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Conserved domains on  [gi|1008849450|gb|KYK32331|]
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hypothetical protein AYK19_03390 [Theionarchaea archaeon DG-70-1]

Protein Classification

PqqD and Radical_SAM domain-containing protein( domain architecture ID 12063004)

PqqD and Radical_SAM domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 137-276 9.72e-64

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: 200.90  E-value: 9.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 137 VSIEITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELFTN 216
Cdd:COG0535     2 LQIELTNRCNLRCKHCYADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIRVNLSTN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 217 GTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAWKRTMKGIQNLKTNGIRIK 276
Cdd:COG0535    82 GTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPGAFDKVLEAIKLLKEAGIPVG 141
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 355-391 8.00e-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: 43.24  E-value: 8.00e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1008849450 355 CGIGTYSLVVGSNGDVRPC--SVFGMEVVVGSIRDQPVK 391
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCfdDDFVGPIVLGNIREQSLA 39
PqqD pfam05402
Coenzyme PQQ synthesis protein D (PqqD); This family contains several bacterial coenzyme PQQ ...
 59-113 5.96e-03

Coenzyme PQQ synthesis protein D (PqqD); This family contains several bacterial coenzyme PQQ synthesis protein D (PqqD) sequences. This protein is required for coenzyme pyrrolo-quinoline-quinone (PQQ) biosynthesis.


:

Pssm-ID: 461641  Cd Length: 65  Bit Score: 35.15  E-value: 5.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450  59 ITPNEATVHLITLCDGTHTVGEIVSHFVEISGENPSSIEEHVEQILERLLTNEVI 113
Cdd:pfam05402  11 ISLNETGAFIWELLDGRTTVEEIVAALAEEYDVDEEEAEADVEAFLEQLREAGLI 65
 
Name Accession Description Interval E-value
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 137-276 9.72e-64

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: 200.90  E-value: 9.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 137 VSIEITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELFTN 216
Cdd:COG0535     2 LQIELTNRCNLRCKHCYADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIRVNLSTN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 217 GTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAWKRTMKGIQNLKTNGIRIK 276
Cdd:COG0535    82 GTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPGAFDKVLEAIKLLKEAGIPVG 141
mycofact_rSAM TIGR03962
mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM ...
 140-296 2.81e-38

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


Pssm-ID: 188477 [Multi-domain]  Cd Length: 339  Bit Score: 140.37  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 140 EITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELFTNGTL 219
Cdd:TIGR03962  17 ELTYACNLACVHCLSSSGKRDPRELTTAECKRLIDELAAMQVFYVNIGGGEPTVRPDFWELMDYATAHGVGVKFSTNGVR 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008849450 220 VTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGiKGAWKRTMKGIQNLKTNGIR-IKPAVSVSQLNMKEvvpLHEFF 296
Cdd:TIGR03962  97 IDPEVADRLAATDYVDVQISLDGATAEVNDAVRG-AGSFDLARRAMDNLAAAGFRgFKISVVLTRRNFGQ---LDEFY 170
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 141-275 3.15e-26

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: 102.99  E-value: 3.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 141 ITDACNLNCVHCYNDYGSKRED--ELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLG----LELF 214
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKgrELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegirITLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008849450 215 TNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGiKGAWKRTMKGIQNLKTNGIRI 275
Cdd:pfam04055  81 TNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINR-GHTFEEVLEALELLREAGIPV 140
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 139-310 9.66e-25

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: 100.49  E-value: 9.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 139 IEITDACNLNCVHCYN--DYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELF-- 214
Cdd:cd01335     1 LELTRGCNLNCGFCSNpaSKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISie 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 215 TNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAWKRTMKGIQNLKTNGIRIKPAVSV------SQLNMKE 288
Cdd:cd01335    81 TNGTLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVglgdedEEDDLEE 160

                         170       180
                  ....*....|....*....|..
gi 1008849450 289 VVPLHEFFFREGFYEYKLQPVF 310
Cdd:cd01335   161 LELLAEFRSPDRVSLFRLLPEE 182
moaA PRK00164
GTP 3',8-cyclase MoaA;
139-296 3.76e-21

