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Conserved domains on  [gi|446466765|ref|WP_000544619|]
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MULTISPECIES: GTP 3',8-cyclase MoaA [Bacillus]

Protein Classification

GTP 3',8-cyclase MoaA( domain architecture ID 11458418)

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 Ontology:  GO:0005525|GO:0006777|GO:0019008|GO:0051539|GO:0061798|GO:1904047|GO:0046872
PubMed:  18307109|17936058|11222759
SCOP:  3000308|4001968

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 1-337 4.57e-179

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: 498.43  E-value: 4.57e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   1 MHEKMKDSLERPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:COG2896    1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEG----YQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNvSTKPVLKGIEAAKAAGL 160
Cdd:COG2896   77 KDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRD-DLDKVLAGIDAALAAGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYPIEPVqPRYFGEVAK 239
Cdd:COG2896  156 TpVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPAR 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 240 LYRYVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDER 319
Cdd:COG2896  235 YYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDE 314

                        330
                 ....*....|....*...
gi 446466765 320 TTEStnkRPKVEMSYIGG 337
Cdd:COG2896  315 GDFP---QPKRSMSAIGG 329
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 1-337 4.57e-179

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: 498.43  E-value: 4.57e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   1 MHEKMKDSLERPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:COG2896    1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEG----YQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNvSTKPVLKGIEAAKAAGL 160
Cdd:COG2896   77 KDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRD-DLDKVLAGIDAALAAGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYPIEPVqPRYFGEVAK 239
Cdd:COG2896  156 TpVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPAR 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 240 LYRYVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDER 319
Cdd:COG2896  235 YYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDE 314

                        330
                 ....*....|....*...
gi 446466765 320 TTEStnkRPKVEMSYIGG 337
Cdd:COG2896  315 GDFP---QPKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 5-337 5.85e-160

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: 450.14  E-value: 5.85e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765    5 MKDSLERPLQDLRISVIDRCNFRCTYCMPAevfGPDYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLP 84
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPE---GGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   85 KLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKPVLKGIEAAKAAGLE-VK 163
Cdd:TIGR02666  78 ELVARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRLEQVLAGIDAALAAGLEpVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  164 VNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVY-PIEPVQPRYFGEVAKLYR 242
Cdd:TIGR02666 158 LNTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFgPLEPVPSPRGNGPAPAYR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  243 --YVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDERT 320
Cdd:TIGR02666 238 wrLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRF 317

                         330
                  ....*....|....*..
gi 446466765  321 TESTNKRPKVEMSYIGG 337
Cdd:TIGR02666 318 TSPANKRRKRAMSQIGG 334
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-337 1.11e-159

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 449.59  E-value: 1.11e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   1 MHEKMKDSLERPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:PRK00164   4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGY----LPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKpVLKGIEAAKAAGL 160
Cdd:PRK00164  80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQ-VLAGIDAALAAGL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYpIEPVQPRYFGEVAK 239
Cdd:PRK00164 159 TpVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERG-WTLQPRARSGGPAQ 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 240 LYRYVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDER 319
Cdd:PRK00164 238 YFRHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHD 317

                        330
                 ....*....|....*...
gi 446466765 320 ttesTNKRPKVEMSYIGG 337
Cdd:PRK00164 318 ----GNTGPTRHMSYIGG 331
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
 189-316 1.86e-50

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: 163.93  E-value: 1.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  189 IQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYPIEPVQPRYfGEVAKLYRYVGSDAEVGLITSVSESFCSSCTRAR 268
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRT-GGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446466765  269 ISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYS 316
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 18-218 6.74e-27

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: 105.11  E-value: 6.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  18 ISVIDRCNFRCTYCMpaevFGPDYAFLQEELLLTfDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLEGLK 97
Cdd:cd01335    1 LELTRGCNLNCGFCS----NPASKGRGPESPPEI-EEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  98 DIGLTTNGIHL-AKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKPVLKGIEAAKAAGLEVKVNMVVKKGMNDS- 175
Cdd:cd01335   76 EISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEe 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446466765 176 QILPMAQYFKE--QEIQLRFIEFMDVGSTNGWNFEQVITKEQLIE 218
Cdd:cd01335  156 DDLEELELLAEfrSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLR 200
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 18-168 7.99e-17

