NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1266662347|gb|PHF41319|]
View 

pyruvate formate-lyase 1-activating enzyme [Bacillus toyonensis]

Protein Classification

pyruvate formate lyase-activating protein( domain architecture ID 11494367)

pyruvate formate lyase-activating protein is a radical SAM protein that activates pyruvate formate-lyase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
5-241 6.38e-133

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


:

Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 374.01  E-value: 6.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   5 RIHSVESCGTVDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQL 84
Cdd:TIGR02493   1 RIHSTESMGTVDGPGIRFVVFMQGCPLRCQYCHNPDTWDLKGGTEVTPEELIKEVGSYKDFFKASGGGVTFSGGEPLLQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  85 DFLIELFKKCKEVGIHTTIDSSGgcysEEPEFQQKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKN 164
Cdd:TIGR02493  81 EFLSELFKACKELGIHTCLDTSG----FLGGCTEAADELLEYTDLVLLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRN 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1266662347 165 KPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLGVYKWEALGHKYPLANVEPPTEKNVEQARHILK 241
Cdd:TIGR02493 157 KPIWIRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGVYKWEALGIEYPLEGVKPPNKEQLERAAEIFK 233
 
Name Accession Description Interval E-value
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
5-241 6.38e-133

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 374.01  E-value: 6.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   5 RIHSVESCGTVDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQL 84
Cdd:TIGR02493   1 RIHSTESMGTVDGPGIRFVVFMQGCPLRCQYCHNPDTWDLKGGTEVTPEELIKEVGSYKDFFKASGGGVTFSGGEPLLQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  85 DFLIELFKKCKEVGIHTTIDSSGgcysEEPEFQQKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKN 164
Cdd:TIGR02493  81 EFLSELFKACKELGIHTCLDTSG----FLGGCTEAADELLEYTDLVLLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRN 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1266662347 165 KPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLGVYKWEALGHKYPLANVEPPTEKNVEQARHILK 241
Cdd:TIGR02493 157 KPIWIRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGVYKWEALGIEYPLEGVKPPNKEQLERAAEIFK 233
pflA PRK11145
pyruvate formate lyase 1-activating protein;
1-240 5.53e-124

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 351.64  E-value: 5.53e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   1 MVKGRIHSVESCGTVDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEP 80
Cdd:PRK11145    2 SVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEELMKEVVTYRHFMNASGGGVTASGGEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  81 LLQLDFLIELFKKCKEVGIHTTIDSSGGCYSEEPefqqKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYL 160
Cdd:PRK11145   82 ILQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDP----VIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 161 SDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLGVYKWEALGHKYPLANVEPPTEKNVEQARHIL 240
Cdd:PRK11145  158 AKRNQKTWIRYVVVPGWTDDDDSAHRLGEFIKDMGNIEKIELLPYHELGKHKWEAMGEEYKLDGVKPPSKETMERVKGIL 237
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
1-242 1.23e-104

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 302.49  E-value: 1.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   1 MVKGRIHSVESCGTVDGPG-IRYVIFTQGCLLRCQYCHNADTWEIG---KGKEITVEEVMQDVTCYLPFIEaSGGGITVS 76
Cdd:COG1180     2 EVRGRIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRpdaAGRELSPEELVEEALKDRGFLD-SCGGVTFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  77 GGEPLLQLDFLIELFKKCKEVGIHTTIDSSGgCYSEEPefqqkLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQF 156
Cdd:COG1180    81 GGEPTLQPEFLLDLAKLAKELGLHTALDTNG-YIPEEA-----LEELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLEN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 157 ARYLSDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLgvykwealghkYPLANVEPPTEKNVEQA 236
Cdd:COG1180   155 LELLAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPL-----------YKLEDVPPPSPETLERA 223

                  ....*.
gi 1266662347 237 RHILKA 242
Cdd:COG1180   224 REIARE 229
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
15-154 5.78e-25

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: 95.70  E-value: 5.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  15 VDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVE---EVMQDvtcylpFIEASGGGITVSGGEPLLQLDFLIELF 91
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEEledEIIED------LAKPYIQGLTLSGGEPLLNAEALLELV 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266662347  92 KKCKEVGIHTTIDSSGGcYSEEpEFQQK-LDKLMDYTDlVLLDLKHIDSKKHRKLT--GKSNEHIL 154
Cdd:pfam13353  75 KRVREECPEKDIWLWTG-YTFE-ELQSKdQLELLKLID-VLVDGKFEQSLKDPSLRfrGSSNQRII 137
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
23-231 8.37e-16

