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Conserved domains on  [gi|569001129|ref|XP_006524745|]
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molybdenum cofactor biosynthesis protein 1 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
219-371 2.65e-82

Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum cofactor biosynthesis enzyme MoaC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


:

Pssm-ID: 440084  Cd Length: 153  Bit Score: 247.66  E-value: 2.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 219 SNQLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVA 298
Cdd:COG0315    1 MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569001129 299 LSHVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRG 371
Cdd:COG0315   81 LTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaA super family cl47076
GTP 3',8-cyclase MoaA;
1-124 8.24e-68

GTP 3',8-cyclase MoaA;


The actual alignment was detected with superfamily member PLN02951:

Pssm-ID: 481416 [Multi-domain]  Cd Length: 373  Bit Score: 218.47  E-value: 8.24e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129   1 MVSYKEMLDTIRQRWPGLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:PLN02951 249 LVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRD 328
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569001129  81 HLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKNRPMILIG 124
Cdd:PLN02951 329 ALRSGADDDELREIIGAAVKRKKAAHAGMFDLAKTANRPMIHIG 372
 
Name Accession Description Interval E-value
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
219-371 2.65e-82

Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum cofactor biosynthesis enzyme MoaC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440084  Cd Length: 153  Bit Score: 247.66  E-value: 2.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 219 SNQLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVA 298
Cdd:COG0315    1 MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569001129 299 LSHVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRG 371
Cdd:COG0315   81 LTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaC PRK09364
cyclic pyranopterin monophosphate synthase MoaC;
219-375 1.08e-81

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 236483  Cd Length: 159  Bit Score: 246.26  E-value: 1.08e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 219 SNQLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVA 298
Cdd:PRK09364   1 MSQLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTSDLIPLCHPLM 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569001129 299 LSHVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRGDFHR 375
Cdd:PRK09364  81 LTGVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDVRLLEKSGGKSGDFKR 157
MoaC_PE cd01420
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ...
233-372 1.35e-75

MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis.


Pssm-ID: 238708  Cd Length: 140  Bit Score: 230.13  E-value: 1.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 233 MVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTR 312
Cdd:cd01420    1 MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEET 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 313 HAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRGD 372
Cdd:cd01420   81 SGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD 140
MoaC pfam01967
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ...
233-368 4.11e-75

MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However their molecular function is not known.


Pssm-ID: 460399  Cd Length: 136  Bit Score: 228.77  E-value: 4.11e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129  233 MVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTR 312
Cdd:pfam01967   1 MVDVSDKPVTLRTAVAEGRIRLSPETLELIREGTVKKGDVLAVARIAGIMAAKKTSDLIPLCHPLPLTGVDVEFELDEEE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569001129  313 HAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGG 368
Cdd:pfam01967  81 DGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDIRLLEKSGG 136
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
1-124 8.24e-68

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 218.47  E-value: 8.24e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129   1 MVSYKEMLDTIRQRWPGLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:PLN02951 249 LVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRD 328
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569001129  81 HLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKNRPMILIG 124
Cdd:PLN02951 329 ALRSGADDDELREIIGAAVKRKKAAHAGMFDLAKTANRPMIHIG 372
moaC TIGR00581
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ...
222-370 2.64e-55

molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum cofactor biosynthesis in E. coli. The Arabidopsis homolog Cnx3 complements MoaC deficiency in E. coli. Eukarotic members of this family branch within the bacterial branch, with the archaeal members as an apparent outgroup. This protein is absent in a number of the pathogens with smaller genomes, including Mycoplasmas, Chlamydias, and spirochetes, but is found in most other complete genomes to date. The homolog form Synechocystis sp. is fused to a MobA-homologous region and is an outlier to all other bacterial forms by both neighbor-joining and UPGMA analyses. Members of this family are well-conserved. The seed for this model excludes both archaeal sequences and the most divergent bacterial sequences, but still finds all candidate MoaC sequences easily between trusted and noise cutoffs. We suggest that sequences branching outside the set that contains all seed members be regarded only as putative functional equivalents of MoaC unless and until a member of the archaeal outgroup is shown to have equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 129670  Cd Length: 147  Bit Score: 178.39  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129  222 LTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSH 301
Cdd:TIGR00581   1 LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLIPLCHPLPLSK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569001129  302 VQVHLELDSTRhaVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQR 370
Cdd:TIGR00581  81 VEVELTVREDR--VEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLLEKSGGKS 147
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
1-107 7.52e-49