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: 77.83  E-value: 7.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765    18 ISVIDRCNFRCTYCMPAEVFGPDYAFLQEELLltfDEIERLARLFISMG-VNKIRLTGGEPLL--RKDLPKLIARLAKLE 94
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYLEALV---REIELLAEKGEKEGlVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446466765    95 GLKDIGLTTNGIHL----AKQAKALKDAGLKRVNISLDAIEDHVFKKINgRNVSTKPVLKGIEAAKAAG-LEVKVNMVV 168
Cdd:smart00729  82 GLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAIN-RGHTVEDVLEAVELLREAGpIKVSTDLIV 159
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 15-133 9.06e-08

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: 53.04  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  15 DLRISVIdrCNFRCTYCMPA----------------EVFGPDYAFLQEELLltFDEIERLARlfismGVNKIRLTGGEPL 78
Cdd:NF033640 113 DLRFGNL--CNLKCRMCGPHsssswakeakklggpkLGDKKKISWFEDEEF--WKWLEELLP-----SLKEIYFAGGEPL 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446466765  79 LRKDLPKLIARLAKLEGLKDIGL--TTNGIHLAKQAKALKDA--GLKRVNI--SLDAIEDH 133
Cdd:NF033640 184 LIKEHYKLLEKLVEKGRAKNIELryNTNLTVLPDKLKDLLDLwkKFKSVSIsaSIDGVGER 244
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
 24-199 1.05e-06

radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide maturase most closely related to the darobactin maturase DarE.


Pssm-ID: 469197 [Multi-domain]  Cd Length: 415  Bit Score: 49.88  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  24 CNFRCTYCMP-AEvfGPDYAflqeellLTFDEIERLARLFISM-GVNKIRLT--GGEPLLRKdlPKLIARLAKLE----- 94
Cdd:NF041300  51 CNLRCTYCRSwAE--GPNQT-------MTFDVLARAVREALSMpGLHGVEFVwhGGEVTLLK--PKVFKKLIWLQqqfrq 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  95 --GLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDA-IEDHVFKKIN-GRNVSTKPVLKGIEAAKAAGLEVKVNMVVKK 170
Cdd:NF041300 120 pgQEVRNSIQTNATHLTDEWIEFLSELGMGVGVSIDGpPEVHDRRRLDkDGRPTSSRVAGGIARLRQAGIPHGALVVVDR 199

                        170       180
                 ....*....|....*....|....*....
gi 446466765 171 GMNDSQILPMAQYFkeQEIQLRFIEFMDV 199
Cdd:NF041300 200 ELIDAGAERLLGYL--AEIGLDKISFLNV 226
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 1-337 4.57e-179

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: 498.43  E-value: 4.57e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   1 MHEKMKDSLERPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:COG2896    1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEG----YQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNvSTKPVLKGIEAAKAAGL 160
Cdd:COG2896   77 KDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRD-DLDKVLAGIDAALAAGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYPIEPVqPRYFGEVAK 239
Cdd:COG2896  156 TpVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPAR 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 240 LYRYVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDER 319
Cdd:COG2896  235 YYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDE 314

                        330
                 ....*....|....*...
gi 446466765 320 TTEStnkRPKVEMSYIGG 337
Cdd:COG2896  315 GDFP---QPKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 5-337 5.85e-160

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: 450.14  E-value: 5.85e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765    5 MKDSLERPLQDLRISVIDRCNFRCTYCMPAevfGPDYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLP 84
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPE---GGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   85 KLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKPVLKGIEAAKAAGLE-VK 163
Cdd:TIGR02666  78 ELVARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRLEQVLAGIDAALAAGLEpVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  164 VNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVY-PIEPVQPRYFGEVAKLYR 242
Cdd:TIGR02666 158 LNTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFgPLEPVPSPRGNGPAPAYR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  243 --YVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDERT 320
Cdd:TIGR02666 238 wrLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRF 317

                         330
                  ....*....|....*..
gi 446466765  321 TESTNKRPKVEMSYIGG 337
Cdd:TIGR02666 318 TSPANKRRKRAMSQIGG 334
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-337 1.11e-159

