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Conserved domains on  [gi|1904408583|gb|QNR61601|]
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GTP 3',8-cyclase [uncultured archaeon GZfos17G11]

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 ...
6-334 4.66e-124

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: 359.69  E-value: 4.66e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583   6 FYENLEGNAVRCHLCPHHCKINESRRGICGVRENRGGVLYSLVYGKVVARGIDPIEKKPFFHFYPGSEAYSIATVGCNFR 85
Cdd:TIGR04337   3 YWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTPVLSFGTAGCNLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  86 CKNCQNFEISqmpKEGEKLIVGEDVSPEEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLAHKEGICNTFISNGHITE 165
Cdd:TIGR04337  83 CKFCQNWDIS---KSREMDTLADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQACRERGIKTVAVTAGYICP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 166 EAIRTVAPYLDAVNVDLKGLSDDLYRKICGGHLKPVQDAIK-LYKSLGVLVEVTTLVIPTLNDFEEDFRGIAEFIKS-VG 243
Cdd:TIGR04337 160 EPRAEFFAHMDAANVDLKAFTEDFYHKLCGGHLQPVLDTLRyLRHETDVWLEITTLLIPGENDSDAELEAMCEWIVEnLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 244 VDIPWHISQFYPTYKLTHIPPTPVTTLREARGIGLDVGLRYVYEGNVPGEGGENTYCYQCGELLIRRYGFQILENTIQDS 323
Cdd:TIGR04337 240 PDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHYVYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQ 319
                         330
                  ....*....|..
gi 1904408583 324 -RCPSCGARIDG 334
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 ...
6-334 4.66e-124

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: 359.69  E-value: 4.66e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583   6 FYENLEGNAVRCHLCPHHCKINESRRGICGVRENRGGVLYSLVYGKVVARGIDPIEKKPFFHFYPGSEAYSIATVGCNFR 85
Cdd:TIGR04337   3 YWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTPVLSFGTAGCNLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  86 CKNCQNFEISqmpKEGEKLIVGEDVSPEEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLAHKEGICNTFISNGHITE 165
Cdd:TIGR04337  83 CKFCQNWDIS---KSREMDTLADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQACRERGIKTVAVTAGYICP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 166 EAIRTVAPYLDAVNVDLKGLSDDLYRKICGGHLKPVQDAIK-LYKSLGVLVEVTTLVIPTLNDFEEDFRGIAEFIKS-VG 243
Cdd:TIGR04337 160 EPRAEFFAHMDAANVDLKAFTEDFYHKLCGGHLQPVLDTLRyLRHETDVWLEITTLLIPGENDSDAELEAMCEWIVEnLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 244 VDIPWHISQFYPTYKLTHIPPTPVTTLREARGIGLDVGLRYVYEGNVPGEGGENTYCYQCGELLIRRYGFQILENTIQDS 323
Cdd:TIGR04337 240 PDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHYVYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQ 319
                         330
                  ....*....|..
gi 1904408583 324 -RCPSCGARIDG 334
Cdd:TIGR04337 320 gRCPRCGTPLAG 331
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
69-292 1.35e-98

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 290.93  E-value: 1.35e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  69 YPGSEAYSIATVGCNFRCKNCQNFEISQMPKEgeklIVGEDVSPEEIVAAAKQY-----GCRSIAYTYTEPTIFFEFAYD 143
Cdd:COG1180    18 GPGSIRLSVFTQGCNLRCPYCHNPEISQGRPD----AAGRELSPEELVEEALKDrgfldSCGGVTFSGGEPTLQPEFLLD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 144 TARLAHKEGICNTFISNGHITEEAIRTVAPYLDAVNVDLKGLSDDLYRKICGGHLKPVQDAIKLYKSLGVLVEVTTLVIP 223
Cdd:COG1180    94 LAKLAKELGLHTALDTNGYIPEEALEELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIP 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904408583 224 TLNDFEEDFRGIAEFIKSVGVDIPWHISQFYPTYKLTHIPPTPVTTLREARGIGLDVGLRYVYEGNVPG 292
Cdd:COG1180   174 GLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLEDVPPPSPETLERAREIAREYGLKYVYIGNVPG 242
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
79-235 1.76e-16