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 93.28  E-value: 3.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 139 IEITDACNLNCVHCYND---YGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLE--L 213
Cdd:PRK00164   21 ISVTDRCNFRCTYCMPEgylPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDIIAALAALPGIRDlaL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 214 FTNGTLVTKNvAKKLKALNILDVSVSLDSPTPEIhdyFRGI--KGAWKRTMKGI--------QNLKTNgirikpAVSVSQ 283
Cdd:PRK00164  101 TTNGYLLARR-AAALKDAGLDRVNVSLDSLDPER---FKAItgRDRLDQVLAGIdaalaaglTPVKVN------AVLMKG 170

                         170
                  ....*....|...
gi 1008849450 284 LNMKEVVPLHEFF 296
Cdd:PRK00164  171 VNDDEIPDLLEWA 183
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
 141-288 2.33e-11

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: 63.72  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 141 ITDACNLNCVHCY-----NDYGSKREDELTLEEIYHLIDELKKL--GVLIIMLSGGEPLLRPD-FFEIAQYVRDnsLGLE 212
Cdd:NF038283    8 LTEACNYRCKYCFakwndVKSPRHHDKGHLEKLLEELAEFFKLLsyGFVRINFAGGEPLLYPDrLLDLIKLAKE--LGFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 213 --LFTNGTLVTKNVAKKLKalNILD-VSVSLDSPTPEIHDYF-RGIKGawKRTM------KGIQNLKTNG--IRIKPAVS 280
Cdd:NF038283   86 tsIITNGSLLTEEFLEELA--PYLDwIGISIDSANEETNRKIgRVDRK--GRVLsleellELIALIRQINpnIKLKINTV 161


                  ....*...
gi 1008849450 281 VSQLNMKE 288
Cdd:NF038283  162 VNRLNWDE 169
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 138-273 1.67e-08

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: 54.33  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450  138 SIEITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIML-----SGGEPLLRP--DFFEIAQYVRD---- 206
Cdd:smart00729   4 LYIITRGCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGEKEGLVgtvfiGGGTPTLLSpeQLEELLEAIREilgl 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008849450  207 -NSLGLELFTNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDyfRGIKGA-WKRTMKGIQNLKTNGI 273
Cdd:smart00729  84 aKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLK--AINRGHtVEDVLEAVELLREAGP 150
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
 137-273 2.26e-06

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: 49.50  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 137 VSIEITDACNLNCVHCyNDYGSKREDELTLEEIYHLIDELKKL----GVLIIMLSGGEPLLRPDFF-----------EIA 201
Cdd:NF041300   43 VVLKATRLCNLRCTYC-RSWAEGPNQTMTFDVLARAVREALSMpglhGVEFVWHGGEVTLLKPKVFkkliwlqqqfrQPG 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450 202 QYVRdNSLGlelfTNGTLVTKNVAKKLKALNIlDVSVSLDSPtPEIHDYFR---GIKGAWKRTMKGIQNLKTNGI 273
Cdd:NF041300  122 QEVR-NSIQ----TNATHLTDEWIEFLSELGM-GVGVSIDGP-PEVHDRRRldkDGRPTSSRVAGGIARLRQAGI 189
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 355-391 8.00e-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: 43.24  E-value: 8.00e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1008849450 355 CGIGTYSLVVGSNGDVRPC--SVFGMEVVVGSIRDQPVK 391
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCfdDDFVGPIVLGNIREQSLA 39
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
 355-392 3.12e-05

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: 41.64  E-value: 3.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1008849450 355 CGIGTYSLVVGSNGDVRPCSVFGM-EVVVGSIRDQPVKS 392
Cdd:cd21109     2 CPAPWTSLYITPDGDVYPCCFDVNeELKLGNIREQSLKE 40
rSAM_more_4Fe4S TIGR04085
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ...
 355-391 3.33e-05

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: 42.18  E-value: 3.33e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1008849450 355 CGIGTYSLVVGSNGDVRPCSVFGM-EVVVGSIRDQPVK 391
Cdd:TIGR04085   1 CGAGRNSLVVDPDGDVYPCDHFVYpEYKLGNIREDSLE 38
PqqD pfam05402
Coenzyme PQQ synthesis protein D (PqqD); This family contains several bacterial coenzyme PQQ ...
 59-113 5.96e-03

Coenzyme PQQ synthesis protein D (PqqD); This family contains several bacterial coenzyme PQQ synthesis protein D (PqqD) sequences. This protein is required for coenzyme pyrrolo-quinoline-quinone (PQQ) biosynthesis.


