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Conserved domains on  [gi|1019415703|emb|SAL13499|]
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radical SAM domain-containing protein [Caballeronia turbans]

Protein Classification

HpnR_B12_rSAM family protein( domain architecture ID 11500119)

HpnR_B12_rSAM family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HpnR_B12_rSAM TIGR04367
hopanoid C-3 methylase HpnR; Members of this are family are a B12-binding domain/radical SAM ...
1-489 0e+00

hopanoid C-3 methylase HpnR; Members of this are family are a B12-binding domain/radical SAM domain protein required for 3-methylhopanoid production. Activity was confirmed by mutant phenotype by disrupting this gene in Methylococcus capsulatus strain Bath. This protein family should only occur in genomes that encode a squalene-hopene cyclase (see TIGR01507). [Fatty acid and phospholipid metabolism, Biosynthesis]


:

Pssm-ID: 275160 [Multi-domain]  Cd Length: 490  Bit Score: 966.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   1 MKVLAVHPSGLMYTRVFLRLEPLGLETVAAAVRQAGHDVRLIDLQVETHRDFDRLVRAWRPDALCFSGNYLANIPEIIDL 80
Cdd:TIGR04367   1 MKVLAVHPSPLMYTKIFLRLEPLGLELVAGAARRAGHEVRLIDLQVESHADYLRLLESFRPDVVGFSLNYLANVPEVIDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  81 ARTVKTLLPDCFVFVGGHSASFTASDILRHAEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPGAVTTDGSGPPPRFVE 160
Cdd:TIGR04367  81 AKETKRRLPGCFVFVGGHSASFVARELLEHAEGAIDCVLRGEGEASAPLLLEAVADGGDLLTVPGVVTLEGEGPPPRFLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 161 SLDDVLPARDLLRHRRKYFIGTLDPCASIEFARGCPWDCTFCSAWTFYGRSYRSRSPEIIAKELASIREPGVFIVDDVAF 240
Cdd:TIGR04367 161 SLDEPRPARDLLRHRRKYFIGVLDPCASIEFTRGCPWDCSFCSAWTFYGRSYRTLSPEVAGEELARIREPGIFIVDDVAF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 241 VHAEHGMEIGRAIERHGIRKKYYLETRGDVLLRNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFA 320
Cdd:TIGR04367 241 IHAEHGMAIGEAIERRGIRKEYYLETRGDVLLRNKEVFEFWKRLGLKYMFLGLEAIDAEGLKLFRKRVSLDKNFEALEFA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 321 RSLGITVALNLIADPEWDRERFETVRQWCLDIPEIVNISVNTPYPGTEIWLREQRRLTSLDYRLYDIQHSVLPTRLPLPE 400
Cdd:TIGR04367 321 RSLGITVAINLIADPDWDRERFEVIRQWCLEIPEIVNISVNTPYPGTEIWHTESRKLTTRDYRLFDIQHAVLPTTLPLEE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 401 FYAELVRTQQVLNRKHMGWAALRGAAGQAMHLLMHGQTNFVRMLWRFNSVFDPRLQLADHAREARYLMTPPPAP-DASAN 479
Cdd:TIGR04367 401 FYEELVKTQQVLNRKHLGWRALRGTAGIVARLLARGQTNFLRMLWKFNSVYNPELQLADHARPVRYEMAPPPAPsTQKPD 480
                         490
                  ....*....|
gi 1019415703 480 VKAVYVHGPA 489
Cdd:TIGR04367 481 PKTLYVHQPA 490
 
Name Accession Description Interval E-value
HpnR_B12_rSAM TIGR04367
hopanoid C-3 methylase HpnR; Members of this are family are a B12-binding domain/radical SAM ...
1-489 0e+00

