NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|517956898|ref|WP_019127106|]
View 

anaerobic sulfatase maturase [Actinomyces sp. ph3]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
sulfatase_rSAM super family cl33218
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
12-392 3.63e-172

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]


The actual alignment was detected with superfamily member TIGR03942:

Pssm-ID: 188457 [Multi-domain]  Cd Length: 363  Bit Score: 485.96  E-value: 3.63e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   12 SVVAKPTGAACNLDCQYCFFLSKELLYDQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGLPFFERLIELCE 91
Cdd:TIGR03942   1 HVMAKPTGAKCNLDCDYCFYLEKEDLYPKPKPKMSDETLETFIKQYIASQDGPEVNFAWQGGEPTLAGLDFYRKAVELQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   92 KYRrPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNILC 171
Cdd:TIGR03942  81 RYA-PGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFERVMRALKLLKEHNVEFNTLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  172 TVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPrehlrqaelgwrsgssallyrqDGDCVTSRSTSPEGYGNFLCSI 251
Cdd:TIGR03942 160 VVNNHNARHGKEVYRFLK-ELGSRYMQFIPCVEPDN----------------------ATREVTDWSVTPKDYGRFLCDV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  252 FDEWVCSDVGSVFVQDFDSSISALFGS-ASVCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKM 330
Cdd:TIGR03942 217 FDEWVKNDVGRVFIRNFENALAIWLGNpSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLGNINETSLAEMASSEKQ 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517956898  331 RAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHALPYFKAM 392
Cdd:TIGR03942 297 KQFGQAKSLsLPEKCRRCDVLFLCNGGCPKHRILATPGGeNGHNYLCAGYKAFFSHTLPYLQAM 360
 
Name Accession Description Interval E-value
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
12-392 3.63e-172

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: 485.96  E-value: 3.63e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   12 SVVAKPTGAACNLDCQYCFFLSKELLYDQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGLPFFERLIELCE 91
Cdd:TIGR03942   1 HVMAKPTGAKCNLDCDYCFYLEKEDLYPKPKPKMSDETLETFIKQYIASQDGPEVNFAWQGGEPTLAGLDFYRKAVELQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   92 KYRrPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNILC 171
Cdd:TIGR03942  81 RYA-PGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFERVMRALKLLKEHNVEFNTLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  172 TVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPrehlrqaelgwrsgssallyrqDGDCVTSRSTSPEGYGNFLCSI 251
Cdd:TIGR03942 160 VVNNHNARHGKEVYRFLK-ELGSRYMQFIPCVEPDN----------------------ATREVTDWSVTPKDYGRFLCDV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  252 FDEWVCSDVGSVFVQDFDSSISALFGS-ASVCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKM 330
Cdd:TIGR03942 217 FDEWVKNDVGRVFIRNFENALAIWLGNpSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLGNINETSLAEMASSEKQ 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517956898  331 RAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHALPYFKAM 392
Cdd:TIGR03942 297 KQFGQAKSLsLPEKCRRCDVLFLCNGGCPKHRILATPGGeNGHNYLCAGYKAFFSHTLPYLQAM 360
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
12-386 4.06e-122

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: 4.06e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  12 SVVAKPTgAACNLDCQYCFFLSKellYDQKRQSMSEETLETYVKNFLSASLDG-EVTMLWQGGEPTLRgLPFFERLIELC 90
Cdd:COG0641    2 ALVLKPT-SRCNLRCSYCYYSEG---DEGSRRRMSEETAEKAIDFLIESSGPGkELTITFFGGEPLLN-FDFIKEIVEYA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  91 EKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNIL 170
Cdd:COG0641   77 RKYAKKGKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVMRNIKLLKEHGVEVNIR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 171 CTVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPREHlrqaelgwrsgssallyrqdgdcvtsrSTSPEGYGNFLCS 250
Cdd:COG0641  157 CTVTRENLDDPEELYDFLK-ELGFRSIQFNPVVEEGEADY---------------------------SLTPEDYGEFLIE 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 251 IFDEWVCSDVGSVFVQDFDSSISALFG-SASVCVhaPSCGANMAMEFNGDVYACDHWV-EPEWLVGNIANSDFPTLATSE 328
Cdd:COG0641  209 LFDEWLERDGGKIFVREFDILLAGLLPpCSSPCV--GAGGNYLVVDPDGDIYPCDEFVgDPEFRLGNVFDGSLAELLDSP 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 329 KMRAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHAL 386
Cdd:COG0641  287 KLRAFGREKNVlLDEECRSCPYLPLCGGGCPANRYAETGDGfKPYSYYCELYKKLFEHAL 346
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
10-392 9.57e-115

