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Conserved domains on  [gi|1284804782|ref|NP_001345458|]
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molybdenum cofactor biosynthesis protein 1 isoform 6 [Homo sapiens]

Protein Classification

Twitch_MoaA and MoaC_PE domain-containing protein( domain architecture ID 11477313)

Twitch_MoaA and MoaC_PE domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 19-370 0e+00

Molybderin biosynthesis protein CNX2


:

Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 569.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  19 RSCSSGAPVTqPCPGESARAAseevsrRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPK 98
Cdd:PLN02951   14 SSFQLQEPGS-SIFSASSSYA------ADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  99 ANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINIS 178
Cdd:PLN02951   87 SHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNIS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 179 LDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNF 258
Cdd:PLN02951  167 LDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 259 KKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSL 338
Cdd:PLN02951  247 KKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSL 326

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1284804782 339 RDHLRAGASEQELLRIIGAAVGRKKRQHAELF 370
Cdd:PLN02951  327 RDALRSGADDDELREIIGAAVKRKKAAHAGMF 358
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
 463-615 4.33e-80

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: 249.59  E-value: 4.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 463 SEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVA 542
Cdd:COG0315     1 MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284804782 543 LSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRG 615
Cdd:COG0315    81 LTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 19-370 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 569.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  19 RSCSSGAPVTqPCPGESARAAseevsrRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPK 98
Cdd:PLN02951   14 SSFQLQEPGS-SIFSASSSYA------ADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  99 ANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINIS 178
Cdd:PLN02951   87 SHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNIS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 179 LDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNF 258
Cdd:PLN02951  167 LDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 259 KKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSL 338
Cdd:PLN02951  247 KKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSL 326

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1284804782 339 RDHLRAGASEQELLRIIGAAVGRKKRQHAELF 370
Cdd:PLN02951  327 RDALRSGADDDELREIIGAAVKRKKAAHAGMF 358
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 61-369 1.25e-169

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: 485.72  E-value: 1.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVA 140
Cdd:COG2896     5 LIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 141 QLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVV 220
Cdd:COG2896    85 RLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 221 MRGLNEDELLDFAALTEGLPLDVRFIEYMPF-DGNKWNFKKMVSYKEMLDTVRQQWPeLEKVPEEESSTAKAFKIPGFQG 299
Cdd:COG2896   165 MRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGG 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 300 QISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAEL 369
Cdd:COG2896   244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFD 313
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 61-379 1.61e-142

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: 417.01  E-value: 1.61e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVP-LTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 140 AQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYNPVKVNC 218
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 219 VVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEKVP---EEESSTAKAFKI 294
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPsprGNGPAPAYRWRL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 295 PGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAELFLMFP 374
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSP 320


                  ....*
gi 1284804782 375 NSPPA 379
Cdd:TIGR02666 321 ANKRR 325
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
 463-615 4.33e-80

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: 249.59  E-value: 4.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 463 SEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVA 542
Cdd:COG0315     1 MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284804782 543 LSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRG 615
Cdd:COG0315    81 LTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaC PRK09364
cyclic pyranopterin monophosphate synthase MoaC;
465-619 4.21e-79

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 236483  Cd Length: 159  Bit Score: 247.03  E-value: 4.21e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 465 QLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALS 544
Cdd:PRK09364    3 QLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTSDLIPLCHPLMLT 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284804782 545 HIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHR 619
Cdd:PRK09364   83 GVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDVRLLEKSGGKSGDFKR 157
MoaC_PE cd01420
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ...
 477-616 1.10e-74

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: 235.13  E-value: 1.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 477 MVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTR 556
Cdd:cd01420     1 MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 557 HAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGD 616
Cdd:cd01420    81 SGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD 140
MoaC pfam01967
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ...
 477-612 3.02e-73

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: 231.08  E-value: 3.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 477 MVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTR 556
Cdd:pfam01967   1 MVDVSDKPVTLRTAVAEGRIRLSPETLELIREGTVKKGDVLAVARIAGIMAAKKTSDLIPLCHPLPLTGVDVEFELDEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1284804782 557 HAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGG 612
Cdd:pfam01967  81 DGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDIRLLEKSGG 136
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
 241-367 9.34e-59