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: 73.52  E-value: 8.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  23 VIFTQGCLLRCQYCHNadtWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQLDFLIELFKKCKEV-GIHT 101
Cdd:cd01335     1 LELTRGCNLNCGFCSN---PASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELpGFEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 102 TIDSSGgcYSEEPEFQQKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKNKPIWVRHVLVPGVTDNE 181
Cdd:cd01335    78 SIETNG--TLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1266662347 182 EDLQKLsSFIQSLSNVQKVEVLPYHKLGvykwealGHKYPLANVEPPTEK 231
Cdd:cd01335   156 DDLEEL-ELLAEFRSPDRVSLFRLLPEE-------GTPLELAAPVVPAEK 197
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
22-231 4.95e-03

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: 37.00  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   22 YVIFTQGCLLRCQYChnADTWEIGKGKEITVEEVMQDV--TCYLPFIEASGGGITVSGGEP-LLQLDFLIELFKKCKEVG 98
Cdd:smart00729   4 LYIITRGCPRRCTFC--SFPSLRGKLRSRYLEALVREIelLAEKGEKEGLVGTVFIGGGTPtLLSPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   99 -----IHTTIDSSGGCYSEEpefqqKLDKLMDY-TDLVLLDLKHIDSKKHRKL-TGKSNEHILQFARYLSDKNKPIWVRH 171
Cdd:smart00729  82 glakdVEITIETRPDTLTEE-----LLEALKEAgVNRVSLGVQSGDDEVLKAInRGHTVEDVLEAVELLREAGPIKVSTD 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266662347  172 VLV--PGVTdnEEDLQKLSSFIQSLsnvqKVEVLPYHKLGVYKWEALGHKYPlaNVEPPTEK 231
Cdd:smart00729 157 LIVglPGET--EEDFEETLKLLKEL----GPDRVSIFPLSPRPGTPLAKMYK--RLKPPTKE 210
 
Name Accession Description Interval E-value
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
5-241 6.38e-133

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 374.01  E-value: 6.38e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   5 RIHSVESCGTVDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQL 84
Cdd:TIGR02493   1 RIHSTESMGTVDGPGIRFVVFMQGCPLRCQYCHNPDTWDLKGGTEVTPEELIKEVGSYKDFFKASGGGVTFSGGEPLLQP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  85 DFLIELFKKCKEVGIHTTIDSSGgcysEEPEFQQKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKN 164
Cdd:TIGR02493  81 EFLSELFKACKELGIHTCLDTSG----FLGGCTEAADELLEYTDLVLLDIKHFNPEKYKKLTGVSLQPTLDFAKYLAKRN 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1266662347 165 KPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLGVYKWEALGHKYPLANVEPPTEKNVEQARHILK 241
Cdd:TIGR02493 157 KPIWIRYVLVPGYTDSEEDIEALAEFVKTLPNVERVEVLPYHQLGVYKWEALGIEYPLEGVKPPNKEQLERAAEIFK 233
pflA PRK11145
pyruvate formate lyase 1-activating protein;
1-240 5.53e-124

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 351.64  E-value: 5.53e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   1 MVKGRIHSVESCGTVDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEP 80
Cdd:PRK11145    2 SVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVEELMKEVVTYRHFMNASGGGVTASGGEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  81 LLQLDFLIELFKKCKEVGIHTTIDSSGGCYSEEPefqqKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYL 160
Cdd:PRK11145   82 ILQAEFVRDWFRACKKEGIHTCLDTNGFVRRYDP----VIDELLDVTDLVMLDLKQMNDEIHQNLVGVSNHRTLEFARYL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 161 SDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLGVYKWEALGHKYPLANVEPPTEKNVEQARHIL 240
Cdd:PRK11145  158 AKRNQKTWIRYVVVPGWTDDDDSAHRLGEFIKDMGNIEKIELLPYHELGKHKWEAMGEEYKLDGVKPPSKETMERVKGIL 237
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
1-242 1.23e-104

