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Conserved domains on  [gi|1929623960|gb|QPA14639|]
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GTP 3',8-cyclase MoaA [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

GTP 3',8-cyclase MoaA( domain architecture ID 11478261)

GTP 3',8-cyclase MoaA catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z)

EC:  4.1.99.22
Gene Symbol:  moaA
PubMed:  8361352

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-329 0e+00

GTP 3',8-cyclase MoaA;


:

Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 556.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   1 MASQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPsGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDF 80
Cdd:PRK00164    4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLP-FLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  81 TDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVK 160
Cdd:PRK00164   83 EDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 161 VNTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHP 240
Cdd:PRK00164  163 VNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 241 DYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNNTGI 320
Cdd:PRK00164  243 DYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGNTGP 322

                  ....*....
gi 1929623960 321 TQNLSYIGG 329
Cdd:PRK00164  323 TRHMSYIGG 331
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-329 0e+00

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 556.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   1 MASQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPsGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDF 80
Cdd:PRK00164    4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLP-FLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  81 TDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVK 160
Cdd:PRK00164   83 EDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 161 VNTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHP 240
Cdd:PRK00164  163 VNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 241 DYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNNTGI 320
Cdd:PRK00164  243 DYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGNTGP 322

                  ....*....
gi 1929623960 321 TQNLSYIGG 329
Cdd:PRK00164  323 TRHMSYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-329 1.30e-170

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: 476.86  E-value: 1.30e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   1 MASQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPsGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDF 80
Cdd:COG2896     1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQ-FLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  81 TDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVK 160
Cdd:COG2896    80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 161 VNTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHP 240
Cdd:COG2896   160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 241 DYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNN-TG 319
Cdd:COG2896   240 GGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDfPQ 319
                         330
                  ....*....|
gi 1929623960 320 ITQNLSYIGG 329
Cdd:COG2896   320 PKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
5-329 6.99e-152

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 429.34  E-value: 6.99e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   5 LTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDII 84
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  85 AAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAIT-GQDKFNQVMAGIDAAFEAGFEKVKVNT 163
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 164 VLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISG-QVLRDELLRRGWIHQLRQRSDG---PAQVFCH 239
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSAdEILERLEQAFGPLEPVPSPRGNgpaPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 240 PDYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTH----FLHQ 315
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHsflrFTSP 320
                         330
                  ....*....|....
gi 1929623960 316 NNTGITQNLSYIGG 329
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
186-312 1.63e-57

Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of Swiss:O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.


Pssm-ID: 428955 [Multi-domain]  Cd Length: 127  Bit Score: 182.03  E-value: 1.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 186 IQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHPDYAGEIGLIMPYEKDFCATCNRLRV 265
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1929623960 266 SSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHF 312
Cdd:pfam06463  81 TADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
252-321 2.30e-26

Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding Twitch domain is found at the C-terminus of GTP 3',8-cyclase (EC 4.1.99.22), which is also called molybdenum cofactor biosynthesis protein A (MoaA) in bacteria and archaea, molybdenum cofactor biosynthesis protein 1 (MOCS1) in most eukaryotes, and molybdenum cofactor biosynthesis enzyme CNX2 in plants. GTP 3',8-cyclase is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the first step in molybdopterin biosynthesis, the cyclization of guanosine triphosphate to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate, which is then converted to molybdopterin in subsequent steps. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. GTP 3',8-cyclase contains an additional iron-sulfur cluster at the C-terminal Twitch domain that is involved in substrate binding. The Twitch domain may be related to another iron-sulfur cluster-binding domain found at the C-terminus of some radical SAM enzymes, the SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSMEs, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively.


Pssm-ID: 411052 [Multi-domain]  Cd Length: 70  Bit Score: 99.16  E-value: 2.30e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 252 YEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNNTGIT 321
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
15-162 9.33e-12

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: 63.57  E-value: 9.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   15 YLRLSITDVCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLG-TEKVRLTGGEPSL--RRDFTDIIAAVREND 91
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGEKEGlVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929623960   92 AIRQ---IAVTTNGYRLERDVAS-WRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKVN 162
Cdd:smart00729  82 GLAKdveITIETRPDTLTEELLEaLKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTD 156
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-329 0e+00

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 556.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   1 MASQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPsGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDF 80
Cdd:PRK00164    4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLP-FLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  81 TDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVK 160
Cdd:PRK00164   83 EDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 161 VNTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHP 240
Cdd:PRK00164  163 VNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHP 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 241 DYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNNTGI 320
Cdd:PRK00164  243 DYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGNTGP 322