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: 192.82  E-value: 9.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 241 LDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEkVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLR 319
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFPLLP-ARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1284804782 320 ITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHA 367
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
moaC TIGR00581
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ...
 466-614 2.00e-53

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: 179.16  E-value: 2.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 466 LTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSH 545
Cdd:TIGR00581   1 LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLIPLCHPLPLSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1284804782 546 IQVQLELDSTRhaVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQR 614
Cdd:TIGR00581  81 VEVELTVREDR--VEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLLEKSGGKS 147
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
 307-373 1.04e-33

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: 123.04  E-value: 1.04e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1284804782 307 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAELFLMF 373
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDS 67
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 70-271 4.28e-12

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 65.89  E-value: 4.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782   70 SYLRISLTEKCNLRCQYCM--PEEGVPLTPKANLLtTEEILTLARLFVKEG-IDKIRLTGGEPLIRP--DVVDIVAQLQR 144
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSfpSLRGKLRSRYLEAL-VREIELLAEKGEKEGlVGTVFIGGGTPTLLSpeQLEELLEAIRE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  145 LEGLRTIGVTTNGINL----ARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGynPVKVNCVV 220
Cdd:smart00729  80 ILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDL 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1284804782  221 MRGL---NEDELLDFAALTEGLPLD-VRFIEYMPFDG----NKWNFKKMVSYKEMLDTV 271
Cdd:smart00729 158 IVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 71-281 4.89e-10

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: 61.90  E-value: 4.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  71 YLRISLTEKCNLRCQYCMP-------EEGVPLTPKANLLTTEEILTLARLFVKE------GIDKIRLTGGEPLIRPDVVD 137
Cdd:NF033640  111 YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 138 IvaqLQRL--EGLR---TIGVTTNG-------INLARLLPQLQKAglsAINISLDTlVPAKFEFIvrRKGFH--KVMEGI 203
Cdd:NF033640  191 L---LEKLveKGRAkniELRYNTNLtvlpdklKDLLDLWKKFKSV---SISASIDG-VGERNEYI--RYGSKwdEIEKNL 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 204 HKAIELGYN-PVKVNCVV--MRGLNEDELLDFaALTEG---------------------LPLDVR--------------- 244
Cdd:NF033640  262 KKLKEECPNvELRINPTVsaLNVLHLPELLDW-LLELGlgpidiylnilrdpeylsiknLPKEIKqkvieklenfleknd 340

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1284804782 245 -------------FIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ-----WPELEKV 281
Cdd:NF033640  341 ngfdkylikklkrLINYMNSEDNSELLKEFKKFTKKLDKIRGEnfldvFPELKEL 395
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 19-370 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 569.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  19 RSCSSGAPVTqPCPGESARAAseevsrRRQFLREHAAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPK 98
Cdd:PLN02951   14 SSFQLQEPGS-SIFSASSSYA------ADQVDPEASNPVSDMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  99 ANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINIS 178
Cdd:PLN02951   87 SHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNIS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 179 LDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFDGNKWNF 258
Cdd:PLN02951  167 LDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 259 KKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSL 338
Cdd:PLN02951  247 KKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSL 326

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1284804782 339 RDHLRAGASEQELLRIIGAAVGRKKRQHAELF 370
Cdd:PLN02951  327 RDALRSGADDDELREIIGAAVKRKKAAHAGMF 358
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 61-369 1.25e-169

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: 485.72  E-value: 1.25e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVA 140
Cdd:COG2896     5 LIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPELIA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 141 QLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVV 220
Cdd:COG2896    85 RLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKINAVV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 221 MRGLNEDELLDFAALTEGLPLDVRFIEYMPF-DGNKWNFKKMVSYKEMLDTVRQQWPeLEKVPEEESSTAKAFKIPGFQG 299
Cdd:COG2896   165 MRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPGGGG 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 300 QISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAEL 369
Cdd:COG2896   244 RIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFD 313
moaA PRK00164
GTP 3',8-cyclase MoaA;
54-366 5.55e-146

