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Conserved domains on  [gi|52549953|gb|AAU83802|]
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pyruvate formate-lyase activating enzyme [uncultured archaeon GZfos34A6]

Protein Classification

AmmeMemoSam_rS superfamily protein( domain architecture ID 1904541)

AmmeMemoSam_rS superfamily protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AmmeMemoSam_rS super family cl44362
AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized ...
6-333 2.87e-129

AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized radical SAM enzymes that occur in a prokaryotic three-gene system along with homologs of mammalian proteins Memo (Mediator of ErbB2-driven cell MOtility) and AMMERCR1 (Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis). Among radical SAM enzymes that have been experimentally characterized, the most closely related in sequence include activases of pyruvate formate-lyase and of benzylsuccinate synthase.


The actual alignment was detected with superfamily member TIGR04337:

Pssm-ID: 275136 [Multi-domain]  Cd Length: 349  Bit Score: 373.17  E-value: 2.87e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953     6 FYEKLEENAVRCHLCAHHCKINESKRGICGVRENRGGVLYSLVYGKVVARGIDSIEKKPFFHFYPGSEAYSIATVGCNFR 85
Cdd:TIGR04337   3 YWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTPVLSFGTAGCNLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    86 CKNCQNFHISQmPKEGDKriVGEDASPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLARKEGICNVFVSNGHITE 165
Cdd:TIGR04337  83 CKFCQNWDISK-SREMDT--LADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQACRERGIKTVAVTAGYICP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   166 EAIRTLAPYLDAVNVDLKG-SEDLYRKICGGHRQPVLDAIK-LYKSLGVWVEVTTLVIPTLNDSEEEFRGTAEFIKS-VG 242
Cdd:TIGR04337 160 EPRAEFFAHMDAANVDLKAfTEDFYHKLCGGHLQPVLDTLRyLRHETDVWLEITTLLIPGENDSDAELEAMCEWIVEnLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   243 VDIPWHISQFYPTYKLTHLPPTPVTTLREAREIGLDVGLRYVYEGNVPGEGGENTYCYQCGELLIRRYGFQIRENKITDL 322
Cdd:TIGR04337 240 PDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHYVYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQ 319
                         330
                  ....*....|..
gi 52549953   323 -RCPSCGAKIDG 333
Cdd:TIGR04337 320 gRCPRCGTPLAG 331
 
Name Accession Description Interval E-value
AmmeMemoSam_rS TIGR04337
AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized ...
6-333 2.87e-129

AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized radical SAM enzymes that occur in a prokaryotic three-gene system along with homologs of mammalian proteins Memo (Mediator of ErbB2-driven cell MOtility) and AMMERCR1 (Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis). Among radical SAM enzymes that have been experimentally characterized, the most closely related in sequence include activases of pyruvate formate-lyase and of benzylsuccinate synthase.


Pssm-ID: 275136 [Multi-domain]  Cd Length: 349  Bit Score: 373.17  E-value: 2.87e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953     6 FYEKLEENAVRCHLCAHHCKINESKRGICGVRENRGGVLYSLVYGKVVARGIDSIEKKPFFHFYPGSEAYSIATVGCNFR 85
Cdd:TIGR04337   3 YWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTPVLSFGTAGCNLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    86 CKNCQNFHISQmPKEGDKriVGEDASPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLARKEGICNVFVSNGHITE 165
Cdd:TIGR04337  83 CKFCQNWDISK-SREMDT--LADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQACRERGIKTVAVTAGYICP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   166 EAIRTLAPYLDAVNVDLKG-SEDLYRKICGGHRQPVLDAIK-LYKSLGVWVEVTTLVIPTLNDSEEEFRGTAEFIKS-VG 242
Cdd:TIGR04337 160 EPRAEFFAHMDAANVDLKAfTEDFYHKLCGGHLQPVLDTLRyLRHETDVWLEITTLLIPGENDSDAELEAMCEWIVEnLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   243 VDIPWHISQFYPTYKLTHLPPTPVTTLREAREIGLDVGLRYVYEGNVPGEGGENTYCYQCGELLIRRYGFQIRENKITDL 322
Cdd:TIGR04337 240 PDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHYVYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQ 319
                         330
                  ....*....|..
gi 52549953   323 -RCPSCGAKIDG 333
Cdd:TIGR04337 320 gRCPRCGTPLAG 331
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
69-291 5.17e-100

