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Conserved domains on  [gi|639319593|ref|WP_024595548|]
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MULTISPECIES: GTP 3',8-cyclase MoaA [Pseudoalteromonas]

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;
1-323 4.70e-168

GTP 3',8-cyclase MoaA;


:

Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 470.01  E-value: 4.70e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   1 MLIDPTGREFSYLRLSITDVCNFKCVYCLPDGYQGGHDRG-FLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:PRK00164   7 QLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEeLLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDII 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGIDSVKINSV 159
Cdd:PRK00164  87 AALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVKVNAV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 160 LMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQG 239
Cdd:PRK00164 167 LMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHPDYGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 240 RIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGNTGITTNL 318
Cdd:PRK00164 247 EIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLrSGADDEELAAAIREALQNKPEGHGLHDGNTGPTRHM 326

                 ....*
gi 639319593 319 SMLGG 323
Cdd:PRK00164 327 SYIGG 331
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-323 4.70e-168

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 470.01  E-value: 4.70e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   1 MLIDPTGREFSYLRLSITDVCNFKCVYCLPDGYQGGHDRG-FLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:PRK00164   7 QLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEeLLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDII 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGIDSVKINSV 159
Cdd:PRK00164  87 AALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVKVNAV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 160 LMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQG 239
Cdd:PRK00164 167 LMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHPDYGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 240 RIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGNTGITTNL 318
Cdd:PRK00164 247 EIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLrSGADDEELAAAIREALQNKPEGHGLHDGNTGPTRHM 326

                 ....*
gi 639319593 319 SMLGG 323
Cdd:PRK00164 327 SYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-323 7.13e-151

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: 426.40  E-value: 7.13e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   1 MLIDPTGREFSYLRLSITDVCNFKCVYCLP-DGYQGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:COG2896    4 PLIDRFGRPIDYLRISVTDRCNFRCTYCMPeEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGIDSVKINSV 159
Cdd:COG2896   84 ARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 160 LMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQG 239
Cdd:COG2896  164 VMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVPGGGG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 240 RIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGN-TGITTN 317
Cdd:COG2896  244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLrSGASDEELAEAIREAIARKPEGHGFDEGDfPQPKRS 323

                 ....*.
gi 639319593 318 LSMLGG 323
Cdd:COG2896  324 MSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
2-323 2.17e-119

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: 346.91  E-value: 2.17e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593    2 LIDPTGREFSYLRLSITDVCNFKCVYCLPDG--YQGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGggLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTIT-GHDKFTSVMKGIDTALETGIDSVKINS 158
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  159 VLMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQT-GWQQVARSAS---AGPAQEFAH 234
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAfGPLEPVPSPRgngPAPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  235 PDYQGRIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSR--YIKTKK--PTHLLHQ 309
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLrGGASDALLEAIIQAilQKKPEGhsFLRFTSP 320
                         330
                  ....*....|....
gi 639319593  310 GNTGITTNLSMLGG 323
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
181-305 4.33e-46

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: 152.37  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  181 VTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQGRIGLIMPYSNDFCSTCNRLRV 260
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 639319593  261 TAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTH 305
Cdd:pfam06463  81 TADGKLKTCLFAEDGIDLRDALrSGDDDEELREAIREALARKPPRH 126
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
247-315 1.33e-24

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: 94.53  E-value: 1.33e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 247 YSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGNTGIT 315
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALrSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
13-125 3.39e-07

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 51.12  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  13 LRLSitDVCNFKCVYC--------------LPDGYQGGHDR-GFLTIDEISNTLKAFAHHgIEKVRITGGEPTLRKDFID 77
Cdd:NF033640 114 LRFG--NLCNLKCRMCgphsssswakeakkLGGPKLGDKKKiSWFEDEEFWKWLEELLPS-LKEIYFAGGEPLLIKEHYK 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639319593  78 VVR------AAKDVagikKIAMTTNGFSLHKNIHDWVD-------VglnAINVSIDSLDSR 125
Cdd:NF033640 191 LLEklvekgRAKNI----ELRYNTNLTVLPDKLKDLLDlwkkfksV---SISASIDGVGER 244
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
11-157 3.59e-07

