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Conserved domains on  [gi|38703987|ref|NP_310129|]
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anaerobic sulfatase maturase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

anaerobic sulfatase maturase( domain architecture ID 11499222)

anaerobic sulfatase maturase is a radical SAM protein with a C-terminal SPASM domain, which prepares the oxygen-sensitive radical required in the active site of anaerobic sulfatases

PubMed:  18408004|18307109
SCOP:  3000308

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
2-365 0e+00

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: 596.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     2 HVTAKPSSFQCNLKCDYCFYLEKESQF-THEKWMDDSTLKEFIKQYIAA-SGNQVYFTWQGGEPTLAGLDFFRKVIHYQQ 79
Cdd:TIGR03942   1 HVMAKPTGAKCNLDCDYCFYLEKEDLYpKPKPKMSDETLETFIKQYIASqDGPEVNFAWQGGEPTLAGLDFYRKAVELQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    80 RYAGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTV 159
Cdd:TIGR03942  81 RYAPGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFERVMRALKLLKEHNVEFNTLTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   160 INNVNVHYPLEVYHFLKSIGSKHMQFIELLEtgtpnidfsgHSENTFRIIDFSVPPTAYGKFMSTIFMQWVKNDVGEIFI 239
Cdd:TIGR03942 161 VNNHNARHGKEVYRFLKELGSRYMQFIPCVE----------PDNATREVTDWSVTPKDYGRFLCDVFDEWVKNDVGRVFI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   240 RQFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMNSVQLT-----AQKKRISAK 314
Cdd:TIGR03942 231 RNFENALAIWLGNPSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLGNINETSLAEMASSEKQkqfgqAKSLSLPEK 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 38703987   315 CQQCAYKPICNGGCPKHRITKVNDET--VSYFCEGYKILFSTMVPYMNAMVEL 365
Cdd:TIGR03942 311 CRRCDVLFLCNGGCPKHRILATPGGEngHNYLCAGYKAFFSHTLPYLQAMAEL 363
 
Name Accession Description Interval E-value
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
2-365 0e+00

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: 596.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     2 HVTAKPSSFQCNLKCDYCFYLEKESQF-THEKWMDDSTLKEFIKQYIAA-SGNQVYFTWQGGEPTLAGLDFFRKVIHYQQ 79
Cdd:TIGR03942   1 HVMAKPTGAKCNLDCDYCFYLEKEDLYpKPKPKMSDETLETFIKQYIASqDGPEVNFAWQGGEPTLAGLDFYRKAVELQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    80 RYAGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTV 159
Cdd:TIGR03942  81 RYAPGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFERVMRALKLLKEHNVEFNTLTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   160 INNVNVHYPLEVYHFLKSIGSKHMQFIELLEtgtpnidfsgHSENTFRIIDFSVPPTAYGKFMSTIFMQWVKNDVGEIFI 239
Cdd:TIGR03942 161 VNNHNARHGKEVYRFLKELGSRYMQFIPCVE----------PDNATREVTDWSVTPKDYGRFLCDVFDEWVKNDVGRVFI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   240 RQFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMNSVQLT-----AQKKRISAK 314
Cdd:TIGR03942 231 RNFENALAIWLGNPSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLGNINETSLAEMASSEKQkqfgqAKSLSLPEK 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 38703987   315 CQQCAYKPICNGGCPKHRITKVNDET--VSYFCEGYKILFSTMVPYMNAMVEL 365
Cdd:TIGR03942 311 CRRCDVLFLCNGGCPKHRILATPGGEngHNYLCAGYKAFFSHTLPYLQAMAEL 363
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
3-352 3.09e-123

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 359.69  E-value: 3.09e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   3 VTAKPSSfQCNLKCDYCFYLEKEsqFTHEKWMDDSTLKEFIKQYIAASGN--QVYFTWQGGEPTLAgLDFFRKVIHYQQR 80
Cdd:COG0641   3 LVLKPTS-RCNLRCSYCYYSEGD--EGSRRRMSEETAEKAIDFLIESSGPgkELTITFFGGEPLLN-FDFIKEIVEYARK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  81 YAGQ-KRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTV 159
Cdd:COG0641  79 YAKKgKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVMRNIKLLKEHGVEVNIRCT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 160 INNVNVHYPLEVYHFLKSIGSKHMQFIELLETGTPnidfsghsentfriiDFSVPPTAYGKFMSTIFMQWVKNDVGEIFI 239
Cdd:COG0641 159 VTRENLDDPEELYDFLKELGFRSIQFNPVVEEGEA---------------DYSLTPEDYGEFLIELFDEWLERDGGKIFV 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 240 RQFESFVSRFLGNGHTSCIfqESCKDNLVVESNGDIYECDHFV-YPQYKLGNINKSELKTMNSVQ-----LTAQKKRISA 313
Cdd:COG0641 224 REFDILLAGLLPPCSSPCV--GAGGNYLVVDPDGDIYPCDEFVgDPEFRLGNVFDGSLAELLDSPklrafGREKNVLLDE 301
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 38703987 314 KCQQCAYKPICNGGCPKHRITKVND--ETVSYFCEGYKILF 352
Cdd:COG0641 302 ECRSCPYLPLCGGGCPANRYAETGDgfKPYSYYCELYKKLF 342
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
1-384 2.90e-111

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 331.44  E-value: 2.90e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    1 MHVTAKPSSFQCNLKCDYCFYLEKESQFTHEK--WMDDSTLKEFIKQYI-AASGNQVYFTWQGGEPTLAGLDFFRKVIHY 77
Cdd:PRK13745  13 LYIMLKPVGAVCNLACDYCYYLEKSKLYQENPkhVMSDELLEKFIKEYInSQTMPQVLFTWHGGETLMRPLSFYKKALEL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   78 QQRYAGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTL 157
Cdd:PRK13745  93 QKKYARGRQIDNCIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEFHDEYRKNKMGKPSFVKVMKGINLLKKHGVEWNAM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  158 TVINNVNVHYPLEVYHFLKSIGSKHMQFIELLETGTPNID----FSGHSENTFRIIDFSVPPTAYGKFMSTIFMQWVKND 233
Cdd:PRK13745 173 AVVNDFNADYPLDFYHFFKELDCHYIQFAPIVERIVSHQDgrhlASLAQQEGGELAPFSVTPEQWGNFLCTIFDEWVKED 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  234 VGEIFIRQFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNI-NKSELKTMNSVQLTA----QK 308
Cdd:PRK13745 253 VGKYYIQLFDSTLANWVGEQPGVCSMAKHCGHAGVMEFNGDVYSCDHFVFPEYKLGNIyQQTLVEMMYSERQTAfgtmKY 332
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38703987  309 KRISAKCQQCAYKPICNGGCPKHRI--TKVNDETVSYFCEGYKILFSTMVPYMNAMVELAKNRVPLYHIMDVAKQMEN 384
Cdd:PRK13745 333 KSLPTQCKECEYLFACHGECPKNRFcrTANGEPGLNYLCKGYHQFFKHVAPYMDFMKKELMNQRPPANVMDAAKENKL 410
SPASM_anSME cd21120
Iron-sulfur cluster-binding SPASM domain of anaerobic sulfatase maturating enzyme; Anaerobic ...
256-357 4.09e-47