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 294.78  E-value: 5.17e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  69 YPGSEAYSIATVGCNFRCKNCQNFHISQMPKEgdkrIVGEDASPKEIVAAAKQY-----GCRSIAYTYTEPTIFFEFAYD 143
Cdd:COG1180  18 GPGSIRLSVFTQGCNLRCPYCHNPEISQGRPD----AAGRELSPEELVEEALKDrgfldSCGGVTFSGGEPTLQPEFLLD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 144 TARLARKEGICNVFVSNGHITEEAIRTLAPYLDAVNVDLKG-SEDLYRKICGGHRQPVLDAIKLYKSLGVWVEVTTLVIP 222
Cdd:COG1180  94 LAKLAKELGLHTALDTNGYIPEEALEELLPYLDAVNIDLKAfDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIP 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52549953 223 TLNDSEEEFRGTAEFIKSVGVDIPWHISQFYPTYKLTHLPPTPVTTLREAREIGLDVGLRYVYEGNVPG 291
Cdd:COG1180 174 GLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLEDVPPPSPETLERAREIAREYGLKYVYIGNVPG 242
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
79-230 4.01e-17

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: 77.57  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    79 TVGCNFRCKNCQNFHISQMPKeGDKRIVGEdasPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLARKEGICNVFV 158
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARGK-GRELSPEE---ILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   159 ---SNG-HITEEAIRTLAPY-LDAVNVDLKGSEDLYRKICGG--HRQPVLDAIKLYKSLGVWVEVTTLV-IPTLNDSEEE 230
Cdd:pfam04055  78 tleTNGtLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRghTFEEVLEALELLREAGIPVVTDNIVgLPGETDEDLE 157
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
81-275 2.02e-14

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: 70.83  E-value: 2.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  81 GCNFRCKNCQNfhiSQMPKEGDKRIVGEDaSPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLAR-KEGICNVFVS 159
Cdd:cd01335   6 GCNLNCGFCSN---PASKGRGPESPPEIE-EILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKeLPGFEISIET 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 160 NGH-ITEEAIRTLAPYL---DAVNVDLKgSEDLYRKICGGHRQP--VLDAIKLYKSLGVWVEVTTLVIPTLNDSEEEFRG 233
Cdd:cd01335  82 NGTlLTEELLKELKELGldgVGVSLDSG-DEEVADKIRGSGESFkeRLEALKELREAGLGLSTTLLVGLGDEDEEDDLEE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 52549953 234 TAEFIKSVGVDiPWHISQFYPTYKLTHLPPTPVTTLREAREI 275
Cdd:cd01335 161 LELLAEFRSPD-RVSLFRLLPEEGTPLELAAPVVPAEKLLRL 201
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
74-254 8.54e-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: 52.02  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953     74 AYSIATVGCNFRCKNCQNFHISQMPKEGD-KRIVGEDASPKEIVAAAKQYGCRSIAY---TYTEPTIFFEFAYDTARLAR 149
Cdd:smart00729   3 ALYIITRGCPRRCTFCSFPSLRGKLRSRYlEALVREIELLAEKGEKEGLVGTVFIGGgtpTLLSPEQLEELLEAIREILG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    150 KEGICNVFVSN--GHITEEAIRTLAPY-LDAVNVDLK-GSEDLYRKICGGH-RQPVLDAIKLYKSLGvWVEVTTLVIPTL 224
Cdd:smart00729  83 LAKDVEITIETrpDTLTEELLEALKEAgVNRVSLGVQsGDDEVLKAINRGHtVEDVLEAVELLREAG-PIKVSTDLIVGL 161
                          170       180       190
                   ....*....|....*....|....*....|.
gi 52549953    225 -NDSEEEFRGTAEFIKSVGVDIpWHISQFYP 254
Cdd:smart00729 162 pGETEEDFEETLKLLKELGPDR-VSIFPLSP 191
 