hopanoid C-3 methylase HpnR; Members of this are family are a B12-binding domain/radical SAM domain protein required for 3-methylhopanoid production. Activity was confirmed by mutant phenotype by disrupting this gene in Methylococcus capsulatus strain Bath. This protein family should only occur in genomes that encode a squalene-hopene cyclase (see TIGR01507). [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 275160 [Multi-domain]  Cd Length: 490  Bit Score: 966.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   1 MKVLAVHPSGLMYTRVFLRLEPLGLETVAAAVRQAGHDVRLIDLQVETHRDFDRLVRAWRPDALCFSGNYLANIPEIIDL 80
Cdd:TIGR04367   1 MKVLAVHPSPLMYTKIFLRLEPLGLELVAGAARRAGHEVRLIDLQVESHADYLRLLESFRPDVVGFSLNYLANVPEVIDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  81 ARTVKTLLPDCFVFVGGHSASFTASDILRHAEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPGAVTTDGSGPPPRFVE 160
Cdd:TIGR04367  81 AKETKRRLPGCFVFVGGHSASFVARELLEHAEGAIDCVLRGEGEASAPLLLEAVADGGDLLTVPGVVTLEGEGPPPRFLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 161 SLDDVLPARDLLRHRRKYFIGTLDPCASIEFARGCPWDCTFCSAWTFYGRSYRSRSPEIIAKELASIREPGVFIVDDVAF 240
Cdd:TIGR04367 161 SLDEPRPARDLLRHRRKYFIGVLDPCASIEFTRGCPWDCSFCSAWTFYGRSYRTLSPEVAGEELARIREPGIFIVDDVAF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 241 VHAEHGMEIGRAIERHGIRKKYYLETRGDVLLRNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFA 320
Cdd:TIGR04367 241 IHAEHGMAIGEAIERRGIRKEYYLETRGDVLLRNKEVFEFWKRLGLKYMFLGLEAIDAEGLKLFRKRVSLDKNFEALEFA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 321 RSLGITVALNLIADPEWDRERFETVRQWCLDIPEIVNISVNTPYPGTEIWLREQRRLTSLDYRLYDIQHSVLPTRLPLPE 400
Cdd:TIGR04367 321 RSLGITVAINLIADPDWDRERFEVIRQWCLEIPEIVNISVNTPYPGTEIWHTESRKLTTRDYRLFDIQHAVLPTTLPLEE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 401 FYAELVRTQQVLNRKHMGWAALRGAAGQAMHLLMHGQTNFVRMLWRFNSVFDPRLQLADHAREARYLMTPPPAP-DASAN 479
Cdd:TIGR04367 401 FYEELVKTQQVLNRKHLGWRALRGTAGIVARLLARGQTNFLRMLWKFNSVYNPELQLADHARPVRYEMAPPPAPsTQKPD 480
                         490
                  ....*....|
gi 1019415703 480 VKAVYVHGPA 489
Cdd:TIGR04367 481 PKTLYVHQPA 490
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
1-397 1.65e-95

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 294.93  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   1 MKVLAVHPSglmytrvFLRLEPLGLETVAAAVRQAGHDVRLIDLQVEtHRDFDRLVR--AWRPDALCFSGnYLANIPEII 78
Cdd:COG1032     1 MKVLLVYPP-------KYPVPPLGLAYLAALLEEAGYEVRIVDLNAE-DRSLEDLLKplREDPDLVGISL-YTPQYPNAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  79 DLARTVKTLLPDCFVFVGGHSASFTASDILrhaEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPGAVTTDGSG----P 154
Cdd:COG1032    72 ELARLIKERNPGVPIVLGGPHASLNPEELL---EPFADFVVIGEGEETLPELLEALEEGRDLADIPGLAYRDDGRivqnP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 155 PPRFVESLDDV-LPARDLLRHRRKYFIgtldpcASIEFARGCPWDCTFCSAWTFYGRSYRSRSPEIIAKELASIRE---- 229
Cdd:COG1032   149 PRPLIEDLDELpFPAYDLLDLEAYHRR------ASIETSRGCPFGCSFCSISALYGRKVRYRSPESVVEEIEELVKrygi 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 230 PGVFIVDDVAFVHAEHGMEIGRAIERHGIRKKYYLETRGDVLlrNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRIT 309
Cdd:COG1032   223 REIFFVDDNFNVDKKRLKELLEELIERGLNVSFPSEVRVDLL--DEELLELLKKAGCRGLFIGIESGSQRVLKAMNKGIT 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 310 LDKNFEALEFARSLGITVALNLIAD-PEWDRERFETVRQWCLDI-PEIVNISVNTPYPGTEIWLREQRRLTSLDYRLY-D 386
Cdd:COG1032   301 VEDILEAVRLLKKAGIRVKLYFIIGlPGETEEDIEETIEFIKELgPDQAQVSIFTPLPGTPLYEELEKEGRLYDWEKYeD 380
                         410
                  ....*....|.
gi 1019415703 387 IQHSVLPTRLP 397
Cdd:COG1032   381 LLEAVLAPRLS 391
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
14-131 7.83e-24

B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding.