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 449.59  E-value: 1.11e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   1 MHEKMKDSLERPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEELLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:PRK00164   4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGY----LPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKpVLKGIEAAKAAGL 160
Cdd:PRK00164  80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQ-VLAGIDAALAAGL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYpIEPVQPRYFGEVAK 239
Cdd:PRK00164 159 TpVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERG-WTLQPRARSGGPAQ 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 240 LYRYVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDER 319
Cdd:PRK00164 238 YFRHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHD 317

                        330
                 ....*....|....*...
gi 446466765 320 ttesTNKRPKVEMSYIGG 337
Cdd:PRK00164 318 ----GNTGPTRHMSYIGG 331
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 7-337 4.69e-90

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 273.94  E-value: 4.69e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   7 DSLERPLQDLRISVIDRCNFRCTYCMPAEvfGPDYAFLQEelLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKL 86
Cdd:PLN02951  51 DSFGRRHNYLRISLTERCNLRCQYCMPEE--GVELTPKSH--LLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  87 IARLAKLEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKpVLKGIEAAKAAGLE-VKVN 165
Cdd:PLN02951 127 CLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDR-VLESIDTAIELGYNpVKVN 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 166 MVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVgSTNGWNFEQVITKEQLIEKINRVYP-IEPVQ--PryfGEVAKLYR 242
Cdd:PLN02951 206 CVVMRGFNDDEICDFVELTRDKPINVRFIEFMPF-DGNVWNVKKLVPYAEMMDRIEQRFPsLKRLQdhP---TDTAKNFR 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 243 YVGSDAEVGLITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDERTTE 322
Cdd:PLN02951 282 IDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREIIGAAVKRKKAAHAGMFDLA 361

                        330
                 ....*....|....*
gi 446466765 323 STNKRPkveMSYIGG 337
Cdd:PLN02951 362 KTANRP---MIHIGG 373
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
 5-315 3.07e-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: 228.73  E-value: 3.07e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765    5 MKDSLERPLQDLRISVIDRCNFRCTYC-MPAEVFGPDYaflqeelLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDL 83
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYChMEGEDRSGGN-------ELSPEEIERIVRVASEFGVRKVKITGGEPLLRKDL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   84 PKLIARLAKlEGLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKpVLKGIEAAKAAGLE-V 162
Cdd:TIGR02668  74 IEIIRRIKD-YGIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDR-VIEGIESAVDAGLTpV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  163 KVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGstngwNFEQVITKEQliekinrvYPIEPVQPRYFG-----EV 237
Cdd:TIGR02668 152 KLNMVVLKGINDNEIPDMVEFAAEGGAILQLIELMPPG-----EGEKEFKKYH--------EDIDPIEEELEKmadrvRT 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  238 AKLYR----YVGSDAEVGLITSVSES-FCSSCTRARISADGKFYTCLF-GEKGTDLRTLLRENISDAsLLKILQHTWRYR 311
Cdd:TIGR02668 219 RRMHNrpkyFIPGGVEVEVVKPMDNPvFCAHCTRLRLTSDGKLKTCLLrDDNLVDILDALRNGEDDE-LREAFREAVARR 297


                  ....
gi 446466765  312 TDRY 315
Cdd:TIGR02668 298 EPYF 301
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
 189-316 1.86e-50

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: 163.93  E-value: 1.86e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  189 IQLRFIEFMDVGSTNGWNFEQVITKEQLIEKINRVYPIEPVQPRYfGEVAKLYRYVGSDAEVGLITSVSESFCSSCTRAR 268
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRT-GGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446466765  269 ISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYS 316
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 16-167 7.65e-36

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: 127.33  E-value: 7.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  16 LRISVIDRCNFRCTYCmpaevFGPDYAFLQEELllTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLeG 95
Cdd:COG0535    2 LQIELTNRCNLRCKHC-----YADAGPKRPGEL--STEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL-G 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446466765  96 LKdIGLTTNGIHLAKQ-AKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKPVLKGIEAAKAAGLEVKVNMV 167
Cdd:COG0535   74 IR-VNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPETHDKIRGVPGAFDKVLEAIKLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 20-177 7.33e-33

