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Conserved domains on  [gi|1063705476|ref|NP_001324733|]
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cofactor of nitrate reductase and xanthine dehydrogenase 2 [Arabidopsis thaliana]

Protein Classification

PLN02951 family protein( domain architecture ID 11477312)

PLN02951 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
5-341 0e+00

Molybderin biosynthesis protein CNX2


:

Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 664.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476   5 FSKITDCHLGFKNSNFLLvgSEVGSgsvtrtittttSERLFSSSYAAHQVDQIKDNPVSDMLIDKFGRLHTYLRISLTER 84
Cdd:PLN02951    1 LSKLADLRLGFRSSSFQL--QEPGS-----------SIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTER 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKNLAITTNGIT 164
Cdd:PLN02951   68 CNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 165 LAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVNCVIMRGLNDDEICDFVELTRDK 244
Cdd:PLN02951  148 LSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 245 PINVRFIEFMPFDGNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHPTETAKNFTIDGHCGSVSFITSMTEHFCAGCNRLR 324
Cdd:PLN02951  228 PINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLR 307
                         330
                  ....*....|....*..
gi 1063705476 325 LLADGNFKVCLFGPSEV 341
Cdd:PLN02951  308 LLADGNLKVCLFGPSEV 324
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
5-341 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 664.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476   5 FSKITDCHLGFKNSNFLLvgSEVGSgsvtrtittttSERLFSSSYAAHQVDQIKDNPVSDMLIDKFGRLHTYLRISLTER 84
Cdd:PLN02951    1 LSKLADLRLGFRSSSFQL--QEPGS-----------SIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTER 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKNLAITTNGIT 164
Cdd:PLN02951   68 CNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 165 LAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVNCVIMRGLNDDEICDFVELTRDK 244
Cdd:PLN02951  148 LSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 245 PINVRFIEFMPFDGNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHPTETAKNFTIDGHCGSVSFITSMTEHFCAGCNRLR 324
Cdd:PLN02951  228 PINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLR 307
                         330
                  ....*....|....*..
gi 1063705476 325 LLADGNFKVCLFGPSEV 341
Cdd:PLN02951  308 LLADGNLKVCLFGPSEV 324
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
63-341 1.34e-148

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: 421.78  E-value: 1.34e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  63 SDMLIDKFGRLHTYLRISLTERCNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEE 142
Cdd:COG2896     2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 143 ICLQLSSLKGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVN 222
Cdd:COG2896    82 LIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKIN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 223 CVIMRGLNDDEICDFVELTRDKPINVRFIEFMPF-DGNVWNVKKLVPYAEVMDKVVKRFPsIKRMQDHPTETAKNFTIDG 301
Cdd:COG2896   162 AVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1063705476 302 HCGSVSFITSMTEHFCAGCNRLRLLADGNFKVCLFGPSEV 341
Cdd:COG2896   241 GGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEV 280
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
66-341 3.01e-121

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: 352.68  E-value: 3.01e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  66 LIDKFGRLHTYLRISLTERCNLRCQYCMPSEGV-ELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEIC 144
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGlDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 145 LQLSSLKGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGH-DRVMKSIDTAIELGYNPVKVNC 223
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRlEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 224 VIMRGLNDDEICDFVELTRDKPINVRFIEFMPFD-GNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHP---TETAKNFTI 299
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPSPRgngPAPAYRWRL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1063705476 300 DGHCGSVSFITSMTEHFCAGCNRLRLLADGNFKVCLFGPSEV 341
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGV 282
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
246-341 6.58e-38

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: 131.96  E-value: 6.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 246 INVRFIEFMPFD-GNVWNVKKLVPYAEVMDKVVKRFPSIKRmQDHPTETAKNFTIDGHCGSVSFITSMTEHFCAGCNRLR 324
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFPLLPA-RKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90
                  ....*....|....*..
gi 1063705476 325 LLADGNFKVCLFGPSEV 341
Cdd:pfam06463  80 LTADGKLKTCLFAEDGI 96
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-256 1.98e-17