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 302.49  E-value: 1.23e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   1 MVKGRIHSVESCGTVDGPG-IRYVIFTQGCLLRCQYCHNADTWEIG---KGKEITVEEVMQDVTCYLPFIEaSGGGITVS 76
Cdd:COG1180     2 EVRGRIYGISPFSTVDGPGsIRLSVFTQGCNLRCPYCHNPEISQGRpdaAGRELSPEELVEEALKDRGFLD-SCGGVTFS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  77 GGEPLLQLDFLIELFKKCKEVGIHTTIDSSGgCYSEEPefqqkLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQF 156
Cdd:COG1180    81 GGEPTLQPEFLLDLAKLAKELGLHTALDTNG-YIPEEA-----LEELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLEN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 157 ARYLSDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPYHKLgvykwealghkYPLANVEPPTEKNVEQA 236
Cdd:COG1180   155 LELLAESGVHVEIRTLVIPGLNDSEEELEAIARFIAELGDVIPVHLLPFHPL-----------YKLEDVPPPSPETLERA 223

                  ....*.
gi 1266662347 237 RHILKA 242
Cdd:COG1180   224 REIARE 229
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
16-242 3.41e-69

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 214.51  E-value: 3.41e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  16 DGPGIRYVIFTQGCLLRCQYCHNADTW-----------------------EIGK-------------------------- 46
Cdd:TIGR02494  11 DGPGIRTTVFLKGCPLRCKWCSNPESQrkspellfkenrclgcgkcvevcPAGTarlseladgrnriiirrekcthcgkc 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  47 ------------GKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQLDFLIELFKKCKEVGIHTTIDSSgGCYSEEp 114
Cdd:TIGR02494  91 teacpsgalsivGEEMTVEEVMRVVLRDSIFYRNSGGGVTLSGGEPLLQPEFALALLQACHERGIHTAVETS-GFTPWE- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 115 efqqKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSL 194
Cdd:TIGR02494 169 ----TIEKVLPYVDLFLFDIKHLDDERHKEVTGVDNEPILENLEALAAAGKNVVIRIPVIPGFNDSEENIEAIAAFLRKL 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1266662347 195 SN-VQKVEVLPYHKLGVYKWEALGHKYPLANVEPPTEKNVEQARHILKA 242
Cdd:TIGR02494 245 EPgVDEIDLLPYHRLGENKYRQLGREYPDSEIPDPAEEQLLELKEIFES 293
activase_YjjW TIGR04041
glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, ...
11-234 1.44e-53

glycine radical enzyme activase, YjjW family; Members of this family are radical SAM enzymes, designated YjjW in E. coli, that are paired with and appear to activate a glycyl radical enzyme of unknown function, designated YjjI. This activase and its target are found in Clostridial species as well as E. coli and cousins. Members of this family may be misannotated as pyruvate formate lyase activating enzyme. [Protein fate, Protein modification and repair]


Pssm-ID: 274938 [Multi-domain]  Cd Length: 276  Bit Score: 173.97  E-value: 1.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  11 SCgtVDGPGIRYVIFTQGCLLRCQYCHNADTWEI---------------------------------------------G 45
Cdd:TIGR04041  11 SC--VDGPGNRLAIFLQGCNFDCKYCHNPETINHcdhcgdcvagcpagalslvdgkvvwdkercigcdtcikvcphqssP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  46 KGKEITVEEVMQDVTCYLPFIEasggGITVSGGEPLLQLDFLIELFKKCKEVGIHTTIDSSGGcYSEEpefqqKLDKLMD 125
Cdd:TIGR04041  89 KTKEYTVEELLDRIRKNMPFIR----GITVSGGECTLQLDFLTELFKAIKAAGLTCFIDSNGS-LDLT-----GWPKLLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 126 YTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSLSNVQKVEVLPY 205
Cdd:TIGR04041 159 VLDGAMLDLKAWDSETHRWLTGRDNHRVLKNIRFLAELGKLYEVRLVHIPGLSDLEQEIDGLARFLGDLPSDTRIKLIAF 238
                         250       260
                  ....*....|....*....|....*....
gi 1266662347 206 HKLGVYKwEALghkyplaNVEPPTEKNVE 234
Cdd:TIGR04041 239 RHHGVRG-EAL-------EWPSPTDEQME 259
PRK10076 PRK10076
pyruvate formate lyase II activase; Provisional
47-237 1.38e-30

pyruvate formate lyase II activase; Provisional


Pssm-ID: 182224 [Multi-domain]  Cd Length: 213  Bit Score: 112.55  E-value: 1.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  47 GKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQLDFLIELFKKCKEVGIHTTIDSSG-GCYSeepefqqKLDKLMD 125
Cdd:PRK10076   16 GRDITLDALEREVMKDDIFFRTSGGGVTLSGGEVLMQAEFATRFLQRLRLWGVSCAIETAGdAPAS-------KLLPLAK 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 126 YTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKNKPIWVRHVLVPGVTDNEEDLQKLSSFIQSLsNVQKVEVLPY 205
Cdd:PRK10076   89 LCDEVLFDLKIMDATQARDVVKMNLPRVLENLRLLVSEGVNVIPRLPLIPGFTLSRENMQQALDVLIPL-GIKQIHLLPF 167
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1266662347 206 HKLGVYKWEALGHKYPLANVEPPTEKNVEQAR 237
Cdd:PRK10076  168 HQYGEPKYRLLGKTWSMKEVPAPSSADVATMR 199
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
15-154 5.78e-25

