEilsKEMLnrEEKGSGFTFYHYMLDLS 337
Cdd:COG0641  157 CTVTRENLDDPEELYdFLKELGFRSIQFNPVVEEGEADYSLTPEDYGEFLIELF---DEWL--ERDGGKIFVREFDILLA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 338 EGPcvQKRISGC-GSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDG----ITKTEIQSQF-KKSNCYSKTECQECWAQ 411
Cdd:COG0641  232 GLL--PPCSSPCvGAGGNYLVVDPDGDIYPCDEFVGDPEFRLGNVFDGslaeLLDSPKLRAFgREKNVLLDEECRSCPYL 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446503973 412 LYCSGGCPANTIHATGSLKGTHEFSCKIFRKRIECSMMVK 451
Cdd:COG0641  310 PLCGGGCPANRYAETGDGFKPYSYYCELYKKLFEHALRLE 349
SPASM_CteB-like cd21124
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ...
346-441 3.72e-33

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: 120.54  E-value: 3.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 346 ISGCGSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDGITKTEIQSQFKKSNCYSKTECQECWAQLYCSGGCPANTIHA 425
Cdd:cd21124    1 LSGCGAGHEYFAVDPDGDIYPCHRFVGMEEYRMGNVYDGSSLMELQSEFWKRHVENKEECRECWARFYCGGGCPANSYAE 80
                         90
                 ....*....|....*.
gi 446503973 426 TGSLKGTHEFSCKIFR 441
Cdd:cd21124   81 NGDIRTPYEPYCEIYK 96
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
109-421 6.42e-18

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 84.97  E-value: 6.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 109 CNLSCEYCFASQgkYNGNRAIMSYEVGKraiDFLLE-------NSGNhQNLDVDFFGGEP-LMAWKTVKQIVAYARNKEK 180
Cdd:PRK13758  15 CNLKCTYCFYHS--LSDNRNVKSYGIMR---DEVLEsmvkrvlNEAE-GHCSFAFQGGEPtLAGLEFFEELMELQRKHNY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 181 EYKKTFrFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIVPKFQEFveKRGDKEYYVRGT 260
Cdd:PRK13758  89 KNLKIY-NSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGLDTFSKVERAAELF--KKYKVEFNILCV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 261 YTHNNVDFTNDIYHI---ADLGFNKI--SMEPvICNPRE--PYALGEEDLLEIYNQ-YEILSKEMLNreekgSGFTFYHY 332
Cdd:PRK13758 166 VTSNTARHVNKIYKYfkeKDFKFLQFinCLDP-LYEEKGkyNYSLKPKDYTKFLKNlFDLWYEDFLN-----GNRVSIRY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 333 MLDLSEGPCVQKRISGCGSGT---EYLaITPWGEIFPCHQFVgEEEYSMGNIWDGITK----TEIQSQFKKSNCYSKTEC 405
Cdd:PRK13758 240 FDGLLETILLGKSSSCGMNGTctcQFV-VESDGSVYPCDFYV-LDKWRLGNIQDMTMKelfeTNKNHEFIKSSFKVHEEC 317
                        330
                 ....*....|....*..
gi 446503973 406 QEC-WAQLyCSGGCPAN 421
Cdd:PRK13758 318 KKCkWFPL-CKGGCRRC 333
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
109-241 9.72e-12

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 62.19  E-value: 9.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  109 CNLSCEYCFASQGK-YNGNRaIMSYEVGKRAIDFLLENSGNhqnlDVDFFGGEPLMAWKTVKQIVAYARnKEKEYKKTFR 187
Cdd:pfam13353  15 CNHHCKGCFNPETWdFKYGK-PFTEELEDEIIEDLAKPYIQ----GLTLSGGEPLLNAEALLELVKRVR-EECPEKDIWL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446503973  188 FTFTTNGMLLNDEITDFLNQemhnVVLSLDGrKKVHDYLRKTVNGRGSYNHIVP 241
Cdd:pfam13353  89 WTGYTFEELQSKDQLELLKL----IDVLVDG-KFEQSLKDPSLRFRGSSNQRII 137
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
109-419 5.44e-10

radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide maturase most closely related to the darobactin maturase DarE.


