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Conserved domains on  [gi|20302057|ref|NP_620236|]
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S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 [Rattus norvegicus]

Protein Classification

radical SAM protein( domain architecture ID 11500009)

radical SAM protein generates radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfer of a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
 11-360 0e+00

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


:

Pssm-ID: 212001  Cd Length: 347  Bit Score: 776.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    11 LLSLFQQQLGSLWSGLAMLFCWLRIALGWPDPGKGQPRVRGEPkETQETHEDPgsAQPTTPVSVNYHFTRQCNYKCGFCF 90
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEP-TRKEEEEDP--DQPTTPTSVNYHFTRQCNYKCGFCF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    91 HTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGD 170
Cdd:TIGR04278  78 HTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   171 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCL 250
Cdd:TIGR04278 158 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   251 LIEGENSGEDALREAERFLISNEEFEAFLQRHKDVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSRSILDVGVEE 330
Cdd:TIGR04278 238 LIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEE 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 20302057   331 AIKFSGFDEKMFLKRGGKYVWSKADLKLDW 360
Cdd:TIGR04278 318 AIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
 11-360 0e+00

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 776.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    11 LLSLFQQQLGSLWSGLAMLFCWLRIALGWPDPGKGQPRVRGEPkETQETHEDPgsAQPTTPVSVNYHFTRQCNYKCGFCF 90
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEP-TRKEEEEDP--DQPTTPTSVNYHFTRQCNYKCGFCF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    91 HTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGD 170
Cdd:TIGR04278  78 HTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   171 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCL 250
Cdd:TIGR04278 158 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   251 LIEGENSGEDALREAERFLISNEEFEAFLQRHKDVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSRSILDVGVEE 330
Cdd:TIGR04278 238 LIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEE 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 20302057   331 AIKFSGFDEKMFLKRGGKYVWSKADLKLDW 360
Cdd:TIGR04278 318 AIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
 73-347 2.14e-102

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 302.93  E-value: 2.14e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   73 SVNYHFTRQCNYKCGFCFHTAKTSF---------VLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQdrGEYLGKLVRFCK 143
Cdd:NF038283   3 VINWHLTEACNYRCKYCFAKWNDVKsprhhdkghLEKLLEELAEFFKLLSYGFVRINFAGGEPLLY--PDRLLDLIKLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  144 EeLALpSVSIVSNGSLIRERWFKDYGDYLDILAISCDSFDEQVNVLIGRGQGKKN--HVENLQKLRKWCRDY--KVAFKI 219
Cdd:NF038283  81 E-LGF-KTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRvlSLEELLELIALIRQInpNIKLKI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  220 NSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENsgedalreaERFLISNEEFEAFLQRHKDV-SCLVPESNQKMKD 298
Cdd:NF038283 159 NTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQN---------DDLLISDEQFDAFVERHKALgSIIVAEDNDDMTG 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20302057  299 SYLILDEYMRFL-NCTGGRK-DPSRSILDVGVEEAIKFSGFDEKMFLKRGG 347
Cdd:NF038283 230 SYLMIDPEGRFFqNSGGGKGyRYSEPILEVGVEEALSQINFDPEKFLSRYG 280
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 77-254 3.24e-23

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 95.86  E-value: 3.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  77 HFTRQCNYKCGFCFHTAKTSFVLPL----EEAKRGLLLLKQAGMEKINFSGGEPFLQdrgEYLGKLVRFCKEELALPSVS 152
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLY---PELAELLRRLKKELPGFEIS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057 153 IVSNGSLIRERWFKDYGDY-LDILAISCDSFDEQVNVLIGRGQGKKNhvENLQKLRKWcRDYKVAFKINSVINRFNVD-E 230
Cdd:cd01335  79 IETNGTLLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKEL-REAGLGLSTTLLVGLGDEDeE 155

                       170       180
                ....*....|....*....|....*...
gi 20302057 231 DMNEHIKAL----SPVRWKVFQCLLIEG 254
Cdd:cd01335 156 DDLEELELLaefrSPDRVSLFRLLPEEG 183
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 73-222 3.19e-19