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: 95.70  E-value: 5.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  15 VDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITVE---EVMQDvtcylpFIEASGGGITVSGGEPLLQLDFLIELF 91
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEEledEIIED------LAKPYIQGLTLSGGEPLLNAEALLELV 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266662347  92 KKCKEVGIHTTIDSSGGcYSEEpEFQQK-LDKLMDYTDlVLLDLKHIDSKKHRKLT--GKSNEHIL 154
Cdd:pfam13353  75 KRVREECPEKDIWLWTG-YTFE-ELQSKdQLELLKLID-VLVDGKFEQSLKDPSLRfrGSSNQRII 137
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
5-153 4.59e-24

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 93.95  E-value: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   5 RIHSVESCGTVDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEIT---VEEVMQDVTCYlPFIEasggGITVSGGEPL 81
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTealEKEIIRDLNDN-PLID----GLTLSGGDPL 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1266662347  82 LQ--LDFLIELFKKCKEVGIHTTIDSSGGCYSEEPEFQQKLDKLMDYTDlVLLDLKHIDSKKHRKLT--GKSNEHI 153
Cdd:TIGR02491  76 YPrnVEELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHLEVLKYID-VLVDGKFELSKKDLKLKfrGSSNQRI 150
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
25-181 1.19e-21

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: 87.97  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  25 FTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYlpfIEASGGGITVSGGEPLLQLDFLIELFKKCKE---VGIHT 101
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKEL---KRLGVEVVILGGGEPLLLPDLVELLERLLKLelaEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 102 TIDSSGGCYSEEpefqqKLDKLMDYT-DLVLLDLKHIDSKKHRKLTGK-SNEHILQFARYLSDKN-KPIWVRHVLVPGVT 178
Cdd:pfam04055  78 TLETNGTLLDEE-----LLELLKEAGlDRVSIGLESGDDEVLKLINRGhTFEEVLEALELLREAGiPVVTDNIVGLPGET 152

                  ...
gi 1266662347 179 DNE 181
Cdd:pfam04055 153 DED 155
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
5-191 4.81e-19

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: 81.64  E-value: 4.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   5 RIHSVESCGTVDGPG-IRYVIFTQGCLLRCQYCHNadtWEI----GKGkEITVEEVMQDVTCYLPFIEasggGITVSGGE 79
Cdd:TIGR02495   1 RIAGLVPFSTVDYPGkLAFTIFLQGCNLKCPYCHN---PLLiprrGSG-EIEVEELLEFLRRRRGLLD----GVVITGGE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  80 PLLQ---LDFLIELFKKCKEVGIHTTidssgGCYseePEFQQKL--DKLMDYtdlVLLDLKHIDSKKHRkLTGK----SN 150
Cdd:TIGR02495  73 PTLQaglPDFLREVRELGFEVKLDTN-----GSN---PRRLEELleEGLVDY---VAMDVKAPPEKYGE-LYGLekngAA 140
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1266662347 151 EHILQFARYLSDKNKPIWVRHVLVPGVTDnEEDLQKLSSFI 191
Cdd:TIGR02495 141 KNILKSLEILLESGIPFELRTTVVRGFLT-EEDLAEIATRI 180
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
23-231 8.37e-16

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: 73.52  E-value: 8.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  23 VIFTQGCLLRCQYCHNadtWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQLDFLIELFKKCKEV-GIHT 101
Cdd:cd01335     1 LELTRGCNLNCGFCSN---PASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELpGFEI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 102 TIDSSGgcYSEEPEFQQKLDKLMDYTDLVLLDLKHIDSKKHRKLTGKSNEHILQFARYLSDKNKPIWVRHVLVPGVTDNE 181
Cdd:cd01335    78 SIETNG--TLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1266662347 182 EDLQKLsSFIQSLSNVQKVEVLPYHKLGvykwealGHKYPLANVEPPTEK 231
Cdd:cd01335   156 DDLEEL-ELLAEFRSPDRVSLFRLLPEE-------GTPLELAAPVVPAEK 197
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
24-196 1.25e-13