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: 119.55  E-value: 7.33e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   20 VIDRCNFRCTYCMPAEVFGPDYAFLqeellLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLEGLKD- 98
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRE-----LSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGi 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   99 -IGLTTNGIHLAK-QAKALKDAGLKRVNISLDAIEDHVfKKINGRNVSTKPVLKGIEAAKAAGLEV-KVNMVVKKGMNDS 175
Cdd:pfam04055  76 rITLETNGTLLDEeLLELLKEAGLDRVSIGLESGDDEV-LKLINRGHTFEEVLEALELLREAGIPVvTDNIVGLPGETDE 154


                  ..
gi 446466765  176 QI 177
Cdd:pfam04055 155 DL 156
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 18-218 6.74e-27

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: 105.11  E-value: 6.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  18 ISVIDRCNFRCTYCMpaevFGPDYAFLQEELLLTfDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLEGLK 97
Cdd:cd01335    1 LELTRGCNLNCGFCS----NPASKGRGPESPPEI-EEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  98 DIGLTTNGIHL-AKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKPVLKGIEAAKAAGLEVKVNMVVKKGMNDS- 175
Cdd:cd01335   76 EISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEe 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446466765 176 QILPMAQYFKE--QEIQLRFIEFMDVGSTNGWNFEQVITKEQLIE 218
Cdd:cd01335  156 DDLEELELLAEfrSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLR 200
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
 256-324 4.24e-25

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: 96.07  E-value: 4.24e-25
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446466765 256 VSESFCSSCTRARISADGKFYTCLFGEKGTDLRTLLRENISDASLLKILQHTWRYRTDRYSDERTTEST 324
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGT 69
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 18-278 9.80e-18

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 82.73  E-value: 9.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  18 ISVIDRCNFRCTYCmpaevFGPDYAFLQEElLLTFDEIERLARLFI--SMGVNKIRLT--GGEPLLRKDLPK-LIARLAK 92
Cdd:COG0641    5 LKPTSRCNLRCSYC-----YYSEGDEGSRR-RMSEETAEKAIDFLIesSGPGKELTITffGGEPLLNFDFIKeIVEYARK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  93 LEGLK---DIGLTTNGIHL-AKQAKALKDAGLkRVNISLDAIED-H----VFKkiNGRNvSTKPVLKGIEAAKAAGLEVK 163
Cdd:COG0641   79 YAKKGkkiRFSIQTNGTLLdDEWIDFLKENGF-SVGISLDGPKEiHdrnrVTK--NGKG-SFDRVMRNIKLLKEHGVEVN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765 164 VNMVVKKGmNDSQILPMAQYFKEQEIqlRFIEFMDVGSTNGWNFEqvITKEQLIEKINRVY------PIEPVQPRYFGEv 237
Cdd:COG0641  155 IRCTVTRE-NLDDPEELYDFLKELGF--RSIQFNPVVEEGEADYS--LTPEDYGEFLIELFdewlerDGGKIFVREFDI- 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446466765 238 aklyryvgsdaevgLITSVSESFCSSCTRAR-----ISADGKFYTC 278
Cdd:COG0641  229 --------------LLAGLLPPCSSPCVGAGgnylvVDPDGDIYPC 260
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 18-168 7.99e-17

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: 77.83  E-value: 7.99e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765    18 ISVIDRCNFRCTYCMPAEVFGPDYAFLQEELLltfDEIERLARLFISMG-VNKIRLTGGEPLL--RKDLPKLIARLAKLE 94
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRSRYLEALV---REIELLAEKGEKEGlVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446466765    95 GLKDIGLTTNGIHL----AKQAKALKDAGLKRVNISLDAIEDHVFKKINgRNVSTKPVLKGIEAAKAAG-LEVKVNMVV 168
Cdd:smart00729  82 GLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAIN-RGHTVEDVLEAVELLREAGpIKVSTDLIV 159
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 24-186 7.61e-14

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 70.21  E-value: 7.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  24 CNFRCTYC-------MPAEVFGPDYAFlqEELLltfDEIERLARLFISMGVnkIRLTGGEPLLRKDLPKLIARLAKLEGL 96
Cdd:COG1180   31 CNLRCPYChnpeisqGRPDAAGRELSP--EELV---EEALKDRGFLDSCGG--VTFSGGEPTLQPEFLLDLAKLAKELGL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  97 KdIGLTTNGIHLAKQAKALK---DAglkrVNISLDAIEDHVFKKINGRNVstKPVLKGIEAAKAAGLEVKVNMVVKKGMN 173
Cdd:COG1180  104 H-TALDTNGYIPEEALEELLpylDA----VNIDLKAFDDEFYRKLTGVSL--EPVLENLELLAESGVHVEIRTLVIPGLN 176