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: 79.68  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  79 ISLTERCNLRCQYCMPSEGVELTPKpQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKNLAI 158
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPE-SPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 159 TTNGITLAKK-LPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRvmKSIDTAIELGYNPVKVNCVIMRGLNDDEICDF 237
Cdd:cd01335    80 ETNGTLLTEElLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKELREAGLGLSTTLLVGLGDEDEEDD 157
                         170       180
                  ....*....|....*....|.
gi 1063705476 238 VELTRDKP--INVRFIEFMPF 256
Cdd:cd01335   158 LEELELLAefRSPDRVSLFRL 178
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
75-280 2.55e-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: 65.50  E-value: 2.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476   75 TYLRISLTERCNLRCQYCMPSegvELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLT-----GGEPTV--RKDIEEICLQL 147
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFP---SLRGKLRSRYLEALVREIELLAEKGEKEGLVGtvfigGGTPTLlsPEQLEELLEAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  148 SSLKGLKN---LAITTNGITL-AKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGynPVKVNC 223
Cdd:smart00729  78 REILGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVST 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705476  224 VIMRGL---NDDEICDFVELTRD-KPINVRFIEFMPFDGNVWNVKKLVPYAEVMDKVVKRF 280
Cdd:smart00729 156 DLIVGLpgeTEEDFEETLKLLKElGPDRVSIFPLSPRPGTPLAKMYKRLKPPTKEERAELL 216
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
41-280 5.04e-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: 60.36  E-value: 5.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  41 SERLFSSSYAAHQVDQIKDNPVSDMLIDKFGRlhtYLRISLTERCNLRCQYCMP-------SEGVELTPKPQLLSQSEIV 113
Cdd:NF033640   79 SLRQESNERWAKHIEDAIKSTDEDGSDDVNPR---YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISW 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 114 RLAGLFVSA------GVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKN--LAITTNGITLAKK-------LPRLKECgld 178
Cdd:NF033640  156 FEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYKLLEKLVEKGRAKNieLRYNTNLTVLPDKlkdlldlWKKFKSV--- 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 179 SLNISLDTlVPAKFEFLtrRKGH--DRVMKSIDTAIELGYN-PVKVNCVIMRgLNDDEICDFVELTRDKPINVRFIEF-M 254
Cdd:NF033640  233 SISASIDG-VGERNEYI--RYGSkwDEIEKNLKKLKEECPNvELRINPTVSA-LNVLHLPELLDWLLELGLGPIDIYLnI 308
                         250       260
                  ....*....|....*....|....*.
gi 1063705476 255 PFDGNVWNVKKLvPYaEVMDKVVKRF 280
Cdd:NF033640  309 LRDPEYLSIKNL-PK-EIKQKVIEKL 332
 
Name Accession Description Interval E-value
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
5-341 0e+00

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 664.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476   5 FSKITDCHLGFKNSNFLLvgSEVGSgsvtrtittttSERLFSSSYAAHQVDQIKDNPVSDMLIDKFGRLHTYLRISLTER 84
Cdd:PLN02951    1 LSKLADLRLGFRSSSFQL--QEPGS-----------SIFSASSSYAADQVDPEASNPVSDMLVDSFGRRHNYLRISLTER 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKNLAITTNGIT 164
Cdd:PLN02951   68 CNLRCQYCMPEEGVELTPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDICLQLSSLKGLKTLAMTTNGIT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 165 LAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVNCVIMRGLNDDEICDFVELTRDK 244
Cdd:PLN02951  148 LSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKVNCVVMRGFNDDEICDFVELTRDK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 245 PINVRFIEFMPFDGNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHPTETAKNFTIDGHCGSVSFITSMTEHFCAGCNRLR 324
Cdd:PLN02951  228 PINVRFIEFMPFDGNVWNVKKLVPYAEMMDRIEQRFPSLKRLQDHPTDTAKNFRIDGHCGSVSFITSMTEHFCAGCNRLR 307
                         330
                  ....*....|....*..
gi 1063705476 325 LLADGNFKVCLFGPSEV 341
Cdd:PLN02951  308 LLADGNLKVCLFGPSEV 324
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
63-341 1.34e-148