Name Accession Description Interval E-value
AmmeMemoSam_rS TIGR04337
AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized ...
6-333 2.87e-129

AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized radical SAM enzymes that occur in a prokaryotic three-gene system along with homologs of mammalian proteins Memo (Mediator of ErbB2-driven cell MOtility) and AMMERCR1 (Alport syndrome, Mental Retardation, Midface hypoplasia, and Elliptocytosis). Among radical SAM enzymes that have been experimentally characterized, the most closely related in sequence include activases of pyruvate formate-lyase and of benzylsuccinate synthase.


Pssm-ID: 275136 [Multi-domain]  Cd Length: 349  Bit Score: 373.17  E-value: 2.87e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953     6 FYEKLEENAVRCHLCAHHCKINESKRGICGVRENRGGVLYSLVYGKVVARGIDSIEKKPFFHFYPGSEAYSIATVGCNFR 85
Cdd:TIGR04337   3 YWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTPVLSFGTAGCNLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    86 CKNCQNFHISQmPKEGDKriVGEDASPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLARKEGICNVFVSNGHITE 165
Cdd:TIGR04337  83 CKFCQNWDISK-SREMDT--LADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQACRERGIKTVAVTAGYICP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   166 EAIRTLAPYLDAVNVDLKG-SEDLYRKICGGHRQPVLDAIK-LYKSLGVWVEVTTLVIPTLNDSEEEFRGTAEFIKS-VG 242
Cdd:TIGR04337 160 EPRAEFFAHMDAANVDLKAfTEDFYHKLCGGHLQPVLDTLRyLRHETDVWLEITTLLIPGENDSDAELEAMCEWIVEnLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   243 VDIPWHISQFYPTYKLTHLPPTPVTTLREAREIGLDVGLRYVYEGNVPGEGGENTYCYQCGELLIRRYGFQIRENKITDL 322
Cdd:TIGR04337 240 PDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHYVYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQ 319
                         330
                  ....*....|..
gi 52549953   323 -RCPSCGAKIDG 333
Cdd:TIGR04337 320 gRCPRCGTPLAG 331
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
69-291 5.17e-100

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 294.78  E-value: 5.17e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  69 YPGSEAYSIATVGCNFRCKNCQNFHISQMPKEgdkrIVGEDASPKEIVAAAKQY-----GCRSIAYTYTEPTIFFEFAYD 143
Cdd:COG1180  18 GPGSIRLSVFTQGCNLRCPYCHNPEISQGRPD----AAGRELSPEELVEEALKDrgfldSCGGVTFSGGEPTLQPEFLLD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 144 TARLARKEGICNVFVSNGHITEEAIRTLAPYLDAVNVDLKG-SEDLYRKICGGHRQPVLDAIKLYKSLGVWVEVTTLVIP 222
Cdd:COG1180  94 LAKLAKELGLHTALDTNGYIPEEALEELLPYLDAVNIDLKAfDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIP 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52549953 223 TLNDSEEEFRGTAEFIKSVGVDIPWHISQFYPTYKLTHLPPTPVTTLREAREIGLDVGLRYVYEGNVPG 291
Cdd:COG1180 174 GLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLEDVPPPSPETLERAREIAREYGLKYVYIGNVPG 242
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
79-230 4.01e-17

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: 77.57  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    79 TVGCNFRCKNCQNFHISQMPKeGDKRIVGEdasPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLARKEGICNVFV 158
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARGK-GRELSPEE---ILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   159 ---SNG-HITEEAIRTLAPY-LDAVNVDLKGSEDLYRKICGG--HRQPVLDAIKLYKSLGVWVEVTTLV-IPTLNDSEEE 230
Cdd:pfam04055  78 tleTNGtLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRghTFEEVLEALELLREAGIPVVTDNIVgLPGETDEDLE 157
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
81-275 2.02e-14