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 341.84  E-value: 9.57e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  10 PFSVVAKPTGAACNLDCQYCFFLSKELLY-DQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGLPFFERLIE 88
Cdd:PRK13745  12 PLYIMLKPVGAVCNLACDYCYYLEKSKLYqENPKHVMSDELLEKFIKEYINSQTMPQVLFTWHGGETLMRPLSFYKKALE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  89 LCEKYRRPTQeVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTN 168
Cdd:PRK13745  92 LQKKYARGRQ-IDNCIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEFHDEYRKNKMGKPSFVKVMKGINLLKKHGVEWN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 169 ILCTVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPR--EHLRQAELGwrsgssallyRQDGDCVTSRSTSPEGYGN 246
Cdd:PRK13745 171 AMAVVNDFNADYPLDFYHFFK-ELDCHYIQFAPIVERIVShqDGRHLASLA----------QQEGGELAPFSVTPEQWGN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 247 FLCSIFDEWVCSDVGSVFVQDFDSSISALFGSA-SVCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLA 325
Cdd:PRK13745 240 FLCTIFDEWVKEDVGKYYIQLFDSTLANWVGEQpGVCSMAKHCGHAGVMEFNGDVYSCDHFVFPEYKLGNIYQQTLVEMM 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517956898 326 TSEKMRAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHALPYFKAM 392
Cdd:PRK13745 320 YSERQTAFGTMKYKsLPTQCKECEYLFACHGECPKNRFCRTANGePGLNYLCKGYHQFFKHVAPYMDFM 388
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
1-384 5.53e-53

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: 182.39  E-value: 5.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   1 MTHSPAPTLPFSVVAKPTgAACNLDCQYCFFLSkellyDQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGL 80
Cdd:NF041300  31 LPPTRSPARWLVVVLKAT-RLCNLRCTYCRSWA-----EGPNQTMTFDVLARAVREALSMPGLHGVEFVWHGGEVTLLKP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  81 PFFERLIELCEKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHL 160
Cdd:NF041300 105 KVFKKLIWLQQQFRQPGQEVRNSIQTNATHLTDEWIEFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIARL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 161 RNADVDTNILCTVHAANEDHGLEVYRYFRDELGAQYMQFIPIverVPREHlrqaelgwrsgssallyrqDGDCVTSRSTS 240
Cdd:NF041300 185 RQAGIPHGALVVVDRELIDAGAERLLGYLAEIGLDKISFLNV---LPEND-------------------PDDPEIVKSTY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 241 ---PEgYGNFLCSIFDEWVCSDVGSVFVQDFDSSISALFGSAS--VCVHAPSC-GANMAMEFNGDVYACDHWV-EPEWLV 313
Cdd:NF041300 243 ftfPE-YVRFLTETFDVWWNSYRDRMEIREFRDLIPKMSVGAKpiGCYWMGNCmGRYVTLEANGDLAPCDKYRgDPGSIL 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517956898 314 GNIANSDFP-TLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKDRFITTDSGPSHNYLCQGYRRFYSH 384
Cdd:NF041300 322 GNVMHSPMAdIIRTSGYLADAKKEASDAKTRMAPCKWFHVCQGGCPHDRHLNSRFVPAVDPRCCGLAPLLDH 393
SPASM_anSME cd21120
Iron-sulfur cluster-binding SPASM domain of anaerobic sulfatase maturating enzyme; Anaerobic ...
281-387 1.26e-46

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: 155.90  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 281 VCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKD 360
Cdd:cd21120    1 SCVMSGTCGDNLVVEHNGDVYPCDHFVLPEYRLGNIQEQTLAELVDSEKQQQFGAQKFKLPAECKQCKYLFACHGGCPKH 80
                         90       100
                 ....*....|....*....|....*..
gi 517956898 361 RFITTDSGPSHNYLCQGYRRFYSHALP 387
Cdd:cd21120   81 RFAKGPSEPGLNYLCEGYKEFFEHLLP 107
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
22-173 3.55e-16

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: 75.64  E-value: 3.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFFlsKELLYDQKRQSMSEETLETYVKNFLSAsldGEVTMLWQGGEPTLRgLPFFERLIELCEKYRRPtqEVR 101
Cdd:pfam04055   5 CNLRCTYCAF--PSIRARGKGRELSPEEILEEAKELKRL---GVEVVILGGGEPLLL-PDLVELLERLLKLELAE--GIR 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517956898  102 HAIQTNGTLITEQWARFFKD-NDVLVGISIDGPkdlHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNILCTV 173
Cdd:pfam04055  77 ITLETNGTLLDEELLELLKEaGLDRVSIGLESG---DDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIV 146
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
21-131 4.34e-07

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 51.01  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  21 ACNLDCQYCF--FLSKELLyDQKRQSMSEETLETYVKNFLSASLDGE----VtmlwqGGEPTLrgLPffERLIELcekyr 94
Cdd:NF038283  11 ACNYRCKYCFakWNDVKSP-RHHDKGHLEKLLEELAEFFKLLSYGFVrinfA-----GGEPLL--YP--DRLLDL----- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517956898  95 rptqeVRHAIQ--------TNGTLITEQWARFFKDNDVLVGISID 131
Cdd:NF038283  76 -----IKLAKElgfktsiiTNGSLLTEEFLEELAPYLDWIGISID 115
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
10-163 5.07e-04