Pssm-ID: 461641  Cd Length: 65  Bit Score: 35.15  E-value: 5.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450  59 ITPNEATVHLITLCDGTHTVGEIVSHFVEISGENPSSIEEHVEQILERLLTNEVI 113
Cdd:pfam05402  11 ISLNETGAFIWELLDGRTTVEEIVAALAEEYDVDEEEAEADVEAFLEQLREAGLI 65
 
Name Accession Description Interval E-value
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 137-276 9.72e-64

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: 200.90  E-value: 9.72e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 137 VSIEITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELFTN 216
Cdd:COG0535     2 LQIELTNRCNLRCKHCYADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIRVNLSTN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 217 GTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAWKRTMKGIQNLKTNGIRIK 276
Cdd:COG0535    82 GTLLTEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPGAFDKVLEAIKLLKEAGIPVG 141
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 136-392 1.81e-39

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 143.97  E-value: 1.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 136 QVSIEITDACNLNCVHCY----NDYGSKREDELTLEE-IYHLIDELKKLGVLIIMLSGGEPLLRPDFF-EIAQYVRD-NS 208
Cdd:COG0641     2 ALVLKPTSRCNLRCSYCYysegDEGSRRRMSEETAEKaIDFLIESSGPGKELTITFFGGEPLLNFDFIkEIVEYARKyAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 209 LGLELF----TNGTLVTKNVAKKLKALNILdVSVSLDSPtPEIHDYFR----GiKGAWKRTMKGIQNLKTNGIRIKPAVS 280
Cdd:COG0641    82 KGKKIRfsiqTNGTLLDDEWIDFLKENGFS-VGISLDGP-KEIHDRNRvtknG-KGSFDRVMRNIKLLKEHGVEVNIRCT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 281 VSQLNMKEVVPLHEFFFREGFYEYKLQPVFATGRSNPlntTITPDEFEKAVRDVL--ILEKKLEKEH---------PLHE 349
Cdd:COG0641   159 VTRENLDDPEELYDFLKELGFRSIQFNPVVEEGEADY---SLTPEDYGEFLIELFdeWLERDGGKIFvrefdillaGLLP 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1008849450 350 KEKMNC-GIGTYSLVVGSNGDVRPCSVF--GMEVVVGSIRDQPVKS 392
Cdd:COG0641   236 PCSSPCvGAGGNYLVVDPDGDIYPCDEFvgDPEFRLGNVFDGSLAE 281
mycofact_rSAM TIGR03962
mycofactocin radical SAM maturase; Members of this family are uncharacterized radical SAM ...
 140-296 2.81e-38

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


Pssm-ID: 188477 [Multi-domain]  Cd Length: 339  Bit Score: 140.37  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 140 EITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELFTNGTL 219
Cdd:TIGR03962  17 ELTYACNLACVHCLSSSGKRDPRELTTAECKRLIDELAAMQVFYVNIGGGEPTVRPDFWELMDYATAHGVGVKFSTNGVR 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008849450 220 VTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGiKGAWKRTMKGIQNLKTNGIR-IKPAVSVSQLNMKEvvpLHEFF 296
Cdd:TIGR03962  97 IDPEVADRLAATDYVDVQISLDGATAEVNDAVRG-AGSFDLARRAMDNLAAAGFRgFKISVVLTRRNFGQ---LDEFY 170
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 132-294 2.81e-32

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: 124.56  E-value: 2.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 132 HPLQQVSIEITDACNLNCVHCYndYGSKREDE------LTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVR 205
Cdd:TIGR04251   1 HPLHQIYFYLTEGCNLKCRHCW--IDPKYQGEgeqhpsLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 206 DNSLGLELFTNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAWKRTMKGIQNLKTNGIRIKPAVSVSQLN 285
Cdd:TIGR04251  79 ENNLQLSVETNGLLCTPQTARDLASCETPFVSVSLDGVDAATHDWMRGVKGAFDKAVRGIHNLVEAGIHPQIIMTVTRRN 158

                         170
                  ....*....|..
gi 1008849450 286 ---MKEVVPLHE 294
Cdd:TIGR04251 159 vgqMEQIVRLAE 170
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 135-346 2.50e-30