Pssm-ID: 469197 [Multi-domain]  Cd Length: 415  Bit Score: 61.05  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 109 CNLSCEYCfasQGKYNGNRAIMSYEVGKRAIDFLLENSGNHQnLDVDFFGGEPLMAWKTVKQIVAYARNKEKEYKKTFRF 188
Cdd:NF041300  51 CNLRCTYC---RSWAEGPNQTMTFDVLARAVREALSMPGLHG-VEFVWHGGEVTLLKPKVFKKLIWLQQQFRQPGQEVRN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 189 TFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIVPKFQEfVEKRG---------DKEyyVRG 259
Cdd:NF041300 127 SIQTNATHLTDEWIEFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIAR-LRQAGiphgalvvvDRE--LID 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 260 TYTHNNVDFTNDIyHIADLGFNKISMEPVICNPREPyalgeEDLLEIYNQYEILSKEMLN---REEKGSGF--TFYHYML 334
Cdd:NF041300 204 AGAERLLGYLAEI-GLDKISFLNVLPENDPDDPEIV-----KSTYFTFPEYVRFLTETFDvwwNSYRDRMEirEFRDLIP 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 335 DLSEGpcvqKRISGC----GSGTEYLAITPWGEIFPCHQFVGEEEYSMGN-----IWDGITKTEIQSQFKKSNCYSKTEC 405
Cdd:NF041300 278 KMSVG----AKPIGCywmgNCMGRYVTLEANGDLAPCDKYRGDPGSILGNvmhspMADIIRTSGYLADAKKEASDAKTRM 353
                        330
                 ....*....|....*
gi 446503973 406 QEC-WAQLyCSGGCP 419
Cdd:NF041300 354 APCkWFHV-CQGGCP 367
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
108-228 1.05e-08

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: 56.89  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 108 TCNLSCEYC--FAS----------QGKYNGNRAIMSYEVGKRAIDFLLENSgnhQNLD-VDFFGGEPLMA---WKTVKQI 171
Cdd:NF033640 119 LCNLKCRMCgpHSSsswakeakklGGPKLGDKKKISWFEDEEFWKWLEELL---PSLKeIYFAGGEPLLIkehYKLLEKL 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446503973 172 VayarnkEKEYKKTFRFTFTTNGMLLNDEITDFLN--QEMHNVVL--SLDGRKKVHDYLRK 228
Cdd:NF033640 196 V------EKGRAKNIELRYNTNLTVLPDKLKDLLDlwKKFKSVSIsaSIDGVGERNEYIRY 250
 
Name Accession Description Interval E-value
rSAM_six_Cys TIGR03974
SCIFF radical SAM maturase; Members of this protein family are predicted radical SAM enzymes ...
2-453 0e+00

SCIFF radical SAM maturase; Members of this protein family are predicted radical SAM enzymes universally associated with Six Cysteines in Forty-Five protein, or SCIFF (family TIGR03973), a predicted ribosomal natural product precursor that is nearly universal in the class Clostridia. Similarity of this family to radical SAM maturases (PqqE and subtilosin A maturase) found in the vicinity of other peptide precursors suggests this protein is the SCIFF radical SAM maturase. [Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274892 [Multi-domain]  Cd Length: 451  Bit Score: 796.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973    2 IHQYKLNGYNIVLDTYSGSVHVVDDLAYEIIMLYENTPMVEILSMMQEKYKYDFhvSEKEIRETIADIEELKRDGKLFTD 81
Cdd:TIGR03974   1 IHQYKNNGYNIVLDVNSGSVHVVDDVTYDVIALYEEGKDKETPEEIKEKLKGKY--SEEDIEEAYDEITELKEAGQLFTE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973   82 DDYKDLSIDLIN-RPTYVKALCLNVAHTCNLSCEYCFASQGKYNGNRAIMSYEVGKRAIDFLLENSGNHQNLDVDFFGGE 160
Cdd:TIGR03974  79 DIYEDYIIDFKKmRKTVVKALCLHVAHDCNLACKYCFAEEGEYHGRRALMSFEVGKKALDFLIANSGSRRNLEVDFFGGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  161 PLMAWKTVKQIVAYARNKEKEYKKTFRFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIV 240
Cdd:TIGR03974 159 PLMNFDVVKDLVAYGRSIEKEHNKNFRFTLTTNGVLLNDEIIEFANKEMSNVVLSLDGRKEVNDRMRPTRNGKGSYDLIV 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  241 PKFQEFVEKRGDKEYYVRGTYTHNNVDFTNDIYHIADLGFNKISMEPVICNPREPYALGEEDLLEIYNQYEILSKEMLNR 320
Cdd:TIGR03974 239 PKFQKLVESRGQKKYYVRGTFTHNNLDFSKDVLHLADLGFKQISVEPVVADPEEPYALTEEDLPIIFEEYEKLAKEMIKR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  321 EEKGSGFTFYHYMLDLSEGPCVQKRISGCGSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDGITKTEIQSQFKKSNCY 400
Cdd:TIGR03974 319 KKEGKGFNFFHFMIDLTGGPCVYKRLSGCGSGTEYLAVTPWGDLYPCHQFVGNEEFKMGNVFDGITNTDIRDEFKKCNVY 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446503973  401 SKTECQECWAQLYCSGGCPANTIHATGSLKGTHEFSCKIFRKRIECSMMVKVA 453
Cdd:TIGR03974 399 SKEKCKDCWARFYCSGGCAANSYNFTGDINDPYDLGCELQRKRIECAIMIKAA 451
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
99-451 1.79e-121