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 41.23  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898    10 PFSVVAKPTGaaCNLDCQYCFFLSKELlydqKRQSMSEETLETYVKNFLSASLDG--EVTMLWQGGEPTLRGLPFFERLI 87
Cdd:smart00729   1 PLALYIITRG--CPRRCTFCSFPSLRG----KLRSRYLEALVREIELLAEKGEKEglVGTVFIGGGTPTLLSPEQLEELL 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517956898    88 ELCEKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVL-VGISID-GPKDLHDayRLNRGghGTHSMVIRGWEHLRNA 163
Cdd:smart00729  75 EAIREILGLAKDVEITIETRPDTLTEELLEALKEAGVNrVSLGVQsGDDEVLK--AINRG--HTVEDVLEAVELLREA 148
 
Name Accession Description Interval E-value
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
12-392 3.63e-172

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: 485.96  E-value: 3.63e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   12 SVVAKPTGAACNLDCQYCFFLSKELLYDQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGLPFFERLIELCE 91
Cdd:TIGR03942   1 HVMAKPTGAKCNLDCDYCFYLEKEDLYPKPKPKMSDETLETFIKQYIASQDGPEVNFAWQGGEPTLAGLDFYRKAVELQQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   92 KYRrPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNILC 171
Cdd:TIGR03942  81 RYA-PGKTISNSLQTNGILLNDEWAEFFKEHNFLVGISIDGPKELHDKYRVTKSGKGTFERVMRALKLLKEHNVEFNTLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  172 TVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPrehlrqaelgwrsgssallyrqDGDCVTSRSTSPEGYGNFLCSI 251
Cdd:TIGR03942 160 VVNNHNARHGKEVYRFLK-ELGSRYMQFIPCVEPDN----------------------ATREVTDWSVTPKDYGRFLCDV 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  252 FDEWVCSDVGSVFVQDFDSSISALFGS-ASVCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKM 330
Cdd:TIGR03942 217 FDEWVKNDVGRVFIRNFENALAIWLGNpSQSCVHSPTCGQNLVVESNGDVYSCDHYVYPEYKLGNINETSLAEMASSEKQ 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517956898  331 RAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHALPYFKAM 392
Cdd:TIGR03942 297 KQFGQAKSLsLPEKCRRCDVLFLCNGGCPKHRILATPGGeNGHNYLCAGYKAFFSHTLPYLQAM 360
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
12-386 4.06e-122

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: 4.06e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  12 SVVAKPTgAACNLDCQYCFFLSKellYDQKRQSMSEETLETYVKNFLSASLDG-EVTMLWQGGEPTLRgLPFFERLIELC 90
Cdd:COG0641    2 ALVLKPT-SRCNLRCSYCYYSEG---DEGSRRRMSEETAEKAIDFLIESSGPGkELTITFFGGEPLLN-FDFIKEIVEYA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  91 EKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNIL 170
Cdd:COG0641   77 RKYAKKGKKIRFSIQTNGTLLDDEWIDFLKENGFSVGISLDGPKEIHDRNRVTKNGKGSFDRVMRNIKLLKEHGVEVNIR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 171 CTVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPREHlrqaelgwrsgssallyrqdgdcvtsrSTSPEGYGNFLCS 250
Cdd:COG0641  157 CTVTRENLDDPEELYDFLK-ELGFRSIQFNPVVEEGEADY---------------------------SLTPEDYGEFLIE 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 251 IFDEWVCSDVGSVFVQDFDSSISALFG-SASVCVhaPSCGANMAMEFNGDVYACDHWV-EPEWLVGNIANSDFPTLATSE 328
Cdd:COG0641  209 LFDEWLERDGGKIFVREFDILLAGLLPpCSSPCV--GAGGNYLVVDPDGDIYPCDEFVgDPEFRLGNVFDGSLAELLDSP 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 329 KMRAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHAL 386
Cdd:COG0641  287 KLRAFGREKNVlLDEECRSCPYLPLCGGGCPANRYAETGDGfKPYSYYCELYKKLFEHAL 346
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
10-392 9.57e-115

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 341.84  E-value: 9.57e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  10 PFSVVAKPTGAACNLDCQYCFFLSKELLY-DQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGLPFFERLIE 88
Cdd:PRK13745  12 PLYIMLKPVGAVCNLACDYCYYLEKSKLYqENPKHVMSDELLEKFIKEYINSQTMPQVLFTWHGGETLMRPLSFYKKALE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  89 LCEKYRRPTQeVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTN 168
Cdd:PRK13745  92 LQKKYARGRQ-IDNCIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEFHDEYRKNKMGKPSFVKVMKGINLLKKHGVEWN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 169 ILCTVHAANEDHGLEVYRYFRdELGAQYMQFIPIVERVPR--EHLRQAELGwrsgssallyRQDGDCVTSRSTSPEGYGN 246
Cdd:PRK13745 171 AMAVVNDFNADYPLDFYHFFK-ELDCHYIQFAPIVERIVShqDGRHLASLA----------QQEGGELAPFSVTPEQWGN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 247 FLCSIFDEWVCSDVGSVFVQDFDSSISALFGSA-SVCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLA 325
Cdd:PRK13745 240 FLCTIFDEWVKEDVGKYYIQLFDSTLANWVGEQpGVCSMAKHCGHAGVMEFNGDVYSCDHFVFPEYKLGNIYQQTLVEMM 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517956898 326 TSEKMRAFDTKKQD-LDDECWSCPFLRLCWGGCPKDRFITTDSG-PSHNYLCQGYRRFYSHALPYFKAM 392
Cdd:PRK13745 320 YSERQTAFGTMKYKsLPTQCKECEYLFACHGECPKNRFCRTANGePGLNYLCKGYHQFFKHVAPYMDFM 388
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
10-387 5.27e-76