                        170
                 ....*....|....*
gi 446466765 174 DS--QILPMAQYFKE 186
Cdd:COG1180  177 DSeeELEAIARFIAE 191
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 23-195 1.04e-12

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 66.75  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  23 RCNFRCTYC---------MPAEVFgPDYAFLQEELlltfdeIERLARLFI-SMGVNKIRLTG-GEPLLRKDLPKLIARLA 91
Cdd:COG0731   33 TCNFDCVYCqrgrttdltRERREF-DDPEEILEEL------IEFLRKLPEeAREPDHITFSGsGEPTLYPNLGELIEEIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  92 KLEGLKdIGLTTNGIHLAKQA--KALKDAGLkrVNISLDAIEDHVFKKINGRNVSTKP--VLKGIEAAKAAG-----LEV 162
Cdd:COG0731  106 KLRGIK-TALLTNGSLLHRPEvrEELLKADQ--VYPSLDAADEETFRKINRPHPGLSWerIIEGLELFRKLYkgrtvIET 182

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446466765 163 kvnMVVkKGMNDS--QILPMAQYFKeqEIQLRFIE 195
Cdd:COG0731  183 ---MLV-KGINDSeeELEAYAELIK--RINPDFVE 211
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
24-168 1.21e-12

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 68.05  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  24 CNFRCTYCMPAEVFGPDYAFLQEELLLtfDEIERLARLFismGVNKIRLTGGEPLL-RKDLPKLIARLAKlEGLK---DI 99
Cdd:COG1032  184 CPFGCSFCSISALYGRKVRYRSPESVV--EEIEELVKRY---GIREIFFVDDNFNVdKKRLKELLEELIE-RGLNvsfPS 257

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446466765 100 GLTTNGIHlAKQAKALKDAGLKRVNISLDAIEDHVFKKINgRNVSTKPVLKGIEAAKAAGLEVKVNMVV 168
Cdd:COG1032  258 EVRVDLLD-EELLELLKKAGCRGLFIGIESGSQRVLKAMN-KGITVEDILEAVRLLKKAGIRVKLYFII 324
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
 20-177 1.05e-11

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 64.93  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  20 VIDR------------CNFRCTYCMPAEvfGP-------DYAFLQEELLltfDEIERLARlFISMGVNKIRLTGGEPLLR 80
Cdd:COG2100   30 VIDRgtnvlqvrpttgCNLNCIFCSVDA--GPhsrtrqaEYIVDPEYLV---EWFEKVAR-FKGKGVEAHIDGVGEPLLY 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQ-AKALKDAGLKRVNISLDAIEDHVFKKINGRN-VSTKPVLKGIE-AAKA 157
Cdd:COG2100  104 PYIVELVKGLKEIKGVKVVSMQTNGTLLSEKlIDELEEAGLDRINLSIDTLDPEKAKKLAGTKwYDVEKVLELAEyIARE 183

                        170       180
                 ....*....|....*....|
gi 446466765 158 AGLEVKVNMVVKKGMNDSQI 177
Cdd:COG2100  184 TKIDLLIAPVWLPGINDEDI 203
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
23-174 1.33e-10

Uncharacterized radical SAM domain-containing protein [Function unknown];


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 61.90  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  23 RCNFRCTYC-MPAEVFGPDYAFLQEELLLTFDEIERLARLFISMGVNkirLTGGEPLLRKDLPKLIARLAKLEGLKD--I 99
Cdd:COG2108   36 LCNRNCFYCpLSEERKGKDVIYANERPVESDEDVIEEARRMGALGAG---ITGGEPLLVLDRTLEYIRLLKEEFGPDhhI 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446466765 100 GLTTNGIHLAKQA-KALKDAGlkrvnisLDAIEDHVFKKINGRNVStkPVLKGIEAAKAAGLEVKVNMVVKKGMND 174
Cdd:COG2108  113 HLYTNGILADEDVlRKLADAG-------LDEIRFHPPQELWGLLGT--PYLESIKLAKEYGLDVGVEIPAIPGEEE 179
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 12-168 7.29e-08