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: 70.83  E-value: 2.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  81 GCNFRCKNCQNfhiSQMPKEGDKRIVGEDaSPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLAR-KEGICNVFVS 159
Cdd:cd01335   6 GCNLNCGFCSN---PASKGRGPESPPEIE-EILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKeLPGFEISIET 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 160 NGH-ITEEAIRTLAPYL---DAVNVDLKgSEDLYRKICGGHRQP--VLDAIKLYKSLGVWVEVTTLVIPTLNDSEEEFRG 233
Cdd:cd01335  82 NGTlLTEELLKELKELGldgVGVSLDSG-DEEVADKIRGSGESFkeRLEALKELREAGLGLSTTLLVGLGDEDEEDDLEE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 52549953 234 TAEFIKSVGVDiPWHISQFYPTYKLTHLPPTPVTTLREAREI 275
Cdd:cd01335 161 LELLAEFRSPD-RVSLFRLLPEEGTPLELAAPVVPAEKLLRL 201
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
40-244 6.39e-10

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: 58.66  E-value: 6.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  40 RGGVLYSLVYGKVVAR------GIDSIEKKpffhfypgseaysiatvGCNFRCKNCQNFHISQMPKEGDkrivgEDASPK 113
Cdd:COG0731   3 RGGLCYKYVYGPVPSRrlgrslGINLIPNK-----------------TCNFDCVYCQRGRTTDLTRERR-----EFDDPE 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 114 EIVAAAKQY------GCRSIAY-TYT---EPTIFFEFAyDTARLARKEGICNVFV-SNG-HITEEAIR-------TLAPY 174
Cdd:COG0731  61 EILEELIEFlrklpeEAREPDHiTFSgsgEPTLYPNLG-ELIEEIKKLRGIKTALlTNGsLLHRPEVReellkadQVYPS 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52549953 175 LDAVNvdlkgsEDLYRKICGGHR----QPVLDAIKLYKSLG---VWVEvtTLVIPTLNDSEEEFRGTAEFIKSVGVD 244
Cdd:COG0731 140 LDAAD------EETFRKINRPHPglswERIIEGLELFRKLYkgrTVIE--TMLVKGINDSEEELEAYAELIKRINPD 208
PflX COG1313
Radical SAM superfamily enzyme PflX [General function prediction only];
7-280 1.56e-09

Radical SAM superfamily enzyme PflX [General function prediction only];


Pssm-ID: 440924  Cd Length: 295  Bit Score: 58.23  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   7 YEKLEenavRCHLCAHHCKIN--ESKRGICGVRENrggvlyslvygKVVARGidsiekkpFFHF--------YPGSeays 76
Cdd:COG1313   2 YELLE----SCTLCPRNCGVNrlAGEKGFCGAGRK-----------AKVASA--------GLHFgeepplsgTNGS---- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  77 iATV---GCNFRCKNCQNFHISQMPKegdkrivGEDASPKEIVAAA---KQYGCRSIAY-TytePTIFFEFAYDTARLAR 149
Cdd:COG1313  55 -GTIffsGCNLRCVFCQNYEISQEGE-------GKEISVEELAEIMlelQEQGAHNINLvT---PTHYVPQILEALKIAK 123
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 150 KEG-----ICNvfvSNGHITEEAIRTLAPYLDAVNVDLK-GSEDLYRKICGG--------------HRQ---PVLDAIKL 206
Cdd:COG1313 124 EKGlrlpiVYN---TSGYESVETLRLLDGIVDIYLPDFKyADDELAKRYSGApdypevaraaikemHRQvgdLVFDEDGI 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 207 YKSlGVWVEvtTLVIPT-LNDSEEEFRgtaeFIK-SVGVDIPWHI-SQFYPTYKLTHLPPT--PVTT------LREAREI 275
Cdd:COG1313 201 AKR-GLIVR--HLVLPGnLAGSKKVLR----FIAeELSPDTYVSLmSQYTPAYKAREYPELnrRITReeyeeaLDYAREL 273

                ....*
gi 52549953 276 GLDVG 280
Cdd:COG1313 274 GLENG 278
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
82-219 2.52e-09