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 241.36  E-value: 5.27e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  10 PFSVVAKPTGAACNLDCQYCFFLSkeLLYDQKRQS---MSEETLETYVKNFLSASlDGEVTMLWQGGEPTLRGLPFFERL 86
Cdd:PRK13758   3 PLSLLIKPASSGCNLKCTYCFYHS--LSDNRNVKSygiMRDEVLESMVKRVLNEA-EGHCSFAFQGGEPTLAGLEFFEEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  87 IELCEKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVD 166
Cdd:PRK13758  80 MELQRKHNYKNLKIYNSLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEIHNLNRKDCCGLDTFSKVERAAELFKKYKVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 167 TNILCTVHAANEDHGLEVYRYFRDElGAQYMQFIPIVERV--PREHlrqaelgwrsgssallyrqdgdcvTSRSTSPEGY 244
Cdd:PRK13758 160 FNILCVVTSNTARHVNKIYKYFKEK-DFKFLQFINCLDPLyeEKGK------------------------YNYSLKPKDY 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 245 GNFLCSIFDEWVCS--DVGSVFVQDFDSSISALF-GSASVCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDF 321
Cdd:PRK13758 215 TKFLKNLFDLWYEDflNGNRVSIRYFDGLLETILlGKSSSCGMNGTCTCQFVVESDGSVYPCDFYVLDKWRLGNIQDMTM 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517956898 322 PTLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKDRFITTDSGPSHNYLCQGYRRFYSHALP 387
Cdd:PRK13758 295 KELFETNKNHEFIKSSFKVHEECKKCKWFPLCKGGCRRCRDSKEDSGLELNYYCQSYKEFFEYAFP 360
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
1-384 5.53e-53

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: 182.39  E-value: 5.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   1 MTHSPAPTLPFSVVAKPTgAACNLDCQYCFFLSkellyDQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGL 80
Cdd:NF041300  31 LPPTRSPARWLVVVLKAT-RLCNLRCTYCRSWA-----EGPNQTMTFDVLARAVREALSMPGLHGVEFVWHGGEVTLLKP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  81 PFFERLIELCEKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHL 160
Cdd:NF041300 105 KVFKKLIWLQQQFRQPGQEVRNSIQTNATHLTDEWIEFLSELGMGVGVSIDGPPEVHDRRRLDKDGRPTSSRVAGGIARL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 161 RNADVDTNILCTVHAANEDHGLEVYRYFRDELGAQYMQFIPIverVPREHlrqaelgwrsgssallyrqDGDCVTSRSTS 240
Cdd:NF041300 185 RQAGIPHGALVVVDRELIDAGAERLLGYLAEIGLDKISFLNV---LPEND-------------------PDDPEIVKSTY 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 241 ---PEgYGNFLCSIFDEWVCSDVGSVFVQDFDSSISALFGSAS--VCVHAPSC-GANMAMEFNGDVYACDHWV-EPEWLV 313
Cdd:NF041300 243 ftfPE-YVRFLTETFDVWWNSYRDRMEIREFRDLIPKMSVGAKpiGCYWMGNCmGRYVTLEANGDLAPCDKYRgDPGSIL 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517956898 314 GNIANSDFP-TLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKDRFITTDSGPSHNYLCQGYRRFYSH 384
Cdd:NF041300 322 GNVMHSPMAdIIRTSGYLADAKKEASDAKTRMAPCKWFHVCQGGCPHDRHLNSRFVPAVDPRCCGLAPLLDH 393
SPASM_anSME cd21120
Iron-sulfur cluster-binding SPASM domain of anaerobic sulfatase maturating enzyme; Anaerobic ...
281-387 1.26e-46

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: 155.90  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 281 VCVHAPSCGANMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKD 360
Cdd:cd21120    1 SCVMSGTCGDNLVVEHNGDVYPCDHFVLPEYRLGNIQEQTLAELVDSEKQQQFGAQKFKLPAECKQCKYLFACHGGCPKH 80
                         90       100
                 ....*....|....*....|....*..
gi 517956898 361 RFITTDSGPSHNYLCQGYRRFYSHALP 387
Cdd:cd21120   81 RFAKGPSEPGLNYLCEGYKEFFEHLLP 107
rSAM_GlyRichRpt TIGR04261
radical SAM/SPASM domain protein, GRRM system; Members of this protein family are radical SAM ...
22-190 5.17e-42

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: 151.73  E-value: 5.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFFLSKellydQKRQSMSEETLETYVKNFL-SASLDGEVTMLWQGGEPTLRGLPF----FERLIELCEKYRRP 96
Cdd:TIGR04261   7 CNLDCDYCYLPDR-----QLKNRLSLDLIEPILKRILeSPFVGPGFTICWHAGEPLTVPISFydeaTEIIREALEEYNQQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   97 TQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNILCTVHAA 176
Cdd:TIGR04261  82 PVQIEQSVQTNGTLINQAWCDCFKRNRIVVGVSLDGPAFIHDAHRRTRTGRGSHAATMRGIRALQKNEIPFSVIAVLTED 161
                         170
                  ....*....|....
gi 517956898  177 NEDHGLEVYRYFRD 190
Cdd:TIGR04261 162 SLDYPDEIFDFFRD 175
rSAM_pep_methan TIGR04083
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ...
22-366 1.23e-27