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: 83.41  E-value: 3.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  73 SVNYHFTRQCNYKCGFCFHTAKTSFV--LPLEEAKRGLLLLKQAGMEKINFSGGEPFLqdRgEYLGKLVRFCKEelALPS 150
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPgeLSTEEAKRILDELAELGVKVVGLTGGEPLL--R-PDLFELVEYAKE--LGIR 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20302057 151 VSIVSNGSLIRE---RWFKDYGdyLDILAISCDSFDEQVNVLIGRGQGKKNHV-ENLqklrKWCRDYKVAFKINSV 222
Cdd:COG0535  76 VNLSTNGTLLTEelaERLAEAG--LDHVTISLDGVDPETHDKIRGVPGAFDKVlEAI----KLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 78-235 9.91e-18

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: 79.49  E-value: 9.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    78 FTRQCNYKCGFCF----HTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFcKEELALPSVSI 153
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLK-LELAEGIRITL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   154 VSNGSLIRERWFKDYGDY-LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKwcRDYKVAfKINSVINRFNVDEDM 232
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLRE--AGIPVV-TDNIVGLPGETDEDL 156


                  ...
gi 20302057   233 NEH 235
Cdd:pfam04055 157 EET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 76-254 4.60e-13

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: 67.43  E-value: 4.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057     76 YHFTRQCNYKCGFC--FHTAKTSFVLPLEEAKRGLLLLKQAG-----MEKINFSGGEPFLQDRgEYLGKLVRFCKEELAL 148
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSP-EQLEELLEAIREILGL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    149 P---SVSIVSNGSLIRERWFKDYGDY-LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKwcrdykvAFKINsvin 224
Cdd:smart00729  84 AkdvEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLRE-------AGPIK---- 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 20302057    225 rFNVD-------------EDMNEHIKALSPVRWKVFQCLLIEG 254
Cdd:smart00729 153 -VSTDlivglpgeteedfEETLKLLKELGPDRVSIFPLSPRPG 194
moaA PRK00164
GTP 3',8-cyclase MoaA;
72-237 1.33e-07

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 52.45  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   72 VSVnyhfTRQCNYKCGFCFHTAKTSF-----VLPLEEAKRgllLLKQA---GMEKINFSGGEPFL-QDrgeyLGKLVRFC 142
Cdd:PRK00164  21 ISV----TDRCNFRCTYCMPEGYLPFlpkeeLLSLEEIER---LVRAFvalGVRKVRLTGGEPLLrKD----LEDIIAAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  143 KEELALPSVSIVSNGSLIRER---WfKDYGdyLDILAISCDSFDEQVNVLI-GRGqgkknhvenlqKLRKWCRDYKVAF- 217
Cdd:PRK00164  90 AALPGIRDLALTTNGYLLARRaaaL-KDAG--LDRVNVSLDSLDPERFKAItGRD-----------RLDQVLAGIDAALa 155

                        170       180
                 ....*....|....*....|....*....
gi 20302057  218 ------KINSVINR-FNVDE--DMNEHIK 237
Cdd:PRK00164 156 agltpvKVNAVLMKgVNDDEipDLLEWAK 184
 
Name Accession Description Interval E-value
viperin TIGR04278
antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, ...
 11-360 0e+00

antiviral radical SAM protein viperin; Viperin (Virus Inhibitory Protein, ER-associated, Iterferon-inducible) is a radical SAM enzyme found in human and other vertebrates. It is both induced by interferon and demonstrably active in blocking replication by several types of virus, apparently by modifying lipid chemistries in lipid droplets and membrane rafts.


Pssm-ID: 212001  Cd Length: 347  Bit Score: 776.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    11 LLSLFQQQLGSLWSGLAMLFCWLRIALGWPDPGKGQPRVRGEPkETQETHEDPgsAQPTTPVSVNYHFTRQCNYKCGFCF 90
Cdd:TIGR04278   1 LLSAFRQPLGSLWSSLLSLLCWLRAALWLAGSEKSRQQLRGEP-TRKEEEEDP--DQPTTPTSVNYHFTRQCNYKCGFCF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    91 HTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGD 170
Cdd:TIGR04278  78 HTAKTSFVLPLEEAKRGLRLLKEAGMEKINFSGGEPFLHDRGEFLGKLVQFCKEELQLPSVSIVSNGSLIRERWFKKYGE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   171 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCL 250
Cdd:TIGR04278 158 YLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRNWCRDYKVAFKINSVINRFNVEEDMREQIKALNPVRWKVFQCL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   251 LIEGENSGEDALREAERFLISNEEFEAFLQRHKDVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSRSILDVGVEE 330
Cdd:TIGR04278 238 LIEGENAGEDALREAERFVISDEEFEGFLERHKSVSCLVPESNQKMRDSYLILDEYMRFLNCRNGRKDPSKSILDVGVEE 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 20302057   331 AIKFSGFDEKMFLKRGGKYVWSKADLKLDW 360
Cdd:TIGR04278 318 AIKFSGFDEKMFLKRGGKYVWSKADMKLDW 347
viperin_w_prok NF038283
viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme ...
 73-347 2.14e-102