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: 421.78  E-value: 1.34e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  63 SDMLIDKFGRLHTYLRISLTERCNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEE 142
Cdd:COG2896     2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 143 ICLQLSSLKGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVN 222
Cdd:COG2896    82 LIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVKIN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 223 CVIMRGLNDDEICDFVELTRDKPINVRFIEFMPF-DGNVWNVKKLVPYAEVMDKVVKRFPsIKRMQDHPTETAKNFTIDG 301
Cdd:COG2896   162 AVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLgEGGGWRRDQVVSAAEILERLEARFP-LEPLPARGGGPARYYRVPG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1063705476 302 HCGSVSFITSMTEHFCAGCNRLRLLADGNFKVCLFGPSEV 341
Cdd:COG2896   241 GGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEV 280
moaA PRK00164
GTP 3',8-cyclase MoaA;
60-337 3.18e-131

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 377.94  E-value: 3.18e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  60 NPVSDMLIDKFGRLHTYLRISLTERCNLRCQYCMPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKD 139
Cdd:PRK00164    2 VPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 140 IEEICLQLSSLKGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPV 219
Cdd:PRK00164   82 LEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLTPV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 220 KVNCVIMRGLNDDEICDFVELTRDKPINVRFIEFMPFD-GNVWNVKKLVPYAEVMDKVVKRFPSIKrMQDHPTETAKNFT 298
Cdd:PRK00164  162 KVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGeGNEWFRKHHLSGAEIRARLAERGWTLQ-PRARSGGPAQYFR 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1063705476 299 IDGHCGSVSFITSMTEHFCAGCNRLRLLADGNFKVCLFG 337
Cdd:PRK00164  241 HPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFA 279
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
66-341 3.01e-121

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: 352.68  E-value: 3.01e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  66 LIDKFGRLHTYLRISLTERCNLRCQYCMPSEGV-ELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEIC 144
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGlDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 145 LQLSSLKGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGH-DRVMKSIDTAIELGYNPVKVNC 223
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRGGRlEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 224 VIMRGLNDDEICDFVELTRDKPINVRFIEFMPFD-GNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHP---TETAKNFTI 299
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGeGNGWREKKFVSADEILERLEQAFGPLEPVPSPRgngPAPAYRWRL 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1063705476 300 DGHCGSVSFITSMTEHFCAGCNRLRLLADGNFKVCLFGPSEV 341
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGV 282
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
66-335 1.08e-71

probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an archaeal family related, and predicted to be functionally equivalent, to molybdenum cofactor biosynthesis protein A (MoaA) of bacteria (see TIGR02666). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274251 [Multi-domain]  Cd Length: 302  Bit Score: 225.26  E-value: 1.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  66 LIDKFGRLHTYLRISLTERCNLRCQYCMpSEGVELTPKPqLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICL 145
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYCH-MEGEDRSGGN-ELSPEEIERIVRVASEFGVRKVKITGGEPLLRKDLIEIIR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 146 QLSSLkGLKNLAITTNGITLAKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVNCVI 225
Cdd:TIGR02668  79 RIKDY-GIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDRVIEGIESAVDAGLTPVKLNMVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 226 MRGLNDDEICDFVELTRDKPINVRFIEFMPFDgnvWNVKKLVPYAEVMDKVVKRF------PSIKRMQDHPTetaknFTI 299
Cdd:TIGR02668 158 LKGINDNEIPDMVEFAAEGGAILQLIELMPPG---EGEKEFKKYHEDIDPIEEELekmadrVRTRRMHNRPK-----YFI 229
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1063705476 300 DGHcGSVSFITSM--TEhFCAGCNRLRLLADGNFKVCL 335
Cdd:TIGR02668 230 PGG-VEVEVVKPMdnPV-FCAHCTRLRLTSDGKLKTCL 265
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
246-341 6.58e-38

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: 131.96  E-value: 6.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 246 INVRFIEFMPFD-GNVWNVKKLVPYAEVMDKVVKRFPSIKRmQDHPTETAKNFTIDGHCGSVSFITSMTEHFCAGCNRLR 324
Cdd:pfam06463   1 IDLRFIELMPVGeGNGWRRKKFVSLDEILERIEARFPLLPA-RKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLR 79
                          90
                  ....*....|....*..
gi 1063705476 325 LLADGNFKVCLFGPSEV 341
Cdd:pfam06463  80 LTADGKLKTCLFAEDGI 96
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-237 9.28e-31

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: 114.16  E-value: 9.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  81 LTERCNLRCQYCMPSEGvELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKN--LAI 158
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSI-RARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGirITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 159 TTNGITLAK-KLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGYNPVKVNCVIMRGLNDDEICDF 237
Cdd:pfam04055  80 ETNGTLLDEeLLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLEET 159
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
76-224 4.70e-30

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: 112.30  E-value: 4.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  76 YLRISLTERCNLRCQYCMPSEGVELTPKpqlLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSlKGLKn 155
Cdd:COG0535     1 RLQIELTNRCNLRCKHCYADAGPKRPGE---LSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKE-LGIR- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705476 156 LAITTNGITLAKKLP-RLKECGLDSLNISLDTLVPAKFEFLTRRKG-HDRVMKSIDTAIELGYnPVKVNCV 224
Cdd:COG0535    76 VNLSTNGTLLTEELAeRLAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGI-PVGINTV 145
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-256 1.98e-17

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: 79.68  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  79 ISLTERCNLRCQYCMPSEGVELTPKpQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKNLAI 158
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPE-SPPEIEEILDIVLEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEISI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 159 TTNGITLAKK-LPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRvmKSIDTAIELGYNPVKVNCVIMRGLNDDEICDF 237
Cdd:cd01335    80 ETNGTLLTEElLKELKELGLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKELREAGLGLSTTLLVGLGDEDEEDD 157
                         170       180
                  ....*....|....*....|.
gi 1063705476 238 VELTRDKP--INVRFIEFMPF 256
Cdd:cd01335   158 LEELELLAefRSPDRVSLFRL 178
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
312-341 5.26e-14

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: 66.03  E-value: 5.26e-14
                          10        20        30
                  ....*....|....*....|....*....|
gi 1063705476 312 MTEHFCAGCNRLRLLADGNFKVCLFGPSEV 341
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEV 30
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
85-243 2.65e-13

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 69.94  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYCMPSEG-----------VELTpkpQLLSQ-SEIVRLAGLFVSA---GVnkirltgGEPTVRKDIEEICLQLSS 149
Cdd:COG2100    46 CNLNCIFCSVDAGphsrtrqaeyiVDPE---YLVEWfEKVARFKGKGVEAhidGV-------GEPLLYPYIVELVKGLKE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 150 LKGLKNLAITTNGITLAKKL-PRLKECGLDSLNISLDTLVPAKFEFLTRRKGHD--RVMKSID-TAIELGYNpVKVNCVI 225
Cdd:COG2100   116 IKGVKVVSMQTNGTLLSEKLiDELEEAGLDRINLSIDTLDPEKAKKLAGTKWYDveKVLELAEyIARETKID-LLIAPVW 194
                         170
                  ....*....|....*...
gi 1063705476 226 MRGLNDDEICDFVELTRD 243
Cdd:COG2100   195 LPGINDEDIPKIIEWALE 212
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
75-280 2.55e-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: 65.50  E-value: 2.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476   75 TYLRISLTERCNLRCQYCMPSegvELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLT-----GGEPTV--RKDIEEICLQL 147
Cdd:smart00729   1 PLALYIITRGCPRRCTFCSFP---SLRGKLRSRYLEALVREIELLAEKGEKEGLVGtvfigGGTPTLlsPEQLEELLEAI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  148 SSLKGLKN---LAITTNGITL-AKKLPRLKECGLDSLNISLDTLVPAKFEFLTRRKGHDRVMKSIDTAIELGynPVKVNC 223
Cdd:smart00729  78 REILGLAKdveITIETRPDTLtEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAG--PIKVST 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063705476  224 VIMRGL---NDDEICDFVELTRD-KPINVRFIEFMPFDGNVWNVKKLVPYAEVMDKVVKRF 280
Cdd:smart00729 156 DLIVGLpgeTEEDFEETLKLLKElGPDRVSIFPLSPRPGTPLAKMYKRLKPPTKEERAELL 216
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
85-256 3.58e-12

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 65.21  E-value: 3.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYC---------MPSEGVELTPKpQLLsqSEIVRLAGLFVSAGVnkIRLTGGEPTVRKD-IEEICLQLSSLkGLK 154
Cdd:COG1180    31 CNLRCPYChnpeisqgrPDAAGRELSPE-ELV--EEALKDRGFLDSCGG--VTFSGGEPTLQPEfLLDLAKLAKEL-GLH 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 155 NlAITTNGITLAKKLPRLKEcGLDSLNISLDTLVPAKFEFLTRRKGhDRVMKSIDTAIELGYnPVKVNCVIMRGLNDDE- 233
Cdd:COG1180   105 T-ALDTNGYIPEEALEELLP-YLDAVNIDLKAFDDEFYRKLTGVSL-EPVLENLELLAESGV-HVEIRTLVIPGLNDSEe 180
                         170       180
                  ....*....|....*....|....*...
gi 1063705476 234 ----ICDFV-ELTRDKPinvrfIEFMPF 256
Cdd:COG1180   181 eleaIARFIaELGDVIP-----VHLLPF 203
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
81-339 3.33e-10

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: 60.62  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  81 LTERCNLRCQYC-----MPSEGVELTPKPQLLSQSeIVRLAglfVSAGVNKIRLTGGEPTVRKDIEEIcLQLSSLKGLKn 155
Cdd:TIGR04251  10 LTEGCNLKCRHCwidpkYQGEGEQHPSLDPSLFRS-IIRQA---IPLGLTSVKLTGGEPLLHPAIGEI-LECIGENNLQ- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 156 LAITTNGITLAKKLPR-LKECGLDSLNISLDTLVPAKFEFLTRRKG-HDRVMKSIDTAIELGYNPVKVNCVIMRglNDDE 233
Cdd:TIGR04251  84 LSVETNGLLCTPQTARdLASCETPFVSVSLDGVDAATHDWMRGVKGaFDKAVRGIHNLVEAGIHPQIIMTVTRR--NVGQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 234 ICDFVELTRD-KPINVRFIEFMPF--------DGNVWNVKKLVPYAEVMDKVVKRFPSIKRMQDHPTE---TAKNFTIDG 301
Cdd:TIGR04251 162 MEQIVRLAESlGAESVKFNHVQPTsrgskmheNGETLSIGELVALGEWMERTLIPSTALRIDFGHPPAfrpLGRMFGEKP 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1063705476 302 H-CGsvsfitsmtehFCAGCNRLRLLADGNFKVCLFGPS 339
Cdd:TIGR04251 242 GgCG-----------LCGIFGILGVLSDGSYALCGIGES 269
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
41-280 5.04e-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: 60.36  E-value: 5.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  41 SERLFSSSYAAHQVDQIKDNPVSDMLIDKFGRlhtYLRISLTERCNLRCQYCMP-------SEGVELTPKPQLLSQSEIV 113
Cdd:NF033640   79 SLRQESNERWAKHIEDAIKSTDEDGSDDVNPR---YLDLRFGNLCNLKCRMCGPhsssswaKEAKKLGGPKLGDKKKISW 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 114 RLAGLFVSA------GVNKIRLTGGEPTVRKDIEEICLQLSSLKGLKN--LAITTNGITLAKK-------LPRLKECgld 178
Cdd:NF033640  156 FEDEEFWKWleellpSLKEIYFAGGEPLLIKEHYKLLEKLVEKGRAKNieLRYNTNLTVLPDKlkdlldlWKKFKSV--- 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 179 SLNISLDTlVPAKFEFLtrRKGH--DRVMKSIDTAIELGYN-PVKVNCVIMRgLNDDEICDFVELTRDKPINVRFIEF-M 254
Cdd:NF033640  233 SISASIDG-VGERNEYI--RYGSkwDEIEKNLKKLKEECPNvELRINPTVSA-LNVLHLPELLDWLLELGLGPIDIYLnI 308
                         250       260
                  ....*....|....*....|....*.
gi 1063705476 255 PFDGNVWNVKKLvPYaEVMDKVVKRF 280
Cdd:NF033640  309 LRDPEYLSIKNL-PK-EIKQKVIEKL 332
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
79-280 1.06e-08

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 56.15  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  79 ISLTERCNLRCQYCMPSEGVEltPKPQLLSQSEIVRLAGLFVSAGVNKIRLT----GGEPTVRKD-IEEIC-LQLSSLKG 152
Cdd:COG0641     5 LKPTSRCNLRCSYCYYSEGDE--GSRRRMSEETAEKAIDFLIESSGPGKELTitffGGEPLLNFDfIKEIVeYARKYAKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 153 LKNL--AITTNGITL-AKKLPRLKECGLdSLNISLDTlvPAKFEFLTRR----KG-HDRVMKSIDTAIELGYnPVKVNCV 224
Cdd:COG0641    83 GKKIrfSIQTNGTLLdDEWIDFLKENGF-SVGISLDG--PKEIHDRNRVtkngKGsFDRVMRNIKLLKEHGV-EVNIRCT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 225 ImrglNDDEICDFVE----LTRDKPINVRFIEFMPFDGNVWNVKKLVpYAEVMDKVVKRF 280
Cdd:COG0641   159 V----TRENLDDPEElydfLKELGFRSIQFNPVVEEGEADYSLTPED-YGEFLIELFDEW 213
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
72-252 5.97e-07

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: 49.80  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  72 RLHTYLRISLT--ERCNLRCQYC-------MPSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTG-GEPTVRKDIE 141
Cdd:COG0731    19 RLGRSLGINLIpnKTCNFDCVYCqrgrttdLTRERREFDDPEEILEELIEFLRKLPEEAREPDHITFSGsGEPTLYPNLG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 142 EICLQLSSLKGLKnLAITTNGITLAKK--LPRLKEcgLDSLNISLDTLVPAKFEFLTRRKGH---DRVMKSIDTAIELGY 216
Cdd:COG0731    99 ELIEEIKKLRGIK-TALLTNGSLLHRPevREELLK--ADQVYPSLDAADEETFRKINRPHPGlswERIIEGLELFRKLYK 175
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063705476 217 NPVKVNCVIMRGLNDD--EICDFVELtrDKPINVRFIE 252
Cdd:COG0731   176 GRTVIETMLVKGINDSeeELEAYAEL--IKRINPDFVE 211
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
79-232 2.83e-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: 48.70  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  79 ISLTERCNLRCQYCmpSEGVELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKDIEEIclqlssLKGL-KN-- 155
Cdd:TIGR04250   7 IDITGRCNLRCRYC--SHFSSAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREI------IDGIvKNrm 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 156 -LAITTNG--IT--LAKKLPRLKECglDSLNISLDTLVPAKFEFLtrrKGHDRVMKSIDtAIEL--GYN-PVKVNCVIMR 227
Cdd:TIGR04250  79 rFSILSNGtlITdaIASFLAATRRC--DYVQVSIDGSTPGTHDRL---RGTGSFLQAVE-GIELlrKHAiPVVVRVTIHR 152

                  ....*
gi 1063705476 228 GLNDD 232
Cdd:TIGR04250 153 WNVDD 157
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
85-279 4.57e-06

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: 46.67  E-value: 4.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYC------MPSEGVELTPkPQLLsqSEIVRLAGLFVSagvnkirLTGGEPTVRKDIEEICLQLSSlKGLKnLAI 158
Cdd:COG0602    30 CNLRCSWCdtkyawDGEGGKRMSA-EEIL--EEVAALGARHVV-------ITGGEPLLQDDLAELLEALKD-AGYE-VAL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 159 TTNGiTLAKKLprlkecGLDSLNISLDTlvPAKFEfLTRRKGHDRVMKSIDTaielgynpVKVncVIMrglNDDEICDFV 238
Cdd:COG0602    98 ETNG-TLPIPA------GIDWVTVSPKL--PSSGE-EEDNRENLEVLRRADE--------LKF--VVA---DETDLEEAE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063705476 239 ELTRDKPINVRFIeFMPfdgnVWNVKKLVPYAEVMDKVVKR 279
Cdd:COG0602   155 ELLARLDFRCPVY-LQP----VWGNKLEENTELLAEWCLAH 190
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
85-251 9.96e-06