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: 161.23  E-value: 7.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129    1 MVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:pfam06463  22 FVSLDEILERIEARFP-LLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRLTADGKLKTCLFAEDGIDLRD 100
                          90       100
                  ....*....|....*....|....*..
gi 569001129   81 HLRAGASEEELLRIIGAAVGRKKRQHA 107
Cdd:pfam06463 101 ALRSGDDDEELREAIREALARKPPRHS 127
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-124 6.17e-47

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: 162.54  E-value: 6.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129   1 MVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:COG2896  206 VVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRA 284
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569001129  81 HLRAGASEEELLRIIGAAVGRKKRQHagMFNIAQMK--NRPMILIG 124
Cdd:COG2896  285 LLRSGASDEELAEAIREAIARKPEGH--GFDEGDFPqpKRSMSAIG 328
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
47-116 8.69e-38

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: 130.36  E-value: 8.69e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129  47 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMK 116
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
1-124 1.74e-32

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: 124.26  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129    1 MVSYKEMLDTIRQRWPGLEKLP-EEDSSTAKAFK--IPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVS 77
Cdd:TIGR02666 204 FVSADEILERLEQAFGPLEPVPsPRGNGPAPAYRwrLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVD 283
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 569001129   78 LRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIA---QMKNRPMILIG 124
Cdd:TIGR02666 284 LRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSpanKRRKRAMSQIG 333
 
Name Accession Description Interval E-value
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
219-371 2.65e-82

Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum cofactor biosynthesis enzyme MoaC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440084  Cd Length: 153  Bit Score: 247.66  E-value: 2.65e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 219 SNQLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVA 298
Cdd:COG0315    1 MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569001129 299 LSHVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRG 371
Cdd:COG0315   81 LTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaC PRK09364
cyclic pyranopterin monophosphate synthase MoaC;
219-375 1.08e-81

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 236483  Cd Length: 159  Bit Score: 246.26  E-value: 1.08e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 219 SNQLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVA 298
Cdd:PRK09364   1 MSQLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTSDLIPLCHPLM 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569001129 299 LSHVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRGDFHR 375
Cdd:PRK09364  81 LTGVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDVRLLEKSGGKSGDFKR 157
MoaC_PE cd01420
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ...
233-372 1.35e-75

MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis.


Pssm-ID: 238708  Cd Length: 140  Bit Score: 230.13  E-value: 1.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 233 MVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTR 312
Cdd:cd01420    1 MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEET 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 313 HAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRGD 372
Cdd:cd01420   81 SGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD 140
MoaC pfam01967
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ...
233-368 4.11e-75

MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However their molecular function is not known.


Pssm-ID: 460399  Cd Length: 136  Bit Score: 228.77  E-value: 4.11e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129  233 MVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTR 312
Cdd:pfam01967   1 MVDVSDKPVTLRTAVAEGRIRLSPETLELIREGTVKKGDVLAVARIAGIMAAKKTSDLIPLCHPLPLTGVDVEFELDEEE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 569001129  313 HAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGG 368
Cdd:pfam01967  81 DGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDIRLLEKSGG 136
MoaC cd00528
MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, ...
233-368 1.61e-70

MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis.


Pssm-ID: 238293  Cd Length: 136  Bit Score: 217.00  E-value: 1.61e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 233 MVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTR 312
Cdd:cd00528    1 MVDVSDKAVTERTAVAEGRVRLSPETLDLIREGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEDT 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569001129 313 HAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGG 368
Cdd:cd00528   81 SGVRIRATVRTTGKTGVEMEALTAVSVAALTIYDMCKAVDKDMVIENIRLLEKSGG 136
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
1-124 8.24e-68

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 218.47  E-value: 8.24e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129   1 MVSYKEMLDTIRQRWPGLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:PLN02951 249 LVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRD 328
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569001129  81 HLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKNRPMILIG 124
Cdd:PLN02951 329 ALRSGADDDELREIIGAAVKRKKAAHAGMFDLAKTANRPMIHIG 372
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
223-371 2.56e-62