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: 119.58  E-value: 2.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 135 QQVSIEITDACNLNCVHCYNdYGSKRE--DELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLE 212
Cdd:TIGR04250   3 RSVDIDITGRCNLRCRYCSH-FSSAAEtpTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVKNRMRFS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 213 LFTNGTLVTKNVAKKLKALNILD-VSVSLDSPTPEIHDYFRGiKGAWKRTMKGIQNLKTNGIRIKPAVSVSQLNMKEVVP 291
Cdd:TIGR04250  82 ILSNGTLITDAIASFLAATRRCDyVQVSIDGSTPGTHDRLRG-TGSFLQAVEGIELLRKHAIPVVVRVTIHRWNVDDLRP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1008849450 292 LHEFFFRE-GFYEYKLQPVFATG--RSNPLNTTITPDEFEKAVRDVLilekKLEKEHP 346
Cdd:TIGR04250 161 IAALLLDDlGLPAFSTNAASYMGlcRSNTDDVQLDTAERTLAMEILL----ELEKEYP 214
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 141-275 3.15e-26

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: 102.99  E-value: 3.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 141 ITDACNLNCVHCYNDYGSKRED--ELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLG----LELF 214
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKgrELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegirITLE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1008849450 215 TNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGiKGAWKRTMKGIQNLKTNGIRI 275
Cdd:pfam04055  81 TNGTLLDEELLELLKEAGLDRVSIGLESGDDEVLKLINR-GHTFEEVLEALELLREAGIPV 140
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 139-310 9.66e-25

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: 100.49  E-value: 9.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 139 IEITDACNLNCVHCYN--DYGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELF-- 214
Cdd:cd01335     1 LELTRGCNLNCGFCSNpaSKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISie 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 215 TNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAWKRTMKGIQNLKTNGIRIKPAVSV------SQLNMKE 288
Cdd:cd01335    81 TNGTLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVglgdedEEDDLEE 160

                         170       180
                  ....*....|....*....|..
gi 1008849450 289 VVPLHEFFFREGFYEYKLQPVF 310
Cdd:cd01335   161 LELLAEFRSPDRVSLFRLLPEE 182
moaA PRK00164
GTP 3',8-cyclase MoaA;
139-296 3.76e-21

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 93.28  E-value: 3.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 139 IEITDACNLNCVHCYND---YGSKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLE--L 213
Cdd:PRK00164   21 ISVTDRCNFRCTYCMPEgylPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDIIAALAALPGIRDlaL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 214 FTNGTLVTKNvAKKLKALNILDVSVSLDSPTPEIhdyFRGI--KGAWKRTMKGI--------QNLKTNgirikpAVSVSQ 283
Cdd:PRK00164  101 TTNGYLLARR-AAALKDAGLDRVNVSLDSLDPER---FKAItgRDRLDQVLAGIdaalaaglTPVKVN------AVLMKG 170

                         170
                  ....*....|...
gi 1008849450 284 LNMKEVVPLHEFF 296
Cdd:PRK00164  171 VNDDEIPDLLEWA 183
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 141-301 1.29e-20

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: 91.66  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 141 ITDACNLNCVHC--YNDYG-SKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSlGLE---LF 214
Cdd:COG2896    20 VTDRCNFRCTYCmpEEGYQfLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIARLAALP-GIEdlaLT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 215 TNGTLVTKNvAKKLKALNILDVSVSLDSPTPEIhdyFRGI--KGAWKRTMKGIQNLKTNGI-RIK-PAVSVSQLNMKEVV 290
Cdd:COG2896    99 TNGSLLARY-AEALKAAGLDRVNVSLDSLDPER---FRRItrRDDLDKVLAGIDAALAAGLtPVKiNAVVMRGVNDDEIL 174

                         170
                  ....*....|.
gi 1008849450 291 PLHEFFFREGF 301
Cdd:COG2896   175 DLLEFAKERGI 185
rSAM_pep_methan TIGR04083
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ...
 137-389 3.80e-20

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: 90.94  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 137 VSIEITDACNLNCVHCY-NDYGSKREDELTLEEIYHLIDELKKLGVlIIMLSGGEPLLR-PDFFE-----IAQYVRDNSL 209
Cdd:TIGR04083   2 VMIIPTLGCPSKCKYCWsSEETSPVMSIDTVKDIVEWLKDFRDDRV-TFTFHGGEPLLAgADFYRqalplLSEGLAHLKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 210 GLELFTNGTLVTKNVAKKLKALNIlDVSVSLDSPTpEIHDYFRGiKGAWKRTMKGIQNLKTNGIRIKPAVSVSQLNMKEV 289
Cdd:TIGR04083  81 EFAMQTNLWLMTPELAEIFAEYNV-PIGSSIDGPE-EINDYQRG-EGYYQKTMKGYEIAKEHGLDVRFICTFTSYSVKQK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 290 VPLHEFFFREGFyEYKLQPVFATGRS-NPLNTTITPDEFEKAVrdVLILEKKLEKehpLHEKEKMN-------------- 354
Cdd:TIGR04083 158 EEIFNFFLENGF-TLKLHPALPSLRSdNPGEWALDPEEYGELL--VYLLDKYLEN---MDKIEVMNindlcrcvftrrgt 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1008849450 355 ------CgIGTySLVVGSNGDVRPCSVF-GM-EVVVGSIRDQP 389
Cdd:TIGR04083 232 vctfvdC-MGT-TFAVGPDGSIYPCYRFvGMpEYVMGNVRDRP 272
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
 145-282 1.60e-11