Pssm-ID: 426713 [Multi-domain]  Cd Length: 121  Bit Score: 96.24  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  14 TRVFLRLEPLGLETVAAAVRQAGHDVRLIDLQVEtHRDFDRLVRAWRPDALCFSGNYLANIPEIIDLARTVKTLLPDCFV 93
Cdd:pfam02310   6 ATVGGDLHPLGLNYVAAALRAAGFEVIILGANVP-PEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRPRVKV 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1019415703  94 FVGGHSASFTASDILRHAEGaIDCVLKGEGEASVNALL 131
Cdd:pfam02310  85 VVGGPHPTFDPEELLEARPG-VDDVVFGEGEDALEALL 121
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
187-375 1.04e-20

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: 90.54  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  187 ASIEFARGCPWDCTFCSAWTFYGRsYRSRSPEIIAKELASIREPG--------VFIVDDVAFVHAEHGME--IGRAIERH 256
Cdd:smart00729   3 ALYIITRGCPRRCTFCSFPSLRGK-LRSRYLEALVREIELLAEKGekeglvgtVFIGGGTPTLLSPEQLEelLEAIREIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  257 GIRKKYYLETRGDVLLRNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFARSLG-ITVALNLIAD- 334
Cdd:smart00729  82 GLAKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTDLIVGl 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1019415703  335 PEWDRERFETVRQWCLDI-PEIVNISVNTPYPGTEIWLREQR 375
Cdd:smart00729 162 PGETEEDFEETLKLLKELgPDRVSIFPLSPRPGTPLAKMYKR 203
radical_SAM_B12_BD cd02068
B12 binding domain_like associated with radical SAM domain. This domain shows similarity with ...
21-145 1.10e-20

B12 binding domain_like associated with radical SAM domain. This domain shows similarity with B12 (adenosylcobamide) binding domains found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase, but it lacks the signature motif Asp-X-His-X-X-Gly, which contains the histidine that acts as a cobalt ligand. The function of this domain remains unclear.


Pssm-ID: 239019 [Multi-domain]  Cd Length: 127  Bit Score: 87.76  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  21 EPLGLETVAAAVRQAGHDVRLIDLQVEtHRDFDRLVRAWRPDALCFSGnYLANIPEIIDLARTVKTLLPDCFVFVGGHSA 100
Cdd:cd02068     1 PPLGLAYLAAVLEDAGFIVAEHDVLSA-DDIVEDIKELLKPDVVGISL-MTSAIYEALELAKIAKEVLPNVIVVVGGPHA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1019415703 101 SFTASDILRhaEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPG 145
Cdd:cd02068    79 TFFPEEILE--EPGVDFVVIGEGEETFLKLLEELEEGEDLSEVPG 121
rSAM_Sden_1168 NF038361
Sden_1168 family B12-binding radical SAM P-methyltransferase;
2-254 1.81e-17

Sden_1168 family B12-binding radical SAM P-methyltransferase;


Pssm-ID: 439654 [Multi-domain]  Cd Length: 560  Bit Score: 85.32  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   2 KVLAVHPSGLMYTRVFLRL-EPLGLETVAAAVRQAGHDVRLIDLQVE-----------------THRDFDRLVRAWRPDA 63
Cdd:NF038361   64 RTLLVLPPMCMYEGAVKRVvPPLGLCYIAGALEKEGIDVDILDCIVEgideetpvapgvwnlgmTEERFRAYIAENDFDV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  64 LCFSGNYLANIPEIIDLARTVKTLLPDCFVFVGGHSASFTASDILRHA----EGAIDCVLKGEGEASVNALLQAAAT-KS 138
Cdd:NF038361  144 IGFTMIYSSDLQNLYRYAQIVKEVRPETTVIAGGLHASIYAERFLQDAvqddVPFIDFVLRGEGEIRLGDFLRNLADgRI 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 139 DLLAVPGAVTTDG---SGPPPRFVESLDDV-LPARdllrHR---RKYFIGTL--------DPCASIEFARGCPWDCTFCS 203
Cdd:NF038361  224 DIHADGLAGWHDGkvfANPQFARITDLDDLpFPAY----HKlplEKYFAHNVpfspyprgKRVMQLYTSRGCPIGCTFCA 299
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1019415703 204 AwTFYGRSYRSRSPEIIAKELASIREpgVFIVDDVAFVHAEHGMEIGRAIE 254
Cdd:NF038361  300 S-TNFSKQYRARSVENVIAEIRHYKD--EYGVDEVQFADDNLTFDRKRAIE 347
 