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 75.64  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  79 TVGCNFRCKNCQNFEISQMPKegeklivGEDVSPEEIVAAAKQY---GCRSIAYTYTEPTIFFEFAYDTARLA---HKEG 152
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARGK-------GRELSPEEILEEAKELkrlGVEVVILGGGEPLLLPDLVELLERLLkleLAEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 153 ICNTFISNG-HITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICGGH-LKPVQDAIKLYKSLGVLVEVTTLV-IPTLNDf 228
Cdd:pfam04055  75 IRITLETNGtLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHtFEEVLEALELLREAGIPVVTDNIVgLPGETD- 153

                  ....*..
gi 1904408583 229 eEDFRGI 235
Cdd:pfam04055 154 -EDLEET 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
81-274 8.61e-13

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: 66.20  E-value: 8.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  81 GCNFRCKNCQNFEISQMPKEGEKLIvgedVSPEEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLA-HKEGICNTFIS 159
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEI----EEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKkELPGFEISIET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 160 NGH-ITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICGG--HLKPVQDAIKLYKSLGVLVEVTTLVIPTLNDFEEDFRGI 235
Cdd:cd01335    82 NGTlLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSgeSFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1904408583 236 AEFIKSVGVDiPWHISQFYPTYKLTHIPPTPVTTLREAR 274
Cdd:cd01335   162 ELLAEFRSPD-RVSLFRLLPEEGTPLELAAPVVPAEKLL 199
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
74-266 1.36e-04

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 42.39  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583   74 AYSIATVGCNFRCKNCQNFEISQMPKegeklivgeDVSPEEIVAAAK----------QYGCRSIAY---TYTEPTIFFEF 140
Cdd:smart00729   3 ALYIITRGCPRRCTFCSFPSLRGKLR---------SRYLEALVREIEllaekgekegLVGTVFIGGgtpTLLSPEQLEEL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  141 AYDTARLAHKEGICNTFISN--GHITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICGGH-LKPVQDAIKLYKSLGVLVE 216
Cdd:smart00729  74 LEAIREILGLAKDVEITIETrpDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHtVEDVLEAVELLREAGPIKV 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1904408583  217 VTTLVI--PTLNdfEEDFRGIAEFIKSVGVDipwHISqfypTYKLTHIPPTP 266
Cdd:smart00729 154 STDLIVglPGET--EEDFEETLKLLKELGPD---RVS----IFPLSPRPGTP 196
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
82-239 1.86e-04

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 42.82  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  82 CNFRCKNCqnfeisqMPKEGEKLIVGED-VSPEEIVAAAK---QYGCRSIAYTYTEPTIFFEFAYDTARLAHKEGICNTF 157
Cdd:PLN02951   68 CNLRCQYC-------MPEEGVELTPKSHlLSQDEIVRLAGlfvAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLA 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 158 I-SNGHITEEAI-RTVAPYLDAVNVDLKGLSDDLY-----RKicgGH---LKPVQDAIKL-YKSlgvlVEVTTLVIPTLN 226
Cdd:PLN02951  141 MtTNGITLSRKLpRLKEAGLTSLNISLDTLVPAKFefltrRK---GHdrvLESIDTAIELgYNP----VKVNCVVMRGFN 213
                         170
                  ....*....|...
gi 1904408583 227 DFEedfrgIAEFI 239
Cdd:PLN02951  214 DDE-----ICDFV 221
 
Name Accession Description Interval E-value
AmmeMemoSam_rS TIGR04337
AmmeMemoRadiSam system radical SAM enzyme; Members of this protein family are uncharacterized ...
6-334 4.66e-124

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: 359.69  E-value: 4.66e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583   6 FYENLEGNAVRCHLCPHHCKINESRRGICGVRENRGGVLYSLVYGKVVARGIDPIEKKPFFHFYPGSEAYSIATVGCNFR 85
Cdd:TIGR04337   3 YWHRLDDGRIQCDLCPRFCKLREGQRGLCFVRARQDGQIVLTTYGRSSGFCIDPIEKKPLNHFLPGTPVLSFGTAGCNLA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  86 CKNCQNFEISqmpKEGEKLIVGEDVSPEEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLAHKEGICNTFISNGHITE 165
Cdd:TIGR04337  83 CKFCQNWDIS---KSREMDTLADQASPEQIARAALRLGCRSVAFTYNDPVIFAEYAIDVAQACRERGIKTVAVTAGYICP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 166 EAIRTVAPYLDAVNVDLKGLSDDLYRKICGGHLKPVQDAIK-LYKSLGVLVEVTTLVIPTLNDFEEDFRGIAEFIKS-VG 243
Cdd:TIGR04337 160 EPRAEFFAHMDAANVDLKAFTEDFYHKLCGGHLQPVLDTLRyLRHETDVWLEITTLLIPGENDSDAELEAMCEWIVEnLG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 244 VDIPWHISQFYPTYKLTHIPPTPVTTLREARGIGLDVGLRYVYEGNVPGEGGENTYCYQCGELLIRRYGFQILENTIQDS 323
Cdd:TIGR04337 240 PDVPLHFTAFHPDFKMLDTPPTPPATLTRAREIALANGLHYVYTGNVHDPDGGSTYCPGCGARLIGRDWYELGEWRLDAQ 319
                         330
                  ....*....|..
gi 1904408583 324 -RCPSCGARIDG 334
Cdd:TIGR04337 320 gRCPRCGTPLAG 331
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
69-292 1.35e-98