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: 112.90  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFFlskellYDQKRQSMSEETLETYVKnFLSASLDGEVTMLWQGGEPTLRGLPFFERLIELCEKyRRPTQEVR 101
Cdd:TIGR04083  10 CPSKCKYCWS------SEETSPVMSIDTVKDIVE-WLKDFRDDRVTFTFHGGEPLLAGADFYRQALPLLSE-GLAHLKPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  102 HAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRlnrgGHGTHSMVIRGWEHLRNADVDTNILCTVHAANEDHG 181
Cdd:TIGR04083  82 FAMQTNLWLMTPELAEIFAEYNVPIGSSIDGPEEINDYQR----GEGYYQKTMKGYEIAKEHGLDVRFICTFTSYSVKQK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  182 LEVYRYFRDElgaqymqfipivervprehlrqaelGWRSGSSALLYRQDGDCVTSRSTSPEGYGNFLCSIFDEWVcSDVG 261
Cdd:TIGR04083 158 EEIFNFFLEN-------------------------GFTLKLHPALPSLRSDNPGEWALDPEEYGELLVYLLDKYL-ENMD 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  262 SVFVQDFDSSISALF-GSASVCVHAPSCGANMAMEFNGDVYACDHWV-EPEWLVGNI-ANSDFPTLATSE---KMRAFdt 335
Cdd:TIGR04083 212 KIEVMNINDLCRCVFtRRGTVCTFVDCMGTTFAVGPDGSIYPCYRFVgMPEYVMGNVrDRPTMEDLMESDagkLMLAF-- 289
                         330       340       350
                  ....*....|....*....|....*....|.
gi 517956898  336 kKQDLDDECWSCPFLRLCWGGCPKDRFITTD 366
Cdd:TIGR04083 290 -KEYVDTHCAKCSHIKYCRGGCPYNAIAPTD 319
SAM_SPASM_FxsB TIGR04269
radical SAM/SPASM domain protein, FxsB family; This model describes a radical SAM (pfam04055) ...
22-385 2.10e-27

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: 112.13  E-value: 2.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFflskelLYDQKRQS-------MSEETLETY---VKNFLSASLDGEVTMLWQGGEPTLRGLpffERLIELCE 91
Cdd:TIGR04269  12 CDLACDHCY------VYEHADQSwrarpkvMSAETRRAFarrLAEHAAAHDLPSVAVILHGGEPLLAGA---ERLRAFAA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   92 KYRR---PTQEVRHAIQTNGTLITEQWARFFKDNDVLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNAD---V 165
Cdd:TIGR04269  83 ELRSaldPVTALDLRLQTNGVLLDDEALDLLVEHDIGVGVSLDGDRAANDRHRLTRDGRSSHDQVLRALELLRRPEyrhL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  166 DTNILCTVHAANEdhGLEVYRYFrDELGAQYMQFIpiverVPreHLRQAELGWRSGssallyrQDGdcvtsrstSPEGYG 245
Cdd:TIGR04269 163 FAGLLCTVDVAND--PVAVYEAL-AALDPPRIDFL-----LP--HATWDRPPPRRG-------PDG--------SPTAYA 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  246 NFLCSIFDEWVcSDVGSVFVQDFDSSISAL-----------FGSASVCVhapscganmaMEFNG-----DVYACDHWVEP 309
Cdd:TIGR04269 218 RWLLAVFDRWL-ADGRPMPVRTFDSLLSTLrggpsltealgLGPVDLAV----------IETDGtyeqlDSLKVAYDGAP 286
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517956898  310 EwLVGNIANSDFPTLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKDRFiTTDSGPSH-NYLCQGYRRFYSHA 385
Cdd:TIGR04269 287 A-TGGDVFDHTIDEVAAHPGIAARRAGLAGLSETCRACPVVDSCGGGLYPHRY-RSDSGFDNpSVYCADLKALIAHV 361
rSAM_more_4Fe4S TIGR04085
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ...
288-375 5.26e-22

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: 89.94  E-value: 5.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  288 CGA---NMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKMRAF-DTKKQDLDDECWSCPFLRLCWGGCPKDRFI 363
Cdd:TIGR04085   1 CGAgrnSLVVDPDGDVYPCDHFVYPEYKLGNIREDSLEEILNSSKQLEFgRWKSPKLPEECRSCKYLPLCGGGCPANRYL 80
                          90
                  ....*....|...
gi 517956898  364 TT-DSGPSHNYLC 375
Cdd:TIGR04085  81 KTgDINGPKNPLC 93
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
21-184 4.56e-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: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  21 ACNLDCQYCFFLSkellYDQKRQSMSEETLETYVKNFlsASLDGEVTMLWqGGEPTLRglPFFERLIELCEKYRRPTqev 100
Cdd:COG0535    9 RCNLRCKHCYADA----GPKRPGELSTEEAKRILDEL--AELGVKVVGLT-GGEPLLR--PDLFELVEYAKELGIRV--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 101 rhAIQTNGTLITEQWARFFKDNDVL-VGISIDGP-KDLHDAYrlnRGGHGTHSMVIRGWEHLRNADVDTNIlCTVHAANE 178
Cdd:COG0535   77 --NLSTNGTLLTEELAERLAEAGLDhVTISLDGVdPETHDKI---RGVPGAFDKVLEAIKLLKEAGIPVGI-NTVYPCPF 150