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: 156.28  E-value: 4.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 256 SCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMN----SVQLTAQKKRISAKCQQCAYKPICNGGCPKH 331
Cdd:cd21120   1 SCVMSGTCGDNLVVEHNGDVYPCDHFVLPEYRLGNIQEQTLAELVdsekQQQFGAQKFKLPAECKQCKYLFACHGGCPKH 80
                        90       100
                ....*....|....*....|....*..
gi 38703987 332 RITKVNDET-VSYFCEGYKILFSTMVP 357
Cdd:cd21120  81 RFAKGPSEPgLNYLCEGYKEFFEHLLP 107
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
12-369 6.63e-45

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: 159.67  E-value: 6.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   12 CNLKCDYCfyleKESQFTHEKWMDDSTLKEFIKQYIAASGNQ-VYFTWQGGEPTLAGLDFFRKVIHYQQRY--AGQKrIF 88
Cdd:NF041300  51 CNLRCTYC----RSWAEGPNQTMTFDVLARAVREALSMPGLHgVEFVWHGGEVTLLKPKVFKKLIWLQQQFrqPGQE-VR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   89 NALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTVINNVNVHY- 167
Cdd:NF041300 126 NSIQTNATHLTDEWIEFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIARLRQAGIPHGALVVVDRELIDAg 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  168 PLEVYHFLKSIGSKHMQFIELLETGTPNIDfsGHSENTFriidFSVPptAYGKFMSTIFMQWVKNDVGEIFIRQFESFVS 247
Cdd:NF041300 206 AERLLGYLAEIGLDKISFLNVLPENDPDDP--EIVKSTY----FTFP--EYVRFLTETFDVWWNSYRDRMEIREFRDLIP 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  248 RfLGNGHTS--CIFQESCKDNLV-VESNGDIYECDHFVY-PQYKLGNINKSEL-KTMNSVQLTAQKKRISAKCQQ----C 318
Cdd:NF041300 278 K-MSVGAKPigCYWMGNCMGRYVtLEANGDLAPCDKYRGdPGSILGNVMHSPMaDIIRTSGYLADAKKEASDAKTrmapC 356
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 38703987  319 AYKPICNGGCPKHRitKVNDETVSYF---CEGYKILFSTMVPYMNAMVELAKNR 369
Cdd:NF041300 357 KWFHVCQGGCPHDR--HLNSRFVPAVdprCCGLAPLLDHMRRTAGRTMERAGIR 408
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
12-171 3.01e-18

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: 81.03  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCFYlEKESQFTHEKWMDDSTLKEFIKQYIAASGNQVYFTwqGGEPTLaGLDFFRKVIHYQQRyAGQKRIFNAL 91
Cdd:pfam04055   5 CNLRCTYCAF-PSIRARGKGRELSPEEILEEAKELKRLGVEVVILG--GGEPLL-LPDLVELLERLLKL-ELAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    92 QTNGILLNNEWCAFLKEHEF-LVGISIDGPqelHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNT--LTVINNVNVHYP 168
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAGLdRVSIGLESG---DDEVLKLINRGHTFEEVLEALELLREAGIPVVTdnIVGLPGETDEDL 156

                  ...
gi 38703987   169 LEV 171
Cdd:pfam04055 157 EET 159
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
12-185 2.97e-09

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


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 58.05  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   12 CNLKCDYC--------------FYLEKESQFTHEKWMDDstlKEFIKQYIAASGN--QVYFTwqGGEPTLAG--LDFFRK 73
Cdd:NF033640 120 CNLKCRMCgphsssswakeakkLGGPKLGDKKKISWFED---EEFWKWLEELLPSlkEIYFA--GGEPLLIKehYKLLEK 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   74 VIhyQQRYAGQKRIFnaLQTNGILLNNEWCAFLKE----HEFLVGISIDGPQELHDrYRRSNSgngTFAKVIAAIERLKS 149
Cdd:NF033640 195 LV--EKGRAKNIELR--YNTNLTVLPDKLKDLLDLwkkfKSVSISASIDGVGERNE-YIRYGS---KWDEIEKNLKKLKE 266
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 38703987  150 Y--QVEFNTLTVINNVNVHYPLEVYHFLKSIGSKHMQF 185
Cdd:NF033640 267 EcpNVELRINPTVSALNVLHLPELLDWLLELGLGPIDI 304
 
Name Accession Description Interval E-value
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
2-365 0e+00

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: 596.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     2 HVTAKPSSFQCNLKCDYCFYLEKESQF-THEKWMDDSTLKEFIKQYIAA-SGNQVYFTWQGGEPTLAGLDFFRKVIHYQQ 79
Cdd:TIGR03942   1 HVMAKPTGAKCNLDCDYCFYLEKEDLYpKPKPKMSDETLETFIKQYIASqDGPEVNFAWQGGEPTLAGLDFYRKAVELQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    80 RYAGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTV 159
Cdd:TIGR03942  81 RYAPGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFERVMRALKLLKEHNVEFNTLTV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   160 INNVNVHYPLEVYHFLKSIGSKHMQFIELLEtgtpnidfsgHSENTFRIIDFSVPPTAYGKFMSTIFMQWVKNDVGEIFI 239
Cdd:TIGR03942 161 VNNHNARHGKEVYRFLKELGSRYMQFIPCVE----------PDNATREVTDWSVTPKDYGRFLCDVFDEWVKNDVGRVFI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   240 RQFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMNSVQLT-----AQKKRISAK 314
Cdd:TIGR03942 231 RNFENALAIWLGNPSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLGNINETSLAEMASSEKQkqfgqAKSLSLPEK 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 38703987   315 CQQCAYKPICNGGCPKHRITKVNDET--VSYFCEGYKILFSTMVPYMNAMVEL 365
Cdd:TIGR03942 311 CRRCDVLFLCNGGCPKHRILATPGGEngHNYLCAGYKAFFSHTLPYLQAMAEL 363
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
3-352 3.09e-123