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: 55.29  E-value: 2.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  82 CNFRCKNCQNFHISQMPKEGDKrivgEDAspKEIVAAAKQYGCRSIAYTYTEPTIFFEFaYDTARLARKEGICNVFVSNG 161
Cdd:COG0535  10 CNLRCKHCYADAGPKRPGELST----EEA--KRILDELAELGVKVVGLTGGEPLLRPDL-FELVEYAKELGIRVNLSTNG 82
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52549953 162 H-ITEEAIRTLAPY-LDAVNVDLKGSE----DLYRKICGGHRQpVLDAIKLYKSLGVWVEVTTL 219
Cdd:COG0535  83 TlLTEELAERLAEAgLDHVTISLDGVDpethDKIRGVPGAFDK-VLEAIKLLKEAGIPVGINTV 145
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
74-254 8.54e-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: 52.02  E-value: 8.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953     74 AYSIATVGCNFRCKNCQNFHISQMPKEGD-KRIVGEDASPKEIVAAAKQYGCRSIAY---TYTEPTIFFEFAYDTARLAR 149
Cdd:smart00729   3 ALYIITRGCPRRCTFCSFPSLRGKLRSRYlEALVREIELLAEKGEKEGLVGTVFIGGgtpTLLSPEQLEELLEAIREILG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    150 KEGICNVFVSN--GHITEEAIRTLAPY-LDAVNVDLK-GSEDLYRKICGGH-RQPVLDAIKLYKSLGvWVEVTTLVIPTL 224
Cdd:smart00729  83 LAKDVEITIETrpDTLTEELLEALKEAgVNRVSLGVQsGDDEVLKAINRGHtVEDVLEAVELLREAG-PIKVSTDLIVGL 161
                          170       180       190
                   ....*....|....*....|....*....|.
gi 52549953    225 -NDSEEEFRGTAEFIKSVGVDIpWHISQFYP 254
Cdd:smart00729 162 pGETEEDFEETLKLLKELGPDR-VSIFPLSP 191
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
69-243 8.96e-08

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: 51.60  E-value: 8.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953    69 YPGSEAYSIATVGCNFRCKNCQNFHISQMPKEGDKrivgedaSPKEIVAAAKQygcRS-----IAYTYTEPTIFFEFAyD 143
Cdd:TIGR02495  13 YPGKLAFTIFLQGCNLKCPYCHNPLLIPRRGSGEI-------EVEELLEFLRR---RRglldgVVITGGEPTLQAGLP-D 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953   144 TARLARKEGICNVFVSNGHITEEAIRTLAP-YLDAVNVDLKGSEDLYRKICG----GHRQPVLDAIKLYKSLGVWVEVTT 218
Cdd:TIGR02495  82 FLREVRELGFEVKLDTNGSNPRRLEELLEEgLVDYVAMDVKAPPEKYGELYGleknGAAKNILKSLEILLESGIPFELRT 161
                         170       180
                  ....*....|....*....|....*
gi 52549953   219 LVIPTLNDsEEEFRGTAEFIKSVGV 243
Cdd:TIGR02495 162 TVVRGFLT-EEDLAEIATRIKENGT 185
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
44-194 4.52e-07

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 50.37  E-value: 4.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  44 LYSLVYgKVVARGIDSIEKKPFFHFYpGSEAYS-IAT---VGCNFRCKNCQNFHISQMPkegdkRIVGEDASPKEivAAA 119
Cdd:COG5014  10 LGELVE-KRVARGEGGVEYRKYYRFR-GGRWYGgIATadvVGCNLRCGFCWSWRFRDFP-----LTIGKFYSPEE--VAE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 120 KQYG-CRSIAYTYT-----EPTIFFEFAYDTARLARKEGICNVFVSNGHI---TEEAIRTLAPYLDA-VNVDLKG-SEDL 188
Cdd:COG5014  81 RLIEiARERGYRQVrlsggEPTIGFEHLLKVLELFSERGLTFILETNGILigyDRELARELASFRNIvVRVSIKGcTPEE 160