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: 50.09  E-value: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593    11 SYLRLSITDVCNFKCVYClpDGYQGGHDRGFLTIDEISNTLKAFAHHG-----IEKVRITGGEPTL--RKDFIDVVRAAK 83
Cdd:smart00729   1 PLALYIITRGCPRRCTFC--SFPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLlsPEQLEELLEAIR 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639319593    84 DVAGIKK---IAMTTNGFSL-HKNIHDWVDVGLNAINVSIDSLDSRMFNTI-TGHDkFTSVMKGIDTALETGIDSVKIN 157
Cdd:smart00729  79 EILGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAInRGHT-VEDVLEAVELLREAGPIKVSTD 156
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-323 4.70e-168

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 470.01  E-value: 4.70e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   1 MLIDPTGREFSYLRLSITDVCNFKCVYCLPDGYQGGHDRG-FLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:PRK00164   7 QLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEeLLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDII 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGIDSVKINSV 159
Cdd:PRK00164  87 AALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPVKVNAV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 160 LMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQG 239
Cdd:PRK00164 167 LMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYFRHPDYGG 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 240 RIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGNTGITTNL 318
Cdd:PRK00164 247 EIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLrSGADDEELAAAIREALQNKPEGHGLHDGNTGPTRHM 326

                 ....*
gi 639319593 319 SMLGG 323
Cdd:PRK00164 327 SYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-323 7.13e-151

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: 426.40  E-value: 7.13e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   1 MLIDPTGREFSYLRLSITDVCNFKCVYCLP-DGYQGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:COG2896    4 PLIDRFGRPIDYLRISVTDRCNFRCTYCMPeEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGIDSVKINSV 159
Cdd:COG2896   84 ARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 160 LMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQG 239
Cdd:COG2896  164 VMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVPGGGG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 240 RIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGN-TGITTN 317
Cdd:COG2896  244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLrSGASDEELAEAIREAIARKPEGHGFDEGDfPQPKRS 323

                 ....*.
gi 639319593 318 LSMLGG 323
Cdd:COG2896  324 MSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
2-323 2.17e-119

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: 346.91  E-value: 2.17e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593    2 LIDPTGREFSYLRLSITDVCNFKCVYCLPDG--YQGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGggLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTIT-GHDKFTSVMKGIDTALETGIDSVKINS 158
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  159 VLMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQT-GWQQVARSAS---AGPAQEFAH 234
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAfGPLEPVPSPRgngPAPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  235 PDYQGRIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSR--YIKTKK--PTHLLHQ 309
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLrGGASDALLEAIIQAilQKKPEGhsFLRFTSP 320
                         330
                  ....*....|....
gi 639319593  310 GNTGITTNLSMLGG 323
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
1-305 1.71e-85

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 262.00  E-value: 1.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   1 MLIDPTGREFSYLRLSITDVCNFKCVYCLP-DGYQGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVV 79
Cdd:PLN02951  48 MLVDSFGRRHNYLRISLTERCNLRCQYCMPeEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDIC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  80 RAAKDVAGIKKIAMTTNGFSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTIT---GHDKftsVMKGIDTALETGIDSVKI 156
Cdd:PLN02951 128 LQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTrrkGHDR---VLESIDTAIELGYNPVKV 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 157 NSVLMKQYNAKEFDTFLNWVKHRPVTIRFIELMQTNDNKaFFDANHVSGQVLKTQLLQtGWQQVAR--SASAGPAQEFAH 234
Cdd:PLN02951 205 NCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNV-WNVKKLVPYAEMMDRIEQ-RFPSLKRlqDHPTDTAKNFRI 282
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639319593 235 PDYQGRIGLIMPYSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYMND-SSNSELMALLSRYIKTKKPTH 305
Cdd:PLN02951 283 DGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSgADDDELREIIGAAVKRKKAAH 354
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
181-305 4.33e-46