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 359.69  E-value: 3.09e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   3 VTAKPSSfQCNLKCDYCFYLEKEsqFTHEKWMDDSTLKEFIKQYIAASGN--QVYFTWQGGEPTLAgLDFFRKVIHYQQR 80
Cdd:COG0641   3 LVLKPTS-RCNLRCSYCYYSEGD--EGSRRRMSEETAEKAIDFLIESSGPgkELTITFFGGEPLLN-FDFIKEIVEYARK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  81 YAGQ-KRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTV 159
Cdd:COG0641  79 YAKKgKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVMRNIKLLKEHGVEVNIRCT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 160 INNVNVHYPLEVYHFLKSIGSKHMQFIELLETGTPnidfsghsentfriiDFSVPPTAYGKFMSTIFMQWVKNDVGEIFI 239
Cdd:COG0641 159 VTRENLDDPEELYDFLKELGFRSIQFNPVVEEGEA---------------DYSLTPEDYGEFLIELFDEWLERDGGKIFV 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 240 RQFESFVSRFLGNGHTSCIfqESCKDNLVVESNGDIYECDHFV-YPQYKLGNINKSELKTMNSVQ-----LTAQKKRISA 313
Cdd:COG0641 224 REFDILLAGLLPPCSSPCV--GAGGNYLVVDPDGDIYPCDEFVgDPEFRLGNVFDGSLAELLDSPklrafGREKNVLLDE 301
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 38703987 314 KCQQCAYKPICNGGCPKHRITKVND--ETVSYFCEGYKILF 352
Cdd:COG0641 302 ECRSCPYLPLCGGGCPANRYAETGDgfKPYSYYCELYKKLF 342
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
1-384 2.90e-111

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 331.44  E-value: 2.90e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    1 MHVTAKPSSFQCNLKCDYCFYLEKESQFTHEK--WMDDSTLKEFIKQYI-AASGNQVYFTWQGGEPTLAGLDFFRKVIHY 77
Cdd:PRK13745  13 LYIMLKPVGAVCNLACDYCYYLEKSKLYQENPkhVMSDELLEKFIKEYInSQTMPQVLFTWHGGETLMRPLSFYKKALEL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   78 QQRYAGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTL 157
Cdd:PRK13745  93 QKKYARGRQIDNCIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEFHDEYRKNKMGKPSFVKVMKGINLLKKHGVEWNAM 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  158 TVINNVNVHYPLEVYHFLKSIGSKHMQFIELLETGTPNID----FSGHSENTFRIIDFSVPPTAYGKFMSTIFMQWVKND 233
Cdd:PRK13745 173 AVVNDFNADYPLDFYHFFKELDCHYIQFAPIVERIVSHQDgrhlASLAQQEGGELAPFSVTPEQWGNFLCTIFDEWVKED 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  234 VGEIFIRQFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNI-NKSELKTMNSVQLTA----QK 308
Cdd:PRK13745 253 VGKYYIQLFDSTLANWVGEQPGVCSMAKHCGHAGVMEFNGDVYSCDHFVFPEYKLGNIyQQTLVEMMYSERQTAfgtmKY 332
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38703987  309 KRISAKCQQCAYKPICNGGCPKHRI--TKVNDETVSYFCEGYKILFSTMVPYMNAMVELAKNRVPLYHIMDVAKQMEN 384
Cdd:PRK13745 333 KSLPTQCKECEYLFACHGECPKNRFcrTANGEPGLNYLCKGYHQFFKHVAPYMDFMKKELMNQRPPANVMDAAKENKL 410
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
6-357 3.63e-76

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 240.20  E-value: 3.63e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    6 KPSSFQCNLKCDYCFY--LEKESQFTHEKWMDDSTLKEFIKQYIAASGNQVYFTWQGGEPTLAGLDFFRKVIHYQQRYAG 83
Cdd:PRK13758   9 KPASSGCNLKCTYCFYhsLSDNRNVKSYGIMRDEVLESMVKRVLNEAEGHCSFAFQGGEPTLAGLEFFEELMELQRKHNY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   84 QK-RIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTVINN 162
Cdd:PRK13758  89 KNlKIYNSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGLDTFSKVERAAELFKKYKVEFNILCVVTS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  163 VNVHYPLEVYHFLKSIGSKHMQFIELLEtgtPNIDFSGHSentfriiDFSVPPTAYGKFMSTIFMQWVKN--DVGEIFIR 240
Cdd:PRK13758 169 NTARHVNKIYKYFKEKDFKFLQFINCLD---PLYEEKGKY-------NYSLKPKDYTKFLKNLFDLWYEDflNGNRVSIR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  241 QFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMNSVQLTAQKKRIS----AKCQ 316
Cdd:PRK13758 239 YFDGLLETILLGKSSSCGMNGTCTCQFVVESDGSVYPCDFYVLDKWRLGNIQDMTMKELFETNKNHEFIKSSfkvhEECK 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 38703987  317 QCAYKPICNGGCPKHRITKVNDET-VSYFCEGYKILFSTMVP 357
Cdd:PRK13758 319 KCKWFPLCKGGCRRCRDSKEDSGLeLNYYCQSYKEFFEYAFP 360
SPASM_anSME cd21120
Iron-sulfur cluster-binding SPASM domain of anaerobic sulfatase maturating enzyme; Anaerobic ...
256-357 4.09e-47

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: 156.28  E-value: 4.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 256 SCIFQESCKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMN----SVQLTAQKKRISAKCQQCAYKPICNGGCPKH 331
Cdd:cd21120   1 SCVMSGTCGDNLVVEHNGDVYPCDHFVLPEYRLGNIQEQTLAELVdsekQQQFGAQKFKLPAECKQCKYLFACHGGCPKH 80
                        90       100
                ....*....|....*....|....*..
gi 38703987 332 RITKVNDET-VSYFCEGYKILFSTMVP 357
Cdd:cd21120  81 RFAKGPSEPgLNYLCEGYKEFFEHLLP 107
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
12-369 6.63e-45