                  ....*....
gi 1929623960 321 TQNLSYIGG 329
Cdd:PRK00164  323 TRHMSYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-329 1.30e-170

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: 476.86  E-value: 1.30e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   1 MASQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPsGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDF 80
Cdd:COG2896     1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQ-FLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  81 TDIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVK 160
Cdd:COG2896    80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 161 VNTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHP 240
Cdd:COG2896   160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 241 DYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNN-TG 319
Cdd:COG2896   240 GGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDfPQ 319
                         330
                  ....*....|
gi 1929623960 320 ITQNLSYIGG 329
Cdd:COG2896   320 PKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
5-329 6.99e-152

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 429.34  E-value: 6.99e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   5 LTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDII 84
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  85 AAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAIT-GQDKFNQVMAGIDAAFEAGFEKVKVNT 163
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 164 VLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISG-QVLRDELLRRGWIHQLRQRSDG---PAQVFCH 239
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSAdEILERLEQAFGPLEPVPSPRGNgpaPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 240 PDYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTH----FLHQ 315
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHsflrFTSP 320
                         330
                  ....*....|....
gi 1929623960 316 NNTGITQNLSYIGG 329
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
5-311 2.18e-83

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 256.61  E-value: 2.18e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   5 LTDAFARKFYYLRLSITDVCNFRCTYCLPdgykPSGVT---NKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFT 81
Cdd:PLN02951   49 LVDSFGRRHNYLRISLTERCNLRCQYCMP----EEGVEltpKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  82 DIIAAVRENDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKV 161
Cdd:PLN02951  125 DICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 162 NTVLMRDVNHHQLDTFLNWIQHRPIQLRFIELMETgEGSELFRKHHISGQVLRDELLRRgwIHQLRQRSDGPAQV---FC 238
Cdd:PLN02951  205 NCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPF-DGNVWNVKKLVPYAEMMDRIEQR--FPSLKRLQDHPTDTaknFR 281
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929623960 239 HPDYAGEIGLIMPYEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTH 311
Cdd:PLN02951  282 IDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREIIGAAVKRKKAAH 354
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
5-306 3.85e-73

probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an archaeal family related, and predicted to be functionally equivalent, to molybdenum cofactor biosynthesis protein A (MoaA) of bacteria (see TIGR02666). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274251 [Multi-domain]  Cd Length: 302  Bit Score: 227.96  E-value: 3.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   5 LTDAFARKFYYLRLSITDVCNFRCTYCLPDGykpSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDII 84
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYCHMEG---EDRSGGNELSPEEIERIVRVASEFGVRKVKITGGEPLLRKDLIEII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  85 AAVReNDAIRQIAVTTNGYRLERDVASWRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKVNTV 164
Cdd:TIGR02668  78 RRIK-DYGIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDRVIEGIESAVDAGLTPVKLNMV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 165 LMRDVNHHQLDTFLNWIQHRPIQLRFIELMETGEGSELFRKHHISGQVLRDELlrrgwihqlRQRSDGPAQVFCH--PDY 242
Cdd:TIGR02668 157 VLKGINDNEIPDMVEFAAEGGAILQLIELMPPGEGEKEFKKYHEDIDPIEEEL---------EKMADRVRTRRMHnrPKY 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1929623960 243 ----AGEIGLIMPYEK-DFCATCNRLRVSSIGKLHLCLFGEGG-VNLRDLLEDDTQQQALEA-RISAALRE 306
Cdd:TIGR02668 228 fipgGVEVEVVKPMDNpVFCAHCTRLRLTSDGKLKTCLLRDDNlVDILDALRNGEDDELREAfREAVARRE 298
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
186-312 1.63e-57

Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of Swiss:O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.


Pssm-ID: 428955 [Multi-domain]  Cd Length: 127  Bit Score: 182.03  E-value: 1.63e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 186 IQLRFIELMETGEGSELFRKHHISGQVLRDELLRRGWIHQLRQRSDGPAQVFCHPDYAGEIGLIMPYEKDFCATCNRLRV 265
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1929623960 266 SSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHF 312
Cdd:pfam06463  81 TADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
15-165 1.34e-34

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: 123.86  E-value: 1.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  15 YLRLSITDVCNFRCTYClpdgYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIr 94
Cdd:COG0535     1 RLQIELTNRCNLRCKHC----YADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIR- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1929623960  95 qIAVTTNGYRLERDVA-SWRDAGLTGINVSVDSLDARQFHAITGQDK-FNQVMAGIDAAFEAGFeKVKVNTVL 165
Cdd:COG0535    76 -VNLSTNGTLLTEELAeRLAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGI-PVGINTVY 146
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
20-175 2.59e-29

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: 109.92  E-value: 2.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  20 ITDVCNFRCTYClpDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAV--RENDAIRQIA 97
Cdd:pfam04055   1 ITRGCNLRCTYC--AFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLlkLELAEGIRIT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1929623960  98 VTTNGYRLERDVAS-WRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKVNTVLMRDVNHHQLD 175
Cdd:pfam04055  79 LETNGTLLDEELLElLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLE 157
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
252-321 2.30e-26

Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding Twitch domain is found at the C-terminus of GTP 3',8-cyclase (EC 4.1.99.22), which is also called molybdenum cofactor biosynthesis protein A (MoaA) in bacteria and archaea, molybdenum cofactor biosynthesis protein 1 (MOCS1) in most eukaryotes, and molybdenum cofactor biosynthesis enzyme CNX2 in plants. GTP 3',8-cyclase is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the first step in molybdopterin biosynthesis, the cyclization of guanosine triphosphate to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate, which is then converted to molybdopterin in subsequent steps. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. GTP 3',8-cyclase contains an additional iron-sulfur cluster at the C-terminal Twitch domain that is involved in substrate binding. The Twitch domain may be related to another iron-sulfur cluster-binding domain found at the C-terminus of some radical SAM enzymes, the SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSMEs, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively.


Pssm-ID: 411052 [Multi-domain]  Cd Length: 70  Bit Score: 99.16  E-value: 2.30e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 252 YEKDFCATCNRLRVSSIGKLHLCLFGEGGVNLRDLLEDDTQQQALEARISAALREKKQTHFLHQNNTGIT 321
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
18-274 1.42e-15

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 76.56  E-value: 1.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  18 LSITDVCNFRCTYClpdgYKPSGVTNKGFL----TVDE-IRRVTRAFARLGTEKVRLTGGEPSLRRDF----TDIIAAVR 88
Cdd:COG0641     5 LKPTSRCNLRCSYC----YYSEGDEGSRRRmseeTAEKaIDFLIESSGPGKELTITFFGGEPLLNFDFikeiVEYARKYA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  89 ENDAIRQIAVTTNGYRLERDVASW-RDAgltGINVSVdSLDARQ-FH-----AITGQDKFNQVMAGIDAAFEAGFEkVKV 161
Cdd:COG0641    81 KKGKKIRFSIQTNGTLLDDEWIDFlKEN---GFSVGI-SLDGPKeIHdrnrvTKNGKGSFDRVMRNIKLLKEHGVE-VNI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 162 NTVLMRDvNHHQLDTFLNWI-QHRPIQLRFIELMETGEGSELFRKHHIsGQVLRdELLRRgWIhqlrqRSDGPAQVFCHp 240
Cdd:COG0641   156 RCTVTRE-NLDDPEELYDFLkELGFRSIQFNPVVEEGEADYSLTPEDY-GEFLI-ELFDE-WL-----ERDGGKIFVRE- 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1929623960 241 dYAGEIGLIMPYEKDFC-ATCNR-LRVSSIGKLHLC 274
Cdd:COG0641   226 -FDILLAGLLPPCSSPCvGAGGNyLVVDPDGDIYPC 260
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
18-171 3.44e-15

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: 73.14  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  18 LSITDVCNFRCTYClpDGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIRQIA 97
Cdd:cd01335     1 LELTRGCNLNCGFC--SNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEIS 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1929623960  98 VTTNGYRLERD-VASWRDAGLTGINVSVDSLDARQFHAITG-QDKFNQVMAGIDAAFEAGFekvKVNTVLMRDVNH 171
Cdd:cd01335    79 IETNGTLLTEElLKELKELGLDGVGVSLDSGDEEVADKIRGsGESFKERLEALKELREAGL---GLSTTLLVGLGD 151
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
13-278 2.50e-12

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 66.79  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  13 FYYLrlsiTDVCNFRCTYCLPD-GYKPSGVTNKGfLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVREND 91
Cdd:TIGR04251   7 YFYL----TEGCNLKCRHCWIDpKYQGEGEQHPS-LDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGENN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  92 AirQIAVTTNGYRLERDVA-SWRDAGLTGINVSVDSLDARQFHAITG-QDKFNQVMAGIDAAFEAGFEKVKVNTVLMRDV 169
Cdd:TIGR04251  82 L--QLSVETNGLLCTPQTArDLASCETPFVSVSLDGVDAATHDWMRGvKGAFDKAVRGIHNLVEAGIHPQIIMTVTRRNV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 170 NhhQLDTFLNWIQHRPIQ-LRFIELMETGEGSELFRkhhiSGQVLR-DELLRRG-WIHQLRQRSDGPAQVFCHPDYAGEI 246
Cdd:TIGR04251 160 G--QMEQIVRLAESLGAEsVKFNHVQPTSRGSKMHE----NGETLSiGELVALGeWMERTLIPSTALRIDFGHPPAFRPL 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1929623960 247 GLIMPYEKDFCATC---NRLRVSSIGKLHLCLFGE 278
Cdd:TIGR04251 234 GRMFGEKPGGCGLCgifGILGVLSDGSYALCGIGE 268
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
15-162 9.33e-12

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: 63.57  E-value: 9.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   15 YLRLSITDVCNFRCTYCLPDGYKPSGVTNKGFLTVDEIRRVTRAFARLG-TEKVRLTGGEPSL--RRDFTDIIAAVREND 91
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGEKEGlVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929623960   92 AIRQ---IAVTTNGYRLERDVAS-WRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGFEKVKVN 162
Cdd:smart00729  82 GLAKdveITIETRPDTLTEELLEaLKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTD 156
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
20-142 1.73e-10

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 61.08  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  20 ITDVCNFRCTYCLPD-GykPSGVTNKGFLTVD------EIRRVtrafARLGTEKVRL---TGGEPSLRRDFTDIIAAVRE 89
Cdd:COG2100    42 PTTGCNLNCIFCSVDaG--PHSRTRQAEYIVDpeylveWFEKV----ARFKGKGVEAhidGVGEPLLYPYIVELVKGLKE 115
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1929623960  90 NDAIRQIAVTTNGYRLERDVA-SWRDAGLTGINVSVDSLDARQFHAITGQDKFN 142
Cdd:COG2100   116 IKGVKVVSMQTNGTLLSEKLIdELEEAGLDRINLSIDTLDPEKAKKLAGTKWYD 169
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
23-193 9.28e-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: 58.28  E-value: 9.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  23 VCNFRCTYC-LPDGYKPSgVTNKGFLTVDEIRRVTRAFARLGTEKVR------LTG-GEPSLRRDFTDIIAAVRENDAIR 94
Cdd:COG0731    33 TCNFDCVYCqRGRTTDLT-RERREFDDPEEILEELIEFLRKLPEEARepdhitFSGsGEPTLYPNLGELIEEIKKLRGIK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  95 qIAVTTNGYRLER-DVAswrdAGLTGIN---VSVDSLDARQFHAIT---GQDKFNQVMAGIDAAFEAGFEKVKVNTVLMR 167
Cdd:COG0731   112 -TALLTNGSLLHRpEVR----EELLKADqvyPSLDAADEETFRKINrphPGLSWERIIEGLELFRKLYKGRTVIETMLVK 186
                         170       180
                  ....*....|....*....|....*...
gi 1929623960 168 DVN--HHQLDTFLNWIqhRPIQLRFIEL 193
Cdd:COG0731   187 GINdsEEELEAYAELI--KRINPDFVEL 212
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
24-190 2.61e-09

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 56.73  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  24 CNFRCTYCL-PDGYKPSGVTNKGFLTVDEIRRVTRAFARL--GTEKVRLTGGEPSLRRDFT-DIIAAVRENDaIRqIAVT 99
Cdd:COG1180    31 CNLRCPYCHnPEISQGRPDAAGRELSPEELVEEALKDRGFldSCGGVTFSGGEPTLQPEFLlDLAKLAKELG-LH-TALD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960 100 TNGYRLERDVASWRDaGLTGINVSVDSLDARQFHAITGQDkfNQ-VMAGIDAAFEAGFEkVKVNTVLMRDVN--HHQLDT 176
Cdd:COG1180   109 TNGYIPEEALEELLP-YLDAVNIDLKAFDDEFYRKLTGVS--LEpVLENLELLAESGVH-VEIRTLVIPGLNdsEEELEA 184
                         170
                  ....*....|....*....
gi 1929623960 177 FLNWIQH----RPIQL-RF 190
Cdd:COG1180   185 IARFIAElgdvIPVHLlPF 203
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
11-141 1.71e-07

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 51.53  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  11 RKFYYLR-------LSITDV--CNFRCTYCLpdGYKP-SGVTNKG-FLTVDEI-RRVTRAFARLGTEKVRLTGGEPSLRR 78
Cdd:COG5014    28 RKYYRFRggrwyggIATADVvgCNLRCGFCW--SWRFrDFPLTIGkFYSPEEVaERLIEIARERGYRQVRLSGGEPTIGF 105
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  79 D-FTDIIAAVRENDAIrqIAVTTNGY------RLERDVASWRDAgltGINVSVDSLDARQFHAITGQDKF 141
Cdd:COG5014   106 EhLLKVLELFSERGLT--FILETNGIligydrELARELASFRNI---VVRVSIKGCTPEEFSMLTGADPE 170
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
18-150 3.73e-07

SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 51.01  E-value: 3.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  18 LSITDVCNFRCTYClpdGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAirQIA 97
Cdd:TIGR04250   7 IDITGRCNLRCRYC---SHFSSAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVKNRM--RFS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1929623960  98 VTTNGYRLERDVASWRDAglTG----INVSVDSLDARQFHAITGQDKFNQVMAGIDA 150
Cdd:TIGR04250  82 ILSNGTLITDAIASFLAA--TRrcdyVQVSIDGSTPGTHDRLRGTGSFLQAVEGIEL 136
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
24-102 3.13e-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: 47.05  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  24 CNFRCTYC------LPDGYKpsgvtnkgFLTVDEIrrVTRAfARLGTEKVRLTGGEPSLRRDFTDIIAAVRENDaiRQIA 97
Cdd:COG0602    30 CNLRCSWCdtkyawDGEGGK--------RMSAEEI--LEEV-AALGARHVVITGGEPLLQDDLAELLEALKDAG--YEVA 96

                  ....*
gi 1929623960  98 VTTNG 102
Cdd:COG0602    97 LETNG 101
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
1-120 6.40e-06

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 47.43  E-value: 6.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   1 MASQLTDA-FARKFYYLR---LSITDVCNFRCTYC-------LPDGYKpsgvtnkgfLTVDEIRRVTRAFARLGTEKVRL 69
Cdd:COG1060    34 LADELRRRrFGNTVTFVVnrpINLTNVCVNGCKFCafsrdngDIDRYT---------LSPEEILEEAEEAKALGATEILL 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1929623960  70 TGGE-PSLRRD-FTDIIAAVREndAIRQIAV------------TTNGYRLERDVASWRDAGLTGI 120
Cdd:COG1060   105 VGGEhPDLPLEyYLDLLRAIKE--RFPNIHIhalspeeiahlaRASGLSVEEVLERLKEAGLDSL 167
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
7-162 2.62e-04

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 42.24  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960   7 DAFARKFYYLRLSITDV--CNFRCTYCLpdgykPSGVTNKGFLT------VDEIRRVTRAFarlGTEKVRLTGGEPSL-R 77
Cdd:COG1032   165 DLLDLEAYHRRASIETSrgCPFGCSFCS-----ISALYGRKVRYrspesvVEEIEELVKRY---GIREIFFVDDNFNVdK 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1929623960  78 RDFTDIIAAVRENDAIRQIAVTTNGYRLERDVAS-WRDAGLTGINVSVDSLDARQFHAITGQDKFNQVMAGIDAAFEAGF 156
Cdd:COG1032   237 KRLKELLEELIERGLNVSFPSEVRVDLLDEELLElLKKAGCRGLFIGIESGSQRVLKAMNKGITVEDILEAVRLLKKAGI 316

                  ....*.
gi 1929623960 157 eKVKVN 162
Cdd:COG1032   317 -RVKLY 321
F420_cofG TIGR03550
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents ...
20-73 8.34e-03

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofG subunit; This model represents either a subunit or a domain, depending on whether or not the genes are fused, of a bifunctional protein that completes the synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin, or FO. FO is the chromophore of coenzyme F(420), involved in methanogenesis in methanogenic archaea but found in certain other lineages as well. The chromophore also occurs as a cofactor in DNA photolyases in Cyanobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132589 [Multi-domain]  Cd Length: 322  Bit Score: 37.66  E-value: 8.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1929623960  20 ITDVCNFRCTYCLpdGYKPSGVTNKGFLTVDEIRRVTRAFARLGTEKVRLTGGE 73
Cdd:TIGR03550  10 LTRLCRNRCGYCT--FRRPPGELEAALLSPEEVLEILRKGAAAGCTEALFTFGE 61
 
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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