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 290.93  E-value: 1.35e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  69 YPGSEAYSIATVGCNFRCKNCQNFEISQMPKEgeklIVGEDVSPEEIVAAAKQY-----GCRSIAYTYTEPTIFFEFAYD 143
Cdd:COG1180    18 GPGSIRLSVFTQGCNLRCPYCHNPEISQGRPD----AAGRELSPEELVEEALKDrgfldSCGGVTFSGGEPTLQPEFLLD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 144 TARLAHKEGICNTFISNGHITEEAIRTVAPYLDAVNVDLKGLSDDLYRKICGGHLKPVQDAIKLYKSLGVLVEVTTLVIP 223
Cdd:COG1180    94 LAKLAKELGLHTALDTNGYIPEEALEELLPYLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIP 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1904408583 224 TLNDFEEDFRGIAEFIKSVGVDIPWHISQFYPTYKLTHIPPTPVTTLREARGIGLDVGLRYVYEGNVPG 292
Cdd:COG1180   174 GLNDSEEELEAIARFIAELGDVIPVHLLPFHPLYKLEDVPPPSPETLERAREIAREYGLKYVYIGNVPG 242
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
79-235 1.76e-16

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 75.64  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  79 TVGCNFRCKNCQNFEISQMPKegeklivGEDVSPEEIVAAAKQY---GCRSIAYTYTEPTIFFEFAYDTARLA---HKEG 152
Cdd:pfam04055   2 TRGCNLRCTYCAFPSIRARGK-------GRELSPEEILEEAKELkrlGVEVVILGGGEPLLLPDLVELLERLLkleLAEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 153 ICNTFISNG-HITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICGGH-LKPVQDAIKLYKSLGVLVEVTTLV-IPTLNDf 228
Cdd:pfam04055  75 IRITLETNGtLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHtFEEVLEALELLREAGIPVVTDNIVgLPGETD- 153

                  ....*..
gi 1904408583 229 eEDFRGI 235
Cdd:pfam04055 154 -EDLEET 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
81-274 8.61e-13

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: 66.20  E-value: 8.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  81 GCNFRCKNCQNFEISQMPKEGEKLIvgedVSPEEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLA-HKEGICNTFIS 159
Cdd:cd01335     6 GCNLNCGFCSNPASKGRGPESPPEI----EEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKkELPGFEISIET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 160 NGH-ITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICGG--HLKPVQDAIKLYKSLGVLVEVTTLVIPTLNDFEEDFRGI 235
Cdd:cd01335    82 NGTlLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSgeSFKERLEALKELREAGLGLSTTLLVGLGDEDEEDDLEEL 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1904408583 236 AEFIKSVGVDiPWHISQFYPTYKLTHIPPTPVTTLREAR 274
Cdd:cd01335   162 ELLAEFRSPD-RVSLFRLLPEEGTPLELAAPVVPAEKLL 199
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
82-220 1.80e-11

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: 61.46  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  82 CNFRCKNCqnfEISQMPKEGEKLivgedvSPEE---IVAAAKQYGCRSIAYTYTEPTIFFEFaYDTARLAHKEGICNTFI 158
Cdd:COG0535    10 CNLRCKHC---YADAGPKRPGEL------STEEakrILDELAELGVKVVGLTGGEPLLRPDL-FELVEYAKELGIRVNLS 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1904408583 159 SNGH-ITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICG--GHLKPVQDAIKLYKSLGVLVEVTTL 220
Cdd:COG0535    80 TNGTlLTEELAERLAEAgLDHVTISLDGVDPETHDKIRGvpGAFDKVLEAIKLLKEAGIPVGINTV 145
PflX COG1313
Radical SAM superfamily enzyme PflX [General function prediction only];
7-281 3.60e-11