Name Accession Description Interval E-value
HpnR_B12_rSAM TIGR04367
hopanoid C-3 methylase HpnR; Members of this are family are a B12-binding domain/radical SAM ...
1-489 0e+00

hopanoid C-3 methylase HpnR; Members of this are family are a B12-binding domain/radical SAM domain protein required for 3-methylhopanoid production. Activity was confirmed by mutant phenotype by disrupting this gene in Methylococcus capsulatus strain Bath. This protein family should only occur in genomes that encode a squalene-hopene cyclase (see TIGR01507). [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 275160 [Multi-domain]  Cd Length: 490  Bit Score: 966.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   1 MKVLAVHPSGLMYTRVFLRLEPLGLETVAAAVRQAGHDVRLIDLQVETHRDFDRLVRAWRPDALCFSGNYLANIPEIIDL 80
Cdd:TIGR04367   1 MKVLAVHPSPLMYTKIFLRLEPLGLELVAGAARRAGHEVRLIDLQVESHADYLRLLESFRPDVVGFSLNYLANVPEVIDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  81 ARTVKTLLPDCFVFVGGHSASFTASDILRHAEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPGAVTTDGSGPPPRFVE 160
Cdd:TIGR04367  81 AKETKRRLPGCFVFVGGHSASFVARELLEHAEGAIDCVLRGEGEASAPLLLEAVADGGDLLTVPGVVTLEGEGPPPRFLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 161 SLDDVLPARDLLRHRRKYFIGTLDPCASIEFARGCPWDCTFCSAWTFYGRSYRSRSPEIIAKELASIREPGVFIVDDVAF 240
Cdd:TIGR04367 161 SLDEPRPARDLLRHRRKYFIGVLDPCASIEFTRGCPWDCSFCSAWTFYGRSYRTLSPEVAGEELARIREPGIFIVDDVAF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 241 VHAEHGMEIGRAIERHGIRKKYYLETRGDVLLRNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFA 320
Cdd:TIGR04367 241 IHAEHGMAIGEAIERRGIRKEYYLETRGDVLLRNKEVFEFWKRLGLKYMFLGLEAIDAEGLKLFRKRVSLDKNFEALEFA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 321 RSLGITVALNLIADPEWDRERFETVRQWCLDIPEIVNISVNTPYPGTEIWLREQRRLTSLDYRLYDIQHSVLPTRLPLPE 400
Cdd:TIGR04367 321 RSLGITVAINLIADPDWDRERFEVIRQWCLEIPEIVNISVNTPYPGTEIWHTESRKLTTRDYRLFDIQHAVLPTTLPLEE 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 401 FYAELVRTQQVLNRKHMGWAALRGAAGQAMHLLMHGQTNFVRMLWRFNSVFDPRLQLADHAREARYLMTPPPAP-DASAN 479
Cdd:TIGR04367 401 FYEELVKTQQVLNRKHLGWRALRGTAGIVARLLARGQTNFLRMLWKFNSVYNPELQLADHARPVRYEMAPPPAPsTQKPD 480
                         490
                  ....*....|
gi 1019415703 480 VKAVYVHGPA 489
Cdd:TIGR04367 481 PKTLYVHQPA 490
YgiQ COG1032
Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];
1-397 1.65e-95

Radical SAM superfamily enzyme YgiQ, UPF0313 family [General function prediction only];