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 358.53  E-value: 1.79e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  99 KALCLNVAHTCNLSCEYCFASQGKYNGNRaIMSYEVGKRAIDFLLENSGNHQNLDVDFFGGEPLMAWKTVKQIVAYARNK 178
Cdd:COG0641    1 KALVLKPTSRCNLRCSYCYYSEGDEGSRR-RMSEETAEKAIDFLIESSGPGKELTITFFGGEPLLNFDFIKEIVEYARKY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 179 EKeYKKTFRFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIVPKFQEFVEKrgDKEYYVR 258
Cdd:COG0641   80 AK-KGKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVMRNIKLLKEH--GVEVNIR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 259 GTYTHNNVDFTNDIY-HIADLGFNKISMEPVICNPREPYALGEEDLLEIYNQYEilsKEMLnrEEKGSGFTFYHYMLDLS 337
Cdd:COG0641  157 CTVTRENLDDPEELYdFLKELGFRSIQFNPVVEEGEADYSLTPEDYGEFLIELF---DEWL--ERDGGKIFVREFDILLA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 338 EGPcvQKRISGC-GSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDG----ITKTEIQSQF-KKSNCYSKTECQECWAQ 411
Cdd:COG0641  232 GLL--PPCSSPCvGAGGNYLVVDPDGDIYPCDEFVGDPEFRLGNVFDGslaeLLDSPKLRAFgREKNVLLDEECRSCPYL 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 446503973 412 LYCSGGCPANTIHATGSLKGTHEFSCKIFRKRIECSMMVK 451
Cdd:COG0641  310 PLCGGGCPANRYAETGDGFKPYSYYCELYKKLFEHALRLE 349
SPASM_CteB-like cd21124
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ...
346-441 3.72e-33

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: 120.54  E-value: 3.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 346 ISGCGSGTEYLAITPWGEIFPCHQFVGEEEYSMGNIWDGITKTEIQSQFKKSNCYSKTECQECWAQLYCSGGCPANTIHA 425
Cdd:cd21124    1 LSGCGAGHEYFAVDPDGDIYPCHRFVGMEEYRMGNVYDGSSLMELQSEFWKRHVENKEECRECWARFYCGGGCPANSYAE 80
                         90
                 ....*....|....*.
gi 446503973 426 TGSLKGTHEFSCKIFR 441
Cdd:cd21124   81 NGDIRTPYEPYCEIYK 96
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
99-444 1.86e-30

radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain protein are predicted peptide maturases, similar to PqqE, AlbA, the mycofactocin radical SAM maturase, and many others that share the peptide modification radical SAM protein C-terminal additional 4Fe4S-binding domain (TIGR04085). Members co-occur with a protein of unknown function that may be a chaperone or immunity protein and with a peptide that may have twelve or more cysteines occurring regularly spaced every fourth residue. These Cys residues tend to be flanked by residues with small side chains that provide minimal steric hindrance to crosslink formation by the radical SAM enzyme as in the subtilosin A system.


Pssm-ID: 200366 [Multi-domain]  Cd Length: 359  Bit Score: 121.15  E-value: 1.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973   99 KALCLNVAHTCNLSCEYCFASqGKYNGNRaiMSYEVGKRAIDFLLENSGN--HQNLDVDFFGGEPLMAWKTVKQIVAYAR 176
Cdd:TIGR04115   2 KSITFIVTDDCQLACKYCYQT-GKNKNKR--MSFETAKKAVDYILSGNKGfgEPSVIWDFIGGEPLLEIELIDRICDYIK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  177 NKEKE----YKKTFRFTFTTNGMLLNDE-ITDFLNQEMHNVVLSL--DGRKKVHDYLRKTVNGRGSYNHIVPKFQEFVEK 249
Cdd:TIGR04115  79 NRMIElnhpWFNSYRFSFSTNGVCYFEEkVQRFIQKNNQHLSISItiDGTKEKHDSCRVFPDGRGSYDLVVSNAPLWLNQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  250 RGDKEYYVrgTYTHNNVDFTND-IYHIADLGFNKISMEPVICNPREPY--ALGEEDLLEIYNQyeILSKEMLNreekgsg 326
Cdd:TIGR04115 159 FPYASTKV--TIAPADVPHVKEsVTHLIDLGYNEVNINCVYEEGWQMGddTVFEDQLKKLADY--ILEHDMYN------- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  327 fTFYHYMLDLSEG---PCVQKRISGCGSGTeYLAITPWGEIFPCHQFV-----GEEEYSMGNIWDGITKTEIQSQFKKSN 398
Cdd:TIGR04115 228 -DYYCSFFSENFGhplDCKLDNENWCGGGV-MLAVDPDGIFYPCLRFAeyslrQKEAYSIGNVDDGIDRNRVRPFLKLDR 305
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 446503973  399 CYSKT-ECQECWAQLYCSgGCPANT--IHATGSLKGTHEFSCKIFRKRI 444
Cdd:TIGR04115 306 RTQSTdECINCPVASGCA-WCQGYNydVAGTPTIYQRATYICDMHKARV 353
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
109-454 1.10e-23

anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family enzymes, maturases that prepare the oxygen-sensitive radical required in the active site of anaerobic sulfatases. This maturase role has led to many misleading legacy annotations suggesting that this enzyme maturase is instead a sulfatase regulatory protein. All members of the seed alignment are radical SAM enzymes encoded next to or near an anaerobic sulfatase. Note that a single genome may encode more than one sulfatase/maturase pair. [Protein fate, Protein modification and repair]


Pssm-ID: 188457 [Multi-domain]  Cd Length: 363  Bit Score: 101.92  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  109 CNLSCEYCFASQGK--YNGNRAIMSYEVGKRAIDFLLEnSGNHQNLDVDFFGGEP-LMAWKTVKQIVAYarnkEKEYK-- 183
Cdd:TIGR03942  11 CNLDCDYCFYLEKEdlYPKPKPKMSDETLETFIKQYIA-SQDGPEVNFAWQGGEPtLAGLDFYRKAVEL----QQRYApg 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  184 KTFRFTFTTNGMLLNDEITDFLNQemHN--VVLSLDGRKKVHDYLRKTVNGRGSYNHIVpKFQEFVEKRGdKEYYVRGTY 261
Cdd:TIGR03942  86 KTISNSLQTNGILLNDEWAEFFKE--HNflVGISIDGPKELHDKYRVTKSGKGTFERVM-RALKLLKEHN-VEFNTLTVV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  262 THNNVDFTNDIY-HIADLGFNKISMEPVI-----CNPREPYALGEED----LLEIYNQYEilskemlnREEKGSGF--TF 329
Cdd:TIGR03942 162 NNHNARHGKEVYrFLKELGSRYMQFIPCVepdnaTREVTDWSVTPKDygrfLCDVFDEWV--------KNDVGRVFirNF 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  330 YHYM---LDLSEGPCVQKRIsgCGSGteyLAITPWGEIFPCHQFVgEEEYSMGNIWDG----ITKTEIQSQF--KKSNCY 400
Cdd:TIGR03942 234 ENALaiwLGNPSQSCVHSPT--CGQN---LVVESNGDVYSCDHYV-YPEYKLGNINETslaeMASSEKQKQFgqAKSLSL 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446503973  401 SKtECQECWAQLYCSGGCPANTIHATGSLKGTHEFSC---KIFRKRIEcSMMVKVAQ 454
Cdd:TIGR03942 308 PE-KCRRCDVLFLCNGGCPKHRILATPGGENGHNYLCagyKAFFSHTL-PYLQAMAE 362
geopep_mat_rSAM TIGR04280
putative geopeptide radical SAM maturase; This family is the radical SAM/SPASM domain putative ...
67-431 1.81e-22

putative geopeptide radical SAM maturase; This family is the radical SAM/SPASM domain putative peptide maturase for geopeptide, described by model TIGR04229. The SPASM domain (see model TIGR04085) frequently marks peptide-modifying radical SAM enzymes.


Pssm-ID: 275100 [Multi-domain]  Cd Length: 428  Bit Score: 99.40  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973   67 ADIEELKRDGKLFTDDDYKDLS----IDLINRPTYVKA--LCLNVAhtCNLSCEYCFasQGKYNGNRAiMSYEVGKRAID 140
Cdd:TIGR04280  48 AEAETLSRLGFLVEDREAEREEmrslFDRINRERRHFAaiVVLNLD--CNLACPYCF--EGPFRGKRY-MDDATADLLVS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  141 FLLENS-GNHQNLDVDFFGGEPLMAWKTVKQIVAYARNKEKEYKKTFRFTFTTNGMLLNDEIT-DFLNQEMHNVVLSLDG 218
Cdd:TIGR04280 123 YLVRERlAQGRDVSLDFYGGEPLLSLDLIRRIATPLKAAAASRGLSFSFSLVTNGTLLTRDVVeELLPLGLTGAKVTLDG 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  219 RKKVHDYLRKTVNGRGSYNHIVPKFQEFVEKRGDKeyyVRGTYTHNNV-DFTNDIYHIADLGFNKISMEPVICNPREPYA 297
Cdd:TIGR04280 203 PPEIHDRQRPFVSGKGSFDTIVANLKAVCDLIAIQ---IGGNYTRENYrEFPRLLDLLLAEGLTPERLALVRFSPVVSRA 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  298 lGEEDLLE------------IYNQYEILSKEMLNReekgsGFTfyhyMLDLSEGPCVQKrisgcgsGTEYLAITPWGEIF 365
Cdd:TIGR04280 280 -GGAALPDfnsgcassnepwLIEASLFLREETLKR-----GYP----VPKLRPGACMVE-------LEDDLVVNHDGTLY 342
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446503973  366 PCHQFVGEEEYSMGNIWDGItkteiqSQFKKS---NCYSKTECQECWAQLYCSGGCPANTIHATGSLKG 431
Cdd:TIGR04280 343 KCPAFMGREGLAVGSLADGL------SDYRDShglDLWKNEECLDCAYLPLCFGGCRFLTLLKTGAIDG 405
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
101-240 5.60e-21