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 64.24  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 145 CNLNCVHC----YNDYGSKREDELTLEEIYHLIDEL-KKLGVLIIMLSGGEPLLRPD-FFEIAQYVRDNSLGLELFTNGT 218
Cdd:COG5014    50 CNLRCGFCwswrFRDFPLTIGKFYSPEEVAERLIEIaRERGYRQVRLSGGEPTIGFEhLLKVLELFSERGLTFILETNGI 129

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1008849450 219 LVT--KNVAKKLKALNILDVSVSLDSPTPEIhdyFRGIKGA----WKRTMKGIQNLKTNGIR----IKPAVSVS 282
Cdd:COG5014   130 LIGydRELARELASFRNIVVRVSIKGCTPEE---FSMLTGAdpefFELQLRALKNLVDAGLEpgreVYPAVMLS 200
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 144-269 2.27e-11

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: 63.29  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 144 ACNLNCVHCY----NDYGSKREDELTLEEIYH-LIDELKKL---GVLI--IMLSG-GEPLLRPDFFEIAQYVRDNSlGLE 212
Cdd:COG0731    33 TCNFDCVYCQrgrtTDLTRERREFDDPEEILEeLIEFLRKLpeeAREPdhITFSGsGEPTLYPNLGELIEEIKKLR-GIK 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450 213 LF--TNGTLVTKnvAKKLKALNILD-VSVSLDSPTPEIhdyFRGI-----KGAWKRTMKGIQNLK 269
Cdd:COG0731   112 TAllTNGSLLHR--PEVREELLKADqVYPSLDAADEET---FRKInrphpGLSWERIIEGLELFR 171
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
 141-288 2.33e-11

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: 63.72  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 141 ITDACNLNCVHCY-----NDYGSKREDELTLEEIYHLIDELKKL--GVLIIMLSGGEPLLRPD-FFEIAQYVRDnsLGLE 212
Cdd:NF038283    8 LTEACNYRCKYCFakwndVKSPRHHDKGHLEKLLEELAEFFKLLsyGFVRINFAGGEPLLYPDrLLDLIKLAKE--LGFK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 213 --LFTNGTLVTKNVAKKLKalNILD-VSVSLDSPTPEIHDYF-RGIKGawKRTM------KGIQNLKTNG--IRIKPAVS 280
Cdd:NF038283   86 tsIITNGSLLTEEFLEELA--PYLDwIGISIDSANEETNRKIgRVDRK--GRVLsleellELIALIRQINpnIKLKINTV 161


                  ....*...
gi 1008849450 281 VSQLNMKE 288
Cdd:NF038283  162 VNRLNWDE 169
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 139-266 1.74e-10

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 62.08  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 139 IEITDACNLNCVHCYNDYG---SKREDELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRdNSLGLE--- 212
Cdd:PLN02951   62 ISLTERCNLRCQYCMPEEGvelTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLS-SLKGLKtla 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1008849450 213 LFTNGTLVTKNVaKKLKALNILDVSVSLDSPTPEIHDYFRGIKGAwKRTMKGIQ 266
Cdd:PLN02951  141 MTTNGITLSRKL-PRLKEAGLTSLNISLDTLVPAKFEFLTRRKGH-DRVLESID 192
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 145-275 9.57e-10