                 ....*.
gi 517956898 179 DHGLEV 184
Cdd:COG0535  151 LPELSL 156
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
22-173 3.55e-16

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: 75.64  E-value: 3.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFFlsKELLYDQKRQSMSEETLETYVKNFLSAsldGEVTMLWQGGEPTLRgLPFFERLIELCEKYRRPtqEVR 101
Cdd:pfam04055   5 CNLRCTYCAF--PSIRARGKGRELSPEEILEEAKELKRL---GVEVVILGGGEPLLL-PDLVELLERLLKLELAE--GIR 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517956898  102 HAIQTNGTLITEQWARFFKD-NDVLVGISIDGPkdlHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNILCTV 173
Cdd:pfam04055  77 ITLETNGTLLDEELLELLKEaGLDRVSIGLESG---DDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIV 146
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
22-353 5.41e-11

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: 63.75  E-value: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFFLSKellydQKRQSMSEETLETYVKNFLSASLD-GEVTMLWQ--GGEPTLRglpfFERLIELCEKYRRPTQ 98
Cdd:TIGR04115  12 CQLACKYCYQTGK-----NKNKRMSFETAKKAVDYILSGNKGfGEPSVIWDfiGGEPLLE----IELIDRICDYIKNRMI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   99 EVRH--------AIQTNGTLI-TEQWARFFKDND--VLVGISIDGPKDLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDT 167
Cdd:TIGR04115  83 ELNHpwfnsyrfSFSTNGVCYfEEKVQRFIQKNNqhLSISITIDGTKEKHDSCRVFPDGRGSYDLVVSNAPLWLNQFPYA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  168 NILCTVHAANEDHGLEVYRYFRDeLGAQYMQFIPIVERvprehlrqaelGWRSGSSALLYRQ---DGDCVTSRSTspegY 244
Cdd:TIGR04115 163 STKVTIAPADVPHVKESVTHLID-LGYNEVNINCVYEE-----------GWQMGDDTVFEDQlkkLADYILEHDM----Y 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  245 GNFLCSIFDEwvcsdvgSVFV-QDFDSSISALFGSasvcvhapscGANMAMEFNGDVYACDHWVE------PEWLVGNIa 317
Cdd:TIGR04115 227 NDYYCSFFSE-------NFGHpLDCKLDNENWCGG----------GVMLAVDPDGIFYPCLRFAEyslrqkEAYSIGNV- 288
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 517956898  318 nSDFPTLATSEKMRAFDTKKQDlDDECWSCPFLRLC 353
Cdd:TIGR04115 289 -DDGIDRNRVRPFLKLDRRTQS-TDECINCPVASGC 322
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
17-169 6.54e-11

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 61.58  E-value: 6.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  17 PTGAACNLDCQYCFFLSKEllydQKRQSMSEETLEtYVKNFLSASLDGEVTMLWQGGEPTLRG--LPFFERLIELCEKYR 94
Cdd:cd01335    2 ELTRGCNLNCGFCSNPASK----GRGPESPPEIEE-ILDIVLEAKERGVEVVILTGGEPLLYPelAELLRRLKKELPGFE 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517956898  95 RptqevrhAIQTNGTLITEQWARFFKD-NDVLVGISIDGPkdLHDAYRLNRGGHGTHSMVIRGWEHLRNADVDTNI 169
Cdd:cd01335   77 I-------SIETNGTLLTEELLKELKElGLDGVGVSLDSG--DEEVADKIRGSGESFKERLEALKELREAGLGLST 143
geopep_mat_rSAM TIGR04280
putative geopeptide radical SAM maturase; This family is the radical SAM/SPASM domain putative ...
2-364 1.29e-10