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: 89.19  E-value: 5.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 101 LCLNVAHTCNLSCEYCFASQGKYNGNRaiMSYEVGKRAIDFLLEnsgnHQNLDVDFFGGEPLMaWKTVKQIVAYARnkek 180
Cdd:COG0535    2 LQIELTNRCNLRCKHCYADAGPKRPGE--LSTEEAKRILDELAE----LGVKVVGLTGGEPLL-RPDLFELVEYAK---- 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446503973 181 eyKKTFRFTFTTNGMLLNDEITDFLNQE-MHNVVLSLDG-RKKVHDYLRKtvnGRGSYNHIV 240
Cdd:COG0535   71 --ELGIRVNLSTNGTLLTEELAERLAEAgLDHVTISLDGvDPETHDKIRG---VPGAFDKVL 127
rSAM_more_4Fe4S TIGR04085
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ...
349-437 9.99e-21

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: 86.48  E-value: 9.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  349 CGSGTEYLAITPWGEIFPCHQFVgEEEYSMGNIWDG----ITKTEIQSQFKKS-NCYSKTECQECWAQLYCSGGCPANTI 423
Cdd:TIGR04085   1 CGAGRNSLVVDPDGDVYPCDHFV-YPEYKLGNIREDsleeILNSSKQLEFGRWkSPKLPEECRSCKYLPLCGGGCPANRY 79
                          90
                  ....*....|....
gi 446503973  424 HATGSLKGTHEFSC 437
Cdd:TIGR04085  80 LKTGDINGPKNPLC 93
rSAM_pep_methan TIGR04083
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ...
109-431 1.72e-19

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: 89.79  E-value: 1.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  109 CNLSCEYCFASQGkyngNRAIMSYEVGKRAIDFLLENSGNhqNLDVDFFGGEPLMA-WKTVKQivAYARNKEKEYKKTFR 187
Cdd:TIGR04083  10 CPSKCKYCWSSEE----TSPVMSIDTVKDIVEWLKDFRDD--RVTFTFHGGEPLLAgADFYRQ--ALPLLSEGLAHLKPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  188 FTFTTNGMLLNDEITDFLNQemHNVVL--SLDGRKKVHDYLRktvnGRGSYNHIVPKFQEFVEKRGDKEYYVrgTYTHNN 265
Cdd:TIGR04083  82 FAMQTNLWLMTPELAEIFAE--YNVPIgsSIDGPEEINDYQR----GEGYYQKTMKGYEIAKEHGLDVRFIC--TFTSYS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  266 VDFTNDIY-HIADLGFNkISMEPVICNPR----EPYALGEEDL-----------LEIYNQYEILSKEMLNR---EEKGSG 326
Cdd:TIGR04083 154 VKQKEEIFnFFLENGFT-LKLHPALPSLRsdnpGEWALDPEEYgellvylldkyLENMDKIEVMNINDLCRcvfTRRGTV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  327 FTFYHYMldlsegpcvqkrisgcgsGTEYlAITPWGEIFPCHQFVGEEEYSMGNIWDGITKTEIQS--------QFKKsn 398
Cdd:TIGR04083 233 CTFVDCM------------------GTTF-AVGPDGSIYPCYRFVGMPEYVMGNVRDRPTMEDLMEsdagklmlAFKE-- 291
                         330       340       350
                  ....*....|....*....|....*....|....
gi 446503973  399 cYSKTECQECWAQLYCSGGCPANTIHAT-GSLKG 431
Cdd:TIGR04083 292 -YVDTHCAKCSHIKYCRGGCPYNAIAPTdGEIKG 324
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
109-421 6.42e-18