viperin family antiviral radical SAM protein; Homologs of a viral defense radical SAM enzyme found in Homo sapiens, viperin (RSAD2), occur in prokaryotes with a strong bias toward placement in phage defense islands, encoded next to CRISPR system and restriction enzyme genes. Further investigation shows members indeed perform the anti-viral function of synthesizing modified ribonucleotides such as ddhCTP, ddh-guanosine triphosphate (ddhGTP) and ddh-uridine triphosphate (ddhUTP). Those non-standard ribonucleotides can interfere with viral replication machinery.


Pssm-ID: 468450 [Multi-domain]  Cd Length: 280  Bit Score: 302.93  E-value: 2.14e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   73 SVNYHFTRQCNYKCGFCFHTAKTSF---------VLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQdrGEYLGKLVRFCK 143
Cdd:NF038283   3 VINWHLTEACNYRCKYCFAKWNDVKsprhhdkghLEKLLEELAEFFKLLSYGFVRINFAGGEPLLY--PDRLLDLIKLAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  144 EeLALpSVSIVSNGSLIRERWFKDYGDYLDILAISCDSFDEQVNVLIGRGQGKKN--HVENLQKLRKWCRDY--KVAFKI 219
Cdd:NF038283  81 E-LGF-KTSIITNGSLLTEEFLEELAPYLDWIGISIDSANEETNRKIGRVDRKGRvlSLEELLELIALIRQInpNIKLKI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  220 NSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENsgedalreaERFLISNEEFEAFLQRHKDV-SCLVPESNQKMKD 298
Cdd:NF038283 159 NTVVNRLNWDEDLSELIRELNPDRWKVLQVLPVVGQN---------DDLLISDEQFDAFVERHKALgSIIVAEDNDDMTG 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 20302057  299 SYLILDEYMRFL-NCTGGRK-DPSRSILDVGVEEAIKFSGFDEKMFLKRGG 347
Cdd:NF038283 230 SYLMIDPEGRFFqNSGGGKGyRYSEPILEVGVEEALSQINFDPEKFLSRYG 280
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 77-254 3.24e-23

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


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 95.86  E-value: 3.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  77 HFTRQCNYKCGFCFHTAKTSFVLPL----EEAKRGLLLLKQAGMEKINFSGGEPFLQdrgEYLGKLVRFCKEELALPSVS 152
Cdd:cd01335   2 ELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLY---PELAELLRRLKKELPGFEIS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057 153 IVSNGSLIRERWFKDYGDY-LDILAISCDSFDEQVNVLIGRGQGKKNhvENLQKLRKWcRDYKVAFKINSVINRFNVD-E 230
Cdd:cd01335  79 IETNGTLLTEELLKELKELgLDGVGVSLDSGDEEVADKIRGSGESFK--ERLEALKEL-REAGLGLSTTLLVGLGDEDeE 155

                       170       180
                ....*....|....*....|....*...
gi 20302057 231 DMNEHIKAL----SPVRWKVFQCLLIEG 254
Cdd:cd01335 156 DDLEELELLaefrSPDRVSLFRLLPEEG 183
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 73-222 3.19e-19