Pssm-ID: 440655 [Multi-domain]  Cd Length: 394  Bit Score: 294.93  E-value: 1.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   1 MKVLAVHPSglmytrvFLRLEPLGLETVAAAVRQAGHDVRLIDLQVEtHRDFDRLVR--AWRPDALCFSGnYLANIPEII 78
Cdd:COG1032     1 MKVLLVYPP-------KYPVPPLGLAYLAALLEEAGYEVRIVDLNAE-DRSLEDLLKplREDPDLVGISL-YTPQYPNAL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  79 DLARTVKTLLPDCFVFVGGHSASFTASDILrhaEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPGAVTTDGSG----P 154
Cdd:COG1032    72 ELARLIKERNPGVPIVLGGPHASLNPEELL---EPFADFVVIGEGEETLPELLEALEEGRDLADIPGLAYRDDGRivqnP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 155 PPRFVESLDDV-LPARDLLRHRRKYFIgtldpcASIEFARGCPWDCTFCSAWTFYGRSYRSRSPEIIAKELASIRE---- 229
Cdd:COG1032   149 PRPLIEDLDELpFPAYDLLDLEAYHRR------ASIETSRGCPFGCSFCSISALYGRKVRYRSPESVVEEIEELVKrygi 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 230 PGVFIVDDVAFVHAEHGMEIGRAIERHGIRKKYYLETRGDVLlrNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRIT 309
Cdd:COG1032   223 REIFFVDDNFNVDKKRLKELLEELIERGLNVSFPSEVRVDLL--DEELLELLKKAGCRGLFIGIESGSQRVLKAMNKGIT 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 310 LDKNFEALEFARSLGITVALNLIAD-PEWDRERFETVRQWCLDI-PEIVNISVNTPYPGTEIWLREQRRLTSLDYRLY-D 386
Cdd:COG1032   301 VEDILEAVRLLKKAGIRVKLYFIIGlPGETEEDIEETIEFIKELgPDQAQVSIFTPLPGTPLYEELEKEGRLYDWEKYeD 380
                         410
                  ....*....|.
gi 1019415703 387 IQHSVLPTRLP 397
Cdd:COG1032   381 LLEAVLAPRLS 391
B12-binding pfam02310
B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several ...
14-131 7.83e-24

B12 binding domain; This domain binds to B12 (adenosylcobamide), it is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. It contains a conserved DxHxxGx(41)SxVx(26)GG motif, which is important for B12 binding.


Pssm-ID: 426713 [Multi-domain]  Cd Length: 121  Bit Score: 96.24  E-value: 7.83e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  14 TRVFLRLEPLGLETVAAAVRQAGHDVRLIDLQVEtHRDFDRLVRAWRPDALCFSGNYLANIPEIIDLARTVKTLLPDCFV 93
Cdd:pfam02310   6 ATVGGDLHPLGLNYVAAALRAAGFEVIILGANVP-PEDIVAAARDEKPDVVGLSALMTTTLPGAKELIRLLKGIRPRVKV 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1019415703  94 FVGGHSASFTASDILRHAEGaIDCVLKGEGEASVNALL 131
Cdd:pfam02310  85 VVGGPHPTFDPEELLEARPG-VDDVVFGEGEDALEALL 121
B12_SAM_MJ_0865 TIGR04014
B12-binding domain/radical SAM domain protein, MJ_0865 family; Members of this family have ...
28-369 4.81e-21

B12-binding domain/radical SAM domain protein, MJ_0865 family; Members of this family have both a B12 binding homology domain (pfam02310) and a radical SAM domain (pfam04055), and occur only once per genome. This protein occurs so far only in methanogenic archaea. Some species with members of this family have a related protein with similar domain architecture (see TIGR04013). [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274918 [Multi-domain]  Cd Length: 434  Bit Score: 95.58  E-value: 4.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  28 VAAAVRQAGHDVRLIdlqvethRDFDRLvrawRPDALCFSGNYLANI--PEIIDLARTVKTLLPdcFVFVGGhSASFTAS 105
Cdd:TIGR04014  17 IGGILRDAGHSVILR-------RSPDPK----KSDVVILSLFSTLHLldPAIREIVRKAREFGG--PVYVGG-PVSIVPE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 106 DILRhaEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPGAVTTDGSGP---PPRFVESLDDVLP------ARDLLRHRR 176
Cdd:TIGR04014  83 MVLG--ELDVDLVVMGEGEETVPPLLETGEDEGDFEDVPGIAYLEDGEIvvtEPKPPPDLDHPLPlipddiGRQDIRGAN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 177 KYfigtldpcasIEFARGCPWDCTFCSAWTFYGRSYRSRSPEIIAKELASIREPGV----------------FIVDDVAF 240
Cdd:TIGR04014 161 VY----------IETHRGCPGNCTFCQVPRFFGRRIRSRPLEDIVEEVRELKRGGArrfaisggtgslygskKGIDEEAF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 241 VHAEHGMEigraiERHGIRKKYYLETRGDVLlrNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFA 320
Cdd:TIGR04014 231 IELLERLS-----EVLGRKNVSVPDIRVDLV--DDEILEAIREYTIGWVFFGIESGSDRMLRLMRKGITVDDVCEAVELA 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1019415703 321 RSLGITVALNLI-ADPEWDRERFETVRQWCLDIP-EIVNISVNTPYPGTEI 369
Cdd:TIGR04014 304 REYGVKVAGSFIvGYPGETEDDYEATKDLMEELMlDDVFVSIAEPIPGTEL 354
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
187-375 1.04e-20