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: 62.80  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898    2 THSPAPTLPFSVVAKPTgAACNLDCQYCFflsKELLYDqkRQSMSEET----LETYVKNFLSASLDgeVTMLWQGGEPTL 77
Cdd:TIGR04280  75 DRINRERRHFAAIVVLN-LDCNLACPYCF---EGPFRG--KRYMDDATadllVSYLVRERLAQGRD--VSLDFYGGEPLL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   78 RglpfferlIELCEKYRRPTQEVRHA--------IQTNGTLITEQWARffkdnDVL------VGISIDGPKDLHDAYRLN 143
Cdd:TIGR04280 147 S--------LDLIRRIATPLKAAAASrglsfsfsLVTNGTLLTRDVVE-----ELLplgltgAKVTLDGPPEIHDRQRPF 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  144 RGGHGTHSMVIRgwehlrnadvdtNILctvhAANEDHGLEVYRYFRDElgaQYMQFIPIVERVPREHLRQAELGwrsgss 223
Cdd:TIGR04280 214 VSGKGSFDTIVA------------NLK----AVCDLIAIQIGGNYTRE---NYREFPRLLDLLLAEGLTPERLA------ 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  224 ALLYrqdgDCVTSRStspegyGNFLCSIFDEwVCSDVGSVFVQDfdssiSALFGSASVC-----VHAPSCGA-------N 291
Cdd:TIGR04280 269 LVRF----SPVVSRA------GGAALPDFNS-GCASSNEPWLIE-----ASLFLREETLkrgypVPKLRPGAcmveledD 332
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517956898  292 MAMEFNGDVYACDHWV-EPEWLVGNIAN--SDFptlATSEKMRAFDtkkqdlDDECWSCPFLRLCWGGCpkdRFIT 364
Cdd:TIGR04280 333 LVVNHDGTLYKCPAFMgREGLAVGSLADglSDY---RDSHGLDLWK------NEECLDCAYLPLCFGGC---RFLT 396
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
10-193 2.16e-09

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: 58.71  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   10 PFSVVAKPTGAaCNLDCQYCFFLSKEllYDQKRQSMSEETLETYVKNFLSASLDgeVTMlwQGGEPTLRGlpFFERLIEL 89
Cdd:TIGR04250   2 PRSVDIDITGR-CNLRCRYCSHFSSA--AETPTDLETAEWLRFFRELNRCSVLR--VVL--SGGEPFMRS--DFREIIDG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   90 CEKYRrptqeVRHAIQTNGTLITEQWARFFKDNDVL--VGISIDGPK-DLHDAYRlnrgGHGTHSMVIRGWEHLRNADVD 166
Cdd:TIGR04250  73 IVKNR-----MRFSILSNGTLITDAIASFLAATRRCdyVQVSIDGSTpGTHDRLR----GTGSFLQAVEGIELLRKHAIP 143
                         170       180
                  ....*....|....*....|....*..
gi 517956898  167 TNILCTVHAANEDHGLEVYRYFRDELG 193
Cdd:TIGR04250 144 VVVRVTIHRWNVDDLRPIAALLLDDLG 170
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
21-131 4.34e-07

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 51.01  E-value: 4.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  21 ACNLDCQYCF--FLSKELLyDQKRQSMSEETLETYVKNFLSASLDGE----VtmlwqGGEPTLrgLPffERLIELcekyr 94
Cdd:NF038283  11 ACNYRCKYCFakWNDVKSP-RHHDKGHLEKLLEELAEFFKLLSYGFVrinfA-----GGEPLL--YP--DRLLDL----- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 517956898  95 rptqeVRHAIQ--------TNGTLITEQWARFFKDNDVLVGISID 131
Cdd:NF038283  76 -----IKLAKElgfktsiiTNGSLLTEEFLEELAPYLDWIGISID 115
SPASM_AlbA-like cd21125
Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis ...
288-357 1.93e-06

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: 45.94  E-value: 1.93e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517956898 288 CGA---NMAMEFNGDVYACDHWVEPEWLVGNIANSDFPTLATSEKMRAFDTKKQDLDDECWSCPFLRLCWGGC 357
Cdd:cd21125    3 CGAgwkSIVIDPDGEVYPCHLLHPTEFKLGNIFEDSLASILKNPVLEIWQTYDPRFSEHCKKCPFYGICGGGC 75
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
292-348 3.37e-06

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: 44.39  E-value: 3.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 517956898  292 MAMEFNGDVYAC-DHWVEPEWLVGNIANSDFPTLATSEKMRAFDT-KKQDLDDECWSCP 348
Cdd:pfam13186   8 LVILPDGDVYPCfDDDFVGPIVLGNIREQSLAEIWNSPKYREFRKlGKFALIELCRDCP 66
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
22-199 1.26e-05

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: 47.14  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898   22 CNLDCQYCFFLSKELLYDQKRQSMSEETLETYVKNFLSASLDGevtMLWQGGEPTLRglPFFERLIELCEKYRRPTqevr 101
Cdd:TIGR04251  14 CNLKCRHCWIDPKYQGEGEQHPSLDPSLFRSIIRQAIPLGLTS---VKLTGGEPLLH--PAIGEILECIGENNLQL---- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  102 hAIQTNGTLITEQWARFFKD-NDVLVGISIDGPK-DLHDAYrlnRGGHGTHSMVIRGWEHLRNADVDTNILCTVHAANED 179
Cdd:TIGR04251  85 -SVETNGLLCTPQTARDLAScETPFVSVSLDGVDaATHDWM---RGVKGAFDKAVRGIHNLVEAGIHPQIIMTVTRRNVG 160
                         170       180
                  ....*....|....*....|
gi 517956898  180 hGLEVYRYFRDELGAQYMQF 199
Cdd:TIGR04251 161 -QMEQIVRLAESLGAESVKF 179
SPASM_CteB-like cd21124
Iron-sulfur cluster-binding SPASM domain of sactionine bond-forming enzyme CteB and similar ...
288-367 2.59e-04