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: 53.30  E-value: 7.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   12 PLQDLRISVIDRCNFRCTYCMpaevFGPDYAFLQEELL-LTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIaRL 90
Cdd:TIGR04251   2 PLHQIYFYLTEGCNLKCRHCW----IDPKYQGEGEQHPsLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEIL-EC 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446466765   91 AKLEGLKdIGLTTNGIHLAKQ-AKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKPVLKGIEAAKAAGLEVKVNMVV 168
Cdd:TIGR04251  77 IGENNLQ-LSVETNGLLCTPQtARDLASCETPFVSVSLDGVDAATHDWMRGVKGAFDKAVRGIHNLVEAGIHPQIIMTV 154
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 15-133 9.06e-08

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: 53.04  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  15 DLRISVIdrCNFRCTYCMPA----------------EVFGPDYAFLQEELLltFDEIERLARlfismGVNKIRLTGGEPL 78
Cdd:NF033640 113 DLRFGNL--CNLKCRMCGPHsssswakeakklggpkLGDKKKISWFEDEEF--WKWLEELLP-----SLKEIYFAGGEPL 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446466765  79 LRKDLPKLIARLAKLEGLKDIGL--TTNGIHLAKQAKALKDA--GLKRVNI--SLDAIEDH 133
Cdd:NF033640 184 LIKEHYKLLEKLVEKGRAKNIELryNTNLTVLPDKLKDLLDLwkKFKSVSIsaSIDGVGER 244
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 24-105 4.14e-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: 49.75  E-value: 4.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  24 CNFRCTYCMPAEVFGPDYAFLQ--EELLltfDEIERLARLFISmgvnkirLTGGEPLLRKDLPKLIARLAKlEGLKdIGL 101
Cdd:COG0602   30 CNLRCSWCDTKYAWDGEGGKRMsaEEIL---EEVAALGARHVV-------ITGGEPLLQDDLAELLEALKD-AGYE-VAL 97


                 ....
gi 446466765 102 TTNG 105
Cdd:COG0602   98 ETNG 101
rSAM_mat_DarW NF041300
radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide ...
 24-199 1.05e-06

radical SAM/SPASM peptide maturase DarW; DarW is a radical SAM/SPASM domain-containing peptide maturase most closely related to the darobactin maturase DarE.


Pssm-ID: 469197 [Multi-domain]  Cd Length: 415  Bit Score: 49.88  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  24 CNFRCTYCMP-AEvfGPDYAflqeellLTFDEIERLARLFISM-GVNKIRLT--GGEPLLRKdlPKLIARLAKLE----- 94
Cdd:NF041300  51 CNLRCTYCRSwAE--GPNQT-------MTFDVLARAVREALSMpGLHGVEFVwhGGEVTLLK--PKVFKKLIWLQqqfrq 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  95 --GLKDIGLTTNGIHLAKQAKALKDAGLKRVNISLDA-IEDHVFKKIN-GRNVSTKPVLKGIEAAKAAGLEVKVNMVVKK 170
Cdd:NF041300 120 pgQEVRNSIQTNATHLTDEWIEFLSELGMGVGVSIDGpPEVHDRRRLDkDGRPTSSRVAGGIARLRQAGIPHGALVVVDR 199

                        170       180
                 ....*....|....*....|....*....
gi 446466765 171 GMNDSQILPMAQYFkeQEIQLRFIEFMDV 199
Cdd:NF041300 200 ELIDAGAERLLGYL--AEIGLDKISFLNV 226
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
 252-337 6.12e-05

DNA repair protein rad18; All proteins in this family for which functions are known are involved in nucleotide excision repair.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273165 [Multi-domain]  Cd Length: 397  Bit Score: 44.61  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  252 LITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLR--TLLRENI-----SDASLLKILQhTWRYRTDRYSDERTTEST 324
Cdd:TIGR00599  40 VLTSCSHTFCSLCIRRCLSNQPKCPLCRAEDQESKLRsnWLVSEIVesfknLRPSLLEFLR-IPKTTPVENPDLAGPENS 118