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: 90.54  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  187 ASIEFARGCPWDCTFCSAWTFYGRsYRSRSPEIIAKELASIREPG--------VFIVDDVAFVHAEHGME--IGRAIERH 256
Cdd:smart00729   3 ALYIITRGCPRRCTFCSFPSLRGK-LRSRYLEALVREIELLAEKGekeglvgtVFIGGGTPTLLSPEQLEelLEAIREIL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  257 GIRKKYYLETRGDVLLRNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFARSLG-ITVALNLIAD- 334
Cdd:smart00729  82 GLAKDVEITIETRPDTLTEELLEALKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGpIKVSTDLIVGl 161
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1019415703  335 PEWDRERFETVRQWCLDI-PEIVNISVNTPYPGTEIWLREQR 375
Cdd:smart00729 162 PGETEEDFEETLKLLKELgPDRVSIFPLSPRPGTPLAKMYKR 203
radical_SAM_B12_BD cd02068
B12 binding domain_like associated with radical SAM domain. This domain shows similarity with ...
21-145 1.10e-20

B12 binding domain_like associated with radical SAM domain. This domain shows similarity with B12 (adenosylcobamide) binding domains found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase, but it lacks the signature motif Asp-X-His-X-X-Gly, which contains the histidine that acts as a cobalt ligand. The function of this domain remains unclear.


Pssm-ID: 239019 [Multi-domain]  Cd Length: 127  Bit Score: 87.76  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  21 EPLGLETVAAAVRQAGHDVRLIDLQVEtHRDFDRLVRAWRPDALCFSGnYLANIPEIIDLARTVKTLLPDCFVFVGGHSA 100
Cdd:cd02068     1 PPLGLAYLAAVLEDAGFIVAEHDVLSA-DDIVEDIKELLKPDVVGISL-MTSAIYEALELAKIAKEVLPNVIVVVGGPHA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1019415703 101 SFTASDILRhaEGAIDCVLKGEGEASVNALLQAAATKSDLLAVPG 145
Cdd:cd02068    79 TFFPEEILE--EPGVDFVVIGEGEETFLKLLEELEEGEDLSEVPG 121
rSAM_Sden_1168 NF038361
Sden_1168 family B12-binding radical SAM P-methyltransferase;
2-254 1.81e-17

Sden_1168 family B12-binding radical SAM P-methyltransferase;


Pssm-ID: 439654 [Multi-domain]  Cd Length: 560  Bit Score: 85.32  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703   2 KVLAVHPSGLMYTRVFLRL-EPLGLETVAAAVRQAGHDVRLIDLQVE-----------------THRDFDRLVRAWRPDA 63
Cdd:NF038361   64 RTLLVLPPMCMYEGAVKRVvPPLGLCYIAGALEKEGIDVDILDCIVEgideetpvapgvwnlgmTEERFRAYIAENDFDV 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  64 LCFSGNYLANIPEIIDLARTVKTLLPDCFVFVGGHSASFTASDILRHA----EGAIDCVLKGEGEASVNALLQAAAT-KS 138
Cdd:NF038361  144 IGFTMIYSSDLQNLYRYAQIVKEVRPETTVIAGGLHASIYAERFLQDAvqddVPFIDFVLRGEGEIRLGDFLRNLADgRI 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 139 DLLAVPGAVTTDG---SGPPPRFVESLDDV-LPARdllrHR---RKYFIGTL--------DPCASIEFARGCPWDCTFCS 203
Cdd:NF038361  224 DIHADGLAGWHDGkvfANPQFARITDLDDLpFPAY----HKlplEKYFAHNVpfspyprgKRVMQLYTSRGCPIGCTFCA 299
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1019415703 204 AwTFYGRSYRSRSPEIIAKELASIREpgVFIVDDVAFVHAEHGMEIGRAIE 254
Cdd:NF038361  300 S-TNFSKQYRARSVENVIAEIRHYKD--EYGVDEVQFADDNLTFDRKRAIE 347
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
191-332 2.77e-15