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: 83.41  E-value: 3.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  73 SVNYHFTRQCNYKCGFCFHTAKTSFV--LPLEEAKRGLLLLKQAGMEKINFSGGEPFLqdRgEYLGKLVRFCKEelALPS 150
Cdd:COG0535   1 RLQIELTNRCNLRCKHCYADAGPKRPgeLSTEEAKRILDELAELGVKVVGLTGGEPLL--R-PDLFELVEYAKE--LGIR 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20302057 151 VSIVSNGSLIRE---RWFKDYGdyLDILAISCDSFDEQVNVLIGRGQGKKNHV-ENLqklrKWCRDYKVAFKINSV 222
Cdd:COG0535  76 VNLSTNGTLLTEelaERLAEAG--LDHVTISLDGVDPETHDKIRGVPGAFDKVlEAI----KLLKEAGIPVGINTV 145
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 78-235 9.91e-18

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: 79.49  E-value: 9.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    78 FTRQCNYKCGFCF----HTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFcKEELALPSVSI 153
Cdd:pfam04055   1 ITRGCNLRCTYCAfpsiRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLLK-LELAEGIRITL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   154 VSNGSLIRERWFKDYGDY-LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKwcRDYKVAfKINSVINRFNVDEDM 232
Cdd:pfam04055  80 ETNGTLLDEELLELLKEAgLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLRE--AGIPVV-TDNIVGLPGETDEDL 156


                  ...
gi 20302057   233 NEH 235
Cdd:pfam04055 157 EET 159
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
 76-254 4.60e-13

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: 67.43  E-value: 4.60e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057     76 YHFTRQCNYKCGFC--FHTAKTSFVLPLEEAKRGLLLLKQAG-----MEKINFSGGEPFLQDRgEYLGKLVRFCKEELAL 148
Cdd:smart00729   5 YIITRGCPRRCTFCsfPSLRGKLRSRYLEALVREIELLAEKGekeglVGTVFIGGGTPTLLSP-EQLEELLEAIREILGL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    149 P---SVSIVSNGSLIRERWFKDYGDY-LDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKwcrdykvAFKINsvin 224
Cdd:smart00729  84 AkdvEITIETRPDTLTEELLEALKEAgVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLRE-------AGPIK---- 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 20302057    225 rFNVD-------------EDMNEHIKALSPVRWKVFQCLLIEG 254
Cdd:smart00729 153 -VSTDlivglpgeteedfEETLKLLKELGPDRVSIFPLSPRPG 194
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
 79-281 2.20e-11

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


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 64.24  E-value: 2.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  79 TRQCNYKCGFCF---HTAKTSFVLPLEEAKRGLLLLKQAGME----KINFSGGEPFLqdRGEYLGKLVRFCKEELALP-- 149
Cdd:COG0641   8 TSRCNLRCSYCYyseGDEGSRRRMSEETAEKAIDFLIESSGPgkelTITFFGGEPLL--NFDFIKEIVEYARKYAKKGkk 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057 150 -SVSIVSNGSLIRERW---FKDYGDYldiLAISCDSfDEQVN----VLIGrgqGKKNH---VENLQKLRKwcrdYKVAFK 218
Cdd:COG0641  86 iRFSIQTNGTLLDDEWidfLKENGFS---VGISLDG-PKEIHdrnrVTKN---GKGSFdrvMRNIKLLKE----HGVEVN 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20302057 219 INSVINRFNVD--EDMNEHIKALspvRWKVFQCLLIEGENSGEDALREaerflisnEEFEAFLQR 281
Cdd:COG0641 155 IRCTVTRENLDdpEELYDFLKEL---GFRSIQFNPVVEEGEADYSLTP--------EDYGEFLIE 208
moaA PRK00164
GTP 3',8-cyclase MoaA;
72-237 1.33e-07

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 52.45  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   72 VSVnyhfTRQCNYKCGFCFHTAKTSF-----VLPLEEAKRgllLLKQA---GMEKINFSGGEPFL-QDrgeyLGKLVRFC 142
Cdd:PRK00164  21 ISV----TDRCNFRCTYCMPEGYLPFlpkeeLLSLEEIER---LVRAFvalGVRKVRLTGGEPLLrKD----LEDIIAAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  143 KEELALPSVSIVSNGSLIRER---WfKDYGdyLDILAISCDSFDEQVNVLI-GRGqgkknhvenlqKLRKWCRDYKVAF- 217
Cdd:PRK00164  90 AALPGIRDLALTTNGYLLARRaaaL-KDAG--LDRVNVSLDSLDPERFKAItGRD-----------RLDQVLAGIDAALa 155