                ....*.
gi 52549953 189 YRKICG 194
Cdd:COG5014 161 FSMLTG 166
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
82-245 7.67e-04

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: 40.81  E-value: 7.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  82 CNFRCKNCqnfhisqMPKEGDKRIVGEDA-SPKEI---VAAAKQYGCRSIAYTYTEPTI---FFEFAydtARLARKEGIC 154
Cdd:COG2896  24 CNFRCTYC-------MPEEGYQFLPKEELlSFEEIerlVRAFVELGVRKIRLTGGEPLLrkdLPELI---ARLAALPGIE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 155 NVFVS-NGHITEEAIRTLAPY-LDAVNV--D-LKgsEDLYRKICGGHR-QPVLDAIKLYKSLGVW-VEVTTLVIPTLNDS 227
Cdd:COG2896  94 DLALTtNGSLLARYAEALKAAgLDRVNVslDsLD--PERFRRITRRDDlDKVLAGIDAALAAGLTpVKINAVVMRGVNDD 171
                       170
                ....*....|....*....
gi 52549953 228 E-EEFrgtAEFIKSVGVDI 245
Cdd:COG2896 172 EiLDL---LEFAKERGIDL 187
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
81-183 7.98e-04

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: 40.12  E-value: 7.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  81 GCNFRCKNC---QNFHISQmpkegdkrivGEDASPKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLaRKEGIcNVF 157
Cdd:COG0602  29 GCNLRCSWCdtkYAWDGEG----------GKRMSAEEILEEVAALGARHVVITGGEPLLQDDLAELLEAL-KDAGY-EVA 96
                        90       100
                ....*....|....*....|....*..
gi 52549953 158 V-SNGHIteeairTLAPYLDAVNVDLK 183
Cdd:COG0602  97 LeTNGTL------PIPAGIDWVTVSPK 117
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
64-255 8.03e-03

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 37.62  E-value: 8.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  64 PFFHFYPGSEAYSIATV----GCNFRCKNCQnfhISQMpkEGDK-------RIVgedaspKEIVAAAKQYGCRSIAYTYT 132
Cdd:COG1032 162 PAYDLLDLEAYHRRASIetsrGCPFGCSFCS---ISAL--YGRKvryrspeSVV------EEIEELVKRYGIREIFFVDD 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 133 EPTIFFEFAYDTARLARKEGICNVFVSNG---HITEEAIRTLApylDAVNVDLK-----GSEDLyRKICG-GHR-QPVLD 202
Cdd:COG1032 231 NFNVDKKRLKELLEELIERGLNVSFPSEVrvdLLDEELLELLK---KAGCRGLFigiesGSQRV-LKAMNkGITvEDILE 306
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 52549953 203 AIKLYKSLGVWVEVTTLV-IPTlnDSEEEFRGTAEFIKSVGVDIPwHISQFYPT 255
Cdd:COG1032 307 AVRLLKKAGIRVKLYFIIgLPG--ETEEDIEETIEFIKELGPDQA-QVSIFTPL 357
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
82-244 9.15e-03

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 37.66  E-value: 9.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953  82 CNFRCKNCQNFHISQ-----MPKEGDKRIVgedaspKEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLARKEG---- 152
Cdd:COG0641  11 CNLRCSYCYYSEGDEgsrrrMSEETAEKAI------DFLIESSGPGKELTITFFGGEPLLNFDFIKEIVEYARKYAkkgk 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52549953 153 -ICNVFVSNG-HITEEAIRTLAPYLDAVNVDLKGSE---DLYRKICGG---HRQpVLDAIKLYKSLGVWVEVTTlvipTL 224
Cdd:COG0641  85 kIRFSIQTNGtLLDDEWIDFLKENGFSVGISLDGPKeihDRNRVTKNGkgsFDR-VMRNIKLLKEHGVEVNIRC----TV 159
                       170       180
                ....*....|....*....|.
gi 52549953 225 N-DSEEEFRGTAEFIKSVGVD 244
Cdd:COG0641 160 TrENLDDPEELYDFLKELGFR 180
 
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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