NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446467166|ref|WP_000545020|]
View 

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)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.27e-178

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: 497.28  E-value: 1.27e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   1 MHENMKDSLKRPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:COG2896    1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEG----YQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHvSTKPVLKGIEAAKEAGL 160
Cdd:COG2896   77 KDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRD-DLDKVLAGIDAALAAGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYPIEPVkPRYFGEVAK 239
Cdd:COG2896  156 TpVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPAR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 240 LYRYVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDER 319
Cdd:COG2896  235 YYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDE 314
                        330
                 ....*....|....*...
gi 446467166 320 TAESTNKRqkvEMSYIGG 337
Cdd:COG2896  315 GDFPQPKR---SMSAIGG 329
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-337 1.27e-178

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: 497.28  E-value: 1.27e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   1 MHENMKDSLKRPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:COG2896    1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEG----YQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHvSTKPVLKGIEAAKEAGL 160
Cdd:COG2896   77 KDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRD-DLDKVLAGIDAALAAGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYPIEPVkPRYFGEVAK 239
Cdd:COG2896  156 TpVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPAR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 240 LYRYVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDER 319
Cdd:COG2896  235 YYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDE 314
                        330
                 ....*....|....*...
gi 446467166 320 TAESTNKRqkvEMSYIGG 337
Cdd:COG2896  315 GDFPQPKR---SMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
5-337 1.40e-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: 452.07  E-value: 1.40e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    5 MKDSLKRPLQDLRISVIDRCNFRCTYCMPAevfGPDYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLP 84
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPE---GGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   85 KLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKPVLKGIEAAKEAGLE-VK 163
Cdd:TIGR02666  78 ELVARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRLEQVLAGIDAALAAGLEpVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  164 VNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVY-PIEPVKPRYFGEVAKLYR 242
Cdd:TIGR02666 158 LNTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFgPLEPVPSPRGNGPAPAYR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  243 --YVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDERT 320
Cdd:TIGR02666 238 wrLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRF 317
                         330
                  ....*....|....*..
gi 446467166  321 AESTNKRQKVEMSYIGG 337
Cdd:TIGR02666 318 TSPANKRRKRAMSQIGG 334
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-337 4.62e-157

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 442.66  E-value: 4.62e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   1 MHENMKDSLKRPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:PRK00164   4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGY----LPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKpVLKGIEAAKEAGL 160
Cdd:PRK00164  80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQ-VLAGIDAALAAGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYpIEPVKPRYFGEVAK 239
Cdd:PRK00164 159 TpVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERG-WTLQPRARSGGPAQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 240 LYRYVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDER 319
Cdd:PRK00164 238 YFRHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHD 317
                        330
                 ....*....|....*...
gi 446467166 320 TAESTnkrqKVEMSYIGG 337
Cdd:PRK00164 318 GNTGP----TRHMSYIGG 331
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
189-316 4.53e-51

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: 165.47  E-value: 4.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  189 IQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYPIEPVKPRYfGEVAKLYRYVGNDAEVGFITSVSESFCSSCTRAR 268
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRT-GGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446467166  269 ISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYS 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 9.68e-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: 104.72  E-value: 9.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  18 ISVIDRCNFRCTYCMPAEVFGPDyaflqEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLEGLK 97
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRG-----PESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  98 DIGLTTNGIHL-AKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKPVLKGIEAAKEAGLEVKVNMVVKKGMNDS- 175
Cdd:cd01335   76 EISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEe 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446467166 176 QILPMAQYFKE--QEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIE 218
Cdd:cd01335  156 DDLEELELLAEfrSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLR 200
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
18-168 5.94e-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: 78.21  E-value: 5.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    18 ISVIDRCNFRCTYCMPAEVFGPDYAflqeeclLTFDEIERLARLFISMGVNKIRLT-----GGEPLL--RKDLPKLIARL 90
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRS-------RYLEALVREIELLAEKGEKEGLVGtvfigGGTPTLlsPEQLEELLEAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    91 AKLEGLKDIGLTTNGIHL----AKQAKALKEAGLKRVNISLDAIEDRVFQKINgRHVSTKPVLKGIEAAKEAG-LEVKVN 165
Cdd:smart00729  78 REILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAIN-RGHTVEDVLEAVELLREAGpIKVSTD 156