                        170       180
                 ....*....|....*....|....*....
gi 20302057  218 ------KINSVINR-FNVDE--DMNEHIK 237
Cdd:PRK00164 156 agltpvKVNAVLMKgVNDDEipDLLEWAK 184
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
 72-282 1.75e-07

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: 52.37  E-value: 1.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  72 VSVnyhfTRQCNYKCGFC-----FHTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQdRGeyLGKLVRFCKEEL 146
Cdd:COG2896  18 ISV----TDRCNFRCTYCmpeegYQFLPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLR-KD--LPELIARLAALP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057 147 ALPSVSIVSNGSLIRER--WFKDYGdyLDILAISCDSFDEQVNVLIGRGqGKKNHV-ENLQKLRkwcrdyKVAF---KIN 220
Cdd:COG2896  91 GIEDLALTTNGSLLARYaeALKAAG--LDRVNVSLDSLDPERFRRITRR-DDLDKVlAGIDAAL------AAGLtpvKIN 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057 221 SVINR-FNVDE--DMNEHIKALS-PVRwkvfqclLIE----GENSGEDalreAERFlISNEEFEAFLQRH 282
Cdd:COG2896 162 AVVMRgVNDDEilDLLEFAKERGiDLR-------FIElmplGEGGGWR----RDQV-VSAAEILERLEAR 219
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 78-177 4.55e-07

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 50.18  E-value: 4.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  78 FTRQCNYKCGFCfH---------TAKTSFVLP---LEEAKRGLLLLKQAGMekINFSGGEPFLQdrGEYLGKLVRFCKEE 145
Cdd:COG1180  27 FTQGCNLRCPYC-HnpeisqgrpDAAGRELSPeelVEEALKDRGFLDSCGG--VTFSGGEPTLQ--PEFLLDLAKLAKEL 101

                        90       100       110
                ....*....|....*....|....*....|...
gi 20302057 146 -LAlpsVSIVSNGSLIRERwFKDYGDYLDILAI 177
Cdd:COG1180 102 gLH---TALDTNGYIPEEA-LEELLPYLDAVNI 130
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
 70-230 1.03e-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: 49.85  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    70 TPVSVNYHFTRQCNYKCGFCFH---TAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQ-DRGEYLGKLV----RF 141
Cdd:TIGR04250   1 TPRSVDIDITGRCNLRCRYCSHfssAAETPTDLETAEWLRFFRELNRCSVLRVVLSGGEPFMRsDFREIIDGIVknrmRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   142 ckeelalpsvSIVSNGSLIRErwfkDYGDYL------DILAISCD-SFDEQVNVLIGRGQGKKNhVENLQKLRKwcrdYK 214
Cdd:TIGR04250  81 ----------SILSNGTLITD----AIASFLaatrrcDYVQVSIDgSTPGTHDRLRGTGSFLQA-VEGIELLRK----HA 141

                         170
                  ....*....|....*.
gi 20302057   215 VAFKINSVINRFNVDE 230
Cdd:TIGR04250 142 IPVVVRVTIHRWNVDD 157
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
 81-211 8.96e-06

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 46.34  E-value: 8.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057  81 QCNYKCGFC------FHTAKTSFVLPLEEAKRGLL-LLKQAGMEKIN-----FSG-GEPFLQdrgEYLGKLVRFCKEELA 147
Cdd:COG0731  33 TCNFDCVYCqrgrttDLTRERREFDDPEEILEELIeFLRKLPEEAREpdhitFSGsGEPTLY---PNLGELIEEIKKLRG 109

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20302057 148 LPsVSIVSNGSLI-----RERWFKdygdyLDILAISCDSFDEQVNVLIGRGQGK---KNHVENLQKLRKWCR 211
Cdd:COG0731 110 IK-TALLTNGSLLhrpevREELLK-----ADQVYPSLDAADEETFRKINRPHPGlswERIIEGLELFRKLYK 175
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
 24-230 9.05e-05