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: 159.67  E-value: 6.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   12 CNLKCDYCfyleKESQFTHEKWMDDSTLKEFIKQYIAASGNQ-VYFTWQGGEPTLAGLDFFRKVIHYQQRY--AGQKrIF 88
Cdd:NF041300  51 CNLRCTYC----RSWAEGPNQTMTFDVLARAVREALSMPGLHgVEFVWHGGEVTLLKPKVFKKLIWLQQQFrqPGQE-VR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   89 NALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTVINNVNVHY- 167
Cdd:NF041300 126 NSIQTNATHLTDEWIEFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIARLRQAGIPHGALVVVDRELIDAg 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  168 PLEVYHFLKSIGSKHMQFIELLETGTPNIDfsGHSENTFriidFSVPptAYGKFMSTIFMQWVKNDVGEIFIRQFESFVS 247
Cdd:NF041300 206 AERLLGYLAEIGLDKISFLNVLPENDPDDP--EIVKSTY----FTFP--EYVRFLTETFDVWWNSYRDRMEIREFRDLIP 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  248 RfLGNGHTS--CIFQESCKDNLV-VESNGDIYECDHFVY-PQYKLGNINKSEL-KTMNSVQLTAQKKRISAKCQQ----C 318
Cdd:NF041300 278 K-MSVGAKPigCYWMGNCMGRYVtLEANGDLAPCDKYRGdPGSILGNVMHSPMaDIIRTSGYLADAKKEASDAKTrmapC 356
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 38703987  319 AYKPICNGGCPKHRitKVNDETVSYF---CEGYKILFSTMVPYMNAMVELAKNR 369
Cdd:NF041300 357 KWFHVCQGGCPHDR--HLNSRFVPAVdprCCGLAPLLDHMRRTAGRTMERAGIR 408
rSAM_GlyRichRpt TIGR04261
radical SAM/SPASM domain protein, GRRM system; Members of this protein family are radical SAM ...
6-329 3.43e-34

radical SAM/SPASM domain protein, GRRM system; Members of this protein family are radical SAM/SPASM domain proteins (see pfam04055 and TIGR04085) related to anaeroboic sulfatase maturating enzymes and the peptide modification enzyme PqqE. Members are found primarily in Cyanobacteria adjacent to a short protein, ~150 residues, in which the last ~60 residues tends to be repetitive and highly glycine-rich (see TIGR04260). The arrangement suggests modifications to the repetitive C-terminal region by this radical SAM domain enzyme, but the purpose of this system on the whole is unknown.


Pssm-ID: 211984 [Multi-domain]  Cd Length: 363  Bit Score: 129.77  E-value: 3.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     6 KPSSFqCNLKCDYCfYLEKEsqftHEKWMDDSTLKEFIKQYIAAS---GNQVYFTWQGGEPTLAGLDFFRKVIH----YQ 78
Cdd:TIGR04261   2 QPTSF-CNLDCDYC-YLPDR----QLKNRLSLDLIEPILKRILESpfvGPGFTICWHAGEPLTVPISFYDEATEiireAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    79 QRYA-GQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTL 157
Cdd:TIGR04261  76 EEYNqQPVQIEQSVQTNGTLINQAWCDCFKRNRIVVGVSLDGPAFIHDAHRRTRTGRGSHAATMRGIRALQKNEIPFSVI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   158 TVINNVNVHYPLEVYHFLKSIGSKHMQF-IEllETGTPNIDFSGHSENTfriidfsvpPTAYGKFMSTiFMQWVKNDVGE 236
Cdd:TIGR04261 156 AVLTEDSLDYPDEIFDFFRDNGITDVGFnME--ETEGVNTSSSLQGQGT---------EERYRAFLQR-FWELTAQAGGE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   237 IFIRQFESFvsrflgnghTSCIFQESCKDN---------LVVESNGDI---------YECDHfvYPQYKLGNINKSELKt 298
Cdd:TIGR04261 224 LRLREFEDI---------CSLIYTGQRLLQtdmnrpfaiVSVDHQGNFstfdpellsVKTDH--YGDFILGNVLTDSLE- 291
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 38703987   299 mnSVQLTAQKKRI-------SAKCQQ-CAYKPICNGGCP 329
Cdd:TIGR04261 292 --SACQTEKFQKLyqdmtagVELCRQtCDYFGLCGGGAG 328
rSAM_pep_methan TIGR04083
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ...
2-360 9.09e-33

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: 126.38  E-value: 9.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     2 HVTAKPSsFQCNLKCDYCFYLEKESQFthekwMDDSTLKEFIKQYIAASGNQVYFTWQGGEPTLAGLDFFRKVIHYQQRY 81
Cdd:TIGR04083   1 HVMIIPT-LGCPSKCKYCWSSEETSPV-----MSIDTVKDIVEWLKDFRDDRVTFTFHGGEPLLAGADFYRQALPLLSEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    82 AGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRrsnsGNGTFAKVIAAIERLKSYQVEFNTLTVIN 161
Cdd:TIGR04083  75 LAHLKPEFAMQTNLWLMTPELAEIFAEYNVPIGSSIDGPEEINDYQR----GEGYYQKTMKGYEIAKEHGLDVRFICTFT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   162 NVNVHYPLEVYHFLKSIGskhmqFIELLETGTPNIdfsgHSENTFRiidFSVPPTAYGKFMSTIFMQWVKNdVGEIFIRQ 241
Cdd:TIGR04083 151 SYSVKQKEEIFNFFLENG-----FTLKLHPALPSL----RSDNPGE---WALDPEEYGELLVYLLDKYLEN-MDKIEVMN 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   242 FESFV-SRFLGNGhTSCIFQESCKDNLVVESNGDIYECDHFV-YPQYKLGNI--NKSELKTMNS---VQLTAQKKRISAK 314
Cdd:TIGR04083 218 INDLCrCVFTRRG-TVCTFVDCMGTTFAVGPDGSIYPCYRFVgMPEYVMGNVrdRPTMEDLMESdagKLMLAFKEYVDTH 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 38703987   315 CQQCAYKPICNGGCPKHRI--TKVNDETVSYFCEGYKILFSTMVPYMN 360
Cdd:TIGR04083 297 CAKCSHIKYCRGGCPYNAIapTDGEIKGVDPHCIAYKRIFDEITDRLN 344
SAM_SPASM_FxsB TIGR04269
radical SAM/SPASM domain protein, FxsB family; This model describes a radical SAM (pfam04055) ...
12-332 6.28e-31

radical SAM/SPASM domain protein, FxsB family; This model describes a radical SAM (pfam04055)/SPASM domain (TIGR04085) fusion subfamily distinct from PqqE, MftC, anaerobic sulfatase maturases, and other peptide maturases. The combined region described in this model can itself be fused to another domain, such as TIGR04267, or stand alone. Members occurring in the same cassette as a member of family TIGR04268 should be designated FxsB.