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 84.97  E-value: 6.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 109 CNLSCEYCFASQgkYNGNRAIMSYEVGKraiDFLLE-------NSGNhQNLDVDFFGGEP-LMAWKTVKQIVAYARNKEK 180
Cdd:PRK13758  15 CNLKCTYCFYHS--LSDNRNVKSYGIMR---DEVLEsmvkrvlNEAE-GHCSFAFQGGEPtLAGLEFFEELMELQRKHNY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 181 EYKKTFrFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIVPKFQEFveKRGDKEYYVRGT 260
Cdd:PRK13758  89 KNLKIY-NSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGLDTFSKVERAAELF--KKYKVEFNILCV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 261 YTHNNVDFTNDIYHI---ADLGFNKI--SMEPvICNPRE--PYALGEEDLLEIYNQ-YEILSKEMLNreekgSGFTFYHY 332
Cdd:PRK13758 166 VTSNTARHVNKIYKYfkeKDFKFLQFinCLDP-LYEEKGkyNYSLKPKDYTKFLKNlFDLWYEDFLN-----GNRVSIRY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 333 MLDLSEGPCVQKRISGCGSGT---EYLaITPWGEIFPCHQFVgEEEYSMGNIWDGITK----TEIQSQFKKSNCYSKTEC 405
Cdd:PRK13758 240 FDGLLETILLGKSSSCGMNGTctcQFV-VESDGSVYPCDFYV-LDKWRLGNIQDMTMKelfeTNKNHEFIKSSFKVHEEC 317
                        330
                 ....*....|....*..
gi 446503973 406 QEC-WAQLyCSGGCPAN 421
Cdd:PRK13758 318 KKCkWFPL-CKGGCRRC 333
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
94-462 5.51e-14

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 73.36  E-value: 5.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  94 RPTYVkaLCLNVAHTCNLSCEYCFASQGK--YNGN-RAIMSYEVGKRAIDFLLENSGNHQNLdVDFFGGEPLMawktvKQ 170
Cdd:PRK13745  11 KPLYI--MLKPVGAVCNLACDYCYYLEKSklYQENpKHVMSDELLEKFIKEYINSQTMPQVL-FTWHGGETLM-----RP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 171 IVAYARNKEKEYK----KTFRFTFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYnHIVPKFQEF 246
Cdd:PRK13745  83 LSFYKKALELQKKyargRQIDNCIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEFHDEYRKNKMGKPSF-VKVMKGINL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 247 VEKRGdKEYYVRGTYTHNNVDFTNDIYH-IADLGFNKISMEPVI------CNPREPYALGEEDLLEIyNQYEILSKEMLN 319
Cdd:PRK13745 162 LKKHG-VEWNAMAVVNDFNADYPLDFYHfFKELDCHYIQFAPIVerivshQDGRHLASLAQQEGGEL-APFSVTPEQWGN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 320 ----------REEKGSgftFYHYMLD------LSEGPCVQKRISGCGSG--TEYLaitpwGEIFPCHQFVgEEEYSMGNI 381
Cdd:PRK13745 240 flctifdewvKEDVGK---YYIQLFDstlanwVGEQPGVCSMAKHCGHAgvMEFN-----GDVYSCDHFV-FPEYKLGNI 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 382 WDG----ITKTEIQSQFKKSNCYS-KTECQECWAQLYCSGGCPANTIHATGSLKGTHEFSCKIFRKRIEcsmmvKVAQSI 456
Cdd:PRK13745 311 YQQtlveMMYSERQTAFGTMKYKSlPTQCKECEYLFACHGECPKNRFCRTANGEPGLNYLCKGYHQFFK-----HVAPYM 385

                 ....*.
gi 446503973 457 RAMKKE 462
Cdd:PRK13745 386 DFMKKE 391
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
109-241 9.72e-12

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 62.19  E-value: 9.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  109 CNLSCEYCFASQGK-YNGNRaIMSYEVGKRAIDFLLENSGNhqnlDVDFFGGEPLMAWKTVKQIVAYARnKEKEYKKTFR 187
Cdd:pfam13353  15 CNHHCKGCFNPETWdFKYGK-PFTEELEDEIIEDLAKPYIQ----GLTLSGGEPLLNAEALLELVKRVR-EECPEKDIWL 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446503973  188 FTFTTNGMLLNDEITDFLNQemhnVVLSLDGrKKVHDYLRKTVNGRGSYNHIVP 241
Cdd:pfam13353  89 WTGYTFEELQSKDQLELLKL----IDVLVDG-KFEQSLKDPSLRFRGSSNQRII 137
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
99-420 2.46e-11