                          90
                  ....*....|...
gi 446466765  325 NKRPKVEMSYIGG 337
Cdd:TIGR00599 119 SKIELIEESESDG 131
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
 44-162 8.87e-05

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 43.50  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  44 LQEELLLTFDEIERLARLFISMGVNKIRL-TGGEPLLRKDLPKLIARLAKLEGLKDIGLT-TNGIHLAKQAKALKDAGLK 121
Cdd:COG0502   67 IERYRLLSVEEILEAARAAKEAGARRFCLvASGRDPSDRDFEKVLEIVRAIKEELGLEVCaSLGELSEEQAKRLKEAGVD 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446466765 122 RVNISLDAIEDHvFKKI-NGRNVSTKpvLKGIEAAKAAGLEV 162
Cdd:COG0502  147 RYNHNLETSPEL-YPKIcTTHTYEDR--LDTLKNAREAGLEV 185
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 18-203 1.70e-04

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: 42.92  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   18 ISVIDRCNFRCTYCMPAEVFGPDYAFL-QEELLLTFDEIERLArlfismgVNKIRLTGGEPLLRKDLPKLIARLAKleGL 96
Cdd:TIGR04250   7 IDITGRCNLRCRYCSHFSSAAETPTDLeTAEWLRFFRELNRCS-------VLRVVLSGGEPFMRSDFREIIDGIVK--NR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   97 KDIGLTTNGIhLAKQAKALKDAGLKR---VNISLDAIEDHVFKKINGRNVSTKpVLKGIEAAKAAGLEVKVNMVVKKGmN 173
Cdd:TIGR04250  78 MRFSILSNGT-LITDAIASFLAATRRcdyVQVSIDGSTPGTHDRLRGTGSFLQ-AVEGIELLRKHAIPVVVRVTIHRW-N 154

                         170       180       190
                  ....*....|....*....|....*....|
gi 446466765  174 DSQILPMAQYFKEqeiQLRFIEFmdvgSTN 203
Cdd:TIGR04250 155 VDDLRPIAALLLD---DLGLPAF----STN 177
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
 24-106 3.02e-04

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 41.90  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  24 CNFRCTYCMP--AEVFGPDYAFLqeellLTFDEI-ERLARLFISMGVNKIRLTGGEPLL-RKDLPKLiarlakLEGLKDI 99
Cdd:COG5014   50 CNLRCGFCWSwrFRDFPLTIGKF-----YSPEEVaERLIEIARERGYRQVRLSGGEPTIgFEHLLKV------LELFSER 118

                         90
                 ....*....|.
gi 446466765 100 GLT----TNGI 106
Cdd:COG5014  119 GLTfileTNGI 129
Fer4_14 pfam13394
4Fe-4S single cluster domain;
20-105 3.34e-04

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 39.65  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   20 VIDRCNFRCTYCMPAEVFGPDYAFLQ-EELLLTfdEIERLARLFIsmGVNKIRLTGGEPLLRKDLP---KLIARLAKLEG 95
Cdd:pfam13394   2 FVSGCNHSCPGCDNKETWKFNYGEPFtEELEDQ--IIADLKDSYI--KRQGLVLTGGEPLHPWNLPvllKLLKRVKEEYP 77

                          90
                  ....*....|
gi 446466765   96 LKDIGLTTNG 105
Cdd:pfam13394  78 SKDIWLETGY 87
GG_samocin_CFB TIGR04148
radical SAM peptide maturase, GG-Bacteroidales family; Members of this protein family are ...
 7-110 6.32e-04

radical SAM peptide maturase, GG-Bacteroidales family; Members of this protein family are radical SAM enzymes (pfam04055) with the additional C-terminal region (TIGR04085) that is frequently a marker of peptide modification. Many members of this family are found in the vicinity of one or several ORFs encoding short polypeptides with a Gly-Gly motif (common for bacteriocin leader peptide cleavage), followed by a Cys-rich patch and then poorly conserved sequences.