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 58.66  E-value: 9.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 145 CNLNCVHCYNDYGSKRE-----DELTLEEIyhlIDELKKLGVLI-----IMLSGGEPLLRPDFF-EIAQYVRDNSL--GL 211
Cdd:COG1180    31 CNLRCPYCHNPEISQGRpdaagRELSPEEL---VEEALKDRGFLdscggVTFSGGEPTLQPEFLlDLAKLAKELGLhtAL 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450 212 ElfTNGTlVTKNVAKKLkaLNILD-VSVSLDSPTPEIHDYFrgIKGAWKRTMKGIQNLKTNGIRI 275
Cdd:COG1180   108 D--TNGY-IPEEALEEL--LPYLDaVNIDLKAFDDEFYRKL--TGVSLEPVLENLELLAESGVHV 165
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 145-239 9.78e-09

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: 53.33  E-value: 9.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 145 CNLNCVHCYN------DYGskreDELTLEEIYHLIDELKKLGVLIIMLSGGEPLL-RPDFFEIAQYVRdnSLGLE----L 213
Cdd:pfam13353  15 CNHHCKGCFNpetwdfKYG----KPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVR--EECPEkdiwL 88

                          90       100
                  ....*....|....*....|....*.
gi 1008849450 214 FTNGTLVTKNVAKKLKALNILDVSVS 239
Cdd:pfam13353  89 WTGYTFEELQSKDQLELLKLIDVLVD 114
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
132-296 1.14e-08

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 56.41  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 132 HPLQQVSIEITDACNLNCVHCYNDYGSKREDE-----LTLEEIYHLIDEL---KKLGVLIIMLSGGEPLLRP-DFFEIA- 201
Cdd:PRK13745   11 KPLYIMLKPVGAVCNLACDYCYYLEKSKLYQEnpkhvMSDELLEKFIKEYinsQTMPQVLFTWHGGETLMRPlSFYKKAl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 202 ----QYVRDNSLGLELFTNGTLVTKNVAKKLKALNILdVSVSLDSPTpEIHDYFRGIK---GAWKRTMKGIQNLKTNGIR 274
Cdd:PRK13745   91 elqkKYARGRQIDNCIQTNGTLLTDEWCEFFRENNFL-VGVSIDGPQ-EFHDEYRKNKmgkPSFVKVMKGINLLKKHGVE 168

                         170       180
                  ....*....|....*....|..
gi 1008849450 275 IKPAVSVSQLNMKEVVPLHEFF 296
Cdd:PRK13745  169 WNAMAVVNDFNADYPLDFYHFF 190
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 138-273 1.67e-08

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: 54.33  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450  138 SIEITDACNLNCVHCYNDYGSKREDELTLEEIYHLIDELKKLGVLIIML-----SGGEPLLRP--DFFEIAQYVRD---- 206
Cdd:smart00729   4 LYIITRGCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGEKEGLVgtvfiGGGTPTLLSpeQLEELLEAIREilgl 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1008849450  207 -NSLGLELFTNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDyfRGIKGA-WKRTMKGIQNLKTNGI 273
Cdd:smart00729  84 aKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLK--AINRGHtVEDVLEAVELLREAGP 150
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
 145-391 2.77e-08

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 55.31  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 145 CNLNCVHC-YNDYGSKRE--------DELTLEEIYHLIDELKklGVLIIMLSGGEP-LLRPDFF-EIAQYVRD-NSLGLE 212
Cdd:PRK13758   15 CNLKCTYCfYHSLSDNRNvksygimrDEVLESMVKRVLNEAE--GHCSFAFQGGEPtLAGLEFFeELMELQRKhNYKNLK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 213 LF----TNGTLVTKNVAKKLKALNILdVSVSLDSPTpEIHDYFR---GIKGAWKRTMKGIQNLKTNGIRIKPAVSVSQLN 285
Cdd:PRK13758   93 IYnslqTNGTLIDESWAKFLSENKFL-VGLSMDGPK-EIHNLNRkdcCGLDTFSKVERAAELFKKYKVEFNILCVVTSNT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 286 MKEVVPLHEFFFREGFYEYK----LQPVFATGRSNPLntTITPDEFEKAVRDVLIL--EKKLEK------------EHPL 347
Cdd:PRK13758  171 ARHVNKIYKYFKEKDFKFLQfincLDPLYEEKGKYNY--SLKPKDYTKFLKNLFDLwyEDFLNGnrvsiryfdgllETIL 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1008849450 348 HEKEKMNCGIGTYS--LVVGSNGDVRPCSVFGM-EVVVGSIRDQPVK 391
Cdd:PRK13758  249 LGKSSSCGMNGTCTcqFVVESDGSVYPCDFYVLdKWRLGNIQDMTMK 295
Fer4_14 pfam13394
4Fe-4S single cluster domain;
145-239 7.59e-08

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 50.44  E-value: 7.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 145 CNLNCVHCYN--DYGSKREDELTLEEIYHLIDELKKLGVLI--IMLSGGEPLL---RPDFFEIAQYVRDNSLGLE--LFT 215
Cdd:pfam13394   6 CNHSCPGCDNkeTWKFNYGEPFTEELEDQIIADLKDSYIKRqgLVLTGGEPLHpwnLPVLLKLLKRVKEEYPSKDiwLET 85

                          90       100
                  ....*....|....*....|....*...
gi 1008849450 216 NGTLV----TKNVAKKLKALNILDVSVS 239
Cdd:pfam13394  86 GYTLAidfeYPDTEEQLFTLSVIDVLVD 113
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 145-219 1.05e-07

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


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 52.06  E-value: 1.05e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1008849450 145 CNLNCVHC---YNDYGSKREdELTLEEIyhlIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDNSLGLELFTNGTL 219
Cdd:COG0602    30 CNLRCSWCdtkYAWDGEGGK-RMSAEEI---LEEVAALGARHVVITGGEPLLQDDLAELLEALKDAGYEVALETNGTL 103
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 145-273 3.81e-07

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


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 50.05  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 145 CNLNCVHCYNDYGSKRE--DELTLEEIYHLIDELKKL--GVLIimlSGGEPLLRPDFFEIAQYVRDNSLGLELFTNGTLV 220
Cdd:TIGR02495  26 CNLKCPYCHNPLLIPRRgsGEIEVEELLEFLRRRRGLldGVVI---TGGEPTLQAGLPDFLREVRELGFEVKLDTNGSNP 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1008849450 221 tkNVAKKLKALNILDvSVSLDSPTPEIHD---YFRGIKGAWKRTMKGIQNLKTNGI 273
Cdd:TIGR02495 103 --RRLEELLEEGLVD-YVAMDVKAPPEKYgelYGLEKNGAAKNILKSLEILLESGI 155
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
 137-273 2.26e-06

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: 49.50  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 137 VSIEITDACNLNCVHCyNDYGSKREDELTLEEIYHLIDELKKL----GVLIIMLSGGEPLLRPDFF-----------EIA 201
Cdd:NF041300   43 VVLKATRLCNLRCTYC-RSWAEGPNQTMTFDVLARAVREALSMpglhGVEFVWHGGEVTLLKPKVFkkliwlqqqfrQPG 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450 202 QYVRdNSLGlelfTNGTLVTKNVAKKLKALNIlDVSVSLDSPtPEIHDYFR---GIKGAWKRTMKGIQNLKTNGI 273
Cdd:NF041300  122 QEVR-NSIQ----TNATHLTDEWIEFLSELGM-GVGVSIDGP-PEVHDRRRldkDGRPTSSRVAGGIARLRQAGI 189
SPASM pfam13186
Iron-sulfur cluster-binding domain; This domain occurs as an additional C-terminal iron-sulfur ...
 355-391 8.00e-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: 43.24  E-value: 8.00e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1008849450 355 CGIGTYSLVVGSNGDVRPC--SVFGMEVVVGSIRDQPVK 391
Cdd:pfam13186   1 CFAGWTSLVILPDGDVYPCfdDDFVGPIVLGNIREQSLA 39
SPASM cd21109
Iron-sulfur cluster-binding SPASM domain; This iron-sulfur cluster-binding domain is named ...
 355-392 3.12e-05

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: 41.64  E-value: 3.12e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1008849450 355 CGIGTYSLVVGSNGDVRPCSVFGM-EVVVGSIRDQPVKS 392
Cdd:cd21109     2 CPAPWTSLYITPDGDVYPCCFDVNeELKLGNIREQSLKE 40
rSAM_more_4Fe4S TIGR04085
radical SAM additional 4Fe4S-binding SPASM domain; This domain contains regions binding ...
 355-391 3.33e-05

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: 42.18  E-value: 3.33e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1008849450 355 CGIGTYSLVVGSNGDVRPCSVFGM-EVVVGSIRDQPVK 391
Cdd:TIGR04085   1 CGAGRNSLVVDPDGDVYPCDHFVYpEYKLGNIREDSLE 38
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
 139-255 5.86e-05