Pssm-ID: 275093 [Multi-domain]  Cd Length: 363  Bit Score: 120.99  E-value: 6.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCFYLEKESQF--THEKWMDDSTLKEF---IKQYIAASG-NQVYFTWQGGEPTLAGLDFFRKVIHyQQRYA--G 83
Cdd:TIGR04269  12 CDLACDHCYVYEHADQSwrARPKVMSAETRRAFarrLAEHAAAHDlPSVAVILHGGEPLLAGAERLRAFAA-ELRSAldP 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    84 QKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTVINNV 163
Cdd:TIGR04269  91 VTALDLRLQTNGVLLDDEALDLLVEHDIGVGVSLDGDRAANDRHRLTRDGRSSHDQVLRALELLRRPEYRHLFAGLLCTV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   164 NVHY-PLEVYHFlksigskhmqfieLLETGTPNIDF---SGHSENTFRIIDFSVPPTAYGKFMSTIFMQWVkNDVGEIFI 239
Cdd:TIGR04269 171 DVANdPVAVYEA-------------LAALDPPRIDFllpHATWDRPPPRRGPDGSPTAYARWLLAVFDRWL-ADGRPMPV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   240 RQFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHF--VYP-QYKLG-NINKSELKTMNSVQLTAQKKR----I 311
Cdd:TIGR04269 237 RTFDSLLSTLRGGPSLTEALGLGPVDLAVIETDGTYEQLDSLkvAYDgAPATGgDVFDHTIDEVAAHPGIAARRAglagL 316
                         330       340
                  ....*....|....*....|.
gi 38703987   312 SAKCQQCAYKPICNGGCPKHR 332
Cdd:TIGR04269 317 SETCRACPVVDSCGGGLYPHR 337
rSAM_ocin_clost TIGR04068
Cys-rich peptide radical SAM maturase CcpM; Members of this family are radical SAM enzymes ...
11-161 3.42e-25

Cys-rich peptide radical SAM maturase CcpM; Members of this family are radical SAM enzymes that occur next to clostridial Cys-rich predicted bacteriocin (or other class of ribosomal natural product) precursors (see families TIGR04065 and TIGR04067). They include a TIGR04085 C-terminal additional 4Fe4S cluster-binding domain that is associated with peptide modification by radical SAM enzymes, and they are proposed to be ribosomal natural product maturases. The gene symbol ccpM is assigned, for Clostridial Cys-rich Peptide Maturase. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274958 [Multi-domain]  Cd Length: 459  Bit Score: 106.23  E-value: 3.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    11 QCNLKCDYCFYLEKESQFTH-EKWMDDSTLKEFIKQYIAASGN--QVYFTWQGGEPTLAgLDFFRKVIHY-QQRYAGQKR 86
Cdd:TIGR04068  91 QCNLRCKYCAYSGSYDNRVHsNKRMSIETAKKAIDFLIKHSEDtdELNLGFYGGEPLLE-FELIKECVEYaKEKAEGKKI 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    87 IFNaLQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSY------QVEFNtlTVI 160
Cdd:TIGR04068 170 NFN-MTTNGTLLTEEIIEFLYDNEFNLTISLDGPKEIHDKNRVFADGKGSFDKIMENIKMIKKKypeyysKVRFN--TVL 246

                  .
gi 38703987   161 N 161
Cdd:TIGR04068 247 D 247
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
12-158 5.33e-25

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: 99.59  E-value: 5.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  12 CNLKCDYCFYlekESQFTHEKWMDDSTLKEFIKQYIAASGNQVYFTwqGGEPTLAGlDFFRKVihyqqRYAGQKRIFNAL 91
Cdd:COG0535  10 CNLRCKHCYA---DAGPKRPGELSTEEAKRILDELAELGVKVVGLT--GGEPLLRP-DLFELV-----EYAKELGIRVNL 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38703987  92 QTNGILLNNEWCAFLKEHEFL-VGISIDGP-QELHDRYRRsnsGNGTFAKVIAAIERLKS--YQVEFNTLT 158
Cdd:COG0535  79 STNGTLLTEELAERLAEAGLDhVTISLDGVdPETHDKIRG---VPGAFDKVLEAIKLLKEagIPVGINTVY 146
rSAM_more_4Fe4S TIGR04085
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ...
263-345 6.75e-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: 6.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   263 CKDNLVVESNGDIYECDHFVYPQYKLGNINKSELKTMNSVQLT-----AQKKRISAKCQQCAYKPICNGGCPKHRITKVN 337
Cdd:TIGR04085   4 GRNSLVVDPDGDVYPCDHFVYPEYKLGNIREDSLEEILNSSKQlefgrWKSPKLPEECRSCKYLPLCGGGCPANRYLKTG 83
                          90
                  ....*....|
gi 38703987   338 D--ETVSYFC 345
Cdd:TIGR04085  84 DinGPKNPLC 93
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
12-171 3.01e-18

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: 81.03  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCFYlEKESQFTHEKWMDDSTLKEFIKQYIAASGNQVYFTwqGGEPTLaGLDFFRKVIHYQQRyAGQKRIFNAL 91
Cdd:pfam04055   5 CNLRCTYCAF-PSIRARGKGRELSPEEILEEAKELKRLGVEVVILG--GGEPLL-LPDLVELLERLLKL-ELAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    92 QTNGILLNNEWCAFLKEHEF-LVGISIDGPqelHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNT--LTVINNVNVHYP 168
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAGLdRVSIGLESG---DDEVLKLINRGHTFEEVLEALELLREAGIPVVTdnIVGLPGETDEDL 156

                  ...
gi 38703987   169 LEV 171
Cdd:pfam04055 157 EET 159
geopep_mat_rSAM TIGR04280
putative geopeptide radical SAM maturase; This family is the radical SAM/SPASM domain putative ...
12-328 5.57e-17

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: 82.06  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCFylekESQFTHEKWMDDSTLKEFI----KQYIAAsGNQVYFTWQGGEPTLAgLDFFRKVIHYQQRYA---GQ 84
Cdd:TIGR04280  94 CNLACPYCF----EGPFRGKRYMDDATADLLVsylvRERLAQ-GRDVSLDFYGGEPLLS-LDLIRRIATPLKAAAasrGL 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    85 KRIFNaLQTNGILLNNEwcafLKEhEFL------VGISIDGPQELHDRYRRSNSGNGTFAKVIA---AIERLKSYQVEFN 155
Cdd:TIGR04280 168 SFSFS-LVTNGTLLTRD----VVE-ELLplgltgAKVTLDGPPEIHDRQRPFVSGKGSFDTIVAnlkAVCDLIAIQIGGN 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   156 tltvinnvnvhYPLEVYHflksigskhmQFIELLETgtpnIDFSGHSENTFRIIDFS-VPPTAyGKFMSTIF-------- 226
Cdd:TIGR04280 242 -----------YTRENYR----------EFPRLLDL----LLAEGLTPERLALVRFSpVVSRA-GGAALPDFnsgcassn 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   227 MQWVKNdvGEIFIRQfESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFV-YPQYKLGNINKSELKTMNSVQLT 305
Cdd:TIGR04280 296 EPWLIE--ASLFLRE-ETLKRGYPVPKLRPGACMVELEDDLVVNHDGTLYKCPAFMgREGLAVGSLADGLSDYRDSHGLD 372
                         330       340
                  ....*....|....*....|...
gi 38703987   306 AQKKRisaKCQQCAYKPICNGGC 328
Cdd:TIGR04280 373 LWKNE---ECLDCAYLPLCFGGC 392
rSAM_FibroRumin TIGR04136
radical SAM peptide maturase, FibroRumin system; Members of this protein family are radical ...
9-329 1.78e-12