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: 67.47  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  24 IF--TQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIeasgggITVSGGEPLLQLDFLiELFKKCKEVGIHT 101
Cdd:COG0602    23 VFvrLAGCNLRCSWCDTKYAWDGEGGKRMSAEEILEEVAALGARH------VVITGGEPLLQDDLA-ELLEALKDAGYEV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 102 TIDSSgGCYSEEPEFqqkldklmdytDLVLLDLKHIDSKKHRKLtgKSNEHILQFARYLsdknkpiwvRHVLvpgvtDNE 181
Cdd:COG0602    96 ALETN-GTLPIPAGI-----------DWVTVSPKLPSSGEEEDN--RENLEVLRRADEL---------KFVV-----ADE 147
                         170
                  ....*....|....*
gi 1266662347 182 EDLQKLSSFIQSLSN 196
Cdd:COG0602   148 TDLEEAEELLARLDF 162
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
29-242 2.21e-12

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: 64.44  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  29 CLLRCQYCH--NADTWEIGKGKEITVEEVMQDVTCYLPFIEASGGG---ITVSG-GEPLL--QLDFLIELFKKCKevGIH 100
Cdd:COG0731    34 CNFDCVYCQrgRTTDLTRERREFDDPEEILEELIEFLRKLPEEAREpdhITFSGsGEPTLypNLGELIEEIKKLR--GIK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 101 TTIDSSGGCYSEePEFQQKLDKLmdytDLVLLDLKHIDSKKHRKLTG--------KSNEHILQFArylSDKNKPIWVRHV 172
Cdd:COG0731   112 TALLTNGSLLHR-PEVREELLKA----DQVYPSLDAADEETFRKINRphpglsweRIIEGLELFR---KLYKGRTVIETM 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347 173 LVPGVTDNEEDLQKLSSFIQSLsNVQKVEVLPYHKLGVYKWealghkyplanVEPPTEKNVEQARHILKA 242
Cdd:COG0731   184 LVKGINDSEEELEAYAELIKRI-NPDFVELKTYMRPPALSR-----------VNMPSHEELEEFAERLAE 241
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
26-173 4.39e-10

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: 56.84  E-value: 4.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  26 TQGCLLRCQYCHNAdtWEIGKGKEITVEEVMQdvtcYLPFIEASGGG-ITVSGGEPLLQLDFLiELFKKCKEVGIHTTID 104
Cdd:COG0535     7 TNRCNLRCKHCYAD--AGPKRPGELSTEEAKR----ILDELAELGVKvVGLTGGEPLLRPDLF-ELVEYAKELGIRVNLS 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266662347 105 SSGGCYSEEpefqqKLDKLMDY-TDLVLLDLKHIDSKKHRKLTGKSN--EHILQFARYLSDKNKPIWVRHVL 173
Cdd:COG0535    80 TNGTLLTEE-----LAERLAEAgLDHVTISLDGVDPETHDKIRGVPGafDKVLEAIKLLKEAGIPVGINTVY 146
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
15-156 4.05e-06

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 45.37  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  15 VDGPGIRYVIFTQGCLLRCQYCHNADTWEIGKGKEITveEVMQD-VTCYLPFIEASGGGITVSGGEPLL--QLDFLIELF 91
Cdd:PRK11121   12 VNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFT--KEMEDqIIADLNDTRIKRQGLSLSGGDPLHpqNVPDILKLV 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1266662347  92 KK----C--KEVGIHTtidssGGCYSEEPEFQQkldKLMDYTDlVLLDLKHIDSKKHRKLT--GKSNEHILQF 156
Cdd:PRK11121   90 QRvkaeCpgKDIWVWT-----GYKLDELNAAQR---QVVDLID-VLVDGKFVQDLADPSLIwrGSSNQVIHRL 153
Fer4_14 pfam13394
4Fe-4S single cluster domain;
24-135 1.89e-05