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: 73.33  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 191 FARGCPWDCTFCSAWTFYGRS-YRSRSPEIIAKELASIREPG---VFIVDDVAFVHAEHGMEIGRAIERHGIRKKYY-LE 265
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGkGRELSPEEILEEAKELKRLGvevVILGGGEPLLLPDLVELLERLLKLELAEGIRItLE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1019415703 266 TRGDVLlrNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRITLDKNFEALEFARSLGITVALNLI 332
Cdd:pfam04055  81 TNGTLL--DEELLELLKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNI 145
B12_rSAM_oligo TIGR04295
B12-binding domain/radical SAM domain protein, rhizo-twelve system; A variety of bacteria, ...
22-399 5.21e-14

B12-binding domain/radical SAM domain protein, rhizo-twelve system; A variety of bacteria, including multiple species of Bradyrhizobium, Mesorhizobium, and Methylobacterium, have a typically twelve-gene cassette (hence the designation rhizo-twelve) for the biosynthesis of some unknown oligosaccaride. This family is a B12-binding domain/radical SAM domain protein found in roughly have of these cassettes, but nowhere else.


Pssm-ID: 275111 [Multi-domain]  Cd Length: 422  Bit Score: 74.05  E-value: 5.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  22 PLGLETVAAAVRQAGHDVRLIDLQVE--THRDFDRLVRAWRPDALCFSG--NYL---ANIPEIIDLARTVKTL--LPDCF 92
Cdd:TIGR04295  25 PLELGYARALLENAGHAALLVDAQADglSLEELRRRVAAFRPDMTVVTTapSYLfwrCAPPELRVPMATLRALreTGGTL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  93 VFVGGHsASFTASDILRHAegAIDCVLKGEGEASVNALLQAAATKSDLLAVP--GAVTTDGSGPPPRFVE----SLDDVL 166
Cdd:TIGR04295 105 VAVGPH-ASTTPRAALRKL--GVDVVVLGECEEVLVELAGGPWRQIDGICYRrgDEVHVQGGPAAADMTTlpalRWPEAT 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 167 PARDLLRHRRkyFIGTLD-PCASIEFARGCPWDCTFCSAWTFYGRsYRSRSPEIIAKELASIREPG---VFIVDDVAFVH 242
Cdd:TIGR04295 182 IARHAHHHHR--FDAAPEgPGAEVETSRGCPYHCTFCAKDNFRNK-YRKRPLATILEEIDALIAQGvryVYFIDEIFLPD 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 243 AEHGMEI-GRAIerhgirkKYYLETRGDvlLRNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRK--RITLDKNFEALEF 319
Cdd:TIGR04295 259 RPLLEEIvARNV-------SFGVQTRID--LWKEEMLDLLGRAGCVSIEAGVESITEEGRELLAKncRMSTEELTELLIH 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 320 ARSLGITVALNLIADPEWD-------RERFETVRQWCLD-IPEIvnisvntPYPGT------------EIWLREQRRLTS 379
Cdd:TIGR04295 330 AKRSVPFVQANLIDSPKDDpaevarwRQRLQGHGVWANEpVPLF-------PYPGSpdytrrwgapddNAWERAHAHYLA 402
                         410       420
                  ....*....|....*....|
gi 1019415703 380 LDYRLYDIQHSvlptrLPLP 399
Cdd:TIGR04295 403 EFRTFSDIQDQ-----RPLP 417
rSAM_ladder_B12 TIGR04072
lipid biosynthesis B12-binding/radical SAM protein; Members of this protein family occur in ...
22-131 1.48e-09

lipid biosynthesis B12-binding/radical SAM protein; Members of this protein family occur in conserved genomic contexts highly suggestive of lipid biosynthesis, including an island shared between Kuenenia stuttgartiensis, which produces ladderanes, and Desulfotalea psychrophila, which produces a different kind of unusual polyunsaturated hydrocarbon.