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: 64.88  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973   99 KALCLNVAHTCNLSCEYC--FASQGKyngnraiMSYEVGKRAIDFLLENSGNHQNLDVDFFGGEPLMAWKTVKQIVAYAR 176
Cdd:TIGR04250   3 RSVDIDITGRCNLRCRYCshFSSAAE-------TPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  177 NKekeykktFRFTFTTNGMLLNDEITDFL--NQEMHNVVLSLDG-RKKVHDYLRktvnGRGSynhivpkFQEFVE----- 248
Cdd:TIGR04250  76 NR-------MRFSILSNGTLITDAIASFLaaTRRCDYVQVSIDGsTPGTHDRLR----GTGS-------FLQAVEgiell 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  249 KRGDKEYYVRGTYTHNNVDftnDIYHIADLGFNKISMEPVICNPREPYAL--GEEDLLEIYNQYEILSKEMLNREEKGsg 326
Cdd:TIGR04250 138 RKHAIPVVVRVTIHRWNVD---DLRPIAALLLDDLGLPAFSTNAASYMGLcrSNTDDVQLDTAERTLAMEILLELEKE-- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  327 ftfYHYMLDLSEGPCVQKR---------------------ISGCGSGTEYLAITPWGEIFPCHQFVGEE-----EYSMGN 380
Cdd:TIGR04250 213 ---YPGRISASAGPLADARtwasmeqaridqqgnmpgrgyLSGCGGIFMSLAVRADGVIVPCNQLSHIElgrinRDSLRE 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 446503973  381 IWDGITKTEiqsQFKKSNCYSKTE---CQECWAQLYCSGGCPA 420
Cdd:TIGR04250 290 LWQNHPVLL---QLRNRVTIPLTDfefCKDCDYIPYCTGNCPA 329
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
109-240 1.17e-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: 59.85  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973  109 CNLSCEYCFASQGKYNGNRAIMSYEVGKRAIDFLLENSGNHqnldVDFFGGEPLMAWKTVKQIVAYARNKEKEYkktFRF 188
Cdd:pfam04055   5 CNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEV----VILGGGEPLLLPDLVELLERLLKLELAEG---IRI 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446503973  189 TFTTNGMLLNDEITDFL-NQEMHNVVLSLDGrkkVHDYLRKTVNGRGSYNHIV 240
Cdd:pfam04055  78 TLETNGTLLDEELLELLkEAGLDRVSIGLES---GDDEVLKLINRGHTFEEVL 127
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
109-419 5.44e-10

radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide maturase most closely related to the darobactin maturase DarE.


Pssm-ID: 469197 [Multi-domain]  Cd Length: 415  Bit Score: 61.05  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 109 CNLSCEYCfasQGKYNGNRAIMSYEVGKRAIDFLLENSGNHQnLDVDFFGGEPLMAWKTVKQIVAYARNKEKEYKKTFRF 188
Cdd:NF041300  51 CNLRCTYC---RSWAEGPNQTMTFDVLARAVREALSMPGLHG-VEFVWHGGEVTLLKPKVFKKLIWLQQQFRQPGQEVRN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 189 TFTTNGMLLNDEITDFLNQEMHNVVLSLDGRKKVHDYLRKTVNGRGSYNHIVPKFQEfVEKRG---------DKEyyVRG 259
Cdd:NF041300 127 SIQTNATHLTDEWIEFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIAR-LRQAGiphgalvvvDRE--LID 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 260 TYTHNNVDFTNDIyHIADLGFNKISMEPVICNPREPyalgeEDLLEIYNQYEILSKEMLN---REEKGSGF--TFYHYML 334
Cdd:NF041300 204 AGAERLLGYLAEI-GLDKISFLNVLPENDPDDPEIV-----KSTYFTFPEYVRFLTETFDvwwNSYRDRMEirEFRDLIP 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 335 DLSEGpcvqKRISGC----GSGTEYLAITPWGEIFPCHQFVGEEEYSMGN-----IWDGITKTEIQSQFKKSNCYSKTEC 405
Cdd:NF041300 278 KMSVG----AKPIGCywmgNCMGRYVTLEANGDLAPCDKYRGDPGSILGNvmhspMADIIRTSGYLADAKKEASDAKTRM 353
                        330
                 ....*....|....*
gi 446503973 406 QEC-WAQLyCSGGCP 419
Cdd:NF041300 354 APCkWFHV-CQGGCP 367
SPASM_AlbA-like cd21125
Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis ...
348-429 7.49e-09

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: 52.88  E-value: 7.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 348 GCGSGTEYLAITPWGEIFPCHQFvGEEEYSMGNIWDG----ITKTEIQSQFKKSNCYSKTECQECWAQLYCSGGCPANTI 423
Cdd:cd21125    2 NCGAGWKSIVIDPDGEVYPCHLL-HPTEFKLGNIFEDslasILKNPVLEIWQTYDPRFSEHCKKCPFYGICGGGCIAKSL 80

                 ....*.
gi 446503973 424 HATGSL 429
Cdd:cd21125   81 ISYGRF 86
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
108-228 1.05e-08

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: 56.89  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 108 TCNLSCEYC--FAS----------QGKYNGNRAIMSYEVGKRAIDFLLENSgnhQNLD-VDFFGGEPLMA---WKTVKQI 171
Cdd:NF033640 119 LCNLKCRMCgpHSSsswakeakklGGPKLGDKKKISWFEDEEFWKWLEELL---PSLKeIYFAGGEPLLIkehYKLLEKL 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446503973 172 VayarnkEKEYKKTFRFTFTTNGMLLNDEITDFLN--QEMHNVVL--SLDGRKKVHDYLRK 228
Cdd:NF033640 196 V------EKGRAKNIELRYNTNLTVLPDKLKDLLDlwKKFKSVSIsaSIDGVGERNEYIRY 250
SPASM_anSME cd21120
Iron-sulfur cluster-binding SPASM domain of anaerobic sulfatase maturating enzyme; Anaerobic ...
349-431 6.84e-07