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


Pssm-ID: 440924  Cd Length: 295  Bit Score: 62.85  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583   7 YENLEgnavRCHLCPHHCKIN--ESRRGICGVRENrggvlyslvygKVVARGidpiekkpFFHF--------YPGSeays 76
Cdd:COG1313     2 YELLE----SCTLCPRNCGVNrlAGEKGFCGAGRK-----------AKVASA--------GLHFgeepplsgTNGS---- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  77 iATV---GCNFRCKNCQNFEISQmpkEGEklivGEDVSPEEIVAAA---KQYGCRSIAY-TytePTIFFEFAYDTARLAH 149
Cdd:COG1313    55 -GTIffsGCNLRCVFCQNYEISQ---EGE----GKEISVEELAEIMlelQEQGAHNINLvT---PTHYVPQILEALKIAK 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 150 KEG-----ICNTfisNGHITEEAIRTVAPYLDAVNVDLKGLSDDLYRKICG--GHLKPVQDAIK-LYKSLGVLVE----- 216
Cdd:COG1313   124 EKGlrlpiVYNT---SGYESVETLRLLDGIVDIYLPDFKYADDELAKRYSGapDYPEVARAAIKeMHRQVGDLVFdedgi 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 217 ------VTTLVIPtlNDfEEDFRGIAEFIK-SVGVDIPWHI-SQFYPTYKLTHIPPT--PVTT------LREARGIGLDV 280
Cdd:COG1313   201 akrgliVRHLVLP--GN-LAGSKKVLRFIAeELSPDTYVSLmSQYTPAYKAREYPELnrRITReeyeeaLDYARELGLEN 277

                  .
gi 1904408583 281 G 281
Cdd:COG1313   278 G 278
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
40-245 3.07e-09

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: 56.74  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  40 RGGVLYSLVYGKVVAR------GIDPIEKKpffhfypgseaysiatvGCNFRCKNCQNFEISQMPKEGEklivgEDVSPE 113
Cdd:COG0731     3 RGGLCYKYVYGPVPSRrlgrslGINLIPNK-----------------TCNFDCVYCQRGRTTDLTRERR-----EFDDPE 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 114 EIVAAAKQY------GCRSIAY-TYT---EPTIFFEFAyDTARLAHKEGICNTF-ISNG-HITEEAIR-------TVAPY 174
Cdd:COG0731    61 EILEELIEFlrklpeEAREPDHiTFSgsgEPTLYPNLG-ELIEEIKKLRGIKTAlLTNGsLLHRPEVReellkadQVYPS 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1904408583 175 LDAVNvdlkglsDDLYRKICG--GHLKP--VQDAIKLYKSLG---VLVEvtTLVIPTLNDFEEDFRGIAEFIKSVGVD 245
Cdd:COG0731   140 LDAAD-------EETFRKINRphPGLSWerIIEGLELFRKLYkgrTVIE--TMLVKGINDSEEELEAYAELIKRINPD 208
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
69-244 1.88e-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: 53.52  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  69 YPGSEAYSIATVGCNFRCKNCQNFEISQMPKEGEklivgedVSPEEIVAAAKQygcRS-----IAYTYTEPTIFFEFAyD 143
Cdd:TIGR02495  13 YPGKLAFTIFLQGCNLKCPYCHNPLLIPRRGSGE-------IEVEELLEFLRR---RRglldgVVITGGEPTLQAGLP-D 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 144 TARLAHKEGICNTFISNGHITEEAIRTVAP-YLDAVNVDLKGLSDDlYRKICG----GHLKPVQDAIKLYKSLGVLVEVT 218
Cdd:TIGR02495  82 FLREVRELGFEVKLDTNGSNPRRLEELLEEgLVDYVAMDVKAPPEK-YGELYGleknGAAKNILKSLEILLESGIPFELR 160
                         170       180
                  ....*....|....*....|....*.
gi 1904408583 219 TLVIPTLNDfEEDFRGIAEFIKSVGV 244
Cdd:TIGR02495 161 TTVVRGFLT-EEDLAEIATRIKENGT 185
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
44-195 3.06e-08

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 53.84  E-value: 3.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  44 LYSLVYgKVVARGIDPIEKKPFFHFYpGSEAYS-IAT---VGCNFRCKNCQNFEISQMPkegekLIVGEDVSPEEivAAA 119
Cdd:COG5014    10 LGELVE-KRVARGEGGVEYRKYYRFR-GGRWYGgIATadvVGCNLRCGFCWSWRFRDFP-----LTIGKFYSPEE--VAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 120 KQYG-CRSIAYTYT-----EPTIFFEFAYDTARLAHKEGIcnTFI--SNGHI---TEEAIRTVAPYLDA-VNVDLKGLSD 187
Cdd:COG5014    81 RLIEiARERGYRQVrlsggEPTIGFEHLLKVLELFSERGL--TFIleTNGILigyDRELARELASFRNIvVRVSIKGCTP 158