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 425.71  E-value: 5.55e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  54 AAPFSAFLTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRP 133
Cdd:PRK00164    1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 134 DVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNP 213
Cdd:PRK00164   81 DLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 214 VKVNCVVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELeKVPEEESSTAKAF 292
Cdd:PRK00164  161 VKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGeGNEWFRKHHLSGAEIRARLAERGWTL-QPRARSGGPAQYF 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284804782 293 KIPGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQH 366
Cdd:PRK00164  240 RHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGH 313
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 61-379 1.61e-142

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: 417.01  E-value: 1.61e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  61 LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVP-LTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 140 AQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYNPVKVNC 218
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPVKLNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 219 VVMRGLNEDELLDFAALTEGLPLDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEKVP---EEESSTAKAFKI 294
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPsprGNGPAPAYRWRL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 295 PGFQGQISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAELFLMFP 374
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHSFLRFTSP 320


                  ....*
gi 1284804782 375 NSPPA 379
Cdd:TIGR02666 321 ANKRR 325
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
 463-615 4.33e-80

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: 249.59  E-value: 4.33e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 463 SEQLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVA 542
Cdd:COG0315     1 MSELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284804782 543 LSHIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRG 615
Cdd:COG0315    81 LTGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaC PRK09364
cyclic pyranopterin monophosphate synthase MoaC;
465-619 4.21e-79

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 236483  Cd Length: 159  Bit Score: 247.03  E-value: 4.21e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 465 QLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALS 544
Cdd:PRK09364    3 QLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTSDLIPLCHPLMLT 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284804782 545 HIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHR 619
Cdd:PRK09364   83 GVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDVRLLEKSGGKSGDFKR 157
MoaC_PE cd01420
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ...
 477-616 1.10e-74

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: 235.13  E-value: 1.10e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 477 MVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTR 556
Cdd:cd01420     1 MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEET 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 557 HAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGD 616
Cdd:cd01420    81 SGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD 140
MoaC pfam01967
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ...
 477-612 3.02e-73

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: 231.08  E-value: 3.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 477 MVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTR 556
Cdd:pfam01967   1 MVDVSDKPVTLRTAVAEGRIRLSPETLELIREGTVKKGDVLAVARIAGIMAAKKTSDLIPLCHPLPLTGVDVEFELDEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1284804782 557 HAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGG 612
Cdd:pfam01967  81 DGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDIRLLEKSGG 136
MoaC cd00528
MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, ...
 477-612 2.76e-69

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: 220.85  E-value: 2.76e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 477 MVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDSTR 556
Cdd:cd00528     1 MVDVSDKAVTERTAVAEGRVRLSPETLDLIREGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEDT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1284804782 557 HAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGG 612
Cdd:cd00528    81 SGVRIRATVRTTGKTGVEMEALTAVSVAALTIYDMCKAVDKDMVIENIRLLEKSGG 136
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 467-615 1.01e-61

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 207.10  E-value: 1.01e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 467 THVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHI 546
Cdd:PRK03604    1 THLDEEGRVRMVDVSGKPGTLRTARASGIIVTSPETIELLRQGDLPKGDVLTTAKIAGIQAAKRTSELIPLCHPLPLSWV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1284804782 547 QVQLELDSTRhaVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRG 615
Cdd:PRK03604   81 DVEFEIEDDR--IRIEATVKTIGKTGVEMEALTAVSVAALTIYDMLKPVDKALEIGGIRLLEKTGGKSG 147
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
 241-367 9.34e-59

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: 192.82  E-value: 9.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 241 LDVRFIEYMPFD-GNKWNFKKMVSYKEMLDTVRQQWPELEkVPEEESSTAKAFKIPGFQGQISFITSMSEHFCGTCNRLR 319
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFPLLP-ARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1284804782 320 ITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHA 367
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
moaC TIGR00581
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ...
 466-614 2.00e-53