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 43.98  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   24 SGLAMLFCWLRiALGWPDPGKGQPRVRGEpketqethEDPGSAQPTTPVSVNYH----------FTRQCNYKCGFCFHTA 93
Cdd:PLN02951   9 LGFRSSSFQLQ-EPGSSIFSASSSYAADQ--------VDPEASNPVSDMLVDSFgrrhnylrisLTERCNLRCQYCMPEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   94 -----KTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRgeyLGKLVRFCKEELALPSVSIVSNG-SLIRE-RWFK 166
Cdd:PLN02951  80 gveltPKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKD---IEDICLQLSSLKGLKTLAMTTNGiTLSRKlPRLK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20302057  167 DYGdyLDILAISCDSFDEQVNVLIGRgqgKKNHVENLQKLRKWCRDYKVAFKINSVINR-FNVDE 230
Cdd:PLN02951 157 EAG--LTSLNISLDTLVPAKFEFLTR---RKGHDRVLESIDTAIELGYNPVKVNCVVMRgFNDDE 216
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 82-175 2.78e-04

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 40.62  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    82 CNYKCGFCFHTA----KTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDrgEYLGKLVRFCKEElaLPSVSIVS-N 156
Cdd:pfam13353  15 CNHHCKGCFNPEtwdfKYGKPFTEELEDEIIEDLAKPYIQGLTLSGGEPLLNA--EALLELVKRVREE--CPEKDIWLwT 90

                          90       100
                  ....*....|....*....|..
gi 20302057   157 GSL---IRERWFKDYGDYLDIL 175
Cdd:pfam13353  91 GYTfeeLQSKDQLELLKLIDVL 112
rSAM_Cxxx_rpt TIGR04115
radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain ...
 73-129 6.94e-04

radical SAM peptide maturase, CXXX-repeat target family; Members of this radical SAM domain protein are predicted peptide maturases, similar to PqqE, AlbA, the mycofactocin radical SAM maturase, and many others that share the peptide modification radical SAM protein C-terminal additional 4Fe4S-binding domain (TIGR04085). Members co-occur with a protein of unknown function that may be a chaperone or immunity protein and with a peptide that may have twelve or more cysteines occurring regularly spaced every fourth residue. These Cys residues tend to be flanked by residues with small side chains that provide minimal steric hindrance to crosslink formation by the radical SAM enzyme as in the subtilosin A system.


Pssm-ID: 200366 [Multi-domain]  Cd Length: 359  Bit Score: 41.03  E-value: 6.94e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20302057    73 SVNYHFTRQCNYKCGFCFHTAKTSF-VLPLEEAKRG--LLLLKQAGMEK----INFSGGEPFLQ 129
Cdd:TIGR04115   3 SITFIVTDDCQLACKYCYQTGKNKNkRMSFETAKKAvdYILSGNKGFGEpsviWDFIGGEPLLE 66
PRK13758 PRK13758
anaerobic sulfatase-maturase; Provisional
 82-225 5.57e-03

anaerobic sulfatase-maturase; Provisional


Pssm-ID: 172296 [Multi-domain]  Cd Length: 370  Bit Score: 38.36  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057   82 CNYKCGFCFH-------TAKTSFVLPLE--EAKRGLLLLKQAGMEKINFSGGEPFLQDRgEYLGKLVRFCKE----ELAL 148
Cdd:PRK13758  15 CNLKCTYCFYhslsdnrNVKSYGIMRDEvlESMVKRVLNEAEGHCSFAFQGGEPTLAGL-EFFEELMELQRKhnykNLKI 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20302057  149 PSvSIVSNGSLIRERWFKDYGDYLDILAISCDSFDE--QVNVLIGRGQGKKNHVENLQKLRKwcrDYKVAFKINSVINR 225
Cdd:PRK13758  94 YN-SLQTNGTLIDESWAKFLSENKFLVGLSMDGPKEihNLNRKDCCGLDTFSKVERAAELFK---KYKVEFNILCVVTS 168
Fer4_14 pfam13394
4Fe-4S single cluster domain;
82-176 8.61e-03

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 35.80  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20302057    82 CNYKCGFCFH------TAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVS 155
Cdd:pfam13394   6 CNHSCPGCDNketwkfNYGEPFTEELEDQIIADLKDSYIKRQGLVLTGGEPLHPWNLPVLLKLLKRVKEEYPSKDIWLET 85

                          90       100
                  ....*....|....*....|.
gi 20302057   156 NGSLIRERWFKDYGDYLDILA 176
Cdd:pfam13394  86 GYTLAIDFEYPDTEEQLFTLS 106
 
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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