Iron-sulfur cluster-binding SPASM domain of anaerobic sulfatase maturating enzyme; Anaerobic sulfatase maturating enzyme (anSME) is a radical S-adenosylmethionine (SAM) enzyme that catalyzes, under anaerobic conditions, the co- or post-translational modification of arylsulfatases to form a catalytically essential formylglycine (FGly) residue to perform their hydrolysis function, removing sulfate groups from a wide array of substrates. 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; anSME contains two auxillary 4Fe-4S clusters in its SPASM domain.


Pssm-ID: 410611 [Multi-domain]  Cd Length: 107  Bit Score: 47.66  E-value: 6.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 349 CGSgteYLAITPWGEIFPCHQFVgEEEYSMGNI----WDGITKTEIQSQFKKSNCYSKTECQECWAQLYCSGGCPANTIH 424
Cdd:cd21120    8 CGD---NLVVEHNGDVYPCDHFV-LPEYRLGNIqeqtLAELVDSEKQQQFGAQKFKLPAECKQCKYLFACHGGCPKHRFA 83

                 ....*..
gi 446503973 425 ATGSLKG 431
Cdd:cd21120   84 KGPSEPG 90
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
103-307 7.40e-06

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: 46.94  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 103 LNVAHTCNLSCEYCFASQGKYNGNraiMSYEVGKRAIDFLLEnsgnHQNLDVDFF---GGEPLMaWKTVKQIVAYArnke 179
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGP---ESPPEIEEILDIVLE----AKERGVEVViltGGEPLL-YPELAELLRRL---- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 180 KEYKKTFRFTFTTNGMLLNDEITD-FLNQEMHNVVLSLDGrkKVHDYLRKTVNGRGSYNHIvpkFQEFVEKRG-DKEYYV 257
Cdd:cd01335   69 KKELPGFEISIETNGTLLTEELLKeLKELGLDGVGVSLDS--GDEEVADKIRGSGESFKER---LEALKELREaGLGLST 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446503973 258 RGTYTHNNVD---------FTNDIYHIADLGFNKISMEPVICNPREPYALGEEDLLEIY 307
Cdd:cd01335  144 TLLVGLGDEDeeddleeleLLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLI 202
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
349-409 1.20e-03

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: 37.46  E-value: 1.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446503973  349 CGSGTEYLAITPWGEIFPCHQFVGEEEYSMGN--------IWDGITKTEIQSQFKKSNCyskTECQECW 409
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCFDDDFVGPIVLGNireqslaeIWNSPKYREFRKLGKFALI---ELCRDCP 66
SurA_N_3 pfam13624
SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a ...
46-87 2.08e-03

SurA N-terminal domain; This domain is found at the N-terminus of the chaperone SurA. It is a helical domain of unknown function. The C-terminus of the SurA protein folds back and forms part of this domain also but is not included in the current alignment.


Pssm-ID: 433358 [Multi-domain]  Cd Length: 162  Bit Score: 38.71  E-value: 2.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446503973   46 MMQEKYKYDFHVSEKEIRETIADIEELKRDGKlFTDDDYKDL 87
Cdd:pfam13624  97 LLQEAKKLGLAVSDEEVRQAIASIPAFQEDGK-FDKERYRQL 137
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
348-381 2.28e-03

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: 36.63  E-value: 2.28e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446503973 348 GCGSGTEYLAITPWGEIFPCHQFVgEEEYSMGNI 381
Cdd:cd21109    1 PCPAPWTSLYITPDGDVYPCCFDV-NEELKLGNI 33
MoaA2 COG1964
C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor ...
102-227 2.99e-03

C-terminal domain of the GTP 3',8'-cyclase MoaA, radical SAM superfamily (molybdenum cofactor biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 441567 [Multi-domain]  Cd Length: 473  Bit Score: 39.86  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 102 CL---NVAHTCNLSCEYCFASQGKYNGNRAimSYEVGKRAIDFLLENSGnhqNLD-VDFFGGEPlmawkTVK----QIVA 173
Cdd:COG1964   95 CLaliEVTNRCNLNCPICFANSGPGYGYEP--SLEEIEKMLDALVREEG---EPDvVQFSGGEP-----TVHpdlfEILD 164
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446503973 174 YARnkekeyKKTFRFT-FTTNGMLL--NDEITDFLNQEM--HNVVLSLDG-RKKVHDYLR 227
Cdd:COG1964  165 LAK------ERPIKHVmINTNGIRIakDPDFAERLAEAGplFEVYLQFDGlSDEPYRRLR 218
 
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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