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 44.51  E-value: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 139 IEITDACNLNCVHCYNDYG--SKRE------DELTLEEIYHLIDELKKLGVLIIMLSGGEPLLRPDFFEIAQYVRDN--- 207
Cdd:COG2100    40 VRPTTGCNLNCIFCSVDAGphSRTRqaeyivDPEYLVEWFEKVARFKGKGVEAHIDGVGEPLLYPYIVELVKGLKEIkgv 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1008849450 208 -SLGLElfTNGTLVTKNVAKKLKALNILDVSVSLDSPTPEIHDYFRGIK 255
Cdd:COG2100   120 kVVSMQ--TNGTLLSEKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTK 166
SAM_SPASM_FxsB TIGR04269
radical SAM/SPASM domain protein, FxsB family; This model describes a radical SAM (pfam04055) ...
 134-270 1.14e-04

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: 43.95  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 134 LQQVSIEITDACNLNCVHCYNDYGS--------KREDELTLEEIYHLIDE---LKKLGVLIIMLSGGEPLL--RPDFFEI 200
Cdd:TIGR04269   1 IRQFVLKVHSRCDLACDHCYVYEHAdqswrarpKVMSAETRRAFARRLAEhaaAHDLPSVAVILHGGEPLLagAERLRAF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1008849450 201 AQYVR-----DNSLGLELFTNGTLVTKNVAKKLKALNIlDVSVSLDSP--TPEIHDYFRGIKGAWKRTMKGIQNLKT 270
Cdd:TIGR04269  81 AAELRsaldpVTALDLRLQTNGVLLDDEALDLLVEHDI-GVGVSLDGDraANDRHRLTRDGRSSHDQVLRALELLRR 156
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
 135-392 1.30e-04

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: 43.72  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 135 QQVSIEITDACNLNCVHCYNDYGSKRED---ELTLEEIYHLIDELKKLG--VLIIMLSGGEPLLRPDFFE-IAQYVRD-- 206
Cdd:TIGR04115   2 KSITFIVTDDCQLACKYCYQTGKNKNKRmsfETAKKAVDYILSGNKGFGepSVIWDFIGGEPLLEIELIDrICDYIKNrm 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 207 --------NSLGLELFTNGTLV-TKNVAKKL-KALNILDVSVSLDSpTPEIHD---YFRGIKGAWKRTMKGIQNLKTNGI 273
Cdd:TIGR04115  82 ielnhpwfNSYRFSFSTNGVCYfEEKVQRFIqKNNQHLSISITIDG-TKEKHDscrVFPDGRGSYDLVVSNAPLWLNQFP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008849450 274 RIKPAVSVSQLN---MKEVVpLHefFFREGFYEYKLQPVFATGRsNPLNTTITPDEFEKAVRdvLILEKKLEKE------ 344
Cdd:TIGR04115 161 YASTKVTIAPADvphVKESV-TH--LIDLGYNEVNINCVYEEGW-QMGDDTVFEDQLKKLAD--YILEHDMYNDyycsff 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450 345 -----HPLHEKEKMN--CGIGTYsLVVGSNGDVRPCSVFgMEVvvgSIRDQPVKS 392
Cdd:TIGR04115 235 senfgHPLDCKLDNEnwCGGGVM-LAVDPDGIFYPCLRF-AEY---SLRQKEAYS 284
PqqD pfam05402
Coenzyme PQQ synthesis protein D (PqqD); This family contains several bacterial coenzyme PQQ ...
 59-113 5.96e-03

Coenzyme PQQ synthesis protein D (PqqD); This family contains several bacterial coenzyme PQQ synthesis protein D (PqqD) sequences. This protein is required for coenzyme pyrrolo-quinoline-quinone (PQQ) biosynthesis.


Pssm-ID: 461641  Cd Length: 65  Bit Score: 35.15  E-value: 5.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1008849450  59 ITPNEATVHLITLCDGTHTVGEIVSHFVEISGENPSSIEEHVEQILERLLTNEVI 113
Cdd:pfam05402  11 ISLNETGAFIWELLDGRTTVEEIVAALAEEYDVDEEEAEADVEAFLEQLREAGLI 65
SPASM_AlbA-like cd21125
Iron-sulfur cluster-binding SPASM domain of antilisterial bacteriocin subtilosin biosynthesis ...
 354-376 7.06e-03

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: 35.93  E-value: 7.06e-03
                          10        20
                  ....*....|....*....|...
gi 1008849450 354 NCGIGTYSLVVGSNGDVRPCSVF 376
Cdd:cd21125     2 NCGAGWKSIVIDPDGEVYPCHLL 24
 
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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