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Conserved domains on  [gi|571738188|gb|ETR26074|]
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molybdenum cofactor biosynthesis protein A [Acinetobacter baumannii UH7707]

Protein Classification

GTP 3',8-cyclase MoaA( domain architecture ID 11458418)

GTP 3',8-cyclase MoaA catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
11-344 8.37e-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: 419.47  E-value: 8.37e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  11 PSLLQDQYGRIKRKLRISVTDRCNFKCVYCMPEHP-EWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVH 89
Cdd:COG2896    2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGyQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  90 FIRDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGL-PFK 167
Cdd:COG2896   82 LIARLAALP--GIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRdDLDKVLAGIDAALAAGLtPVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 168 INCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVLQPYYSVQVIEQQ-HEPARQYLIN 246
Cdd:COG2896  160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARgGGPARYYRVP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 247 GS-YHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHKAKG 325
Cdd:COG2896  240 GGgGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRS----------GASDEELAEAIREAIARKPEG 309
                        330       340
                 ....*....|....*....|
gi 571738188 326 FHALQHQQTR-KISMHMLGG 344
Cdd:COG2896  310 HGFDEGDFPQpKRSMSAIGG 329
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
11-344 8.37e-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: 419.47  E-value: 8.37e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  11 PSLLQDQYGRIKRKLRISVTDRCNFKCVYCMPEHP-EWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVH 89
Cdd:COG2896    2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGyQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  90 FIRDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGL-PFK 167
Cdd:COG2896   82 LIARLAALP--GIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRdDLDKVLAGIDAALAAGLtPVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 168 INCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVLQPYYSVQVIEQQ-HEPARQYLIN 246
Cdd:COG2896  160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARgGGPARYYRVP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 247 GS-YHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHKAKG 325
Cdd:COG2896  240 GGgGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRS----------GASDEELAEAIREAIARKPEG 309
                        330       340
                 ....*....|....*....|
gi 571738188 326 FHALQHQQTR-KISMHMLGG 344
Cdd:COG2896  310 HGFDEGDFPQpKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
14-344 6.23e-137

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: 392.36  E-value: 6.23e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   14 LQDQYGRIKRKLRISVTDRCNFKCVYCMPEH--PEWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVHFI 91
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGggLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   92 RDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK--KLEPVLEGIQAAKEVGL-PFKI 168
Cdd:TIGR02666  81 ARLAALP--GIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRggRLEQVLAGIDAALAAGLePVKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  169 NCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVLQPYYSVQVIEQQHE-----PARQY 243
Cdd:TIGR02666 159 NTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFGPLEPVPSPRgngpaPAYRW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  244 LING-SYHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHK 322
Cdd:TIGR02666 239 RLPGgKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRG----------GASDALLEAIIQAILQKK 308
                         330       340
                  ....*....|....*....|....*.
gi 571738188  323 AKGFHAL----QHQQTRKISMHMLGG 344
Cdd:TIGR02666 309 PEGHSFLrftsPANKRRKRAMSQIGG 334
moaA PRK00164
GTP 3',8-cyclase MoaA;
9-344 2.39e-130

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 375.25  E-value: 2.39e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   9 TAPSLLQDQYGRIKRKLRISVTDRCNFKCVYCMPEHP-EWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGI 87
Cdd:PRK00164   3 PMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYlPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  88 VHFIRDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGL-P 165
Cdd:PRK00164  83 EDIIAALAALP--GIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRdRLDQVLAGIDAALAAGLtP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 166 FKINCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVL-QPYYSVQVIEQQHEPARQYL 244
Cdd:PRK00164 161 VKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLaERGWTLQPRARSGGPAQYFR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 245 IN-GSYHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTLVSkqhtpeygmyIQKLKNLVHPYIWHKA 323
Cdd:PRK00164 241 HPdYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGAD----------DEELAAAIREALQNKP 310
                        330       340
                 ....*....|....*....|.
gi 571738188 324 KGFHALQHQQTRKISMHMLGG 344
Cdd:PRK00164 311 EGHGLHDGNTGPTRHMSYIGG 331
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
195-327 2.00e-29

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: 109.61  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  195 LRFIEFMPLDGDALWSNKDVVSEAEILQVL-QPYYSVQVIEQQHEPARQYLINGSY-HLGIISTITHSFCHQCDRIRLTA 272
Cdd:pfam06463   3 LRFIELMPVGEGNGWRRKKFVSLDEILERIeARFPLLPARKRTGGPAKRYRIPGGGgRIGFIAPVSNPFCASCNRLRLTA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 571738188  273 KGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHKAKGFH 327
Cdd:pfam06463  83 DGKLKTCLFAEDGIDLRDALRS----------GDDDEELREAIREALARKPPRHS 127
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
27-225 4.11e-23

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 95.09  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  27 ISVTDRCNFKCVYCmpeHPEWLNKQDLLSFEALFQFCHFMVQQ---GIQSIRITGGEPLMRQGIVHFIRDLqsLKSLGLK 103
Cdd:cd01335    1 LELTRGCNLNCGFC---SNPASKGRGPESPPEIEEILDIVLEAkerGVEVVILTGGEPLLYPELAELLRRL--KKELPGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 104 RISMTTNGHYL-AKHAKQLKDAGLDDLNISLDSLDPVQFKEL--TKKKLEPVLEGIQAAKEVGLPFKIN-CVLMKDRNDD 179
Cdd:cd01335   76 EISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIrgSGESFKERLEALKELREAGLGLSTTlLVGLGDEDEE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 571738188 180 QILPMVKWsIAHHIPLRFIEFMPLD---GDALWSNKDVVSEAEILQVLQ 225
Cdd:cd01335  156 DDLEELEL-LAEFRSPDRVSLFRLLpeeGTPLELAAPVVPAEKLLRLIA 203
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
23-224 6.35e-10

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: 58.18  E-value: 6.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188    23 RKLRISVTDRCNFKCVYCmPEHPEWLNKQDlLSFEALFQFCHFMVQQG-----IQSIRITGGEPLM--RQGIVHFIRDLQ 95
Cdd:smart00729   1 PLALYIITRGCPRRCTFC-SFPSLRGKLRS-RYLEALVREIELLAEKGekeglVGTVFIGGGTPTLlsPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188    96 SLKSLGLKR-ISMTTN-GHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGlPFKINCVL 172
Cdd:smart00729  79 EILGLAKDVeITIETRpDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGhTVEDVLEAVELLREAG-PIKVSTDL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 571738188   173 M---KDRNDDQILPMVKWSIAHHIP-LRFIEFMPLDGDALWSNKDVVSEAEILQVL 224
Cdd:smart00729 158 IvglPGETEEDFEETLKLLKELGPDrVSIFPLSPRPGTPLAKMYKRLKPPTKEERA 213
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
33-140 2.42e-05

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: 45.72  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  33 CNFKCVYCMPE-----HPEW--LNKQDLLSFEAL--FQFCHFM-----VQQGIQSIRITGGEPLMrqgIVHFIRDLQSLK 98
Cdd:NF033640 120 CNLKCRMCGPHsssswAKEAkkLGGPKLGDKKKIswFEDEEFWkwleeLLPSLKEIYFAGGEPLL---IKEHYKLLEKLV 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 571738188  99 SLGL---KRISMTTNGHYLAKHA-------KQLKDAgldDLNISLDSLDPVQ 140
Cdd:NF033640 197 EKGRaknIELRYNTNLTVLPDKLkdlldlwKKFKSV---SISASIDGVGERN 245
 
Name Accession Description Interval E-value
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
11-344 8.37e-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: 419.47  E-value: 8.37e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  11 PSLLQDQYGRIKRKLRISVTDRCNFKCVYCMPEHP-EWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVH 89
Cdd:COG2896    2 TSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGyQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDLPE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  90 FIRDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGL-PFK 167
Cdd:COG2896   82 LIARLAALP--GIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRdDLDKVLAGIDAALAAGLtPVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 168 INCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVLQPYYSVQVIEQQ-HEPARQYLIN 246
Cdd:COG2896  160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARgGGPARYYRVP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 247 GS-YHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHKAKG 325
Cdd:COG2896  240 GGgGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRS----------GASDEELAEAIREAIARKPEG 309
                        330       340
                 ....*....|....*....|
gi 571738188 326 FHALQHQQTR-KISMHMLGG 344
Cdd:COG2896  310 HGFDEGDFPQpKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
14-344 6.23e-137

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: 392.36  E-value: 6.23e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   14 LQDQYGRIKRKLRISVTDRCNFKCVYCMPEH--PEWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVHFI 91
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGggLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   92 RDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK--KLEPVLEGIQAAKEVGL-PFKI 168
Cdd:TIGR02666  81 ARLAALP--GIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITRRggRLEQVLAGIDAALAAGLePVKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  169 NCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVLQPYYSVQVIEQQHE-----PARQY 243
Cdd:TIGR02666 159 NTVVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSADEILERLEQAFGPLEPVPSPRgngpaPAYRW 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  244 LING-SYHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHK 322
Cdd:TIGR02666 239 RLPGgKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRG----------GASDALLEAIIQAILQKK 308
                         330       340
                  ....*....|....*....|....*.
gi 571738188  323 AKGFHAL----QHQQTRKISMHMLGG 344
Cdd:TIGR02666 309 PEGHSFLrftsPANKRRKRAMSQIGG 334
moaA PRK00164
GTP 3',8-cyclase MoaA;
9-344 2.39e-130

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 375.25  E-value: 2.39e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   9 TAPSLLQDQYGRIKRKLRISVTDRCNFKCVYCMPEHP-EWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGI 87
Cdd:PRK00164   3 PMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYlPFLPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLRKDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  88 VHFIRDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGL-P 165
Cdd:PRK00164  83 EDIIAALAALP--GIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRdRLDQVLAGIDAALAAGLtP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 166 FKINCVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDALWSNKDVVSEAEILQVL-QPYYSVQVIEQQHEPARQYL 244
Cdd:PRK00164 161 VKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLaERGWTLQPRARSGGPAQYFR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 245 IN-GSYHLGIISTITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQTLVSkqhtpeygmyIQKLKNLVHPYIWHKA 323
Cdd:PRK00164 241 HPdYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGAD----------DEELAAAIREALQNKP 310
                        330       340
                 ....*....|....*....|.
gi 571738188 324 KGFHALQHQQTRKISMHMLGG 344
Cdd:PRK00164 311 EGHGLHDGNTGPTRHMSYIGG 331
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
13-283 5.77e-78

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 243.51  E-value: 5.77e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  13 LLQDQYGRIKRKLRISVTDRCNFKCVYCMPEHPEWLN-KQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVHFI 91
Cdd:PLN02951  48 MLVDSFGRRHNYLRISLTERCNLRCQYCMPEEGVELTpKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIEDIC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  92 RDLQSLKslGLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKKK-LEPVLEGIQAAKEVGL-PFKIN 169
Cdd:PLN02951 128 LQLSSLK--GLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKgHDRVLESIDTAIELGYnPVKVN 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 170 CVLMKDRNDDQILPMVKWSIAHHIPLRFIEFMPLDGDAlWSNKDVVSEAEIL-QVLQPYYSVQVIEQQ-HEPARQYLING 247
Cdd:PLN02951 206 CVVMRGFNDDEICDFVELTRDKPINVRFIEFMPFDGNV-WNVKKLVPYAEMMdRIEQRFPSLKRLQDHpTDTAKNFRIDG 284
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 571738188 248 syHLGIISTIT---HSFCHQCDRIRLTAKGELYNCLFAP 283
Cdd:PLN02951 285 --HCGSVSFITsmtEHFCAGCNRLRLLADGNLKVCLFGP 321
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
25-172 1.11e-33

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 121.93  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  25 LRISVTDRCNFKCVYCmpEHPEWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVHFIRdlqSLKSLGLkR 104
Cdd:COG0535    2 LQIELTNRCNLRCKHC--YADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVE---YAKELGI-R 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 571738188 105 ISMTTNGHYLAKH-AKQLKDAGLDDLNISLDSLDPVQFKELTKKK--LEPVLEGIQAAKEVGLPFKINCVL 172
Cdd:COG0535   76 VNLSTNGTLLTEElAERLAEAGLDHVTISLDGVDPETHDKIRGVPgaFDKVLEAIKLLKEAGIPVGINTVY 146
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
195-327 2.00e-29

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: 109.61  E-value: 2.00e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  195 LRFIEFMPLDGDALWSNKDVVSEAEILQVL-QPYYSVQVIEQQHEPARQYLINGSY-HLGIISTITHSFCHQCDRIRLTA 272
Cdd:pfam06463   3 LRFIELMPVGEGNGWRRKKFVSLDEILERIeARFPLLPARKRTGGPAKRYRIPGGGgRIGFIAPVSNPFCASCNRLRLTA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 571738188  273 KGELYNCLFAPEGLNIKPQLQTlvskqhtpeyGMYIQKLKNLVHPYIWHKAKGFH 327
Cdd:pfam06463  83 DGKLKTCLFAEDGIDLRDALRS----------GDDDEELREAIREALARKPPRHS 127
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
29-181 4.07e-28

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: 107.23  E-value: 4.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   29 VTDRCNFKCVYCMPEHPEWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVHFIRDLQSLKSLGLKRISMT 108
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLKLELAEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 571738188  109 TNGHYLAK-HAKQLKDAGLDDLNISLDSLDPvQFKELTKKK--LEPVLEGIQAAKEVGLPF-KINCVLMKDRNDDQI 181
Cdd:pfam04055  81 TNGTLLDEeLLELLKEAGLDRVSIGLESGDD-EVLKLINRGhtFEEVLEALELLREAGIPVvTDNIVGLPGETDEDL 156
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
27-225 4.11e-23

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 95.09  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  27 ISVTDRCNFKCVYCmpeHPEWLNKQDLLSFEALFQFCHFMVQQ---GIQSIRITGGEPLMRQGIVHFIRDLqsLKSLGLK 103
Cdd:cd01335    1 LELTRGCNLNCGFC---SNPASKGRGPESPPEIEEILDIVLEAkerGVEVVILTGGEPLLYPELAELLRRL--KKELPGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 104 RISMTTNGHYL-AKHAKQLKDAGLDDLNISLDSLDPVQFKEL--TKKKLEPVLEGIQAAKEVGLPFKIN-CVLMKDRNDD 179
Cdd:cd01335   76 EISIETNGTLLtEELLKELKELGLDGVGVSLDSGDEEVADKIrgSGESFKERLEALKELREAGLGLSTTlLVGLGDEDEE 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 571738188 180 QILPMVKWsIAHHIPLRFIEFMPLD---GDALWSNKDVVSEAEILQVLQ 225
Cdd:cd01335  156 DDLEELEL-LAEFRSPDRVSLFRLLpeeGTPLELAAPVVPAEKLLRLIA 203
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
33-203 7.37e-19

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 84.47  E-value: 7.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  33 CNFKCVYCM-PE--HPEWLNKQDLLSFEALFQFC----HFMvqQGIQSIRITGGEPLMrQGivHFIRDL-QSLKSLGLKr 104
Cdd:COG1180   31 CNLRCPYCHnPEisQGRPDAAGRELSPEELVEEAlkdrGFL--DSCGGVTFSGGEPTL-QP--EFLLDLaKLAKELGLH- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 105 ISMTTNGHYLAKHAKQLKDaGLDDLNISLDSLDPVQFKELTKKKLEPVLEGIQAAKEVGLPFKINCVLMKDRNDD--QIL 182
Cdd:COG1180  105 TALDTNGYIPEEALEELLP-YLDAVNIDLKAFDDEFYRKLTGVSLEPVLENLELLAESGVHVEIRTLVIPGLNDSeeELE 183
                        170       180
                 ....*....|....*....|...
gi 571738188 183 PMVKW--SIAHHIPLRFIEFMPL 203
Cdd:COG1180  184 AIARFiaELGDVIPVHLLPFHPL 206
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
27-279 8.90e-15

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 74.25  E-value: 8.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  27 ISVTDRCNFKCVYC-MPEHPEwlNKQDLLSFEALFQFCHFMV--QQGIQSIRIT--GGEPLMRQG-IVHFIRDLQSLKSL 100
Cdd:COG0641    5 LKPTSRCNLRCSYCyYSEGDE--GSRRRMSEETAEKAIDFLIesSGPGKELTITffGGEPLLNFDfIKEIVEYARKYAKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 101 GLK-RISMTTNGHYL-AKHAKQLKDAGlddLNISLdSLD-PvqfKEL------TKKKL---EPVLEGIQAAKEVGLPFKI 168
Cdd:COG0641   83 GKKiRFSIQTNGTLLdDEWIDFLKENG---FSVGI-SLDgP---KEIhdrnrvTKNGKgsfDRVMRNIKLLKEHGVEVNI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 169 NCVLmkDR-NDDQILPMVKWsiAHHIPLRFIEFMPL--DGDALWSnkdvVSEAEILQVLQPYYSvQVIEQQHEPARQYLI 245
Cdd:COG0641  156 RCTV--TReNLDDPEELYDF--LKELGFRSIQFNPVveEGEADYS----LTPEDYGEFLIELFD-EWLERDGGKIFVREF 226
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 571738188 246 NGsyHLGIISTITHSFCHQCDRIRL--TAKGELYNC 279
Cdd:COG0641  227 DI--LLAGLLPPCSSPCVGAGGNYLvvDPDGDIYPC 260
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
79-189 4.00e-12