radical SAM peptide maturase, FibroRumin system; Members of this protein family are radical SAM enzymes proposed to act on small, Cys-rich peptides encoded by tandem gene pairs. Members occur in enzymes Fibrobacter succinogenes subsp. succinogenes S85 (genes for their target peptides missed) and in Ruminococcus albus 8. This enzyme family is similar in sequence to the SCIFF (Six Cysteines in Forty-Five) system maturase (TIGR03974).


Pssm-ID: 200387 [Multi-domain]  Cd Length: 458  Bit Score: 68.45  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     9 SFQCNLKCDYCFY----LEKESQFTHE---KWMDDSTLKEFIKQYIA----ASGNQVYFTWQGGEPtLAGLDFFRKVIH- 76
Cdd:TIGR04136  98 SEQCNLACKYCFLgnndKEKRHNFAKElmsKEIADKAIEFFIKQLEAseldAEDNKAAIIFYGGEP-LMNFETLKYVAEk 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    77 YQQRYAGQKRIFNA---LQTNGILLNNEWCAFLKEHEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSYQVE 153
Cdd:TIGR04136 177 FNSLKSEEKCLENAefsMVSNGLLLSEERIIELRDLGVSIAISIDGCDEAANAMRVDLAGNIVFPKILETLDIAKELGVN 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   154 FNTLTVINNVNVHYPLEVYHFLKSIGSKHMQFielletgtpNIDFSGHsenTFriidfsVPPTAY----GKFMSTIFMQW 229
Cdd:TIGR04136 257 VSLSITLSEETIKDQQDVIDLIDEYGIKGLGF---------NIMMGDD---RF------PLPADYndkaAQFIIDEFKEL 318
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   230 VKNDVGE-IFIRQFESFVSR---FLGNGHTScifqescKDNLVVESNGDIYECDHFVYPQ-YKLGNINKSELKTMNS--- 301
Cdd:TIGR04136 319 REIGIYEdRIMRKLKAFAKAqvyFSDCAATG-------AGQIVIAADGAVGICHGCLFDKkYFNSCIDDDDFNAIDDptf 391
                         330       340       350
                  ....*....|....*....|....*....|.
gi 38703987   302 ---VQLTAQKKRisaKCQQCAYKPICNGGCP 329
Cdd:TIGR04136 392 iewNHLSPIEKD---ECQDCEALGICGGGCP 419
rSAM_AF0577 TIGR04084
putative peptide-modifying radical SAM enzyme, AF0577 family; This radical SAM family contains ...
12-328 1.75e-11

putative peptide-modifying radical SAM enzyme, AF0577 family; This radical SAM family contains a C-terminal region motif CXXCX5CX3C that is found in PqqE and other radical SAM enzymes that act on peptide substrates. Members of this family are found primarily in the Archaea, but also several eukaryotes (Trichomonas vaginalis G3, Entamoeba dispar SAW760, Giardia intestinalis ATCC 50581, etc.). The function is unknown.


Pssm-ID: 274967 [Multi-domain]  Cd Length: 347  Bit Score: 64.77  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCFYLEKESQFTHEKWMDDSTLKEFIKQYIAASgnqVYFtwQGGEPtLAGLDFFRKVIH--YQQRYagqkrifn 89
Cdd:TIGR04084   7 CNLRCDYCGGSFPEKVVPWRIKYDINKLKNLIEKDKDAT---VIF--YGGEP-LLNPRFIMQVMDnvRAKRF-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    90 ALQTNGILLNNEWCAFLKEHEfLVGISIDGPQELHDRYRrsnsGNGTFAKVIAAIERLKSYQVE-FNTLTVINNVNVHyp 168
Cdd:TIGR04084  73 GIQTNGTLVKLLPEEYWRRMN-VALLSIDGRPEVTDKHR----GKGVYKRVVKAARYLKELGVEtIARMAVTEDSDIY-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   169 LEVYHFLkSIGSKHMQFiELLETGTPNIDFSGHSENTF-----RIIDFSVPPTAYGKFMSTIFMQwvkndvGEIFIRQFE 243
Cdd:TIGR04084 146 RDVTHLL-SLGFDKVHW-QLNVVWDDEWDFLSWAKNSYlpgirKLVDLFLSELREGRVLGIVPIL------GVISAYFFK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   244 SFVSRFLGNGHtscifqesckDNLVVESNGDIYECDHFVYPQY-KLGNINKSELKTMNSvqltaqkkRISAKCQQCAYKP 322
Cdd:TIGR04084 218 PYRGVPCGAGY----------DSFAITTDGRILSCPIAVREKWaELGNVNVGFRLLEEP--------VLPEECLSCEYRR 279

                  ....*.
gi 38703987   323 ICNGGC 328
Cdd:TIGR04084 280 YCGGRC 285
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
11-329 1.77e-10

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: 61.80  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    11 QCNLKCDYCFYLEKESQFTHE----KWMddstlkEFIKQYIAASGNQVyfTWQGGEPtlagldFFRKVIHYQQRYAGQKR 86
Cdd:TIGR04250  12 RCNLRCRYCSHFSSAAETPTDletaEWL------RFFRELNRCSVLRV--VLSGGEP------FMRSDFREIIDGIVKNR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    87 IFNALQTNGILLNNEWCAFLKEHEFL--VGISIDGPQ-ELHDRYRrsnsGNGTFAKVIAAIERLKSYQVEFNTLTVINNV 163
Cdd:TIGR04250  78 MRFSILSNGTLITDAIASFLAATRRCdyVQVSIDGSTpGTHDRLR----GTGSFLQAVEGIELLRKHAIPVVVRVTIHRW 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   164 NVHYplevyhfLKSIGSKHMQFIELLETGTPNIDFSGHSENTFRIIDFSVppTAYGKFMSTIfMQWVKNDVGEIF----- 238
Cdd:TIGR04250 154 NVDD-------LRPIAALLLDDLGLPAFSTNAASYMGLCRSNTDDVQLDT--AERTLAMEIL-LELEKEYPGRISasagp 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   239 ---IRQFESF-------VSRFLGNGHTS---CIFQEsckdnLVVESNGDIYECDHFVYpqYKLGNINKSELKTM--NSVQ 303
Cdd:TIGR04250 224 ladARTWASMeqaridqQGNMPGRGYLSgcgGIFMS-----LAVRADGVIVPCNQLSH--IELGRINRDSLRELwqNHPV 296
                         330       340       350
                  ....*....|....*....|....*....|..
gi 38703987   304 LTAQKKRISAK------CQQCAYKPICNGGCP 329
Cdd:TIGR04250 297 LLQLRNRVTIPltdfefCKDCDYIPYCTGNCP 328
moaA PRK00164
GTP 3',8-cyclase MoaA;
12-201 2.48e-09

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 58.23  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   12 CNLKCDYCFYLEKESQFTHEKWMDDSTLKEFIKQYIAASGNQVYFTwqGGEPTL-AGLDFFRKVIHyqqRYAGQKRIfnA 90
Cdd:PRK00164  27 CNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLT--GGEPLLrKDLEDIIAALA---ALPGIRDL--A 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   91 LQTNGILLNN---EWC-AFLKEheflVGISIDGpqeLH-DRYRRSNsGNGTFAKVIAAIERLKS---YQVEFNTLtVINN 162
Cdd:PRK00164 100 LTTNGYLLARraaALKdAGLDR----VNVSLDS---LDpERFKAIT-GRDRLDQVLAGIDAALAaglTPVKVNAV-LMKG 170
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 38703987  163 VNVHYPLEVYHFLKSIGSkHMQFIELLETGTPNIDFSGH 201
Cdd:PRK00164 171 VNDDEIPDLLEWAKDRGI-QLRFIELMPTGEGNEWFRKH 208
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
12-185 2.97e-09

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


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 58.05  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   12 CNLKCDYC--------------FYLEKESQFTHEKWMDDstlKEFIKQYIAASGN--QVYFTwqGGEPTLAG--LDFFRK 73
Cdd:NF033640 120 CNLKCRMCgphsssswakeakkLGGPKLGDKKKISWFED---EEFWKWLEELLPSlkEIYFA--GGEPLLIKehYKLLEK 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   74 VIhyQQRYAGQKRIFnaLQTNGILLNNEWCAFLKE----HEFLVGISIDGPQELHDrYRRSNSgngTFAKVIAAIERLKS 149
Cdd:NF033640 195 LV--EKGRAKNIELR--YNTNLTVLPDKLKDLLDLwkkfKSVSISASIDGVGERNE-YIRYGS---KWDEIEKNLKKLKE 266
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 38703987  150 Y--QVEFNTLTVINNVNVHYPLEVYHFLKSIGSKHMQF 185
Cdd:NF033640 267 EcpNVELRINPTVSALNVLHLPELLDWLLELGLGPIDI 304
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
11-164 4.37e-09

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: 55.80  E-value: 4.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  11 QCNLKCDYCfylekeSQFTHEKWMDDSTLKEFIKQ---YIAASGNQVYFTWQGGEPTL--AGLDFFRKVIhyqqRYAGQK 85
Cdd:cd01335   6 GCNLNCGFC------SNPASKGRGPESPPEIEEILdivLEAKERGVEVVILTGGEPLLypELAELLRRLK----KELPGF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  86 RIFnaLQTNGILLNNEWCAFLKEHEFL-VGISIDGPQELHdrYRRSNSGNGTFAKVIAAIERLKSYQVEFN-TLTVINNV 163
Cdd:cd01335  76 EIS--IETNGTLLTEELLKELKELGLDgVGVSLDSGDEEV--ADKIRGSGESFKERLEALKELREAGLGLStTLLVGLGD 151

                .
gi 38703987 164 N 164
Cdd:cd01335 152 E 152
SPASM_CteB-like cd21124
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ...
265-349 3.63e-08

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: 50.81  E-value: 3.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987 265 DNLVVESNGDIYECDHFV-YPQYKLGNInkSELKTMNSVQLTAQKKRI--SAKCQQCAYKPICNGGCPKHRITKVND--E 339
Cdd:cd21124   9 EYFAVDPDGDIYPCHRFVgMEEYRMGNV--YDGSSLMELQSEFWKRHVenKEECRECWARFYCGGGCPANSYAENGDirT 86
                        90
                ....*....|
gi 38703987 340 TVSYFCEGYK 349
Cdd:cd21124  87 PYEPYCEIYK 96
SPASM_AlbA-like cd21125
Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis ...
267-328 2.69e-07

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: 48.26  E-value: 2.69e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 38703987 267 LVVESNGDIYECDHFVYPQYKLGNINKSE----LKTMNSVQLTAQKKRISAKCQQCAYKPICNGGC 328
Cdd:cd21125  10 IVIDPDGEVYPCHLLHPTEFKLGNIFEDSlasiLKNPVLEIWQTYDPRFSEHCKKCPFYGICGGGC 75
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
12-201 3.95e-06

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: 48.13  E-value: 3.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  12 CNLKCDYCFYLEKESQFTHEKWMDDSTLKEFIKqyIAAS-G-NQVYFTwqGGEPTL-AGL-DFFRKVihyqQRYAGQKRI 87
Cdd:COG2896  24 CNFRCTYCMPEEGYQFLPKEELLSFEEIERLVR--AFVElGvRKIRLT--GGEPLLrKDLpELIARL----AALPGIEDL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  88 fnALQTNGILLnnewcaflkeHEFL----------VGISIDGpqeLH-DRYRRSNsGNGTFAKVIAAIERLKS---YQVE 153
Cdd:COG2896  96 --ALTTNGSLL----------ARYAealkaagldrVNVSLDS---LDpERFRRIT-RRDDLDKVLAGIDAALAaglTPVK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 38703987 154 FNTLtVINNVNVHyplEVYHFLKSIGSK--HMQFIELLETGTPNIDFSGH 201
Cdd:COG2896 160 INAV-VMRGVNDD---EILDLLEFAKERgiDLRFIELMPLGEGGGWRRDQ 205
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
12-164 9.60e-06