                  ....*...
gi 1904408583 188 DLYRKICG 195
Cdd:COG5014   159 EEFSMLTG 166
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
81-247 1.34e-06

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: 48.21  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  81 GCNFRCKNC---QNFEISQmpkegeklivGEDVSPEEIVAAAKQYGCRSIAYTYTEPTIFFEFAYDTARLaHKEGIcNTF 157
Cdd:COG0602    29 GCNLRCSWCdtkYAWDGEG----------GKRMSAEEILEEVAALGARHVVITGGEPLLQDDLAELLEAL-KDAGY-EVA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 158 I-SNGHIteeairTVAPYLDAVNVDLK----GLSDDLYRKIcgGHLKPVqDAIKlykslgvlvevttLVIPTLNDFEEdf 232
Cdd:COG0602    97 LeTNGTL------PIPAGIDWVTVSPKlpssGEEEDNRENL--EVLRRA-DELK-------------FVVADETDLEE-- 152
                         170
                  ....*....|....*
gi 1904408583 233 rgIAEFIKSVGVDIP 247
Cdd:COG0602   153 --AEELLARLDFRCP 165
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
82-246 7.75e-06

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 46.98  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  82 CNFRCKNCqnfeisqMPKEGEKLIVGEDV-SPEEI---VAAAKQYGCRSIAYTYTEPTI---FFEFAYDTARLAHKEGIC 154
Cdd:COG2896    24 CNFRCTYC-------MPEEGYQFLPKEELlSFEEIerlVRAFVELGVRKIRLTGGEPLLrkdLPELIARLAALPGIEDLA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 155 NTfiSNGHITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICG-GHLKPVQDAIKLYKSLGVL-VEVTTLVIPTLNDFE-E 230
Cdd:COG2896    97 LT--TNGSLLARYAEALKAAgLDRVNVSLDSLDPERFRRITRrDDLDKVLAGIDAALAAGLTpVKINAVVMRGVNDDEiL 174
                         170
                  ....*....|....*.
gi 1904408583 231 DFrgiAEFIKSVGVDI 246
Cdd:COG2896   175 DL---LEFAKERGIDL 187
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
74-266 1.36e-04

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


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 42.39  E-value: 1.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583   74 AYSIATVGCNFRCKNCQNFEISQMPKegeklivgeDVSPEEIVAAAK----------QYGCRSIAY---TYTEPTIFFEF 140
Cdd:smart00729   3 ALYIITRGCPRRCTFCSFPSLRGKLR---------SRYLEALVREIEllaekgekegLVGTVFIGGgtpTLLSPEQLEEL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  141 AYDTARLAHKEGICNTFISN--GHITEEAIRTVAPY-LDAVNVDLKGLSDDLYRKICGGH-LKPVQDAIKLYKSLGVLVE 216
Cdd:smart00729  74 LEAIREILGLAKDVEITIETrpDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHtVEDVLEAVELLREAGPIKV 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1904408583  217 VTTLVI--PTLNdfEEDFRGIAEFIKSVGVDipwHISqfypTYKLTHIPPTP 266
Cdd:smart00729 154 STDLIVglPGET--EEDFEETLKLLKELGPD---RVS----IFPLSPRPGTP 196
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
82-239 1.86e-04

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 42.82  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583  82 CNFRCKNCqnfeisqMPKEGEKLIVGED-VSPEEIVAAAK---QYGCRSIAYTYTEPTIFFEFAYDTARLAHKEGICNTF 157
Cdd:PLN02951   68 CNLRCQYC-------MPEEGVELTPKSHlLSQDEIVRLAGlfvAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLA 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904408583 158 I-SNGHITEEAI-RTVAPYLDAVNVDLKGLSDDLY-----RKicgGH---LKPVQDAIKL-YKSlgvlVEVTTLVIPTLN 226
Cdd:PLN02951  141 MtTNGITLSRKLpRLKEAGLTSLNISLDTLVPAKFefltrRK---GHdrvLESIDTAIELgYNP----VKVNCVVMRGFN 213
                         170
                  ....*....|...
gi 1904408583 227 DFEedfrgIAEFI 239
Cdd:PLN02951  214 DDE-----ICDFV 221
 
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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