                   ...
gi 446467166   166 MVV 168
Cdd:smart00729 157 LIV 159
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
15-133 1.15e-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: 53.04  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  15 DLRISVIdrCNFRCTYCMPA----------------EVFGPDYAFLQEECLltFDEIERLARlfismGVNKIRLTGGEPL 78
Cdd:NF033640 113 DLRFGNL--CNLKCRMCGPHsssswakeakklggpkLGDKKKISWFEDEEF--WKWLEELLP-----SLKEIYFAGGEPL 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446467166  79 LRKDLPKLIARLAKLEGLKDIGL--TTNGIHLAKQAKALKEA--GLKRVNI--SLDAIEDR 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 2.09e-07

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: 52.20  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  24 CNFRCTYCMP-AEvfGPDYAflqeeclLTFDEIERLARLFISM-GVNKIRLT--GGEPLLRKdlPKLIARLAKLE----- 94
Cdd:NF041300  51 CNLRCTYCRSwAE--GPNQT-------MTFDVLARAVREALSMpGLHGVEFVwhGGEVTLLK--PKVFKKLIWLQqqfrq 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  95 --GLKDIGLTTNGIHLAKQ-AKALKEAGLKrVNISLDA---IEDRVFQKINGRHVStKPVLKGIEAAKEAGLEVKVNMVV 168
Cdd:NF041300 120 pgQEVRNSIQTNATHLTDEwIEFLSELGMG-VGVSIDGppeVHDRRRLDKDGRPTS-SRVAGGIARLRQAGIPHGALVVV 197
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446467166 169 KKGMNDSQILPMAQYFkeQEIQLRFIEFMDV 199
Cdd:NF041300 198 DRELIDAGAERLLGYL--AEIGLDKISFLNV 226
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-337 1.27e-178

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: 497.28  E-value: 1.27e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   1 MHENMKDSLKRPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:COG2896    1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEG----YQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHvSTKPVLKGIEAAKEAGL 160
Cdd:COG2896   77 KDLPELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRD-DLDKVLAGIDAALAAGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYPIEPVkPRYFGEVAK 239
Cdd:COG2896  156 TpVKINAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPL-PARGGGPAR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 240 LYRYVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDER 319
Cdd:COG2896  235 YYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDE 314
                        330
                 ....*....|....*...
gi 446467166 320 TAESTNKRqkvEMSYIGG 337
Cdd:COG2896  315 GDFPQPKR---SMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
5-337 1.40e-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: 452.07  E-value: 1.40e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    5 MKDSLKRPLQDLRISVIDRCNFRCTYCMPAevfGPDYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLP 84
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPE---GGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   85 KLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKPVLKGIEAAKEAGLE-VK 163
Cdd:TIGR02666  78 ELVARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRLEQVLAGIDAALAAGLEpVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  164 VNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVY-PIEPVKPRYFGEVAKLYR 242
Cdd:TIGR02666 158 LNTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFgPLEPVPSPRGNGPAPAYR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  243 --YVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDERT 320
Cdd:TIGR02666 238 wrLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRF 317
                         330
                  ....*....|....*..
gi 446467166  321 AESTNKRQKVEMSYIGG 337
Cdd:TIGR02666 318 TSPANKRRKRAMSQIGG 334
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-337 4.62e-157

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 442.66  E-value: 4.62e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   1 MHENMKDSLKRPLQDLRISVIDRCNFRCTYCMPAEVfgpdYAFLQEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLR 80
Cdd:PRK00164   4 MTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGY----LPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKpVLKGIEAAKEAGL 160
Cdd:PRK00164  80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQ-VLAGIDAALAAGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 161 E-VKVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYpIEPVKPRYFGEVAK 239
Cdd:PRK00164 159 TpVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERG-WTLQPRARSGGPAQ 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 240 LYRYVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDER 319
Cdd:PRK00164 238 YFRHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHD 317
                        330
                 ....*....|....*...
gi 446467166 320 TAESTnkrqKVEMSYIGG 337
Cdd:PRK00164 318 GNTGP----TRHMSYIGG 331
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
7-304 7.55e-92

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 278.56  E-value: 7.55e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   7 DSLKRPLQDLRISVIDRCNFRCTYCMPAEvfGPDYAFLQEecLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKL 86
Cdd:PLN02951  51 DSFGRRHNYLRISLTERCNLRCQYCMPEE--GVELTPKSH--LLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  87 IARLAKLEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKpVLKGIEAAKEAGLE-VKVN 165
Cdd:PLN02951 127 CLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDR-VLESIDTAIELGYNpVKVN 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 166 MVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVgSTNGWNFEQVVTKEQLIEKINRVYP-IEPVK--PryfGEVAKLYR 242
Cdd:PLN02951 206 CVVMRGFNDDEICDFVELTRDKPINVRFIEFMPF-DGNVWNVKKLVPYAEMMDRIEQRFPsLKRLQdhP---TDTAKNFR 281
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446467166 243 YVGNDAEVGFITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKIL 304
Cdd:PLN02951 282 IDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREII 343
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
5-298 4.68e-74

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: 230.65  E-value: 4.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    5 MKDSLKRPLQDLRISVIDRCNFRCTYC-MPAEVFGPDYaflqeecLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDL 83
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYChMEGEDRSGGN-------ELSPEEIERIVRVASEFGVRKVKITGGEPLLRKDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   84 PKLIARLAKlEGLKDIGLTTNGIHLAKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKpVLKGIEAAKEAGLE-V 162
Cdd:TIGR02668  74 IEIIRRIKD-YGIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDR-VIEGIESAVDAGLTpV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  163 KVNMVVKKGMNDSQILPMAQYFKEQEIQLRFIEFMDVGS----TNGWNFEQVVTKEQLIEKINRVypiepvkpryfgEVA 238
Cdd:TIGR02668 152 KLNMVVLKGINDNEIPDMVEFAAEGGAILQLIELMPPGEgekeFKKYHEDIDPIEEELEKMADRV------------RTR 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446467166  239 KLYR----YVGNDAEVGFITSVSES-FCSSCTRARISADGKFYTCLF-GEKGTDLRSLLRENISDA 298
Cdd:TIGR02668 220 RMHNrpkyFIPGGVEVEVVKPMDNPvFCAHCTRLRLTSDGKLKTCLLrDDNLVDILDALRNGEDDE 285
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
189-316 4.53e-51

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: 165.47  E-value: 4.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  189 IQLRFIEFMDVGSTNGWNFEQVVTKEQLIEKINRVYPIEPVKPRYfGEVAKLYRYVGNDAEVGFITSVSESFCSSCTRAR 268
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRT-GGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446467166  269 ISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYS 316
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
16-167 3.76e-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: 128.10  E-value: 3.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  16 LRISVIDRCNFRCTYCmpaevFGPDYAFLQEEclLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLeG 95
Cdd:COG0535    2 LQIELTNRCNLRCKHC-----YADAGPKRPGE--LSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL-G 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446467166  96 LKdIGLTTNGIHLAKQ-AKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKPVLKGIEAAKEAGLEVKVNMV 167
Cdd:COG0535   74 IR-VNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPETHDKIRGVPGAFDKVLEAIKLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
20-177 9.43e-34

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: 121.86  E-value: 9.43e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   20 VIDRCNFRCTYCMPAEVFGPDYAFLqeeclLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLEGLKD- 98
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRE-----LSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGi 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   99 -IGLTTNGIHLAK-QAKALKEAGLKRVNISLDAIEDRVfQKINGRHVSTKPVLKGIEAAKEAGLEV-KVNMVVKKGMNDS 175
Cdd:pfam04055  76 rITLETNGTLLDEeLLELLKEAGLDRVSIGLESGDDEV-LKLINRGHTFEEVLEALELLREAGIPVvTDNIVGLPGETDE 154

                  ..
gi 446467166  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 9.68e-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: 104.72  E-value: 9.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  18 ISVIDRCNFRCTYCMPAEVFGPDyaflqEECLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIARLAKLEGLK 97
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRG-----PESPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  98 DIGLTTNGIHL-AKQAKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKPVLKGIEAAKEAGLEVKVNMVVKKGMNDS- 175
Cdd:cd01335   76 EISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFKERLEALKELREAGLGLSTTLLVGLGDEDEe 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446467166 176 QILPMAQYFKE--QEIQLRFIEFMDVGSTNGWNFEQVVTKEQLIE 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 1.66e-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: 1.66e-24
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446467166 256 VSESFCSSCTRARISADGKFYTCLFGEKGTDLRSLLRENISDASLLKILQHTWEFRTDRYSDERTAEST 324
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGT 69
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
18-278 2.29e-18

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 84.65  E-value: 2.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  18 ISVIDRCNFRCTYCmpaevFGPDYAFLQEEcLLTFDEIERLARLFI--SMGVNKIRLT--GGEPLLRKDLPK-LIARLAK 92
Cdd:COG0641    5 LKPTSRCNLRCSYC-----YYSEGDEGSRR-RMSEETAEKAIDFLIesSGPGKELTITffGGEPLLNFDFIKeIVEYARK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  93 LEGLK---DIGLTTNGIHL-AKQAKALKEAGLkRVNISLDAIED-----RVFqkINGRHvSTKPVLKGIEAAKEAGLEVK 163
Cdd:COG0641   79 YAKKGkkiRFSIQTNGTLLdDEWIDFLKENGF-SVGISLDGPKEihdrnRVT--KNGKG-SFDRVMRNIKLLKEHGVEVN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166 164 VNMVVKKGmNDSQILPMAQYFKEQEIqlRFIEFMDVGSTNGWNFEqvVTKEQLIEKINRVY------PIEPVKPRYFGEV 237
Cdd:COG0641  155 IRCTVTRE-NLDDPEELYDFLKELGF--RSIQFNPVVEEGEADYS--LTPEDYGEFLIELFdewlerDGGKIFVREFDIL 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 446467166 238 AKLYRYvgndaevgfitsvseSFCSSCTRAR-----ISADGKFYTC 278
Cdd:COG0641  230 LAGLLP---------------PCSSPCVGAGgnylvVDPDGDIYPC 260
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
18-168 5.94e-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: 78.21  E-value: 5.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    18 ISVIDRCNFRCTYCMPAEVFGPDYAflqeeclLTFDEIERLARLFISMGVNKIRLT-----GGEPLL--RKDLPKLIARL 90
Cdd:smart00729   5 YIITRGCPRRCTFCSFPSLRGKLRS-------RYLEALVREIELLAEKGEKEGLVGtvfigGGTPTLlsPEQLEELLEAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    91 AKLEGLKDIGLTTNGIHL----AKQAKALKEAGLKRVNISLDAIEDRVFQKINgRHVSTKPVLKGIEAAKEAG-LEVKVN 165
Cdd:smart00729  78 REILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAIN-RGHTVEDVLEAVELLREAGpIKVSTD 156

                   ...
gi 446467166   166 MVV 168
Cdd:smart00729 157 LIV 159
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
24-186 1.33e-13

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 69.44  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  24 CNFRCTYC-------MPAEVFGPDYaflqeecllTFDEIERLA---RLFISMGVNkIRLTGGEPLLRKDLPKLIARLAKL 93
Cdd:COG1180   31 CNLRCPYChnpeisqGRPDAAGREL---------SPEELVEEAlkdRGFLDSCGG-VTFSGGEPTLQPEFLLDLAKLAKE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  94 EGLKdIGLTTNGIHLAKQAKALKEaGLKRVNISLDAIEDRVFQKINGRHVstKPVLKGIEAAKEAGLEVKVNMVVKKGMN 173
Cdd:COG1180  101 LGLH-TALDTNGYIPEEALEELLP-YLDAVNIDLKAFDDEFYRKLTGVSL--EPVLENLELLAESGVHVEIRTLVIPGLN 176
                        170
                 ....*....|....*
gi 446467166 174 DS--QILPMAQYFKE 186
Cdd:COG1180  177 DSeeELEAIARFIAE 191
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
23-195 3.45e-13

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: 68.29  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  23 RCNFRCTYC---------MPAEVFgPDYAFLQEEClltfdeIERLARLFI-SMGVNKIRLTG-GEPLLRKDLPKLIARLA 91
Cdd:COG0731   33 TCNFDCVYCqrgrttdltRERREF-DDPEEILEEL------IEFLRKLPEeAREPDHITFSGsGEPTLYPNLGELIEEIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  92 KLEGLKdIGLTTNGIHLAKQA--KALKEAGLkrVNISLDAIEDRVFQKINGRHVSTKP--VLKGIEAAKEAG-----LEV 162
Cdd:COG0731  106 KLRGIK-TALLTNGSLLHRPEvrEELLKADQ--VYPSLDAADEETFRKINRPHPGLSWerIIEGLELFRKLYkgrtvIET 182
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446467166 163 kvnMVVkKGMNDS--QILPMAQYFKeqEIQLRFIE 195
Cdd:COG0731  183 ---MLV-KGINDSeeELEAYAELIK--RINPDFVE 211
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
20-177 9.84e-13

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 68.01  E-value: 9.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  20 VIDR------------CNFRCTYCMPAEvfGP-------DYaFLQEECLLtfDEIERLARlFISMGVNKIRLTGGEPLLR 80
Cdd:COG2100   30 VIDRgtnvlqvrpttgCNLNCIFCSVDA--GPhsrtrqaEY-IVDPEYLV--EWFEKVAR-FKGKGVEAHIDGVGEPLLY 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  81 KDLPKLIARLAKLEGLKDIGLTTNGIHLAKQ-AKALKEAGLKRVNISLDAIEDRVFQKINGRH-VSTKPVLKGIE-AAKE 157
Cdd:COG2100  104 PYIVELVKGLKEIKGVKVVSMQTNGTLLSEKlIDELEEAGLDRINLSIDTLDPEKAKKLAGTKwYDVEKVLELAEyIARE 183
                        170       180
                 ....*....|....*....|
gi 446467166 158 AGLEVKVNMVVKKGMNDSQI 177
Cdd:COG2100  184 TKIDLLIAPVWLPGINDEDI 203
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
24-168 2.22e-12

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


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 67.28  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  24 CNFRCTYCMPAEVFGPDYAFLQEECLLtfDEIERLARLFismGVNKIRLTGGEPLL-RKDLPKLIARLAKlEGLK---DI 99
Cdd:COG1032  184 CPFGCSFCSISALYGRKVRYRSPESVV--EEIEELVKRY---GIREIFFVDDNFNVdKKRLKELLEELIE-RGLNvsfPS 257
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446467166 100 GLTTNGIHlAKQAKALKEAGLKRVNISLDAIEDRVFQKINgRHVSTKPVLKGIEAAKEAGLEVKVNMVV 168
Cdd:COG1032  258 EVRVDLLD-EELLELLKKAGCRGLFIGIESGSQRVLKAMN-KGITVEDILEAVRLLKKAGIRVKLYFII 324
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
23-174 3.92e-09

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


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 57.28  E-value: 3.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  23 RCNFRCTYC-MPAEVFGPDYAFLQEECLLTFDEIERLARLFISMGVNkirLTGGEPLLRKDLPKLIARLAKLEGLKD--I 99
Cdd:COG2108   36 LCNRNCFYCpLSEERKGKDVIYANERPVESDEDVIEEARRMGALGAG---ITGGEPLLVLDRTLEYIRLLKEEFGPDhhI 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446467166 100 GLTTNGIHLAKQA-KALKEAGlkrvnisLDAIedRVFQKINGRHVSTKPVLKGIEAAKEAGLEVKVNMVVKKGMND 174
Cdd:COG2108  113 HLYTNGILADEDVlRKLADAG-------LDEI--RFHPPQELWGLLGTPYLESIKLAKEYGLDVGVEIPAIPGEEE 179
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
12-168 5.20e-09

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: 56.77  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   12 PLQDLRISVIDRCNFRCTYCMpaevFGPDYAFLQEE-CLLTFDEIERLARLFISMGVNKIRLTGGEPLLRKDLPKLIaRL 90
Cdd:TIGR04251   2 PLHQIYFYLTEGCNLKCRHCW----IDPKYQGEGEQhPSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEIL-EC 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446467166   91 AKLEGLKdIGLTTNGIHLAKQ-AKALKEAGLKRVNISLDAIEDRVFQKINGRHVSTKPVLKGIEAAKEAGLEVKVNMVV 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 1.15e-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: 53.04  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  15 DLRISVIdrCNFRCTYCMPA----------------EVFGPDYAFLQEECLltFDEIERLARlfismGVNKIRLTGGEPL 78
Cdd:NF033640 113 DLRFGNL--CNLKCRMCGPHsssswakeakklggpkLGDKKKISWFEDEEF--WKWLEELLP-----SLKEIYFAGGEPL 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446467166  79 LRKDLPKLIARLAKLEGLKDIGL--TTNGIHLAKQAKALKEA--GLKRVNI--SLDAIEDR 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 2.09e-07

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: 52.20  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  24 CNFRCTYCMP-AEvfGPDYAflqeeclLTFDEIERLARLFISM-GVNKIRLT--GGEPLLRKdlPKLIARLAKLE----- 94
Cdd:NF041300  51 CNLRCTYCRSwAE--GPNQT-------MTFDVLARAVREALSMpGLHGVEFVwhGGEVTLLK--PKVFKKLIWLQqqfrq 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  95 --GLKDIGLTTNGIHLAKQ-AKALKEAGLKrVNISLDA---IEDRVFQKINGRHVStKPVLKGIEAAKEAGLEVKVNMVV 168
Cdd:NF041300 120 pgQEVRNSIQTNATHLTDEwIEFLSELGMG-VGVSIDGppeVHDRRRLDKDGRPTS-SRVAGGIARLRQAGIPHGALVVV 197
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446467166 169 KKGMNDSQILPMAQYFkeQEIQLRFIEFMDV 199
Cdd:NF041300 198 DRELIDAGAERLLGYL--AEIGLDKISFLNV 226
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
24-105 7.34e-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: 48.98  E-value: 7.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  24 CNFRCTYCmpaevfgpD--YAFLQEE-CLLTFDEI-ERLARLfismGVNKIRLTGGEPLLRKDLPKLIARLAKlEGLKdI 99
Cdd:COG0602   30 CNLRCSWC--------DtkYAWDGEGgKRMSAEEIlEEVAAL----GARHVVITGGEPLLQDDLAELLEALKD-AGYE-V 95

                 ....*.
gi 446467166 100 GLTTNG 105
Cdd:COG0602   96 ALETNG 101
rad18 TIGR00599
DNA repair protein rad18; All proteins in this family for which functions are known are ...
253-337 7.50e-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: 44.22  E-value: 7.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  253 ITSVSESFCSSCTRARISADGKFYTCLFGEKGTDLRS--LLRENI-----SDASLLKILQhTWEFRTDRYSDERTAESTN 325
Cdd:TIGR00599  41 LTSCSHTFCSLCIRRCLSNQPKCPLCRAEDQESKLRSnwLVSEIVesfknLRPSLLEFLR-IPKTTPVENPDLAGPENSS 119
                          90
                  ....*....|..
gi 446467166  326 KRQKVEMSYIGG 337
Cdd:TIGR00599 120 KIELIEESESDG 131
GG_samocin_CFB TIGR04148
radical SAM peptide maturase, GG-Bacteroidales family; Members of this protein family are ...
7-128 9.94e-05

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: 43.91  E-value: 9.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166    7 DSLKRPLQDLR---ISVIDRCNFRCTYCmpaeVFGPDYAFL--QEECLLTFDEIERLARLFISMGVNK----------IR 71
Cdd:TIGR04148   7 SDIKQELANLRqltFEVTDACNLQCKYC----SYGDLYNNYdeRENKNIDFDNAKTLIDYLFSLWESKyntsvkntvtIG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446467166   72 LTGGEPLLRKDLPK-LIARLAKL--EGLK-DIGLTTNGIHLAKQAKALKEAGLkRVNISLD 128
Cdd:TIGR04148  83 FYGGEPLLNMDFIKeIINYIEKLhiDGLNfHYNMTTNAMLLRKYMDFLVENDF-HLLISLD 142
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
24-106 3.04e-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: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  24 CNFRCTYCMP--AEVFGPDYAFLqeeclLTFDEI-ERLARLFISMGVNKIRLTGGEPLL-RKDLPKLiarlakLEGLKDI 99
Cdd:COG5014   50 CNLRCGFCWSwrFRDFPLTIGKF-----YSPEEVaERLIEIARERGYRQVRLSGGEPTIgFEHLLKV------LELFSER 118
                         90
                 ....*....|.
gi 446467166 100 GLT----TNGI 106
Cdd:COG5014  119 GLTfileTNGI 129
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
18-203 5.85e-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: 41.38  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   18 ISVIDRCNFRCTYCMPAEVFGPDYAFL-QEECLLTFDEIERLArlfismgVNKIRLTGGEPLLRKDLPKLIARLAKleGL 96
Cdd:TIGR04250   7 IDITGRCNLRCRYCSHFSSAAETPTDLeTAEWLRFFRELNRCS-------VLRVVLSGGEPFMRSDFREIIDGIVK--NR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   97 KDIGLTTNGIhLAKQAKALKEAGLKR---VNISLDAIEDRVFQKINGRHVSTKpVLKGIEAAKEAGLEVKVNMVVKKGmN 173
Cdd:TIGR04250  78 MRFSILSNGT-LITDAIASFLAATRRcdyVQVSIDGSTPGTHDRLRGTGSFLQ-AVEGIELLRKHAIPVVVRVTIHRW-N 154
                         170       180       190
                  ....*....|....*....|....*....|
gi 446467166  174 DSQILPMAQYFKEqeiQLRFIEFmdvgSTN 203
Cdd:TIGR04250 155 VDDLRPIAALLLD---DLGLPAF----STN 177
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
44-162 6.43e-04

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: 40.80  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166  44 LQEECLLTFDEIERLARLFISMGVNKIRL-TGGEPLLRKDLPKLIARLAKLEGLKDIGLT-TNGIHLAKQAKALKEAGLK 121
Cdd:COG0502   67 IERYRLLSVEEILEAARAAKEAGARRFCLvASGRDPSDRDFEKVLEIVRAIKEELGLEVCaSLGELSEEQAKRLKEAGVD 146
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446467166 122 RVNISLDAIEDRvFQKIngrhVSTKPV---LKGIEAAKEAGLEV 162
Cdd:COG0502  147 RYNHNLETSPEL-YPKI----CTTHTYedrLDTLKNAREAGLEV 185
Fer4_14 pfam13394
4Fe-4S single cluster domain;
20-105 8.53e-04

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 38.50  E-value: 8.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   20 VIDRCNFRCTYCMPAEVFGPDYAFLQEECLLTfDEIERLARLFIsmGVNKIRLTGGEPLLRKDLP---KLIARLAKLEGL 96
Cdd:pfam13394   2 FVSGCNHSCPGCDNKETWKFNYGEPFTEELED-QIIADLKDSYI--KRQGLVLTGGEPLHPWNLPvllKLLKRVKEEYPS 78

                  ....*....
gi 446467166   97 KDIGLTTNG 105
Cdd:pfam13394  79 KDIWLETGY 87
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
24-103 1.49e-03

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: 38.31  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446467166   24 CNFRCTYCMPAEVFGPDYAFLqeeclltFDE--IERLARLFISMGVNKIRLTGGEPLL-RKDLPKLIARLAKLEGLKDIG 100
Cdd:pfam13353  15 CNHHCKGCFNPETWDFKYGKP-------FTEelEDEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVREECPEKDIW 87

                  ...
gi 446467166  101 LTT 103
Cdd:pfam13353  88 LWT 90
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH