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Conserved domains on  [gi|628601853|ref|NP_001138912|]
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S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1B isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tyw1 super family cl34023
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
339-581 1.97e-43

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


The actual alignment was detected with superfamily member COG0731:

Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 156.50  E-value: 1.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 339 ESHRC-----METTPSLACANKCVFCWwhhnnpVGTEWLWKMDQ-----PEMILKEAIENHQNMikqfkgvpgvkaerFE 408
Cdd:COG0731   16 PSRRLgrslgINLIPNKTCNFDCVYCQ------RGRTTDLTRERrefddPEEILEELIEFLRKL--------------PE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 409 EGMTVKHCALSLVGEPIMYPEINRFLKLLHQC-KISSFLVTNAQ---FPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPL 484
Cdd:COG0731   76 EAREPDHITFSGSGEPTLYPNLGELIEEIKKLrGIKTALLTNGSllhRPEVREELLKADQVYPSLDAADEETFRKINRPH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 485 FKDFWQQFLDSLKALA-VKQQRTVYRLMLVKAWNVD--ELQAYAQLVSLGNPDFIEVKgvTYCRESSASSLTMahvPWHE 561
Cdd:COG0731  156 PGLSWERIIEGLELFRkLYKGRTVIETMLVKGINDSeeELEAYAELIKRINPDFVELK--TYMRPPALSRVNM---PSHE 230
                        250       260
                 ....*....|....*....|
gi 628601853 562 EVVQFVRELVDLipEYEIAC 581
Cdd:COG0731  231 ELEEFAERLAEL--GYEVVS 248
Flavodoxin_1 pfam00258
Flavodoxin;
44-186 1.38e-18

Flavodoxin;


:

Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 82.80  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853   44 MQGFATVLAEAV----TSLDLPVAIINLKEYDPDdhlIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFrfg 119
Cdd:pfam00258   6 QTGNTEKLAEAIaeglGEAGFEVDVVDLDDVDET---LSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLE--- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 628601853  120 KTYLKGMRDAVFGLGNSAYaSHFNKVGKNVDKWLWMLGVHRVMSRGEGDcdvVKSKHGSIEANFRAW 186
Cdd:pfam00258  80 DGDLSGLKYAVFGLGDSGY-EGFCGAAKKLDEKLSELGASRVGPLGEGD---EDPQEDGLEEAFEAW 142
 
Name Accession Description Interval E-value
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
339-581 1.97e-43

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: 156.50  E-value: 1.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 339 ESHRC-----METTPSLACANKCVFCWwhhnnpVGTEWLWKMDQ-----PEMILKEAIENHQNMikqfkgvpgvkaerFE 408
Cdd:COG0731   16 PSRRLgrslgINLIPNKTCNFDCVYCQ------RGRTTDLTRERrefddPEEILEELIEFLRKL--------------PE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 409 EGMTVKHCALSLVGEPIMYPEINRFLKLLHQC-KISSFLVTNAQ---FPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPL 484
Cdd:COG0731   76 EAREPDHITFSGSGEPTLYPNLGELIEEIKKLrGIKTALLTNGSllhRPEVREELLKADQVYPSLDAADEETFRKINRPH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 485 FKDFWQQFLDSLKALA-VKQQRTVYRLMLVKAWNVD--ELQAYAQLVSLGNPDFIEVKgvTYCRESSASSLTMahvPWHE 561
Cdd:COG0731  156 PGLSWERIIEGLELFRkLYKGRTVIETMLVKGINDSeeELEAYAELIKRINPDFVELK--TYMRPPALSRVNM---PSHE 230
                        250       260
                 ....*....|....*....|
gi 628601853 562 EVVQFVRELVDLipEYEIAC 581
Cdd:COG0731  231 ELEEFAERLAEL--GYEVVS 248
Wyosine_form pfam08608
Wyosine base formation; Some proteins in this family appear to be important in wyosine base ...
530-593 1.48e-22

Wyosine base formation; Some proteins in this family appear to be important in wyosine base formation in a subset of phenylalanine specific tRNAs. It has been proposed that they participates in converting tRNA(Phe)-m(1)G(37) to tRNA(Phe)-yW.


Pssm-ID: 400775  Cd Length: 63  Bit Score: 91.13  E-value: 1.48e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 628601853  530 LGNPDFIEVKGVTYCrESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAH 593
Cdd:pfam08608   1 PAEPDFVELKAYMHV-GYSRNRLTMKNMPWHEEVEDFAQRLAGSAGDYCLLVEQRRSRVVLLAR 63
Flavodoxin_1 pfam00258
Flavodoxin;
44-186 1.38e-18

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 82.80  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853   44 MQGFATVLAEAV----TSLDLPVAIINLKEYDPDdhlIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFrfg 119
Cdd:pfam00258   6 QTGNTEKLAEAIaeglGEAGFEVDVVDLDDVDET---LSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLE--- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 628601853  120 KTYLKGMRDAVFGLGNSAYaSHFNKVGKNVDKWLWMLGVHRVMSRGEGDcdvVKSKHGSIEANFRAW 186
Cdd:pfam00258  80 DGDLSGLKYAVFGLGDSGY-EGFCGAAKKLDEKLSELGASRVGPLGEGD---EDPQEDGLEEAFEAW 142
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
45-200 1.48e-18

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 89.44  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853  45 QGFATVLAEAVTSLDLPVAIINLKEYDPDDhLIEEvtsKNVcVFLVATYTDGLPTESAEWFCKWLEEAsidfRFGKtyLK 124
Cdd:COG0369   41 EGLAEQLAERAKAAGLAVTLASLDDYKPKD-LAKE---GLL-LIVTSTYGEGEPPDNARAFYEFLHSK----KAPK--LD 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 628601853 125 GMRDAVFGLGNSAYAsHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDvvkskhgsIEANFRAWKTKFISQLQALQKG 200
Cdd:COG0369  110 GLRYAVLGLGDSSYE-TFCQTGKDFDARLEELGATRLLPRVDCDVD--------YEEAAEAWLAAVLAALAEALGA 176
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
46-196 2.15e-06

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 50.87  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853  46 GFATVLAEAVTSlDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLeeasidfrFGKTY--L 123
Cdd:PRK10953  73 GNARRVAEQLRD-DLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFL--------FSKKApkL 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 628601853 124 KGMRDAVFGLGNSAYaSHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVvkskhgsiEANFRAWKTKFISQLQA 196
Cdd:PRK10953 144 ENTAFAVFGLGDTSY-EFFCQAGKDFDSKLAELGAERLLDRVDADVEY--------QAAASEWRARVVDALKS 207
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
348-540 2.10e-03

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: 40.01  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 348 PSLACANKCVFCWwhhnnpvgtEWLWKMDQPEMILKEAIEnhqnmikqfkgvpgVKAERFEEGMTVKHCALSLvGEPIMY 427
Cdd:cd01335    3 LTRGCNLNCGFCS---------NPASKGRGPESPPEIEEI--------------LDIVLEAKERGVEVVILTG-GEPLLY 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 428 PEINRFLKLLHQ--CKISSFLVTNAQFPAE--IRNL--EPVTQLYVSVDASTKDSLKKIDRPLFKdfWQQFLDSLKALAV 501
Cdd:cd01335   59 PELAELLRRLKKelPGFEISIETNGTLLTEelLKELkeLGLDGVGVSLDSGDEEVADKIRGSGES--FKERLEALKELRE 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 628601853 502 KQQRTVYRLMLVKAWN--VDELQAYAQLVSLGNPDFIEVKG 540
Cdd:cd01335  137 AGLGLSTTLLVGLGDEdeEDDLEELELLAEFRSPDRVSLFR 177
 
Name Accession Description Interval E-value
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
339-581 1.97e-43

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: 156.50  E-value: 1.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 339 ESHRC-----METTPSLACANKCVFCWwhhnnpVGTEWLWKMDQ-----PEMILKEAIENHQNMikqfkgvpgvkaerFE 408
Cdd:COG0731   16 PSRRLgrslgINLIPNKTCNFDCVYCQ------RGRTTDLTRERrefddPEEILEELIEFLRKL--------------PE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 409 EGMTVKHCALSLVGEPIMYPEINRFLKLLHQC-KISSFLVTNAQ---FPAEIRNLEPVTQLYVSVDASTKDSLKKIDRPL 484
Cdd:COG0731   76 EAREPDHITFSGSGEPTLYPNLGELIEEIKKLrGIKTALLTNGSllhRPEVREELLKADQVYPSLDAADEETFRKINRPH 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 485 FKDFWQQFLDSLKALA-VKQQRTVYRLMLVKAWNVD--ELQAYAQLVSLGNPDFIEVKgvTYCRESSASSLTMahvPWHE 561
Cdd:COG0731  156 PGLSWERIIEGLELFRkLYKGRTVIETMLVKGINDSeeELEAYAELIKRINPDFVELK--TYMRPPALSRVNM---PSHE 230
                        250       260
                 ....*....|....*....|
gi 628601853 562 EVVQFVRELVDLipEYEIAC 581
Cdd:COG0731  231 ELEEFAERLAEL--GYEVVS 248
Wyosine_form pfam08608
Wyosine base formation; Some proteins in this family appear to be important in wyosine base ...
530-593 1.48e-22

Wyosine base formation; Some proteins in this family appear to be important in wyosine base formation in a subset of phenylalanine specific tRNAs. It has been proposed that they participates in converting tRNA(Phe)-m(1)G(37) to tRNA(Phe)-yW.


Pssm-ID: 400775  Cd Length: 63  Bit Score: 91.13  E-value: 1.48e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 628601853  530 LGNPDFIEVKGVTYCrESSASSLTMAHVPWHEEVVQFVRELVDLIPEYEIACEHEHSNCLLIAH 593
Cdd:pfam08608   1 PAEPDFVELKAYMHV-GYSRNRLTMKNMPWHEEVEDFAQRLAGSAGDYCLLVEQRRSRVVLLAR 63
Flavodoxin_1 pfam00258
Flavodoxin;
44-186 1.38e-18

Flavodoxin;


Pssm-ID: 425562 [Multi-domain]  Cd Length: 142  Bit Score: 82.80  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853   44 MQGFATVLAEAV----TSLDLPVAIINLKEYDPDdhlIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLEEASIDFrfg 119
Cdd:pfam00258   6 QTGNTEKLAEAIaeglGEAGFEVDVVDLDDVDET---LSEIEEEDLLLVVVSTWGEGEPPDNAKPFVDWLLLFGTLE--- 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 628601853  120 KTYLKGMRDAVFGLGNSAYaSHFNKVGKNVDKWLWMLGVHRVMSRGEGDcdvVKSKHGSIEANFRAW 186
Cdd:pfam00258  80 DGDLSGLKYAVFGLGDSGY-EGFCGAAKKLDEKLSELGASRVGPLGEGD---EDPQEDGLEEAFEAW 142
CysJ COG0369
Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases ...
45-200 1.48e-18

Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases [Nucleotide transport and metabolism, Inorganic ion transport and metabolism]; Flavoprotein (flavin reductase) subunit CysJ of sulfite and N-hydroxylaminopurine reductases is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440138 [Multi-domain]  Cd Length: 561  Bit Score: 89.44  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853  45 QGFATVLAEAVTSLDLPVAIINLKEYDPDDhLIEEvtsKNVcVFLVATYTDGLPTESAEWFCKWLEEAsidfRFGKtyLK 124
Cdd:COG0369   41 EGLAEQLAERAKAAGLAVTLASLDDYKPKD-LAKE---GLL-LIVTSTYGEGEPPDNARAFYEFLHSK----KAPK--LD 109
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 628601853 125 GMRDAVFGLGNSAYAsHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDvvkskhgsIEANFRAWKTKFISQLQALQKG 200
Cdd:COG0369  110 GLRYAVLGLGDSSYE-TFCQTGKDFDARLEELGATRLLPRVDCDVD--------YEEAAEAWLAAVLAALAEALGA 176
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
352-523 1.69e-06

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: 48.29  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853  352 CANKCVFCwwhHNNPVGTEWLWKMDQPEMILKEAIENHQNMIKQFkgvpgvkaerfeegmtvkhcaLSLVGEPIMYPEIN 431
Cdd:pfam04055   5 CNLRCTYC---AFPSIRARGKGRELSPEEILEEAKELKRLGVEVV---------------------ILGGGEPLLLPDLV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853  432 RFLKLLHQCKISS----FLVTNAQFPAE--IRNL--EPVTQLYVSVDASTKDSLKKIDRplfKDFWQQFLDSLKAL-AVK 502
Cdd:pfam04055  61 ELLERLLKLELAEgiriTLETNGTLLDEelLELLkeAGLDRVSIGLESGDDEVLKLINR---GHTFEEVLEALELLrEAG 137
                         170       180
                  ....*....|....*....|.
gi 628601853  503 QQRTVYRLMLVKAWNVDELQA 523
Cdd:pfam04055 138 IPVVTDNIVGLPGETDEDLEE 158
cysJ PRK10953
NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;
46-196 2.15e-06

NADPH-dependent assimilatory sulfite reductase flavoprotein subunit;


Pssm-ID: 182862 [Multi-domain]  Cd Length: 600  Bit Score: 50.87  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853  46 GFATVLAEAVTSlDLPVAIINLKEYDPDDHLIEEVTSKNVCVFLVATYTDGLPTESAEWFCKWLeeasidfrFGKTY--L 123
Cdd:PRK10953  73 GNARRVAEQLRD-DLLAAKLNVNLVNAGDYKFKQIAQEKLLIVVTSTQGEGEPPEEAVALHKFL--------FSKKApkL 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 628601853 124 KGMRDAVFGLGNSAYaSHFNKVGKNVDKWLWMLGVHRVMSRGEGDCDVvkskhgsiEANFRAWKTKFISQLQA 196
Cdd:PRK10953 144 ENTAFAVFGLGDTSY-EFFCQAGKDFDSKLAELGAERLLDRVDADVEY--------QAAASEWRARVVDALKS 207
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
345-500 8.38e-04

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: 40.66  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 345 ETTPslACANKCVFCWWhhnnpvgteWLWKMDQPEMILKEAIEnhqnMIKQFKGvpgvkaerfeegMTVKHCALSlVGEP 424
Cdd:COG0535    5 ELTN--RCNLRCKHCYA---------DAGPKRPGELSTEEAKR----ILDELAE------------LGVKVVGLT-GGEP 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 425 IMYPEINRFLKLLHQCKISSFLVTNAQF--PAEIRNLEP--VTQLYVSVDASTKDSLKKIdRPLFKDFwQQFLDSLKALA 500
Cdd:COG0535   57 LLRPDLFELVEYAKELGIRVNLSTNGTLltEELAERLAEagLDHVTISLDGVDPETHDKI-RGVPGAF-DKVLEAIKLLK 134
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
348-540 2.10e-03

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: 40.01  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 348 PSLACANKCVFCWwhhnnpvgtEWLWKMDQPEMILKEAIEnhqnmikqfkgvpgVKAERFEEGMTVKHCALSLvGEPIMY 427
Cdd:cd01335    3 LTRGCNLNCGFCS---------NPASKGRGPESPPEIEEI--------------LDIVLEAKERGVEVVILTG-GEPLLY 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 628601853 428 PEINRFLKLLHQ--CKISSFLVTNAQFPAE--IRNL--EPVTQLYVSVDASTKDSLKKIDRPLFKdfWQQFLDSLKALAV 501
Cdd:cd01335   59 PELAELLRRLKKelPGFEISIETNGTLLTEelLKELkeLGLDGVGVSLDSGDEEVADKIRGSGES--FKERLEALKELRE 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 628601853 502 KQQRTVYRLMLVKAWN--VDELQAYAQLVSLGNPDFIEVKG 540
Cdd:cd01335  137 AGLGLSTTLLVGLGDEdeEDDLEELELLAEFRSPDRVSLFR 177
 
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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