Pssm-ID: 188587  Cd Length: 151  Bit Score: 56.58  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  22 PLGLETVAAAVRQAGHDVRLIDLQV--ETHRDFDRLVRAWRPDALCFS------------GNYLANIPEIIDLARTVKtl 87
Cdd:TIGR04072  15 PLGMAVIAGALSGAGHEVRQFDYLAdgASLELLRPLLERFRPDYIGLSirnidnvdslssENYINGAKNIVDLIRELS-- 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1019415703  88 lpDCFVFVGGHSASFTASDILRHAeGAiDCVLKGEGEASVNALL 131
Cdd:TIGR04072  93 --KAPIVLGGPAFSLMPEELLEYL-GA-DYGVVGEGEQLMVWLA 132
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
189-371 1.57e-09

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: 57.73  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 189 IEFARGCPWDCTFCSAWTFYGRSYRS----RSPEIIAKELASIREPGVFIVDDVAFVHaEHGMEIGRAIERHGIRKKYYL 264
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESppeiEEILDIVLEAKERGVEVVILTGGEPLLY-PELAELLRRLKKELPGFEISI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 265 ETRGDVLLRN--KDVFRfwrtLGLQYMFIGMEAIDAEGLKAFR-KRITLDKNFEALEFARSLGITVALNLIADP--EWDR 339
Cdd:cd01335    80 ETNGTLLTEEllKELKE----LGLDGVGVSLDSGDEEVADKIRgSGESFKERLEALKELREAGLGLSTTLLVGLgdEDEE 155
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1019415703 340 ERFETVRQ-WCLDIPEIVNISVNTPYPGTEIWL 371
Cdd:cd01335   156 DDLEELELlAEFRSPDRVSLFRLLPEEGTPLEL 188
B12-binding_like cd02065
B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 ...
24-135 7.15e-08

B12 binding domain (B12-BD). Most of the members bind different cobalamid derivates, like B12 (adenosylcobamide) or methylcobalamin or methyl-Co(III) 5-hydroxybenzimidazolylcobamide. This domain is found in several enzymes, such as glutamate mutase, methionine synthase and methylmalonyl-CoA mutase. Cobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in many cobalamin-binding proteins. Not all members of this family contain the conserved binding motif.


Pssm-ID: 239016 [Multi-domain]  Cd Length: 125  Bit Score: 51.23  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703  24 GLETVAAAVRQAGHDVrlIDLQV-ETHRDFDRLVRAWRPDALCFSGnYLANIPEIIDLARTVKTLLP-DCFVFVGGHSAS 101
Cdd:cd02065    15 GKNIVAIALRDNGFEV--IDLGVdVPPEEIVEAAKEEDADVVGLSA-LSTTHMEAMKLVIEALKELGiDIPVVVGGAHPT 91
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1019415703 102 FtasdilRHAEGAIDCVLKGEGEASVNALLQAAA 135
Cdd:cd02065    92 A------DPEEPKVDAVVIGEGEYAGPALLEVEG 119
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
188-332 1.14e-07

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: 51.44  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 188 SIEFARGCPWDCTFCSAWTFYGRSyRSRSPEIIAKELASIREPGVFIVD----DvAFVHaEHGMEIGRAIERHGIRKkyY 263
Cdd:COG0535     3 QIELTNRCNLRCKHCYADAGPKRP-GELSTEEAKRILDELAELGVKVVGltggE-PLLR-PDLFELVEYAKELGIRV--N 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1019415703 264 LETRGDVLlrNKDVFRFWRTLGLQYMFIGMEAIDAEGLKAFRKRI-TLDKNFEALEFARSLGITVALNLI 332
Cdd:COG0535    78 LSTNGTLL--TEELAERLAEAGLDHVTISLDGVDPETHDKIRGVPgAFDKVLEAIKLLKEAGIPVGINTV 145
 
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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