Pssm-ID: 200399 [Multi-domain]  Cd Length: 411  Bit Score: 41.21  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765    7 DSLERPLQDLR---ISVIDRCNFRCTYCmpaeVFGPDYAFLQEEL--LLTFDEIERLARLFISMGVNK----------IR 71
Cdd:TIGR04148   7 SDIKQELANLRqltFEVTDACNLQCKYC----SYGDLYNNYDEREnkNIDFDNAKTLIDYLFSLWESKyntsvkntvtIG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 446466765   72 LTGGEPLLRKDLPK-LIARLAKL--EGLK-DIGLTTNGIHLAK 110
Cdd:TIGR04148  83 FYGGEPLLNMDFIKeIINYIEKLhiDGLNfHYNMTTNAMLLRK 125
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 24-103 7.92e-04

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 39.08  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   24 CNFRCTYCMPAEVFGPDYAflqeeLLLTFDEIERLARLFISMGVNKIRLTGGEPLL-RKDLPKLIARLAKLEGLKDIGLT 102
Cdd:pfam13353  15 CNHHCKGCFNPETWDFKYG-----KPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVREECPEKDIWLW 89


                  .
gi 446466765  103 T 103
Cdd:pfam13353  90 T 90
DRE_TIM_metallolyase cd03174
DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes ...
 50-166 1.39e-03

DRE-TIM metallolyase superfamily; The DRE-TIM metallolyase superfamily includes 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".


Pssm-ID: 163674 [Multi-domain]  Cd Length: 265  Bit Score: 39.75  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765  50 LTFDEIERLARLFISMGVNKIRLTGG-----EPLLRKDLpKLIARLAKLE-GLKDIGLTTNGIHLAKQAKalkDAGLKRV 123
Cdd:cd03174   16 FSTEDKLEIAEALDEAGVDSIEVGSGaspkaVPQMEDDW-EVLRAIRKLVpNVKLQALVRNREKGIERAL---EAGVDEV 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446466765 124 NISLDAIEDHVFKKIN-GRNVSTKPVLKGIEAAKAAGLEVKVNM 166
Cdd:cd03174   92 RIFDSASETHSRKNLNkSREEDLENAEEAIEAAKEAGLEVEGSL 135
TIGR00089 TIGR00089
radical SAM methylthiotransferase, MiaB/RimO family; This subfamily contains the tRNA-i(6)A37 ...
 18-103 4.58e-03

radical SAM methylthiotransferase, MiaB/RimO family; This subfamily contains the tRNA-i(6)A37 modification enzyme, MiaB (TIGR01574). The phylogenetic tree indicates 4 distinct clades, one of which corresponds to MiaB. The other three clades are modelled by hypothetical equivalogs (TIGR01125, TIGR01579 and TIGR01578). Together, the four models hit every sequence hit by the subfamily model without any overlap between them. This subfamily is aparrently a part of a larger superfamily of enzymes utilizing both a 4Fe4S cluster and S-adenosyl methionine (SAM) to initiate radical reactions. MiaB acts on a particular isoprenylated Adenine base of certain tRNAs causing thiolation at an aromatic carbon, and probably also transferring a methyl grouyp from SAM to the thiol. The particular substrate of the three other clades is unknown but may be very closely related.


Pssm-ID: 272900 [Multi-domain]  Cd Length: 429  Bit Score: 38.76  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466765   18 ISVIDRCNFRCTYCMPAEVFGPDYAFLQEELLltfDEIERLArlfiSMGVNKIRLTG------GEPLLRKD-LPKLIARL 90
Cdd:TIGR00089 143 LKIQEGCDKFCTYCIIPYARGRERSRPPEDIL---EEVKELV----SKGVKEIVLLGqnvgayGKDLEGKTnLADLLREL 215

                          90
                  ....*....|...
gi 446466765   91 AKLEGLKDIGLTT 103
Cdd:TIGR00089 216 SKIDGIFRIRFGS 228
PLN02389 PLN02389
biotin synthase
 90-162 5.36e-03

biotin synthase


Pssm-ID: 215219 [Multi-domain]  Cd Length: 379  Bit Score: 38.29  E-value: 5.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446466765  90 LAKLEGLKDIGL---TTNGIHLAKQAKALKDAGLKRVNISLDAIEDHVFKKINGRNVSTKpvLKGIEAAKAAGLEV 162
Cdd:PLN02389 156 LEYVKEIRGMGMevcCTLGMLEKEQAAQLKEAGLTAYNHNLDTSREYYPNVITTRSYDDR--LETLEAVREAGISV 229
 
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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