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: 179.16  E-value: 2.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 466 LTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSH 545
Cdd:TIGR00581   1 LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLIPLCHPLPLSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1284804782 546 IQVQLELDSTRhaVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQR 614
Cdd:TIGR00581  81 VEVELTVREDR--VEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLLEKSGGKS 147
PRK14499 PRK14499
cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein;
465-619 1.36e-46

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


Pssm-ID: 237733 [Multi-domain]  Cd Length: 308  Bit Score: 166.57  E-value: 1.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 465 QLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALS 544
Cdd:PRK14499    2 EFTHFNKDGLPQMVDVSSKEPTFRVAVASGRIYVGKEVIEAIEERLLPKGDVFSVAKIAAIMAAKKTSELIPLCHNIFLS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1284804782 545 HIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHR 619
Cdd:PRK14499   82 GVDVSYEINREEGYIEAVSEVKTEAKTGAEMEAITAVSIFLETIYDMCKAVKKDMVITDVRLIEKSGGKSGHYIF 156
PLN02375 PLN02375
molybderin biosynthesis protein CNX3
 465-620 5.74e-44

molybderin biosynthesis protein CNX3


Pssm-ID: 178003 [Multi-domain]  Cd Length: 270  Bit Score: 158.39  E-value: 5.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 465 QLTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALS 544
Cdd:PLN02375  115 KLTHVGIAGEAQMVDVSSKDNSKRTALACCKVILGKRVFDLVLANQMGKGDVLGVAKIAGINGAKQTSSLIPLCHNIALT 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1284804782 545 HIQVQLELDSTRHAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQRGDFHRA 620
Cdd:PLN02375  195 HVRVDLRLNPEDFSVDIEGEASCTGKTGVEMEAMTAVSVAGLTVYDMCKAASKDISITDVRLERKTGGKSGSWSRL 270
PRK12343 PRK12343
cyclic pyranopterin monophosphate synthase MoaC;
468-613 1.61e-37

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 237067  Cd Length: 151  Bit Score: 136.19  E-value: 1.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 468 HVDsEGRAAMVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQ 547
Cdd:PRK12343    1 HVD-EDGVKMVDVSEKEDVLRIAVAEGFIKLKPETIEAIREGEVEKGNVLATARVAGILAVKKTPELIPMCHPIPITGVD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1284804782 548 VQLELDSTrhAVKIQASCRARGPTGVEMEALTSAAVAALTLYDMCKAVSRD-------IVLEEIKLISKTGGQ 613
Cdd:PRK12343   80 VDFEVGED--GIEARVTVKTTYKTGVEMEALTGVSVALLTIWDMVKAAEKDedgqypeTRIENIRVVEKIKEE 150
MoaC_A cd01419
MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) ...
 477-598 8.79e-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: 125.55  E-value: 8.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 477 MVDVGRKPDTERVAVASAVVLLGPVAFKLVQQNQLKKGDALVVAQLAGVQAAKVTSQLIPLCHHVALSHIQVQLELDStr 556
Cdd:cd01419     1 MVDISSKEDVAREAVASGFIKLKEETIKAIREGKVEKGNVIATARIAGILAVKKTPELIPMCHPIPITGVDVDFEVEE-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1284804782 557 haVKIQASCRAR--GPTGVEMEALTSAAVAALTLYDMCKAVSRD 598
Cdd:cd01419    79 --DGIEVRCTVKttYKTGVEMEALTGVSVALLTIWDMVKSAEKD 120
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
 307-373 1.04e-33

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: 123.04  E-value: 1.04e-33
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1284804782 307 MSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVGRKKRQHAELFLMF 373
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDS 67
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 71-219 3.79e-33

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: 124.63  E-value: 3.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  71 YLRISLTEKCNLRCQYCMPEEGVPLTPKanlLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLeGLRT 150
Cdd:COG0535     1 RLQIELTNRCNLRCKHCYADAGPKRPGE---LSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKEL-GIRV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1284804782 151 IgVTTNGINLAR-LLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYnPVKVNCV 219
Cdd:COG0535    77 N-LSTNGTLLTEeLAERLAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGI-PVGINTV 145
PRK14500 PRK14500
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ...
 466-614 9.33e-32

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


Pssm-ID: 237734 [Multi-domain]  Cd Length: 346  Bit Score: 126.16  E-value: 9.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 466 LTHVDSEGRAAMVDVGRKPDTERVAVASAVVLLgPVAFKLVQQNQ---LKKGDALVVAQLAGVQAAKVTSQLIPLCHHVA 542
Cdd:PRK14500    2 FTHLNENQQPRMVDISQKVVSDRRAVAQAIVQL-PPAIKDYVTGQdifLKKGPVIQTAIIAGTMAVKRTADLIPFCHTLP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1284804782 543 LSHIQVQLELDSTRHAVKIQASCRAR--GPTGVEMEALTSAAVAALTLYDMCKAVSRDIVLEEIKLISKTGGQR 614
Cdd:PRK14500   81 IHGCKFDINIVYQKRDLEIFLQCAVKtnYKTGVEMEALCGVAVAALTIYDMCKSISPHIIIKETRLIEKSGGKA 154
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 76-232 9.89e-32

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: 120.71  E-value: 9.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  76 LTEKCNLRCQYCMPEEGvPLTPKANLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGL--RTIGV 153
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSI-RARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAegIRITL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 154 TTNGINLA-RLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDF 232
Cdd:pfam04055  80 ETNGTLLDeELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEET 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 74-271 3.24e-23

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: 97.79  E-value: 3.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  74 ISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILtLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGV 153
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILD-IVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 154 TTNG-INLARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGynpVKVNCVVMRGLNEDELLD 231
Cdd:cd01335    80 ETNGtLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSGEsFKERLEALKELREAG---LGLSTTLLVGLGDEDEED 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1284804782 232 FAALTEGL-----PLDVRFIEYMPFDGNKWNFKKMVSYKEMLDTV 271
Cdd:cd01335   157 DLEELELLaefrsPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRL 201
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 74-329 1.12e-14

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 75.79  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  74 ISLTEKCNLRCQYCMpEEGVPLTPKANLltTEEILTLARLFVKE---GIDKIRLT--GGEPLIRPDVV-DIVAQLQRLEG 147
Cdd:COG0641     5 LKPTSRCNLRCSYCY-YSEGDEGSRRRM--SEETAEKAIDFLIEssgPGKELTITffGGEPLLNFDFIkEIVEYARKYAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 148 LR---TIGVTTNGINL-ARLLPQLQKAGLSaINISLDTLvpakfEFI-----VRRKG---FHKVMEGIHKAIELGYnPVK 215
Cdd:COG0641    82 KGkkiRFSIQTNGTLLdDEWIDFLKENGFS-VGISLDGP-----KEIhdrnrVTKNGkgsFDRVMRNIKLLKEHGV-EVN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 216 VNCVVMRGLNED--ELLDFAAlTEGLPlDVRFIEYMPFDGNKWNFkKMVSYKEMLDTVRQQWPELEKVPeeesstakaFK 293
Cdd:COG0641   155 IRCTVTRENLDDpeELYDFLK-ELGFR-SIQFNPVVEEGEADYSL-TPEDYGEFLIELFDEWLERDGGK---------IF 222

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1284804782 294 IPGFQGQISFITSMSEHFC-GTCNR-LRITADGNLKVC 329
Cdd:COG0641   223 VREFDILLAGLLPPCSSPCvGAGGNyLVVDPDGDIYPC 260
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 70-271 4.28e-12

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 65.89  E-value: 4.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782   70 SYLRISLTEKCNLRCQYCM--PEEGVPLTPKANLLtTEEILTLARLFVKEG-IDKIRLTGGEPLIRP--DVVDIVAQLQR 144
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSfpSLRGKLRSRYLEAL-VREIELLAEKGEKEGlVGTVFIGGGTPTLLSpeQLEELLEAIRE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  145 LEGLRTIGVTTNGINL----ARLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGFHKVMEGIHKAIELGynPVKVNCVV 220
Cdd:smart00729  80 ILGLAKDVEITIETRPdtltEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVSTDL 157

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1284804782  221 MRGL---NEDELLDFAALTEGLPLD-VRFIEYMPFDG----NKWNFKKMVSYKEMLDTV 271
Cdd:smart00729 158 IVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 76-239 4.73e-11

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: 64.86  E-value: 4.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  76 LTEKCNLRCQYCMpeegvpLTPK---ANLLTTEEILTLARLFVKE----GIDKIRLTGGEPLIRPDVVDIVaQLQRLEGL 148
Cdd:TIGR04251  10 LTEGCNLKCRHCW------IDPKyqgEGEQHPSLDPSLFRSIIRQaiplGLTSVKLTGGEPLLHPAIGEIL-ECIGENNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 149 RtIGVTTNGINLArllPQLQK--AGLSA--INISLDTLVPAKFEFIVRRKG-FHKVMEGIHKAIELGYNPVKVNCVVMRg 223
Cdd:TIGR04251  83 Q-LSVETNGLLCT---PQTARdlASCETpfVSVSLDGVDAATHDWMRGVKGaFDKAVRGIHNLVEAGIHPQIIMTVTRR- 157

                         170
                  ....*....|....*.
gi 1284804782 224 lNEDELLDFAALTEGL 239
Cdd:TIGR04251 158 -NVGQMEQIVRLAESL 172
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 80-251 5.52e-11

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 62.89  E-value: 5.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYCMPEEGVPLTPKANL--LTTEEILTLA--RLFVKEGIDKIRLTGGEPLIRPD-VVDIVAQLQRLeGLRTIGVt 154
Cdd:COG1180    31 CNLRCPYCHNPEISQGRPDAAGreLSPEELVEEAlkDRGFLDSCGGVTFSGGEPTLQPEfLLDLAKLAKEL-GLHTALD- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 155 TNGIN----LARLLPqlqkaGLSAINISLDTLVPAKFEFIVRRKGfHKVMEGIHKAIELGYnPVKVNCVVMRGLN--EDE 228
Cdd:COG1180   109 TNGYIpeeaLEELLP-----YLDAVNIDLKAFDDEFYRKLTGVSL-EPVLENLELLAESGV-HVEIRTLVIPGLNdsEEE 181

                         170       180
                  ....*....|....*....|...
gi 1284804782 229 LLDFAALTEGLPlDVRFIEYMPF 251
Cdd:COG1180   182 LEAIARFIAELG-DVIPVHLLPF 203
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
 80-233 4.63e-10

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 61.46  E-value: 4.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYCMPEEGvpltPKANLLTTEEILTLARLFvkEGIDKI-RLTG----------GEPLIRPDVVDIVAQLQRLEGL 148
Cdd:COG2100    46 CNLNCIFCSVDAG----PHSRTRQAEYIVDPEYLV--EWFEKVaRFKGkgveahidgvGEPLLYPYIVELVKGLKEIKGV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 149 RTIGVTTNGINLA-RLLPQLQKAGLSAINISLDTLVPAKFEFIVRRKGF--HKVMEGIHKAI-ELGYNpVKVNCVVMRGL 224
Cdd:COG2100   120 KVVSMQTNGTLLSeKLIDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYdvEKVLELAEYIArETKID-LLIAPVWLPGI 198

                         170
                  ....*....|..
gi 1284804782 225 NEDE---LLDFA 233
Cdd:COG2100   199 NDEDipkIIEWA 210
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 71-281 4.89e-10

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: 61.90  E-value: 4.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  71 YLRISLTEKCNLRCQYCMP-------EEGVPLTPKANLLTTEEILTLARLFVKE------GIDKIRLTGGEPLIRPDVVD 137
Cdd:NF033640  111 YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYK 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 138 IvaqLQRL--EGLR---TIGVTTNG-------INLARLLPQLQKAglsAINISLDTlVPAKFEFIvrRKGFH--KVMEGI 203
Cdd:NF033640  191 L---LEKLveKGRAkniELRYNTNLtvlpdklKDLLDLWKKFKSV---SISASIDG-VGERNEYI--RYGSKwdEIEKNL 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 204 HKAIELGYN-PVKVNCVV--MRGLNEDELLDFaALTEG---------------------LPLDVR--------------- 244
Cdd:NF033640  262 KKLKEECPNvELRINPTVsaLNVLHLPELLDW-LLELGlgpidiylnilrdpeylsiknLPKEIKqkvieklenfleknd 340

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1284804782 245 -------------FIEYMPFDGNKWNFKKMVSYKEMLDTVRQQ-----WPELEKV 281
Cdd:NF033640  341 ngfdkylikklkrLINYMNSEDNSELLKEFKKFTKKLDKIRGEnfldvFPELKEL 395
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 74-240 3.52e-07

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


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 52.55  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  74 ISLTEKCNLRCQYCMPEEGVPLTPkaNLLTTEEILTLARLFVKEGIDKIRLTGGEPLIRPDVVDIVAQLQRlEGLRtIGV 153
Cdd:TIGR04250   7 IDITGRCNLRCRYCSHFSSAAETP--TDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVK-NRMR-FSI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 154 TTNGInlarLLPQLQKAGLSA------INISLDTLVPAKFEfIVRRKG-FHKVMEGIhKAIELGYNPVKVNCVVMRGlNE 226
Cdd:TIGR04250  83 LSNGT----LITDAIASFLAAtrrcdyVQVSIDGSTPGTHD-RLRGTGsFLQAVEGI-ELLRKHAIPVVVRVTIHRW-NV 155

                         170
                  ....*....|....*..
gi 1284804782 227 DELLDFAAL---TEGLP 240
Cdd:TIGR04250 156 DDLRPIAALlldDLGLP 172
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 80-157 6.31e-07

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


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 50.52  E-value: 6.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYC------MPEEGVPLTPkanllttEEILTLARlfvKEGIDKIRLTGGEPLIRPDVVDIVAQLQRlEGLRtIGV 153
Cdd:COG0602    30 CNLRCSWCdtkyawDGEGGKRMSA-------EEILEEVA---ALGARHVVITGGEPLLQDDLAELLEALKD-AGYE-VAL 97


                  ....
gi 1284804782 154 TTNG 157
Cdd:COG0602    98 ETNG 101
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
 80-256 3.60e-06

pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain (pfam04055). A single glycine residue in EC 2.3.1.54, formate C-acetyltransferase (formate-pyruvate lyase), is oxidized to the corresponding radical by transfer of H from its CH2 to AdoMet with concomitant cleavage of the latter. The reaction requires Fe2+. The first stage is reduction of the AdoMet to give methionine and the 5'-deoxyadenosin-5-yl radical, which then abstracts a hydrogen radical from the glycine residue. [Energy metabolism, Anaerobic, Protein fate, Protein modification and repair]


Pssm-ID: 131546 [Multi-domain]  Cd Length: 235  Bit Score: 48.52  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYCM------PEEGVPLTPKANLlttEEILTLARLFVKEGiDKIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIgV 153
Cdd:TIGR02493  25 CPLRCQYCHnpdtwdLKGGTEVTPEELI---KEVGSYKDFFKASG-GGVTFSGGEPLLQPEFLSELFKACKELGIHTC-L 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 154 TTNGinLARLLPQLQKAGLSAINISL---DTLVPAKFEFIVRRKG-----FHKVMEGIHKAIELGYnpvkvncVVMRGL- 224
Cdd:TIGR02493 100 DTSG--FLGGCTEAADELLEYTDLVLldiKHFNPEKYKKLTGVSLqptldFAKYLAKRNKPIWIRY-------VLVPGYt 170

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1284804782 225 -NEDELLDFAALTEGLPlDVRFIEYMPFDG---NKW 256
Cdd:TIGR02493 171 dSEEDIEALAEFVKTLP-NVERVEVLPYHQlgvYKW 205
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
80-250 4.08e-06

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 49.47  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYCMPEEGVPLTPK-ANLLTTEEILtlaRLFVKEGID-----KIRLT--GGEPLIRPDVVDIVA-QLQR-LEGLR 149
Cdd:PRK13745   24 CNLACDYCYYLEKSKLYQEnPKHVMSDELL---EKFIKEYINsqtmpQVLFTwhGGETLMRPLSFYKKAlELQKkYARGR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 150 TIG--VTTNGINLARLLPQLQKAGLSAINISLDTlvPAKFEFIVRRK-----GFHKVMEGIHKaieLGYNPVKVNCV-VM 221
Cdd:PRK13745  101 QIDncIQTNGTLLTDEWCEFFRENNFLVGVSIDG--PQEFHDEYRKNkmgkpSFVKVMKGINL---LKKHGVEWNAMaVV 175

                         170       180
                  ....*....|....*....|....*....
gi 1284804782 222 RGLNEDELLDFAALTEglPLDVRFIEYMP 250
Cdd:PRK13745  176 NDFNADYPLDFYHFFK--ELDCHYIQFAP 202
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 80-247 8.24e-06

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: 47.49  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYC-MPEEGVPLTPKANLLTTEEILTLARLFVKEG------IDKIRLTG-GEPLIRPDVVDIVAQLQRLEGLrTI 151
Cdd:COG0731    34 CNFDCVYCqRGRTTDLTRERREFDDPEEILEELIEFLRKLpeearePDHITFSGsGEPTLYPNLGELIEEIKKLRGI-KT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 152 GVTTNGINLARllPQLQKAgLSAIN---ISLDTLVPAKFEFIVR---RKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLN 225
Cdd:COG0731   113 ALLTNGSLLHR--PEVREE-LLKADqvyPSLDAADEETFRKINRphpGLSWERIIEGLELFRKLYKGRTVIETMLVKGIN 189

                         170       180
                  ....*....|....*....|....
gi 1284804782 226 --EDELLDFAALTEGlpLDVRFIE 247
Cdd:COG0731   190 dsEEELEAYAELIKR--INPDFVE 211
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 80-189 6.67e-05

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: 42.93  E-value: 6.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYCMPEEGvpLTPKANLLTTEEIL-TLARLFVKEGIDKIRLTGGEPLI-RPDVVDIVAQLQRLEGLRTIgVTTNG 157
Cdd:pfam13353  15 CNHHCKGCFNPET--WDFKYGKPFTEELEdEIIEDLAKPYIQGLTLSGGEPLLnAEALLELVKRVREECPEKDI-WLWTG 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1284804782 158 INLARLLPQLQKAGLSAInislDTLVPAKFEF 189
Cdd:pfam13353  92 YTFEELQSKDQLELLKLI----DVLVDGKFEQ 119
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
 80-228 1.12e-04

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 44.21  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782  80 CNLRCQYC--------MPEEGVPLTPKAnllTTEEILTLARlfvKEGIDKIRLTGGEPLIRPDVVdivaqLQRLEGLRTI 151
Cdd:COG5014    50 CNLRCGFCwswrfrdfPLTIGKFYSPEE---VAERLIEIAR---ERGYRQVRLSGGEPTIGFEHL-----LKVLELFSER 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1284804782 152 GVT----TNGI------NLARLLPQLQKAglsAINISLDTLVPAKFEFI--VRRKGFHKVMEGIHKAIELGYNPVK-VNC 218
Cdd:COG5014   119 GLTfileTNGIligydrELARELASFRNI---VVRVSIKGCTPEEFSMLtgADPEFFELQLRALKNLVDAGLEPGReVYP 195

                         170
                  ....*....|
gi 1284804782 219 VVMRGLNEDE 228
Cdd:COG5014   196 AVMLSFSTEE 205
 
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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