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: 40.03  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 288 CGA---NMAMEFNGDVYACDHWV-EPEWLVGNIAnsDFPTLAtsEKMRAFDTKKQDLDDECWSCPFLRLCWGGCPKDRFI 363
Cdd:cd21124    4 CGAgheYFAVDPDGDIYPCHRFVgMEEYRMGNVY--DGSSLM--ELQSEFWKRHVENKEECRECWARFYCGGGCPANSYA 79

                 ....
gi 517956898 364 TTDS 367
Cdd:cd21124   80 ENGD 83
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
10-163 5.07e-04

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 41.23  E-value: 5.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898    10 PFSVVAKPTGaaCNLDCQYCFFLSKELlydqKRQSMSEETLETYVKNFLSASLDG--EVTMLWQGGEPTLRGLPFFERLI 87
Cdd:smart00729   1 PLALYIITRG--CPRRCTFCSFPSLRG----KLRSRYLEALVREIELLAEKGEKEglVGTVFIGGGTPTLLSPEQLEELL 74
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517956898    88 ELCEKYRRPTQEVRHAIQTNGTLITEQWARFFKDNDVL-VGISID-GPKDLHDayRLNRGghGTHSMVIRGWEHLRNA 163
Cdd:smart00729  75 EAIREILGLAKDVEITIETRPDTLTEELLEALKEAGVNrVSLGVQsGDDEVLK--AINRG--HTVEDVLEAVELLREA 148
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
297-347 1.14e-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: 37.02  E-value: 1.14e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517956898 297 NGDVYACDHWVEPEWLVGNIANSDFPTLATSEKMRAF-DTKKQDLDDECWSC 347
Cdd:cd21109   14 DGDVYPCCFDVNEELKLGNIREQSLKEIWNSEKYREFrKLLLDGKIKLCKNC 65
SPASM_MftC-like cd21123
Iron-sulfur cluster-binding SPASM domain of mycofactocin radical SAM maturase MftC and similar ...
288-355 2.64e-03

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: 36.85  E-value: 2.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898 288 CGANMA-MEFNGDVYACDHWvepEWLVGNIANSDFPTL-ATSEKMRAFdTKKQDLDDECWSCPFLRLCWG 355
Cdd:cd21123    6 AGRGIAfISPDGDVYPCGFL---PFSAGNVREDSFKDIwENSELFKKL-RDREFLKGKCGKCKYRNVCGG 71
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
21-117 3.00e-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: 39.02  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  21 ACNLDCQYC--------------FFLSKELLY--DQKRQSMSEETLETyvkNFLSASLDgevtmlwqgGEPTLrgLPFFE 84
Cdd:COG0731   33 TCNFDCVYCqrgrttdltrerreFDDPEEILEelIEFLRKLPEEAREP---DHITFSGS---------GEPTL--YPNLG 98
                         90       100       110
                 ....*....|....*....|....*....|....
gi 517956898  85 RLIELCEKYRR-PTqevrhAIQTNGTLITEQWAR 117
Cdd:COG0731   99 ELIEEIKKLRGiKT-----ALLTNGSLLHRPEVR 127
moaA PRK00164
GTP 3',8-cyclase MoaA;
22-110 3.31e-03

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 39.35  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  22 CNLDCQYCffLSKE-LLYDQKRQSMSEETLETYVKNF---------LSasldgevtmlwqGGEPTLRglPFFERLIELCE 91
Cdd:PRK00164  27 CNFRCTYC--MPEGyLPFLPKEELLSLEEIERLVRAFvalgvrkvrLT------------GGEPLLR--KDLEDIIAALA 90
                         90
                 ....*....|....*....
gi 517956898  92 KYrRPTQEVrhAIQTNGTL 110
Cdd:PRK00164  91 AL-PGIRDL--ALTTNGYL 106
COG5210 COG5210
GTPase-activating protein [General function prediction only];
28-105 5.36e-03

GTPase-activating protein [General function prediction only];


Pssm-ID: 227535 [Multi-domain]  Cd Length: 496  Bit Score: 39.01  E-value: 5.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517956898  28 YCFFLSKELLYDQKRQSMSEETLETYVKNFLSASLDGEVTMLWQGGEPTLRGLP-FFERLIELCEKYRRPTQEVRHAIQ 105
Cdd:COG5210  183 DKLWISYLDPNPLSFLPVQLSKLRELIRKGIPNELRGDVWEFLLGIGFDLDKNPgLYERLLNLHREAKIPTQEIISQIE 261
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
22-128 9.37e-03

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 37.47  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517956898  22 CNLDCQYC--FFLSKeLLYDQKRQSMS-EETLETYVKNFLSASLDGEVTmlWQGGEPTLrglpFFERLIELCEKYRRptQ 98
Cdd:COG1180   31 CNLRCPYChnPEISQ-GRPDAAGRELSpEELVEEALKDRGFLDSCGGVT--FSGGEPTL----QPEFLLDLAKLAKE--L 101
                         90       100       110
                 ....*....|....*....|....*....|.
gi 517956898  99 EVRHAIQTNGTLITEQWARFFKDND-VLVGI 128
Cdd:COG1180  102 GLHTALDTNGYIPEEALEELLPYLDaVNIDL 132
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH