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Conserved domains on  [gi|28574490|ref|NP_788494|]
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molybdenum cofactor synthesis 1, isoform C [Drosophila melanogaster]

Protein Classification

molybdenum cofactor biosynthesis protein 1( domain architecture ID 13324805)

molybdenum cofactor biosynthesis protein 1 catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
moaA super family cl47076
GTP 3',8-cyclase MoaA;
43-367 6.51e-172

GTP 3',8-cyclase MoaA;


The actual alignment was detected with superfamily member PLN02951:

Pssm-ID: 481416 [Multi-domain]  Cd Length: 373  Bit Score: 491.58  E-value: 6.51e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   43 ASVQPLEPEKQVLRKNS---PLTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVPLQPKNKLLTTEEILRLARIFVEQGV 119
Cdd:PLN02951  28 ASSSYAADQVDPEASNPvsdMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  120 RKIRLTGGEPTVRRDIVEIVAQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERV 199
Cdd:PLN02951 108 DKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  200 IAGIDLAVQLGYRP-KVNCVLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPFSGNKWHTERLISYKDTLQIIRQRWPDFK 278
Cdd:PLN02951 188 LESIDTAIELGYNPvKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLK 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  279 ALPNGPNDTSKAYAVPGFKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDeSVSEEQLVDLIGAA 358
Cdd:PLN02951 268 RLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRS-GADDDELREIIGAA 346


                 ....*....
gi 28574490  359 VQRKKKQHA 367
Cdd:PLN02951 347 VKRKKAAHA 355
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
 399-550 2.52e-88

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: 269.23  E-value: 2.52e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 399 SQLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISL 478
Cdd:COG0315   2 SELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLPL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574490 479 SSVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRD 550
Cdd:COG0315  82 TGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 43-367 6.51e-172

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 491.58  E-value: 6.51e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   43 ASVQPLEPEKQVLRKNS---PLTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVPLQPKNKLLTTEEILRLARIFVEQGV 119
Cdd:PLN02951  28 ASSSYAADQVDPEASNPvsdMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  120 RKIRLTGGEPTVRRDIVEIVAQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERV 199
Cdd:PLN02951 108 DKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  200 IAGIDLAVQLGYRP-KVNCVLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPFSGNKWHTERLISYKDTLQIIRQRWPDFK 278
Cdd:PLN02951 188 LESIDTAIELGYNPvKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLK 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  279 ALPNGPNDTSKAYAVPGFKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDeSVSEEQLVDLIGAA 358
Cdd:PLN02951 268 RLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRS-GADDDELREIIGAA 346


                 ....*....
gi 28574490  359 VQRKKKQHA 367
Cdd:PLN02951 347 VKRKKAAHA 355
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 58-366 3.85e-159

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: 457.21  E-value: 3.85e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  58 NSPLTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVPLQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVE 137
Cdd:COG2896   2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 138 IVAQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERVIAGIDLAVQLGYRP-KVN 216
Cdd:COG2896  82 LIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPvKIN 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 217 CVLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPF-SGNKWHTERLISYKDTLQIIRQRWPdFKALPNGPNDTSKAYAVPG 295
Cdd:COG2896 162 AVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPG 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574490 296 FKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDESvSEEQLVDLIGAAVQRKKKQH 366
Cdd:COG2896 241 GGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGA-SDEELAEAIREAIARKPEGH 310
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 61-366 5.43e-136

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: 398.52  E-value: 5.43e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    61 LTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVP-LQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVEIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   140 AQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKG-WERVIAGIDLAVQLGYRP-KVNC 217
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPvKLNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   218 VLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPFS-GNKWHTERLISYKDTLQIIRQRWPDFKALPN-GPNDTSKAYAV-- 293
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPSpRGNGPAPAYRWrl 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574490   294 PGFKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDEsVSEEQLVDLIGAAVQRKKKQH 366
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGG-ASDALLEAIIQAILQKKPEGH 312
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
 399-550 2.52e-88

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: 269.23  E-value: 2.52e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 399 SQLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISL 478
Cdd:COG0315   2 SELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLPL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574490 479 SSVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRD 550
Cdd:COG0315  82 TGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaC PRK09364
cyclic pyranopterin monophosphate synthase MoaC;
399-555 6.88e-87

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 236483  Cd Length: 159  Bit Score: 265.90  E-value: 6.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  399 SQLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISL 478
Cdd:PRK09364   2 SQLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTSDLIPLCHPLML 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574490  479 SSVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKR-DFQREE 555
Cdd:PRK09364  82 TGVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDVRLLEKSGGKSgDFKREA 159
MoaC pfam01967
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ...
 412-547 2.11e-80

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: 248.03  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   412 MVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVKVQATLLKTE 491
Cdd:pfam01967   1 MVDVSDKPVTLRTAVAEGRIRLSPETLELIREGTVKKGDVLAVARIAGIMAAKKTSDLIPLCHPLPLTGVDVEFELDEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28574490   492 QSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGG 547
Cdd:pfam01967  81 DGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDIRLLEKSGG 136
MoaC_PE cd01420
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ...
 412-551 3.44e-80

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: 247.85  E-value: 3.44e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 412 MVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVKVQATLLKTE 491
Cdd:cd01420   1 MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEET 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 492 QSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRDF 551
Cdd:cd01420  81 SGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD 140
moaC TIGR00581
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ...
 401-549 2.81e-60

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: 196.50  E-value: 2.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   401 LTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSS 480
Cdd:TIGR00581   1 LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLIPLCHPLPLSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574490   481 VKVQATLLktEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKR 549
Cdd:TIGR00581  81 VEVELTVR--EDRVEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLLEKSGGKS 147
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
 240-367 1.34e-54

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: 180.49  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   240 VDVRFIEYMPF-SGNKWHTERLISYKDTLQIIRQRWPdFKALPNGPNDTSKAYAVPGFKGQVGFITSMTEHFCGTCNRLR 318
Cdd:pfam06463   1 IDLRFIELMPVgEGNGWRRKKFVSLDEILERIEARFP-LLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 28574490   319 LTADGNIKVCLFGNKEFSLRDAMRDEsVSEEQLVDLIGAAVQRKKKQHA 367
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSG-DDDEELREAIREALARKPPRHS 127
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
 306-368 1.69e-30

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: 113.41  E-value: 1.69e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574490 306 MTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRdESVSEEQLVDLIGAAVQRKKKQHAD 368
Cdd:cd21117   1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALR-SGASDEELREAIRAAVQRKPERHSL 62
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 70-270 1.20e-09

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: 58.57  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490     70 TYLRISLTERCNLRCDYCMPAeGVPLQPKNKLLttEEILRLARIFVEQGVRKIRLT-----GGEPTVR-----RDIVEIV 139
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFP-SLRGKLRSRYL--EALVREIELLAEKGEKEGLVGtvfigGGTPTLLspeqlEELLEAI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    140 AQMKALPELEQIGITTN-GLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERVIAGIDLAVQLGyRPKVNCV 218
Cdd:smart00729  78 REILGLAKDVEITIETRpDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG-PIKVSTD 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    219 LMRDF---NEDEICDFVEFTRNRPVD-VRFIEYMPFSG----NKWHTERLISYKDTLQII 270
Cdd:smart00729 157 LIVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 71-220 7.82e-04

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: 41.87  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   71 YLRISLTERCNLRCDYCMP-------AEGVPLQPKNKLLTTEEILRLARIFVEQ------GVRKIRLTGGEPTVRRDIVE 137
Cdd:NF033640 111 YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYK 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  138 IvaqMKALPELEQ-----IGITTNGLVLTRLLLPLqragLD--------NLNISLDTLKrDRFEKItrRKG--WERVIAG 202
Cdd:NF033640 191 L---LEKLVEKGRaknieLRYNTNLTVLPDKLKDL----LDlwkkfksvSISASIDGVG-ERNEYI--RYGskWDEIEKN 260

                        170
                 ....*....|....*...
gi 28574490  203 IDLAVQLGyrPKVNCVLM 220
Cdd:NF033640 261 LKKLKEEC--PNVELRIN 276
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 43-367 6.51e-172

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 491.58  E-value: 6.51e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   43 ASVQPLEPEKQVLRKNS---PLTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVPLQPKNKLLTTEEILRLARIFVEQGV 119
Cdd:PLN02951  28 ASSSYAADQVDPEASNPvsdMLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  120 RKIRLTGGEPTVRRDIVEIVAQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERV 199
Cdd:PLN02951 108 DKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  200 IAGIDLAVQLGYRP-KVNCVLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPFSGNKWHTERLISYKDTLQIIRQRWPDFK 278
Cdd:PLN02951 188 LESIDTAIELGYNPvKVNCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLK 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  279 ALPNGPNDTSKAYAVPGFKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDeSVSEEQLVDLIGAA 358
Cdd:PLN02951 268 RLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRS-GADDDELREIIGAA 346


                 ....*....
gi 28574490  359 VQRKKKQHA 367
Cdd:PLN02951 347 VKRKKAAHA 355
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 58-366 3.85e-159

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: 457.21  E-value: 3.85e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  58 NSPLTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVPLQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVE 137
Cdd:COG2896   2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 138 IVAQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERVIAGIDLAVQLGYRP-KVN 216
Cdd:COG2896  82 LIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPvKIN 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 217 CVLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPF-SGNKWHTERLISYKDTLQIIRQRWPdFKALPNGPNDTSKAYAVPG 295
Cdd:COG2896 162 AVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPG 240

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574490 296 FKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDESvSEEQLVDLIGAAVQRKKKQH 366
Cdd:COG2896 241 GGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGA-SDEELAEAIREAIARKPEGH 310
moaA PRK00164
GTP 3',8-cyclase MoaA;
59-366 1.81e-136

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 399.52  E-value: 1.81e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   59 SPLTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVPLQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVEI 138
Cdd:PRK00164   6 SQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDLEDI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  139 VAQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERVIAGIDLAVQLGYRP-KVNC 217
Cdd:PRK00164  86 IAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPvKVNA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  218 VLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPFS-GNKWHTERLISYKDTLQIIRQRWPDFKALP--NGPndtSKAYAVP 294
Cdd:PRK00164 166 VLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGeGNEWFRKHHLSGAEIRARLAERGWTLQPRArsGGP---AQYFRHP 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574490  295 GFKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDESvSEEQLVDLIGAAVQRKKKQH 366
Cdd:PRK00164 243 DYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGA-DDEELAAAIREALQNKPEGH 313
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
 61-366 5.43e-136

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: 398.52  E-value: 5.43e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    61 LTDSFGRHHTYLRISLTERCNLRCDYCMPAEGVP-LQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVEIV 139
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLdFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   140 AQMKALPELEQIGITTNGLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKG-WERVIAGIDLAVQLGYRP-KVNC 217
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGrLEQVLAGIDAALAAGLEPvKLNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   218 VLMRDFNEDEICDFVEFTRNRPVDVRFIEYMPFS-GNKWHTERLISYKDTLQIIRQRWPDFKALPN-GPNDTSKAYAV-- 293
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPSpRGNGPAPAYRWrl 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574490   294 PGFKGQVGFITSMTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRDEsVSEEQLVDLIGAAVQRKKKQH 366
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGG-ASDALLEAIIQAILQKKPEGH 312
MoaC COG0315
Molybdenum cofactor biosynthesis enzyme MoaC [Coenzyme transport and metabolism]; Molybdenum ...
 399-550 2.52e-88

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: 269.23  E-value: 2.52e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 399 SQLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISL 478
Cdd:COG0315   2 SELTHLDEQGRARMVDVSDKAVTARTAVAEGRVRMSPETLALIREGGVKKGDVLAVARIAGIMAAKRTSELIPLCHPLPL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574490 479 SSVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRD 550
Cdd:COG0315  82 TGVDVDFELDDDLSGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIEDIRLLEKSGGKSG 153
moaC PRK09364
cyclic pyranopterin monophosphate synthase MoaC;
399-555 6.88e-87

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 236483  Cd Length: 159  Bit Score: 265.90  E-value: 6.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  399 SQLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISL 478
Cdd:PRK09364   2 SQLTHINEQGRAKMVDVSDKAETVRTAVAEGSVRMSPETLALIRDGTAKKGDVLATARIAGIMAAKRTSDLIPLCHPLML 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28574490  479 SSVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKR-DFQREE 555
Cdd:PRK09364  82 TGVDVDFEWDPELPGVRITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDVRLLEKSGGKSgDFKREA 159
MoaC pfam01967
MoaC family; Members of this family are involved in molybdenum cofactor biosynthesis. However ...
 412-547 2.11e-80

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: 248.03  E-value: 2.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   412 MVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVKVQATLLKTE 491
Cdd:pfam01967   1 MVDVSDKPVTLRTAVAEGRIRLSPETLELIREGTVKKGDVLAVARIAGIMAAKKTSDLIPLCHPLPLTGVDVEFELDEEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 28574490   492 QSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGG 547
Cdd:pfam01967  81 DGVEITATVKTTGKTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGDIRLLEKSGG 136
MoaC_PE cd01420
MoaC family, prokaryotic and eukaryotic. Members of this family are involved in molybdenum ...
 412-551 3.44e-80

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: 247.85  E-value: 3.44e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 412 MVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVKVQATLLKTE 491
Cdd:cd01420   1 MVDVSDKAVTERTAVAEGRVRMSPETLDLITEGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEET 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 492 QSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRDF 551
Cdd:cd01420  81 SGVRIEATVRTTGRTGVEMEALTAVSVAALTIYDMCKAVDKGMVIGGIRLLEKSGGKSGD 140
MoaC cd00528
MoaC family. Members of this family are involved in molybdenum cofactor (Moco) biosynthesis, ...
 412-547 1.73e-75

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: 235.49  E-value: 1.73e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 412 MVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVKVQATLLKTE 491
Cdd:cd00528   1 MVDVSDKAVTERTAVAEGRVRLSPETLDLIREGQLPKGDVLAVARIAGIMAAKRTSELIPLCHPLPLTGVDVDFELDEDT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 28574490 492 QSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGG 547
Cdd:cd00528  81 SGVRIRATVRTTGKTGVEMEALTAVSVAALTIYDMCKAVDKDMVIENIRLLEKSGG 136
moaC PRK03604
bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional
 402-558 4.02e-65

bifunctional molybdenum cofactor biosynthesis protein MoaC/MogA; Provisional


Pssm-ID: 235138 [Multi-domain]  Cd Length: 312  Bit Score: 214.81  E-value: 4.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  402 THVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSV 481
Cdd:PRK03604   1 THLDEEGRVRMVDVSGKPGTLRTARASGIIVTSPETIELLRQGDLPKGDVLTTAKIAGIQAAKRTSELIPLCHPLPLSWV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574490  482 KVQATLlkTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRDFQREEPQN 558
Cdd:PRK03604  81 DVEFEI--EDDRIRIEATVKTIGKTGVEMEALTAVSVAALTIYDMLKPVDKALEIGGIRLLEKTGGKSGHKRRFRPR 155
moaC TIGR00581
molybdenum cofactor biosynthesis protein MoaC; MoaC catalyzes an early step in molybdenum ...
 401-549 2.81e-60

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: 196.50  E-value: 2.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   401 LTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSS 480
Cdd:TIGR00581   1 LTHIDEQGAARMVDISAKAETVREAVASGFVRMKPETVAMISEGRVPKGDVLATARVAGIMAAKRTGDLIPLCHPLPLSK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574490   481 VKVQATLLktEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKR 549
Cdd:TIGR00581  81 VEVELTVR--EDRVEITATVRTTGRTGVEMEALTAVSVAALTVYDMCKAVDKDMVIGPVRLLEKSGGKS 147
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
 240-367 1.34e-54

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: 180.49  E-value: 1.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   240 VDVRFIEYMPF-SGNKWHTERLISYKDTLQIIRQRWPdFKALPNGPNDTSKAYAVPGFKGQVGFITSMTEHFCGTCNRLR 318
Cdd:pfam06463   1 IDLRFIELMPVgEGNGWRRKKFVSLDEILERIEARFP-LLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 28574490   319 LTADGNIKVCLFGNKEFSLRDAMRDEsVSEEQLVDLIGAAVQRKKKQHA 367
Cdd:pfam06463  80 LTADGKLKTCLFAEDGIDLRDALRSG-DDDEELREAIREALARKPPRHS 127
PRK14499 PRK14499
cyclic pyranopterin monophosphate synthase MoaC/MOSC-domain-containing protein;
400-548 4.13e-53

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


Pssm-ID: 237733 [Multi-domain]  Cd Length: 308  Bit Score: 183.14  E-value: 4.13e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  400 QLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLS 479
Cdd:PRK14499   2 EFTHFNKDGLPQMVDVSSKEPTFRVAVASGRIYVGKEVIEAIEERLLPKGDVFSVAKIAAIMAAKKTSELIPLCHNIFLS 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574490  480 SVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGK 548
Cdd:PRK14499  82 GVDVSYEINREEGYIEAVSEVKTEAKTGAEMEAITAVSIFLETIYDMCKAVKKDMVITDVRLIEKSGGK 150
PLN02375 PLN02375
molybderin biosynthesis protein CNX3
 395-551 1.16e-49

molybderin biosynthesis protein CNX3


Pssm-ID: 178003 [Multi-domain]  Cd Length: 270  Bit Score: 172.64  E-value: 1.16e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  395 ARNYSQLTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCH 474
Cdd:PLN02375 110 ASDMSKLTHVGIAGEAQMVDVSSKDNSKRTALACCKVILGKRVFDLVLANQMGKGDVLGVAKIAGINGAKQTSSLIPLCH 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28574490  475 NISLSSVKVQATLLKTEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRDF 551
Cdd:PLN02375 190 NIALTHVRVDLRLNPEDFSVDIEGEASCTGKTGVEMEAMTAVSVAGLTVYDMCKAASKDISITDVRLERKTGGKSGS 266
PRK12343 PRK12343
cyclic pyranopterin monophosphate synthase MoaC;
403-544 1.12e-45

cyclic pyranopterin monophosphate synthase MoaC;


Pssm-ID: 237067  Cd Length: 151  Bit Score: 157.76  E-value: 1.12e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  403 HVDGQGkAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVK 482
Cdd:PRK12343   1 HVDEDG-VKMVDVSEKEDVLRIAVAEGFIKLKPETIEAIREGEVEKGNVLATARVAGILAVKKTPELIPMCHPIPITGVD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28574490  483 VQATLLktEQSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHD-------ICITNVRLLSK 544
Cdd:PRK12343  80 VDFEVG--EDGIEARVTVKTTYKTGVEMEALTGVSVALLTIWDMVKAAEKDedgqypeTRIENIRVVEK 146
MoaC_A cd01419
MoaC family, archaeal. Members of this family are involved in molybdenum cofactor (Moco) ...
 412-544 2.20e-42

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: 148.66  E-value: 2.20e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 412 MVDVGAKPSTTRLARAEATVQVGEKLTQLIADNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISLSSVKVQATLLktE 491
Cdd:cd01419   1 MVDISSKEDVAREAVASGFIKLKEETIKAIREGKVEKGNVIATARIAGILAVKKTPELIPMCHPIPITGVDVDFEVE--E 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 492 QSVRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHD-------ICITNVRLLSK 544
Cdd:cd01419  79 DGIEVRCTVKTTYKTGVEMEALTGVSVALLTIWDMVKSAEKDedgqypeTRIENVRVVEK 138
PRK14500 PRK14500
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MoaC/MobA; ...
 401-561 7.79e-40

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


Pssm-ID: 237734 [Multi-domain]  Cd Length: 346  Bit Score: 148.12  E-value: 7.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  401 LTHVDGQGKAQMVDVGAKPSTTRLARAEATVQVGEKLTQLIA--DNQVAKGDVLTVAQIAGIMGAKRTAELIPLCHNISL 478
Cdd:PRK14500   2 FTHLNENQQPRMVDISQKVVSDRRAVAQAIVQLPPAIKDYVTgqDIFLKKGPVIQTAIIAGTMAVKRTADLIPFCHTLPI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  479 SSVKVQATLLKTEQS--VRLEATVRCSGQTGVEMEALTAVSVAALTVYDMCKAVSHDICITNVRLLSKSGGKRDFQrEEP 556
Cdd:PRK14500  82 HGCKFDINIVYQKRDleIFLQCAVKTNYKTGVEMEALCGVAVAALTIYDMCKSISPHIIIKETRLIEKSGGKADLS-QTP 160


                 ....*
gi 28574490  557 QNGIV 561
Cdd:PRK14500 161 LYGLV 165
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 71-229 2.38e-31

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: 119.24  E-value: 2.38e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  71 YLRISLTERCNLRCDYCMPAEGVPLQPKnklLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVEIVAQMKALPelEQ 150
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPGE---LSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELG--IR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 151 IGITTNGLVLTRLLLPL-QRAGLDNLNISLDTLKRDRFEKITRRKG-WERVIAGIDLAVQLGYRPKVNCVLMRDFNEDEI 228
Cdd:COG0535  76 VNLSTNGTLLTEELAERlAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGIPVGINTVYPCPFLPELS 155


                .
gi 28574490 229 C 229
Cdd:COG0535 156 L 156
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
 306-368 1.69e-30

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: 113.41  E-value: 1.69e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28574490 306 MTEHFCGTCNRLRLTADGNIKVCLFGNKEFSLRDAMRdESVSEEQLVDLIGAAVQRKKKQHAD 368
Cdd:cd21117   1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALR-SGASDEELREAIRAAVQRKPERHSL 62
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 76-231 4.97e-27

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: 106.84  E-value: 4.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    76 LTERCNLRCDYCMPAEGvPLQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVEIVAQMKALPELEQ--IGI 153
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSI-RARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGirITL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   154 TTNGLVLTRLLLPL-QRAGLDNLNISLDTLkRDRFEKITRRKG-WERVIAGIDLAVQLGYRP-KVNCVLMRDFNEDEICD 230
Cdd:pfam04055  80 ETNGTLLDEELLELlKEAGLDRVSIGLESG-DDEVLKLINRGHtFEEVLEALELLREAGIPVvTDNIVGLPGETDEDLEE 158


                  .
gi 28574490   231 F 231
Cdd:pfam04055 159 T 159
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 74-249 1.44e-18

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: 84.31  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  74 ISLTERCNLRCDYCmpaeGVPLQPKNKLLTTEEILRLARIFVEQ---GVRKIRLTGGEPTVRRDIVEIVAQMKALPELEQ 150
Cdd:cd01335   1 LELTRGCNLNCGFC----SNPASKGRGPESPPEIEEILDIVLEAkerGVEVVILTGGEPLLYPELAELLRRLKKELPGFE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 151 IGITTNGLVLTRLLLPL-QRAGLDNLNISLDTLKRDRFEKITRRKG-WERVIAGIDLAVQLGYRPKV-----NCVLMRDF 223
Cdd:cd01335  77 ISIETNGTLLTEELLKElKELGLDGVGVSLDSGDEEVADKIRGSGEsFKERLEALKELREAGLGLSTtllvgLGDEDEED 156

                       170       180
                ....*....|....*....|....*.
gi 28574490 224 NEDEICDFVEFTRNRPVDVRFIEYMP 249
Cdd:cd01335 157 DLEELELLAEFRSPDRVSLFRLLPEE 182
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 74-337 2.59e-11

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 65.39  E-value: 2.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  74 ISLTERCNLRCDYCMpaEGVPLQPKNKLLTTEEILRLARIFVE--QGVRKIRLT--GGEPTVRRD-IVEIVAQMKALPEL 148
Cdd:COG0641   5 LKPTSRCNLRCSYCY--YSEGDEGSRRRMSEETAEKAIDFLIEssGPGKELTITffGGEPLLNFDfIKEIVEYARKYAKK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 149 EQ---IGITTNGLVltrlllplqragLD------------NLNISLDTLKR--DRFEKITRRKG-WERVIAGIDLAVQLG 210
Cdd:COG0641  83 GKkirFSIQTNGTL------------LDdewidflkengfSVGISLDGPKEihDRNRVTKNGKGsFDRVMRNIKLLKEHG 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 211 YRPKVNCVLMRDfNEDEICDFVEFTRNRPVD-VRFIEYMPFSGNKWhterLISYKDTLQIIRQRWPDFKALPNGPndtsk 289
Cdd:COG0641 151 VEVNIRCTVTRE-NLDDPEELYDFLKELGFRsIQFNPVVEEGEADY----SLTPEDYGEFLIELFDEWLERDGGK----- 220

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 28574490 290 aYAVPGFKGQVGFITSMTEHFC-GTCNR-LRLTADGNIKVC--LFGNKEFSL 337
Cdd:COG0641 221 -IFVREFDILLAGLLPPCSSPCvGAGGNyLVVDPDGDIYPCdeFVGDPEFRL 271
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 70-270 1.20e-09

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: 58.57  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490     70 TYLRISLTERCNLRCDYCMPAeGVPLQPKNKLLttEEILRLARIFVEQGVRKIRLT-----GGEPTVR-----RDIVEIV 139
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFP-SLRGKLRSRYL--EALVREIELLAEKGEKEGLVGtvfigGGTPTLLspeqlEELLEAI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    140 AQMKALPELEQIGITTN-GLVLTRLLLPLQRAGLDNLNISLDTLKRDRFEKITRRKGWERVIAGIDLAVQLGyRPKVNCV 218
Cdd:smart00729  78 REILGLAKDVEITIETRpDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG-PIKVSTD 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    219 LMRDF---NEDEICDFVEFTRNRPVD-VRFIEYMPFSG----NKWHTERLISYKDTLQII 270
Cdd:smart00729 157 LIVGLpgeTEEDFEETLKLLKELGPDrVSIFPLSPRPGtplaKMYKRLKPPTKEERAELL 216
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
 80-233 9.80e-08

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 53.45  E-value: 9.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  80 CNLRCDYC---MPAEGVPlqPKNKLLTTEEIL-RLARIFVEQGVRKIRLTGGEPTVRRD----IVEIVAQMKALPELEqi 151
Cdd:COG5014  50 CNLRCGFCwswRFRDFPL--TIGKFYSPEEVAeRLIEIARERGYRQVRLSGGEPTIGFEhllkVLELFSERGLTFILE-- 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 152 gitTNGLVLTRLLLPLQR-AGLDNL--NISLDTLKRDRFEKIT--RRKGWERVIAGIDLAVQLGYRP--KVNCVLMRDF- 223
Cdd:COG5014 126 ---TNGILIGYDRELARElASFRNIvvRVSIKGCTPEEFSMLTgaDPEFFELQLRALKNLVDAGLEPgrEVYPAVMLSFs 202

                       170
                ....*....|
gi 28574490 224 NEDEICDFVE 233
Cdd:COG5014 203 TEESIRKLIE 212
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
 80-236 4.51e-07

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 52.22  E-value: 4.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  80 CNLRCDYCMPAEGvplqPKNK------------LLttEEILRLARiFVEQGVRKIRLTGGEPTVRRDIVEIVAQMKALPE 147
Cdd:COG2100  46 CNLNCIFCSVDAG----PHSRtrqaeyivdpeyLV--EWFEKVAR-FKGKGVEAHIDGVGEPLLYPYIVELVKGLKEIKG 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 148 LEQIGITTNGLVLTRLLLPL-QRAGLDNLNISLDTLKRDRFEKITRRKGW--ERVI---------AGIDLAVQlgyrPkv 215
Cdd:COG2100 119 VKVVSMQTNGTLLSEKLIDElEEAGLDRINLSIDTLDPEKAKKLAGTKWYdvEKVLelaeyiareTKIDLLIA----P-- 192

                       170       180
                ....*....|....*....|.
gi 28574490 216 ncVLMRDFNEDEICDFVEFTR 236
Cdd:COG2100 193 --VWLPGINDEDIPKIIEWAL 211
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
 76-221 6.62e-06

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: 48.30  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    76 LTERCNLRCDYCMPAegvPLQPKNKLLTTEEILRLARIFVEQ----GVRKIRLTGGEPTVRRDIVEIVAQMKAlpELEQI 151
Cdd:TIGR04251  10 LTEGCNLKCRHCWID---PKYQGEGEQHPSLDPSLFRSIIRQaiplGLTSVKLTGGEPLLHPAIGEILECIGE--NNLQL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28574490   152 GITTNGLVLTRLLLPLQRA-GLDNLNISLDTLKRDRFEKITRRKG-WERVIAGIDLAVQLGYRPKVNCVLMR 221
Cdd:TIGR04251  85 SVETNGLLCTPQTARDLAScETPFVSVSLDGVDAATHDWMRGVKGaFDKAVRGIHNLVEAGIHPQIIMTVTR 156
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 74-139 7.64e-06

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: 48.31  E-value: 7.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574490    74 ISLTERCNLRCDYCMPAEGVPLQPKNklLTTEEILRLARIFVEQGVRKIRLTGGEPTVRRDIVEIV 139
Cdd:TIGR04250   7 IDITGRCNLRCRYCSHFSSAAETPTD--LETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREII 70
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 80-250 8.54e-06

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 47.49  E-value: 8.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  80 CNLRCDYCMPAEGVPLQPKN--KLLTTEEILRLA--RIFVEQGVRKIRLTGGEPTVrrdiveivaQMKALPEL----EQI 151
Cdd:COG1180  31 CNLRCPYCHNPEISQGRPDAagRELSPEELVEEAlkDRGFLDSCGGVTFSGGEPTL---------QPEFLLDLaklaKEL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 152 GITTnglvltrlllplqraGLD-NLNISLDTLKR-----------------DRFEKITRRKgWERVIAGIDLAVQLGYRP 213
Cdd:COG1180 102 GLHT---------------ALDtNGYIPEEALEEllpyldavnidlkafddEFYRKLTGVS-LEPVLENLELLAESGVHV 165

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 28574490 214 KVNCVLMRDFN--EDEICDFVEFTRNRPvDVRFIEYMPF 250
Cdd:COG1180 166 EIRTLVIPGLNdsEEELEAIARFIAELG-DVIPVHLLPF 203
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 79-234 1.80e-05

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: 46.34  E-value: 1.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  79 RCNLRCDYC-------MPAEGVPLQPknklltTEEILRLARIFVEQGVRKIR------LTG-GEPTVRRDIVEIVAQMKA 144
Cdd:COG0731  33 TCNFDCVYCqrgrttdLTRERREFDD------PEEILEELIEFLRKLPEEARepdhitFSGsGEPTLYPNLGELIEEIKK 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490 145 LPELeQIGITTNGLVLTRLLLplqRAGL---DNLNISLDTLKRDRFEKITR---RKGWERVIAGIDLAVQLGYRPKVncV 218
Cdd:COG0731 107 LRGI-KTALLTNGSLLHRPEV---REELlkaDQVYPSLDAADEETFRKINRphpGLSWERIIEGLELFRKLYKGRTV--I 180

                       170       180
                ....*....|....*....|.
gi 28574490 219 ---LMRDFN--EDEICDFVEF 234
Cdd:COG0731 181 etmLVKGINdsEEELEAYAEL 201
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
 80-157 2.66e-05

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: 45.51  E-value: 2.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  80 CNLRCDYC------MPAEGvplqpknKLLTTEEILRLARifvEQGVRKIRLTGGEPTVRRDIVEIVAQMKALP---ELEq 150
Cdd:COG0602  30 CNLRCSWCdtkyawDGEGG-------KRMSAEEILEEVA---ALGARHVVITGGEPLLQDDLAELLEALKDAGyevALE- 98


                ....*..
gi 28574490 151 igitTNG 157
Cdd:COG0602  99 ----TNG 101
PRK13745 PRK13745
anaerobic sulfatase-maturation protein;
80-269 2.52e-04

anaerobic sulfatase-maturation protein;


Pssm-ID: 237489 [Multi-domain]  Cd Length: 412  Bit Score: 43.70  E-value: 2.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   80 CNLRCDYCMPAEGVPLQPKNK--LLTTEEILRLARIFVE-QGVRKIRLT--GGEPTVRrdivEIVAQMKALpELE----- 149
Cdd:PRK13745  24 CNLACDYCYYLEKSKLYQENPkhVMSDELLEKFIKEYINsQTMPQVLFTwhGGETLMR----PLSFYKKAL-ELQkkyar 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  150 --QIG--ITTNGLVLTRLLLPLQRAGLDNLNISLDTLKR--DRFEKITRRK-GWERVIAGIDLAVQLGYRPKVNCVLmRD 222
Cdd:PRK13745  99 grQIDncIQTNGTLLTDEWCEFFRENNFLVGVSIDGPQEfhDEYRKNKMGKpSFVKVMKGINLLKKHGVEWNAMAVV-ND 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 28574490  223 FNEDEICDFVEFTRNrpVDVRFIEYMPFsgnkwhTERLISYKDTLQI 269
Cdd:PRK13745 178 FNADYPLDFYHFFKE--LDCHYIQFAPI------VERIVSHQDGRHL 216
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 80-157 3.42e-04

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 41.97  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    80 CNLRCDYC-----MPAEGVPLQPKNKLLtteEILRLARIFVEQGVrkirLTGGEPTVRRDIVEIVAQMKALPelEQIGIT 154
Cdd:TIGR02495  26 CNLKCPYChnpllIPRRGSGEIEVEELL---EFLRRRRGLLDGVV----ITGGEPTLQAGLPDFLREVRELG--FEVKLD 96


                  ...
gi 28574490   155 TNG 157
Cdd:TIGR02495  97 TNG 99
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
 71-220 7.82e-04

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: 41.87  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490   71 YLRISLTERCNLRCDYCMP-------AEGVPLQPKNKLLTTEEILRLARIFVEQ------GVRKIRLTGGEPTVRRDIVE 137
Cdd:NF033640 111 YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISWFEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYK 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  138 IvaqMKALPELEQ-----IGITTNGLVLTRLLLPLqragLD--------NLNISLDTLKrDRFEKItrRKG--WERVIAG 202
Cdd:NF033640 191 L---LEKLVEKGRaknieLRYNTNLTVLPDKLKDL----LDlwkkfksvSISASIDGVG-ERNEYI--RYGskWDEIEKN 260

                        170
                 ....*....|....*...
gi 28574490  203 IDLAVQLGyrPKVNCVLM 220
Cdd:NF033640 261 LKKLKEEC--PNVELRIN 276
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
 65-173 8.42e-04

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 41.65  E-value: 8.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490  65 FGRHHTYLR---ISLTERCNLRCDYC---MPAEgvplQPKNKLLTTEEILRLARIFVEQGVRKIRLTGGE-PTVRRD-IV 136
Cdd:COG1060  43 FGNTVTFVVnrpINLTNVCVNGCKFCafsRDNG----DIDRYTLSPEEILEEAEEAKALGATEILLVGGEhPDLPLEyYL 118

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 28574490 137 EIVAQMK-ALPELE---------QIGITTNGLVLTRLLLPLQRAGLD 173
Cdd:COG1060 119 DLLRAIKeRFPNIHihalspeeiAHLARASGLSVEEVLERLKEAGLD 165
rSAM_AF0577 TIGR04084
putative peptide-modifying radical SAM enzyme, AF0577 family; This radical SAM family contains ...
 76-157 6.57e-03

putative peptide-modifying radical SAM enzyme, AF0577 family; This radical SAM family contains a C-terminal region motif CXXCX5CX3C that is found in PqqE and other radical SAM enzymes that act on peptide substrates. Members of this family are found primarily in the Archaea, but also several eukaryotes (Trichomonas vaginalis G3, Entamoeba dispar SAW760, Giardia intestinalis ATCC 50581, etc.). The function is unknown.


Pssm-ID: 274967 [Multi-domain]  Cd Length: 347  Bit Score: 38.96  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574490    76 LTERCNLRCDYC---MPAEGVPLQPK---NKLltteeilrlaRIFVEQGVRK-IRLTGGEPTVR-RDIVEIVAQMKAlpe 147
Cdd:TIGR04084   3 TTGKCNLRCDYCggsFPEKVVPWRIKydiNKL----------KNLIEKDKDAtVIFYGGEPLLNpRFIMQVMDNVRA--- 69

                          90
                  ....*....|
gi 28574490   148 lEQIGITTNG 157
Cdd:TIGR04084  70 -KRFGIQTNG 78
 
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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