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 202.09  E-value: 2.56e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 223 THVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHV 302
Cdd:PRK03604   1 THLDEEGRVRMVDVSGKPGTLRTARASGIIVTSPETIELLRQGDLPKGDVLTTAKIAGIQAAKRTSELIPLCHPLPLSWV 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569001129 303 QVHLELDSTRhaVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRG 371
Cdd:PRK03604  81 DVEFEIEDDR--IRIEATVKTIGKTGVEMEALTAVSVAALTIYDMLKPVDKALEIGGIRLLEKTGGKSG 147
moaC TIGR00581
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ...
222-370 2.64e-55

molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum cofactor biosynthesis in E. coli. The Arabidopsis homolog Cnx3 complements MoaC deficiency in E. coli. Eukarotic members of this family branch within the bacterial branch, with the archaeal members as an apparent outgroup. This protein is absent in a number of the pathogens with smaller genomes, including Mycoplasmas, Chlamydias, and spirochetes, but is found in most other complete genomes to date. The homolog form Synechocystis sp. is fused to a MobA-homologous region and is an outlier to all other bacterial forms by both neighbor-joining and UPGMA analyses. Members of this family are well-conserved. The seed for this model excludes both archaeal sequences and the most divergent bacterial sequences, but still finds all candidate MoaC sequences easily between trusted and noise cutoffs. We suggest that sequences branching outside the set that contains all seed members be regarded only as putative functional equivalents of MoaC unless and until a member of the archaeal outgroup is shown to have equivalent function. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 129670  Cd Length: 147  Bit Score: 178.39  E-value: 2.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129  222 LTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSH 301
Cdd:TIGR00581   1 LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLIPLCHPLPLSK 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569001129  302 VQVHLELDSTRhaVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQR 370
Cdd:TIGR00581  81 VEVELTVREDR--VEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLLEKSGGKS 147
PRK14499 PRK14499
cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein;
221-375 1.91e-49

cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein;


Pssm-ID: 237733 [Multi-domain]  Cd Length: 308  Bit Score: 168.50  E-value: 1.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 221 QLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALS 300
Cdd:PRK14499   2 EFTHFNKDGLPQMVDVSSKEPTFRVAVASGRIYVGKEVIEAIEERLLPKGDVFSVAKIAAIMAAKKTSELIPLCHNIFLS 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569001129 301 HVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQRGDFHR 375
Cdd:PRK14499  82 GVDVSYEINREEGYIEAVSEVKTEAKTGAEMEAITAVSIFLETIYDMCKAVKKDMVITDVRLIEKSGGKSGHYIF 156
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
1-107 7.52e-49

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: 161.23  E-value: 7.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129    1 MVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:pfam06463  22 FVSLDEILERIEARFP-LLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRLTADGKLKTCLFAEDGIDLRD 100
                          90       100
                  ....*....|....*....|....*..
gi 569001129   81 HLRAGASEEELLRIIGAAVGRKKRQHA 107
Cdd:pfam06463 101 ALRSGDDDEELREAIREALARKPPRHS 127
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
1-124 6.17e-47

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: 162.54  E-value: 6.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129   1 MVSYKEMLDTIRQRWPgLEKLPEEDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:COG2896  206 VVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRA 284
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 569001129  81 HLRAGASEEELLRIIGAAVGRKKRQHagMFNIAQMK--NRPMILIG 124
Cdd:COG2896  285 LLRSGASDEELAEAIREAIARKPEGH--GFDEGDFPqpKRSMSAIG 328
PLN02375 PLN02375
molybderin biosynthesis protein CNX3
189-376 8.11e-47

molybderin biosynthesis protein CNX3


Pssm-ID: 178003 [Multi-domain]  Cd Length: 270  Bit Score: 160.70  E-value: 8.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 189 YSSYPDPDTHSKCLSTGSQAPDAPSGPGPTSNQLTHVDSAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLK 268
Cdd:PLN02375  83 FRQQIEYHKSTHSSKNDSQAIEQYAKVASDMSKLTHVGIAGEAQMVDVSSKDNSKRTALACCKVILGKRVFDLVLANQMG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 269 KGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTRHAVLIQASCRARGPTGVEMEALTSAAMAALTVYDMC 348
Cdd:PLN02375 163 KGDVLGVAKIAGINGAKQTSSLIPLCHNIALTHVRVDLRLNPEDFSVDIEGEASCTGKTGVEMEAMTAVSVAGLTVYDMC 242
                        170       180
                 ....*....|....*....|....*...
gi 569001129 349 KAVSRDIVVTEVKLISKTGGQRGDFHRA 376
Cdd:PLN02375 243 KAASKDISITDVRLERKTGGKSGSWSRL 270
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
47-116 8.69e-38

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: 130.36  E-value: 8.69e-38
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129  47 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMK 116
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
PRK12343 PRK12343
cyclic pyranopterin monophosphate synthase MoaC;
224-354 1.03e-37

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 237067  Cd Length: 151  Bit Score: 132.73  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 224 HVDsAGRASMVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQ 303
Cdd:PRK12343   1 HVD-EDGVKMVDVSEKEDVLRIAVAEGFIKLKPETIEAIREGEVEKGNVLATARVAGILAVKKTPELIPMCHPIPITGVD 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 569001129 304 VHLELDSTRhavlIQASC--RARGPTGVEMEALTSAAMAALTVYDMCKAVSRD 354
Cdd:PRK12343  80 VDFEVGEDG----IEARVtvKTTYKTGVEMEALTGVSVALLTIWDMVKAAEKD 128
MoaC_A cd01419
MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) ...
233-354 1.12e-34

MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, an essential cofactor of a diverse group of redox enzymes. MoaC, a small hexameric protein, converts, together with MoaA, a guanosine derivative to the precursor Z by inserting the carbon-8 of the purine between the 2' and 3' ribose carbon atoms, which is the first of three phases of Moco biosynthesis.


Pssm-ID: 238707  Cd Length: 141  Bit Score: 124.78  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 233 MVDVGGKPETERVAVASAMVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKLTSQLIPLCHHVALSHVQVHLELDSTR 312
Cdd:cd01419    1 MVDISSKEDVAREAVASGFIKLKEETIKAIREGKVEKGNVIATARIAGILAVKKTPELIPMCHPIPITGVDVDFEVEEDG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569001129 313 havlIQASCRAR--GPTGVEMEALTSAAMAALTVYDMCKAVSRD 354
Cdd:cd01419   81 ----IEVRCTVKttYKTGVEMEALTGVSVALLTIWDMVKSAEKD 120
moaA PRK00164
GTP 3',8-cyclase MoaA;
1-124 5.53e-33

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 125.64  E-value: 5.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129   1 MVSYKEMLDTIRQRWPGLEKLPEeDSSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRD 80
Cdd:PRK00164 209 HLSGAEIRARLAERGWTLQPRAR-SGGPAQYFRHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRD 287
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569001129  81 HLRAGASEEELLRIIGAAVGRKKRQHAGMFNIAQMKnRPMILIG 124
Cdd:PRK00164 288 LLRSGADDEELAAAIREALQNKPEGHGLHDGNTGPT-RHMSYIG 330
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
1-124 1.74e-32

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: 124.26  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129    1 MVSYKEMLDTIRQRWPGLEKLP-EEDSSTAKAFK--IPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVS 77
Cdd:TIGR02666 204 FVSADEILERLEQAFGPLEPVPsPRGNGPAPAYRwrLPGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVD 283
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 569001129   78 LRDHLRAGASEEELLRIIGAAVGRKKRQHAGMFNIA---QMKNRPMILIG 124
Cdd:TIGR02666 284 LRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSpanKRRKRAMSQIG 333
PRK14500 PRK14500
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ...
222-370 1.79e-32

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; Provisional


Pssm-ID: 237734 [Multi-domain]  Cd Length: 346  Bit Score: 124.62  E-value: 1.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569001129 222 LTHVDSAGRASMVDVGGKPETERVAVASAMVLLgPVAFKLVQQNQ---LKKGDALVVAQLAGVQAAKLTSQLIPLCHHVA 298
Cdd:PRK14500   2 FTHLNENQQPRMVDISQKVVSDRRAVAQAIVQL-PPAIKDYVTGQdifLKKGPVIQTAIIAGTMAVKRTADLIPFCHTLP 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569001129 299 LSHVQVHLELDSTRHAVLIQASCRAR--GPTGVEMEALTSAAMAALTVYDMCKAVSRDIVVTEVKLISKTGGQR 370
Cdd:PRK14500  81 IHGCKFDINIVYQKRDLEIFLQCAVKtnYKTGVEMEALCGVAVAALTIYDMCKSISPHIIIKETRLIEKSGGKA 154
 
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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