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: 152.37  E-value: 4.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  181 VTIRFIELMQTNDNKAFFDANHVSGQVLKTQLLQTGWQQVARSASAGPAQEFAHPDYQGRIGLIMPYSNDFCSTCNRLRV 260
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 639319593  261 TAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTH 305
Cdd:pfam06463  81 TADGKLKTCLFAEDGIDLRDALrSGDDDEELREAIREALARKPPRH 126
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
12-160 2.96e-32

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: 117.70  E-value: 2.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  12 YLRLSITDVCNFKCVYCLPDGyqGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVVRAAKDvAGIkKI 91
Cdd:COG0535    1 RLQIELTNRCNLRCKHCYADA--GPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKE-LGI-RV 76
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639319593  92 AMTTNGFSLHKNIHD-WVDVGLNAINVSIDSLDSRMFNTITGHDK-FTSVMKGIDTALETGIDsVKINSVL 160
Cdd:COG0535   77 NLSTNGTLLTEELAErLAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGIP-VGINTVY 146
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
17-172 1.50e-26

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


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 102.60  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   17 ITDVCNFKCVYCLPDGYQGGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVVRAAK--DVAGIKKIAMT 94
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLklELAEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639319593   95 TNGFSLHKN-IHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGIDSVKINSVLMKQYNAKEFDTF 172
Cdd:pfam04055  81 TNGTLLDEElLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEET 159
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
247-315 1.33e-24

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: 94.53  E-value: 1.33e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 247 YSNDFCSTCNRLRVTAKGNLHLCLFSEEGISLREYM-NDSSNSELMALLSRYIKTKKPTHLLHQGNTGIT 315
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALrSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
17-177 1.63e-17

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 81.88  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  17 ITDVCNFKCVYCLPDGYQGGHDRGFLTIDEISNTLKAFAH------HGIEkVRITG-GEPTLRKDFIDVVRAAKDVAGIK 89
Cdd:COG2100   42 PTTGCNLNCIFCSVDAGPHSRTRQAEYIVDPEYLVEWFEKvarfkgKGVE-AHIDGvGEPLLYPYIVELVKGLKEIKGVK 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  90 KIAMTTNGFSL-HKNIHDWVDVGLNAINVSIDSLDSRMFNTITGHDKFtSVMKGIDTA----LETGIDsVKINSVLMKQY 164
Cdd:COG2100  121 VVSMQTNGTLLsEKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWY-DVEKVLELAeyiaRETKID-LLIAPVWLPGI 198
                        170
                 ....*....|...
gi 639319593 165 NAKEFDTFLNWVK 177
Cdd:COG2100  199 NDEDIPKIIEWAL 211
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
15-269 4.25e-17

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 80.80  E-value: 4.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  15 LSITDVCNFKCVYClpdgYQGGHD---RGFLTIDeisnTLKAF------AHHGIEKVRIT--GGEPTLRKDFI-DVVRAA 82
Cdd:COG0641    5 LKPTSRCNLRCSYC----YYSEGDegsRRRMSEE----TAEKAidflieSSGPGKELTITffGGEPLLNFDFIkEIVEYA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  83 KDVAGIKK---IAMTTNGFSLHkniHDWVDVgLNA--INVSIdSLDsrmfntitG----HDK----------FTSVMKGI 143
Cdd:COG0641   77 RKYAKKGKkirFSIQTNGTLLD---DEWIDF-LKEngFSVGI-SLD--------GpkeiHDRnrvtkngkgsFDRVMRNI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593 144 DTALETGIDsVKINSVLMKqYNAKEFDTFLNWVKHRPVT-IRFIELMQTNDNKAFFDANHVSgqvlktQLLQTGWQQVAR 222
Cdd:COG0641  144 KLLKEHGVE-VNIRCTVTR-ENLDDPEELYDFLKELGFRsIQFNPVVEEGEADYSLTPEDYG------EFLIELFDEWLE 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 639319593 223 saSAGPAQEFAHpdYQGRIGLIMPYSNDFCSTC--NRLRVTAKGNLHLC 269
Cdd:COG0641  216 --RDGGKIFVRE--FDILLAGLLPPCSSPCVGAggNYLVVDPDGDIYPC 260
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
15-212 7.92e-16

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 74.68  E-value: 7.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  15 LSITDVCNFKCVYClpdGYQGGHDRGFLTIDEISNTLKAF---AHHGIEKVRITGGEPTLRKDFIDVVRAAKDVAGIKKI 91
Cdd:cd01335    1 LELTRGCNLNCGFC---SNPASKGRGPESPPEIEEILDIVleaKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  92 AMTTNGFSLHKN-IHDWVDVGLNAINVSIDSLDSRMFNTITGHDK-FTSVMKGIDTALETGIdSVKINSVLMKQYNAKEF 169
Cdd:cd01335   78 SIETNGTLLTEElLKELKELGLDGVGVSLDSGDEEVADKIRGSGEsFKERLEALKELREAGL-GLSTTLLVGLGDEDEED 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 639319593 170 DTF---LNWVKHRPVTIRFIELMQTNDNKAFFDANHVSGQVLKTQL 212
Cdd:cd01335  157 DLEeleLLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLI 202
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
6-190 1.90e-13

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 68.67  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   6 TGREFSYLRLSITDV------------CNFKCVYCL-PDGYQGGHDRG--FLTIDEISNTLKAFAH--HGIEKVRITGGE 68
Cdd:COG1180    4 RGRIYGISPFSTVDGpgsirlsvftqgCNLRCPYCHnPEISQGRPDAAgrELSPEELVEEALKDRGflDSCGGVTFSGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  69 PTLRKDF-IDVVRAAKDvAGIkKIAMTTNGFSLHKNIHDWVDVgLNAINVSIDSLDSRMFNTITGHDkFTSVMKGIDTAL 147
Cdd:COG1180   84 PTLQPEFlLDLAKLAKE-LGL-HTALDTNGYIPEEALEELLPY-LDAVNIDLKAFDDEFYRKLTGVS-LEPVLENLELLA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 639319593 148 ETGIDsVKINSVLMKQYN--AKEFDTFLNWVKHRPVTIRfIELMQ 190
Cdd:COG1180  160 ESGVH-VEIRTLVIPGLNdsEEELEAIARFIAELGDVIP-VHLLP 202
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
20-149 8.03e-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: 8.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  20 VCNFKCVYC-LPDGYQGGHDRG-FLTIDEISNTLKAFAHHGIEKVR------ITG-GEPTLRKDFIDVVRAAKDVAGIkK 90
Cdd:COG0731   33 TCNFDCVYCqRGRTTDLTRERReFDDPEEILEELIEFLRKLPEEARepdhitFSGsGEPTLYPNLGELIEEIKKLRGI-K 111
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639319593  91 IAMTTNGFSLHKNihdwvDV--GLNAIN---VSIDSLDSRMFNTIT---GHDKFTSVMKGID---------TALET 149
Cdd:COG0731  112 TALLTNGSLLHRP-----EVreELLKADqvyPSLDAADEETFRKINrphPGLSWERIIEGLElfrklykgrTVIET 182
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
21-108 1.73e-07

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


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 50.91  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  21 CNFKCVYC----LPDGYQGGhdrgFLTIDEISNTLKAFAHHgieKVRITGGEPTLRKDFIDVVRAAKDvAGIkKIAMTTN 96
Cdd:COG0602   30 CNLRCSWCdtkyAWDGEGGK----RMSAEEILEEVAALGAR---HVVITGGEPLLQDDLAELLEALKD-AGY-EVALETN 100
                         90
                 ....*....|...
gi 639319593  97 G-FSLHKNIhDWV 108
Cdd:COG0602  101 GtLPIPAGI-DWV 112
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
13-125 3.39e-07

twitch domain-containing radical SAM protein; Members of this family are unusual among radical SAM proteins in several ways. First, the N-terminal region consists of an iron-sulfur cluster-binding twitch domain (half of a SPASM domain), something usually found C-terminal to the radical SAM domain. Second, the radical SAM domains in many of the members of this family score poorly vs. the Pfam HMM, PF04055 (version 19), used to identify radical SAM. Lastly, the majority of members sequenced to date come from uncultured bacteria from marine or aquifer sources rather than from conventionally cultured bacterial isolates. The function is unknown.


Pssm-ID: 468123 [Multi-domain]  Cd Length: 396  Bit Score: 51.12  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  13 LRLSitDVCNFKCVYC--------------LPDGYQGGHDR-GFLTIDEISNTLKAFAHHgIEKVRITGGEPTLRKDFID 77
Cdd:NF033640 114 LRFG--NLCNLKCRMCgphsssswakeakkLGGPKLGDKKKiSWFEDEEFWKWLEELLPS-LKEIYFAGGEPLLIKEHYK 190
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639319593  78 VVR------AAKDVagikKIAMTTNGFSLHKNIHDWVD-------VglnAINVSIDSLDSR 125
Cdd:NF033640 191 LLEklvekgRAKNI----ELRYNTNLTVLPDKLKDLLDlwkkfksV---SISASIDGVGER 244
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
11-157 3.59e-07

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: 50.09  E-value: 3.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593    11 SYLRLSITDVCNFKCVYClpDGYQGGHDRGFLTIDEISNTLKAFAHHG-----IEKVRITGGEPTL--RKDFIDVVRAAK 83
Cdd:smart00729   1 PLALYIITRGCPRRCTFC--SFPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLlsPEQLEELLEAIR 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639319593    84 DVAGIKK---IAMTTNGFSL-HKNIHDWVDVGLNAINVSIDSLDSRMFNTI-TGHDkFTSVMKGIDTALETGIDSVKIN 157
Cdd:smart00729  79 EILGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAInRGHT-VEDVLEAVELLREAGPIKVSTD 156
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
17-115 9.07e-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: 46.66  E-value: 9.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  17 ITDVCNFKCVYClpdGYQ---GGHDRGFLTIDEISNTLKAFAHHGIEKVRITGGE-PTLRKDFI-DVVRAAKD------- 84
Cdd:COG1060   57 LTNVCVNGCKFC---AFSrdnGDIDRYTLSPEEILEEAEEAKALGATEILLVGGEhPDLPLEYYlDLLRAIKErfpnihi 133
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 639319593  85 ----VAGIKKIAmTTNGFSLHKNIHDWVDVGLNAI 115
Cdd:COG1060  134 halsPEEIAHLA-RASGLSVEEVLERLKEAGLDSL 167
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
17-273 1.67e-05

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: 45.98  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   17 ITDVCNFKCVYCLPD-GYQG-GHDRGFLTIDEISNTLKAFAHHGIEKVRITGGEPTLRKDFIDVVRAAKdvAGIKKIAMT 94
Cdd:TIGR04251  10 LTEGCNLKCRHCWIDpKYQGeGEQHPSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIG--ENNLQLSVE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   95 TNG-FSLHKNIHDWVDVGLNAINVSIDSLDSRMFNTITG-HDKFTSVMKGIDTALETGIDSVKINSVLmkQYNAKEFDTF 172
Cdd:TIGR04251  88 TNGlLCTPQTARDLASCETPFVSVSLDGVDAATHDWMRGvKGAFDKAVRGIHNLVEAGIHPQIIMTVT--RRNVGQMEQI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  173 LNWVKH-RPVTIRFIELMQTNDNKAFfdanHVSGQVLKT-QLLQTG-WQQVARSASAGPAQEFAHPDYQGRIGLIMPYSN 249
Cdd:TIGR04251 166 VRLAESlGAESVKFNHVQPTSRGSKM----HENGETLSIgELVALGeWMERTLIPSTALRIDFGHPPAFRPLGRMFGEKP 241
                         250       260
                  ....*....|....*....|....*..
gi 639319593  250 DFCSTC---NRLRVTAKGNLHLCLFSE 273
Cdd:TIGR04251 242 GGCGLCgifGILGVLSDGSYALCGIGE 268
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
19-152 2.19e-05