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: 45.82  E-value: 9.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYC-----MPSEGVELTPKPQLLsqsEIVRLAGLFVSAGVnkirLTGGEPTVRKDIEEICLQLSSLkGLKnLAIT 159
Cdd:TIGR02495  26 CNLKCPYChnpllIPRRGSGEIEVEELL---EFLRRRRGLLDGVV----ITGGEPTLQAGLPDFLREVREL-GFE-VKLD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 160 TNGiTLAKKLPRLKECGLdsLN-ISLDTLVPA-KFEFLTRRKG---HDRVMKSIDTAIELGYnPVKVNCVIMRGLNDDEi 234
Cdd:TIGR02495  97 TNG-SNPRRLEELLEEGL--VDyVAMDVKAPPeKYGELYGLEKngaAKNILKSLEILLESGI-PFELRTTVVRGFLTEE- 171
                         170
                  ....*....|....*..
gi 1063705476 235 cDFVELTRDKPINVRFI 251
Cdd:TIGR02495 172 -DLAEIATRIKENGTYV 187
PFLA TIGR02493
pyruvate formate-lyase 1-activating enzyme; An iron-sulfur protein with a radical-SAM domain ...
85-256 7.39e-05

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: 43.51  E-value: 7.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYCM------PSEGVELTPKpQLLsqSEIVRLAGLFVSAGvNKIRLTGGEPTVRKDIEEICLQLSSLKGLkNLAI 158
Cdd:TIGR02493  25 CPLRCQYCHnpdtwdLKGGTEVTPE-ELI--KEVGSYKDFFKASG-GGVTFSGGEPLLQPEFLSELFKACKELGI-HTCL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 159 TTNGI--TLAKKLPRLKE----CGLDslnisLDTLVPAKFEFLTRRKGHdrvmKSIDTAIELGY--NPVKVNCVIMRGLN 230
Cdd:TIGR02493 100 DTSGFlgGCTEAADELLEytdlVLLD-----IKHFNPEKYKKLTGVSLQ----PTLDFAKYLAKrnKPIWIRYVLVPGYT 170
                         170       180
                  ....*....|....*....|....*...
gi 1063705476 231 DDE--ICDFVELTRDKPiNVRFIEFMPF 256
Cdd:TIGR02493 171 DSEedIEALAEFVKTLP-NVERVEVLPY 197
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
85-239 1.14e-04

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


Pssm-ID: 444038  Cd Length: 261  Bit Score: 43.05  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  85 CNLRCQYC--------MPSEGVELTPkpqllsQSEIVRLAGLFVSAGVNKIRLTGGEPTVRKdieEICLQLssLKGLKNL 156
Cdd:COG5014    50 CNLRCGFCwswrfrdfPLTIGKFYSP------EEVAERLIEIARERGYRQVRLSGGEPTIGF---EHLLKV--LELFSER 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476 157 AIT----TNGI------TLAKKL---PRLkecgldSLNISLDTLVPAKFEFLT--RRKGHDRVMKSIDTAIELGYNPVK- 220
Cdd:COG5014   119 GLTfileTNGIligydrELARELasfRNI------VVRVSIKGCTPEEFSMLTgaDPEFFELQLRALKNLVDAGLEPGRe 192
                         170       180
                  ....*....|....*....|
gi 1063705476 221 VNCVIMRGLNDDEIC-DFVE 239
Cdd:COG5014   193 VYPAVMLSFSTEESIrKLIE 212
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
79-180 2.47e-03

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  79 ISLTERCNLRCQYCMPSEGvELTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGG-EP------------TVRKDIEEICL 145
Cdd:TIGR03551  43 INFTNVCYGGCGFCAFRKR-KGDADAYLLSLEEIAERAAEAWKAGATEVCIQGGiHPdldgdfyldilrAVKEEVPGMHI 121
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063705476 146 QLSSLKGLKNLAiTTNGITLAKKLPRLKECGLDSL 180
Cdd:TIGR03551 122 HAFSPMEVYYGA-RNSGLSVEEALKRLKEAGLDSM 155
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
68-180 8.03e-03

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: 37.80  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705476  68 DKFGRLHTYLR---ISLTERCNLRCQYC---MPSEgvelTPKPQLLSQSEIVRLAGLFVSAGVNKIRLTGGE-PTVRKD- 139
Cdd:COG1060    41 RRFGNTVTFVVnrpINLTNVCVNGCKFCafsRDNG----DIDRYTLSPEEILEEAEEAKALGATEILLVGGEhPDLPLEy 116
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063705476 140 IEEICLQLSS------LKGL-----KNLAiTTNGITLAKKLPRLKECGLDSL 180
Cdd:COG1060   117 YLDLLRAIKErfpnihIHALspeeiAHLA-RASGLSVEEVLERLKEAGLDSL 167
 
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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