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 46.33  E-value: 9.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  12 CNLKCDYC--FYLEKESQFTHEKWMDDSTLKEFIKQYIA--ASGNQVYFTwqGGEPTLAgLDFFRKVIhyqqRYAGQKRI 87
Cdd:COG1180  31 CNLRCPYChnPEISQGRPDAAGRELSPEELVEEALKDRGflDSCGGVTFS--GGEPTLQ-PEFLLDLA----KLAKELGL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  88 FNALQTNGILLNNEWCAFLkehEFLVGISID---GPQELHDRY-RRSNsgngtfAKVIAAIERLKSYQVEFN-TLTVINN 162
Cdd:COG1180 104 HTALDTNGYIPEEALEELL---PYLDAVNIDlkaFDDEFYRKLtGVSL------EPVLENLELLAESGVHVEiRTLVIPG 174

                ..
gi 38703987 163 VN 164
Cdd:COG1180 175 LN 176
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
5-326 1.27e-05

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: 46.80  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987     5 AKPSSFQ----CNLKCDYCfYLEKESQFTHEKWMDDSTLKEFIKQYIAASGNQ-VYFTWQGGEPTLAgLDFFRKVIHYQQ 79
Cdd:TIGR04115   1 AKSITFIvtddCQLACKYC-YQTGKNKNKRMSFETAKKAVDYILSGNKGFGEPsVIWDFIGGEPLLE-IELIDRICDYIK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    80 R--YAGQKRIFN----ALQTNGILLNNEWCA-FLKE--HEFLVGISIDGPQELHDRYRRSNSGNGTFAKVIAAIERLKSY 150
Cdd:TIGR04115  79 NrmIELNHPWFNsyrfSFSTNGVCYFEEKVQrFIQKnnQHLSISITIDGTKEKHDSCRVFPDGRGSYDLVVSNAPLWLNQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   151 QVEFNTLTVINNVNVHYPLEvyhflksigskhmQFIELLETGTPNIDFSGHSENTFRIIDFSVPPTAYGKFMSTIFMQWV 230
Cdd:TIGR04115 159 FPYASTKVTIAPADVPHVKE-------------SVTHLIDLGYNEVNINCVYEEGWQMGDDTVFEDQLKKLADYILEHDM 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   231 KNDvgeifirQFESFVSRFLGNghtscifQESCK-DN---------LVVESNGDIYECDHFV------YPQYKLGNINKS 294
Cdd:TIGR04115 226 YND-------YYCSFFSENFGH-------PLDCKlDNenwcgggvmLAVDPDGIFYPCLRFAeyslrqKEAYSIGNVDDG 291
                         330       340       350
                  ....*....|....*....|....*....|..
gi 38703987   295 elKTMNSVQLTAQKKRISAKCQQCAYKPICNG 326
Cdd:TIGR04115 292 --IDRNRVRPFLKLDRRTQSTDECINCPVASG 321
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
12-185 1.87e-04

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: 43.29  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCF----YLEKESQFTHekwMDDSTLKEFIKQYIAASGNQVYFTwqGGEPTL-AGLDFFRKVIhyqqryaGQKR 86
Cdd:TIGR04251  14 CNLKCRHCWidpkYQGEGEQHPS---LDPSLFRSIIRQAIPLGLTSVKLT--GGEPLLhPAIGEILECI-------GENN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    87 IFNALQTNGILLNNEWCAFLKEHEF-LVGISIDGPQ-ELHDRYRRSnsgNGTFAKVIAAIERLKSYQVEFNTLTVINNVN 164
Cdd:TIGR04251  82 LQLSVETNGLLCTPQTARDLASCETpFVSVSLDGVDaATHDWMRGV---KGAFDKAVRGIHNLVEAGIHPQIIMTVTRRN 158
                         170       180
                  ....*....|....*....|.
gi 38703987   165 VHYPLEVYHFLKSIGSKHMQF 185
Cdd:TIGR04251 159 VGQMEQIVRLAESLGAESVKF 179
SPASM_MftC-like cd21123
Iron-sulfur cluster-binding SPASM domain of mycofactocin radical SAM maturase MftC and similar ...
269-328 5.17e-04

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: 38.78  E-value: 5.17e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 38703987 269 VESNGDIYECdhfVYPQYKLGNINKSELKT--MNSVQLTAQKKR--ISAKCQQCAYKPICnGGC 328
Cdd:cd21123  13 ISPDGDVYPC---GFLPFSAGNVREDSFKDiwENSELFKKLRDRefLKGKCGKCKYRNVC-GGC 72
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
12-126 7.08e-04

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: 39.46  E-value: 7.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987    12 CNLKCDYCFylEKESQ-FTHEKWMDDSTLKEFIKQYIAASGNQVYFTwqGGEPtLAGLDFFRKVIHYQQRYAGQKRI--F 88
Cdd:pfam13353  15 CNHHCKGCF--NPETWdFKYGKPFTEELEDEIIEDLAKPYIQGLTLS--GGEP-LLNAEALLELVKRVREECPEKDIwlW 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 38703987    89 NALqTNGILLNNEWCAFLKEHEFLVgisiDGP--QELHDR 126
Cdd:pfam13353  90 TGY-TFEELQSKDQLELLKLIDVLV----DGKfeQSLKDP 124
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
11-160 1.56e-03

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: 39.79  E-value: 1.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  11 QCNLKCDYCfYLEKESQFTHEKWMDDST------LKEFIKQ---------YIAASGNqvyftwqgGEPTLA-GLDffrKV 74
Cdd:COG0731  33 TCNFDCVYC-QRGRTTDLTRERREFDDPeeileeLIEFLRKlpeearepdHITFSGS--------GEPTLYpNLG---EL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987  75 IHYQQRYAGqKRIFnaLQTNGILLNNEW-CAFLKEHEfLVGISIDGPQElhDRYRRSN--SGNGTFAKVIAAIERLKSyq 151
Cdd:COG0731 101 IEEIKKLRG-IKTA--LLTNGSLLHRPEvREELLKAD-QVYPSLDAADE--ETFRKINrpHPGLSWERIIEGLELFRK-- 172

                ....*....
gi 38703987 152 vEFNTLTVI 160
Cdd:COG0731 173 -LYKGRTVI 180
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
265-318 2.16e-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: 36.30  E-value: 2.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38703987   265 DNLVVESNGDIYEC-DHFVYPQYKLGNINKSELKTM-NSVQLTA----QKKRISAKCQQC 318
Cdd:pfam13186   6 TSLVILPDGDVYPCfDDDFVGPIVLGNIREQSLAEIwNSPKYREfrklGKFALIELCRDC 65
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
265-318 2.67e-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: 35.86  E-value: 2.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 38703987 265 DNLVVESNGDIYECDHFVYPQYKLGNINKSELKTM-NSVQLT----AQKKRISAKCQQC 318
Cdd:cd21109   7 TSLYITPDGDVYPCCFDVNEELKLGNIREQSLKEIwNSEKYRefrkLLLDGKIKLCKNC 65
 
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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