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 44.98  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593  19 DV--CNFKCVYCLPDGYQGGHDRG--FLTIDEISNTLKAFAH-HGIEKVRITGGEPTL-RKDFIDVVRAAKDvAGIKKIa 92
Cdd:COG5014   46 DVvgCNLRCGFCWSWRFRDFPLTIgkFYSPEEVAERLIEIAReRGYRQVRLSGGEPTIgFEHLLKVLELFSE-RGLTFI- 123
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639319593  93 MTTNG------------FSLHKNIHdwvdvglnaINVSIDSLDSRMFNTITGHDK--FTSVMKGIDTALETGID 152
Cdd:COG5014  124 LETNGiligydrelareLASFRNIV---------VRVSIKGCTPEEFSMLTGADPefFELQLRALKNLVDAGLE 188
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
21-152 9.90e-05

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: 42.74  E-value: 9.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   21 CNFKCVYCLPDGYQGGHDRGFLTIDEISNTLKAFAHHgIEKVRITGGEPTLRKDFIDVVRAAKDVaGIkKIAMTTNGFS- 99
Cdd:TIGR02495  26 CNLKCPYCHNPLLIPRRGSGEIEVEELLEFLRRRRGL-LDGVVITGGEPTLQAGLPDFLREVREL-GF-EVKLDTNGSNp 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 639319593  100 ------LHKNIHDWVdvglnAINVSIDSLDSRMFNTITGHDKFTSVMKGIDTALETGID 152
Cdd:TIGR02495 103 rrleelLEEGLVDYV-----AMDVKAPPEKYGELYGLEKNGAAKNILKSLEILLESGIP 156
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
15-143 3.94e-03

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: 38.68  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   15 LSITDVCNFKCVYClpdgyqgGHdrgFLTIDEISNTL---------KAFAHHGIEKVRITGGEPTLRKDFIDVVRaakdv 85
Cdd:TIGR04250   7 IDITGRCNLRCRYC-------SH---FSSAAETPTDLetaewlrffRELNRCSVLRVVLSGGEPFMRSDFREIID----- 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639319593   86 aGIKKIAMTtngFSLHKN---IHDWVDVGLNA------INVSIDSLDSRMFNTITGHDKFTSVMKGI 143
Cdd:TIGR04250  72 -GIVKNRMR---FSILSNgtlITDAIASFLAAtrrcdyVQVSIDGSTPGTHDRLRGTGSFLQAVEGI 134
sulfatase_rSAM TIGR03942
anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family ...
1-195 4.96e-03

anaerobic sulfatase-maturating enzyme; Members of this protein family are radical SAM family enzymes, maturases that prepare the oxygen-sensitive radical required in the active site of anaerobic sulfatases. This maturase role has led to many misleading legacy annotations suggesting that this enzyme maturase is instead a sulfatase regulatory protein. All members of the seed alignment are radical SAM enzymes encoded next to or near an anaerobic sulfatase. Note that a single genome may encode more than one sulfatase/maturase pair. [Protein fate, Protein modification and repair]


Pssm-ID: 188457 [Multi-domain]  Cd Length: 363  Bit Score: 38.36  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593    1 MLIDPTGrefsylrlsitDVCNFKCVYCLpdgYQGGHDR---GFLTIDEisNTLKAF-----AHHGIEKVRIT--GGEPT 70
Cdd:TIGR03942   2 VMAKPTG-----------AKCNLDCDYCF---YLEKEDLypkPKPKMSD--ETLETFikqyiASQDGPEVNFAwqGGEPT 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639319593   71 LRK-DFI-DVVRAAKDVAGIKKI--AMTTNGFSLHKnihDWVD--------VGLnainvSID---SLDSRMFNTITGHDK 135
Cdd:TIGR03942  66 LAGlDFYrKAVELQQRYAPGKTIsnSLQTNGILLND---EWAEffkehnflVGI-----SIDgpkELHDKYRVTKSGKGT 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639319593  136 FTSVMKGIDtaletgidsvkinsvLMKQYNAkEFDTF-----LNWvkHRPVTI------------RFIELMQTNDNK 195
Cdd:TIGR03942 138 FERVMRALK---------------LLKEHNV-EFNTLtvvnnHNA--RHGKEVyrflkelgsrymQFIPCVEPDNAT 196
 
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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