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


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 66.47  E-value: 4.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  79 GEPLMRQGIVHFIRDLQSLKslGLKRISMTTNGHYLAKH-AKQLKDAGLDDLNISLDSLDPVQFKELTKKK---LEPVLE 154
Cdd:COG2100   98 GEPLLYPYIVELVKGLKEIK--GVKVVSMQTNGTLLSEKlIDELEEAGLDRINLSIDTLDPEKAKKLAGTKwydVEKVLE 175
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 571738188 155 GI-QAAKEVGLPFKINCVLMKDRNDDQILPMVKWSI 189
Cdd:COG2100  176 LAeYIARETKIDLLIAPVWLPGINDEDIPKIIEWAL 211
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
257-293 4.72e-11

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: 57.94  E-value: 4.72e-11
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 571738188 257 ITHSFCHQCDRIRLTAKGELYNCLFAPEGLNIKPQLQ 293
Cdd:cd21117    1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALR 37
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
23-224 6.35e-10

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: 58.18  E-value: 6.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188    23 RKLRISVTDRCNFKCVYCmPEHPEWLNKQDlLSFEALFQFCHFMVQQG-----IQSIRITGGEPLM--RQGIVHFIRDLQ 95
Cdd:smart00729   1 PLALYIITRGCPRRCTFC-SFPSLRGKLRS-RYLEALVREIELLAEKGekeglVGTVFIGGGTPTLlsPEQLEELLEAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188    96 SLKSLGLKR-ISMTTN-GHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKELTKK-KLEPVLEGIQAAKEVGlPFKINCVL 172
Cdd:smart00729  79 EILGLAKDVeITIETRpDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGhTVEDVLEAVELLREAG-PIKVSTDL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 571738188   173 M---KDRNDDQILPMVKWSIAHHIP-LRFIEFMPLDGDALWSNKDVVSEAEILQVL 224
Cdd:smart00729 158 IvglPGETEEDFEETLKLLKELGPDrVSIFPLSPRPGTPLAKMYKRLKPPTKEERA 213
COG2108 COG2108
Uncharacterized radical SAM domain-containing protein [Function unknown];
23-164 2.82e-06

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


Pssm-ID: 441711 [Multi-domain]  Cd Length: 361  Bit Score: 48.42  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  23 RKLRISVTDRCNFKCVYCmPEHPEWLNKQDLLSFEALFQFchfmVQQGIQSIR--------ITGGEPLMRQG-IVHFIRd 93
Cdd:COG2108   27 AKLVLFITGLCNRNCFYC-PLSEERKGKDVIYANERPVES----DEDVIEEARrmgalgagITGGEPLLVLDrTLEYIR- 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 571738188  94 lqslkslGLKR-------ISMTTNGHYLAKHA-KQLKDAGLDDLNIsldslDPVQfkELTKKKLEPVLEGIQAAKEVGL 164
Cdd:COG2108  101 -------LLKEefgpdhhIHLYTNGILADEDVlRKLADAGLDEIRF-----HPPQ--ELWGLLGTPYLESIKLAKEYGL 165
N_Twi_rSAM NF033640
twitch domain-containing radical SAM protein; Members of this family are unusual among radical ...
33-140 2.42e-05

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: 45.72  E-value: 2.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  33 CNFKCVYCMPE-----HPEW--LNKQDLLSFEAL--FQFCHFM-----VQQGIQSIRITGGEPLMrqgIVHFIRDLQSLK 98
Cdd:NF033640 120 CNLKCRMCGPHsssswAKEAkkLGGPKLGDKKKIswFEDEEFWkwleeLLPSLKEIYFAGGEPLL---IKEHYKLLEKLV 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 571738188  99 SLGL---KRISMTTNGHYLAKHA-------KQLKDAgldDLNISLDSLDPVQ 140
Cdd:NF033640 197 EKGRaknIELRYNTNLTVLPDKLkdlldlwKKFKSV---SISASIDGVGERN 245
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
23-186 3.49e-05

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: 45.21  E-value: 3.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   23 RKLRISVTDRCNFKCVYCM--PEHPEWLNKQDLLSFEALFQFCHFMVQQGIQSIRITGGEPLMRQGIVHFirdLQSLKSL 100
Cdd:TIGR04251   4 HQIYFYLTEGCNLKCRHCWidPKYQGEGEQHPSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEI---LECIGEN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  101 GLKrISMTTNGHYLAKH-AKQLKDAGLDDLNISLDSLDPVQFKEL--TKKKLEPVLEGIQAAKEVGLPFKINCVLMKdRN 177
Cdd:TIGR04251  81 NLQ-LSVETNGLLCTPQtARDLASCETPFVSVSLDGVDAATHDWMrgVKGAFDKAVRGIHNLVEAGIHPQIIMTVTR-RN 158

                  ....*....
gi 571738188  178 DDQILPMVK 186
Cdd:TIGR04251 159 VGQMEQIVR 167
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
23-111 4.52e-04

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


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 41.77  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   23 RKLRISVTDRCNFKCVYCM-----PEHPEWLNKQDLLSFEALFQFCHFMvqqgiqSIRITGGEPLMRQGIVHFIRDLqsl 97
Cdd:TIGR04250   3 RSVDIDITGRCNLRCRYCShfssaAETPTDLETAEWLRFFRELNRCSVL------RVVLSGGEPFMRSDFREIIDGI--- 73
                          90
                  ....*....|....
gi 571738188   98 kSLGLKRISMTTNG 111
Cdd:TIGR04250  74 -VKNRMRFSILSNG 86
rSAM_paired_1 TIGR03978
His-Xaa-Ser system radical SAM maturase HxsB; This model describes the upstream member, HxsB, ...
27-114 1.08e-03

His-Xaa-Ser system radical SAM maturase HxsB; This model describes the upstream member, HxsB, of a pair of uncharacterized radical SAM proteins, regularly found in the context of a small protein with four or more repeats of the tripeptide His-Xaa-Ser (HXS). This enzyme appears to be part of a peptide modification system.


Pssm-ID: 274896 [Multi-domain]  Cd Length: 466  Bit Score: 40.70  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188   27 ISVTDRCNFKCVYC-MPEHPEWLNKQDlLSFEALFQFCHFMVQQGIQSIRI--TGGEPLMRQGIVHFIRDL--QSLKSLG 101
Cdd:TIGR03978  87 FVPTLRCNHSCKYCqVSRASEDASGFD-MSEETARKAVDLIFQSPSPSLKIefQGGEPLLRFDLIKKIVEYaeEKNKSEN 165
                          90
                  ....*....|....*
gi 571738188  102 lKRISMT--TNGHYL 114
Cdd:TIGR03978 166 -KEIEFViaTNLSLL 179
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
33-113 1.74e-03

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: 38.97  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  33 CNFKCVYC------MPEHPEWLNKQDLLSfEALfqfchfmvQQGIQSIRITGGEPLMRQGIVHFIrdlQSLKSLGLkRIS 106
Cdd:COG0602   30 CNLRCSWCdtkyawDGEGGKRMSAEEILE-EVA--------ALGARHVVITGGEPLLQDDLAELL---EALKDAGY-EVA 96

                 ....*..
gi 571738188 107 MTTNGHY 113
Cdd:COG0602   97 LETNGTL 103
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
32-179 3.06e-03

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: 38.63  E-value: 3.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188  32 RCNFKCVYC--------MPEHPEWLNKQDLLsfEAL--FQFCHFMVQQGIQSIRITG-GEPLMRQGIVHFIRDlqsLKSL 100
Cdd:COG0731   33 TCNFDCVYCqrgrttdlTRERREFDDPEEIL--EELieFLRKLPEEAREPDHITFSGsGEPTLYPNLGELIEE---IKKL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 571738188 101 GLKRISMTTNGHYLAKHAKQLKDAGLDDLNISLDSLDPVQFKEL--TKKKL--EPVLEGIQAAKEVglpFKINCV----L 172
Cdd:COG0731  108 RGIKTALLTNGSLLHRPEVREELLKADQVYPSLDAADEETFRKInrPHPGLswERIIEGLELFRKL---YKGRTVietmL 184

                 ....*..
gi 571738188 173 MKDRNDD 179
Cdd:COG0731  185 VKGINDS 191
 
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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