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 42.74  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  24 IFTQGCLLRCQYCHNADTWEIgKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQ------LDFLIELFKKCKEV 97
Cdd:pfam13394   1 LFVSGCNHSCPGCDNKETWKF-NYGEPFTEELEDQIIADLKDSYIKRQGLVLTGGEPLHPwnlpvlLKLLKRVKEEYPSK 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1266662347  98 GIHTtidSSGGCYSEEPEF--QQKLDKLMDYTDlVLLDLK 135
Cdd:pfam13394  80 DIWL---ETGYTLAIDFEYpdTEEQLFTLSVID-VLVDGK 115
RNR_activ_nrdG3 TIGR02826
anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family ...
24-96 3.66e-05

anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family represent a set of radical SAM enzymes related to, yet architecturally different from, the activating protein for the glycine radical-containing, oxygen-sensitive ribonucleoside-triphosphate reductase (RNR) as described in model TIGR02491. Members of this family are found paired with members of a similarly divergent set of anaerobic ribonucleoside-triphosphate reductases. Identification of this protein as an RNR activitating protein is partly from pairing with a candidate RNR. It is further supported by our finding that upstream of these operons are examples of a conserved regulatory element (described Rodionov and Gelfand) that is found in nearly all bacteria and that occurs specifically upstream of operons for all three classes of RNR genes. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274317  Cd Length: 147  Bit Score: 42.72  E-value: 3.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1266662347  24 IFTQGCLLRCQYCHNADTWEIGKGKEITVEEVMQDVTCYLPFIEAsgggITVSGGEplLQLDFLIELFKKCKE 96
Cdd:TIGR02826  20 FYISGCPLGCPGCHSPELWHEDEGTPLTPEVLAQLLDKYRSLITC----VLFLGGE--WEPEALLSLLKYVKE 86
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
26-96 1.49e-04

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 42.28  E-value: 1.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1266662347  26 TQGCLLRCQYCHnADTWEIGKGKEITvEEVMQDVTCYLpfIEASGGGITVS----GGEPLLQLDFLIELFKKCKE 96
Cdd:COG0641     8 TSRCNLRCSYCY-YSEGDEGSRRRMS-EETAEKAIDFL--IESSGPGKELTitffGGEPLLNFDFIKEIVEYARK 78
moaA PRK00164
GTP 3',8-cyclase MoaA;
26-96 7.41e-04

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 40.12  E-value: 7.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  26 TQGCLLRCQYCHNAD--TWeIGKGKEITVEEvmqdvtcylpfIE-----ASGGGIT---VSGGEPLLQLDFlIELFKKCK 95
Cdd:PRK00164   24 TDRCNFRCTYCMPEGylPF-LPKEELLSLEE-----------IErlvraFVALGVRkvrLTGGEPLLRKDL-EDIIAALA 90

                  .
gi 1266662347  96 E 96
Cdd:PRK00164   91 A 91
rSAM_pep_methan TIGR04083
putative peptide-modifying radical SAM enzyme, Mhun_1560 family; Members of this family are ...
23-103 2.52e-03

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: 38.55  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347  23 VIFTQGCLLRCQYChnadtWEIGKGKEITVEEVMQDVTCYLPFIEASGGGITVSGGEPLLQ-LDFLIELFKKCKEVGIHT 101
Cdd:TIGR04083   4 IIPTLGCPSKCKYC-----WSSEETSPVMSIDTVKDIVEWLKDFRDDRVTFTFHGGEPLLAgADFYRQALPLLSEGLAHL 78

                  ..
gi 1266662347 102 TI 103
Cdd:TIGR04083  79 KP 80
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
22-231 4.95e-03

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: 37.00  E-value: 4.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   22 YVIFTQGCLLRCQYChnADTWEIGKGKEITVEEVMQDV--TCYLPFIEASGGGITVSGGEP-LLQLDFLIELFKKCKEVG 98
Cdd:smart00729   4 LYIITRGCPRRCTFC--SFPSLRGKLRSRYLEALVREIelLAEKGEKEGLVGTVFIGGGTPtLLSPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1266662347   99 -----IHTTIDSSGGCYSEEpefqqKLDKLMDY-TDLVLLDLKHIDSKKHRKL-TGKSNEHILQFARYLSDKNKPIWVRH 171
Cdd:smart00729  82 glakdVEITIETRPDTLTEE-----LLEALKEAgVNRVSLGVQSGDDEVLKAInRGHTVEDVLEAVELLREAGPIKVSTD 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1266662347  172 VLV--PGVTdnEEDLQKLSSFIQSLsnvqKVEVLPYHKLGVYKWEALGHKYPlaNVEPPTEK 231
Cdd:smart00729 157 LIVglPGET--EEDFEETLKLLKEL----GPDRVSIFPLSPRPGTPLAKMYK--RLKPPTKE 210
 
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