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Conserved domains on  [gi|2074188857|ref|NP_543166|]
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arsenite methyltransferase [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
methyl_ArsM super family cl41856
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ...
 42-321 5.74e-44

arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.


The actual alignment was detected with superfamily member NF040538:

Pssm-ID: 439748  Cd Length: 352  Bit Score: 155.40  E-value: 5.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  42 YIRKSLQNVHEEVTSRYYGCGLVVPEHLENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEYHTEK 121
Cdd:NF040538   33 YDAQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 122 FGFQtpNVTFLHGQI-----------EMLAEAG-----------------------IQKESYDIVISNCVINLV--PDKQ 165
Cdd:NF040538  113 TGSA--NLRFFRASIsdlktdlelaeERLSGEScenlaswknfeqflsdsrqsnplIADNSIDLVVSNCVINLVgtTEKQ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 166 KVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDLAVIAKKIGFcpprlvTANIITVGNKELER 245
Cdd:NF040538  191 NVFAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTK 264

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 246 VLGDCRFVSATFRLFKLPKTEPAGR--CQVVYNGGimghEKELIFDANFTFKEGEAVEVDEETAAILRNSRFAHDFLF 321
Cdd:NF040538  265 RIGSVEFYSVTVTATKPLEAVVGSGdmTTVIYRGP----WTEVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFV 338
 
Name Accession Description Interval E-value
methyl_ArsM NF040538
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ...
 42-321 5.74e-44

arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.


Pssm-ID: 439748  Cd Length: 352  Bit Score: 155.40  E-value: 5.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  42 YIRKSLQNVHEEVTSRYYGCGLVVPEHLENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEYHTEK 121
Cdd:NF040538   33 YDAQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 122 FGFQtpNVTFLHGQI-----------EMLAEAG-----------------------IQKESYDIVISNCVINLV--PDKQ 165
Cdd:NF040538  113 TGSA--NLRFFRASIsdlktdlelaeERLSGEScenlaswknfeqflsdsrqsnplIADNSIDLVVSNCVINLVgtTEKQ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 166 KVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDLAVIAKKIGFcpprlvTANIITVGNKELER 245
Cdd:NF040538  191 NVFAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTK 264

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 246 VLGDCRFVSATFRLFKLPKTEPAGR--CQVVYNGGimghEKELIFDANFTFKEGEAVEVDEETAAILRNSRFAHDFLF 321
Cdd:NF040538  265 RIGSVEFYSVTVTATKPLEAVVGSGdmTTVIYRGP----WTEVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFV 338
arsM PRK11873
arsenite methyltransferase;
60-265 1.66e-43

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 151.64  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  60 GCGLvvPEHLENCR----ILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQ 135
Cdd:PRK11873   65 GCGN--PTALAELKpgetVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGYT--NVEFRLGE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 136 IEMLAEAgiqKESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKD 215
Cdd:PRK11873  137 IEALPVA---DNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEE 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 216 LAVIAKKIGFCPPRLVTANIITVGN-KELERVLG-------DCRFVSATFRLFKLPKT 265
Cdd:PRK11873  214 YLAMLAEAGFVDITIQPKREYRIPDaREFLEDWGiapgrqlDGYIVSATVEATKPAAT 271
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 70-216 5.55e-34

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 122.91  E-value: 5.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  70 ENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQIEMLAEAgIQKESY 149
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARE----NAQKLGFD--NVEFEQGDIEELPEL-LEDDKF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074188857 150 DIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDL 216
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 73-185 5.92e-22

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 90.44  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQlvgQKGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiqkESYDIV 152
Cdd:COG2226    25 RVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELAR-------ERAAEAGLNVEFVVGDAEDLPFPD---GSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-188 3.55e-15

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 70.92  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAYleyhteKFGFQTPNVTFLHGQIEMLAEAGIqkESYDIV 152
Cdd:cd02440     1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEAD--ESFDVI 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2074188857 153 ISNCVIN-LVPDKQKVLREVYQVLKYGGELYFSDVYA 188
Cdd:cd02440    71 ISDPPLHhLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-185 7.01e-11

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 61.53  E-value: 7.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  68 HLENCRILDLGSGSGrdcYVLSQLVGQ--KGHITGIDMTKVQVEVAKAYLeyhtekfgfqTPNVTFLHGQIEMLAeagIQ 145
Cdd:TIGR02072  32 IFIPASVLDIGCGTG---YLTRALLKRfpQAEFIALDISAGMLAQAKTKL----------SENVQFICGDAEKLP---LE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2074188857 146 KESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:TIGR02072  96 DSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
 
Name Accession Description Interval E-value
methyl_ArsM NF040538
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ...
 42-321 5.74e-44

arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.


Pssm-ID: 439748  Cd Length: 352  Bit Score: 155.40  E-value: 5.74e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  42 YIRKSLQNVHEEVTSRYYGCGLVVPEHLENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEYHTEK 121
Cdd:NF040538   33 YDAQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 122 FGFQtpNVTFLHGQI-----------EMLAEAG-----------------------IQKESYDIVISNCVINLV--PDKQ 165
Cdd:NF040538  113 TGSA--NLRFFRASIsdlktdlelaeERLSGEScenlaswknfeqflsdsrqsnplIADNSIDLVVSNCVINLVgtTEKQ 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 166 KVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDLAVIAKKIGFcpprlvTANIITVGNKELER 245
Cdd:NF040538  191 NVFAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTK 264

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 246 VLGDCRFVSATFRLFKLPKTEPAGR--CQVVYNGGimghEKELIFDANFTFKEGEAVEVDEETAAILRNSRFAHDFLF 321
Cdd:NF040538  265 RIGSVEFYSVTVTATKPLEAVVGSGdmTTVIYRGP----WTEVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFV 338
arsM PRK11873
arsenite methyltransferase;
60-265 1.66e-43

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 151.64  E-value: 1.66e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  60 GCGLvvPEHLENCR----ILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQ 135
Cdd:PRK11873   65 GCGN--PTALAELKpgetVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGYT--NVEFRLGE 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 136 IEMLAEAgiqKESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKD 215
Cdd:PRK11873  137 IEALPVA---DNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEE 213

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 216 LAVIAKKIGFCPPRLVTANIITVGN-KELERVLG-------DCRFVSATFRLFKLPKT 265
Cdd:PRK11873  214 YLAMLAEAGFVDITIQPKREYRIPDaREFLEDWGiapgrqlDGYIVSATVEATKPAAT 271
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 70-216 5.55e-34

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 122.91  E-value: 5.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  70 ENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAyleyHTEKFGFQtpNVTFLHGQIEMLAEAgIQKESY 149
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARE----NAQKLGFD--NVEFEQGDIEELPEL-LEDDKF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2074188857 150 DIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSHKVLWGECLGGALYWKDL 216
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 73-185 5.92e-22

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 90.44  E-value: 5.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQlvgQKGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiqkESYDIV 152
Cdd:COG2226    25 RVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELAR-------ERAAEAGLNVEFVVGDAEDLPFPD---GSFDLV 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-179 4.67e-21

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 86.46  E-value: 4.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  74 ILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiqkESYDIVI 153
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERAR-------ERAAEAGLNVEFVQGDAEDLPFPD---GSFDLVV 68

                          90       100
                  ....*....|....*....|....*...
gi 2074188857 154 SNCVINLV--PDKQKVLREVYQVLKYGG 179
Cdd:pfam13649  69 SSGVLHHLpdPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 69-185 2.65e-19

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 82.76  E-value: 2.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  69 LENCRILDLGSGSGRDCYVLSQLvgqkGH-ITGIDMTKVQVEVAKAYLEYHtekfgfqtpNVTFLHGQIEMLAEAGiqkE 147
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARR----GAdVTGVDISPEALEIARERAAEL---------NVDFVQGDLEDLPLED---G 86

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2074188857 148 SYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG2227    87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-183 1.33e-15

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  75 LDLGSGSGRDCYVLSQLVGQkghITGIDMTKVQVEVAKAYLeyhtekfgfQTPNVTFLHGQIEMLaeaGIQKESYDIVIS 154
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKA---------PREGLTFVVGDAEDL---PFPDNSFDLVLS 65

                          90       100
                  ....*....|....*....|....*....
gi 2074188857 155 NCVINLVPDKQKVLREVYQVLKYGGELYF 183
Cdd:pfam08241  66 SEVLHHVEDPERALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-188 3.55e-15

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 70.92  E-value: 3.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAYleyhteKFGFQTPNVTFLHGQIEMLAEAGIqkESYDIV 152
Cdd:cd02440     1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKA------AAALLADNVEVLKGDAEELPPEAD--ESFDVI 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2074188857 153 ISNCVIN-LVPDKQKVLREVYQVLKYGGELYFSDVYA 188
Cdd:cd02440    71 ISDPPLHhLVEDLARFLEEARRLLKPGGVLVLTLVLA 107
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
73-185 3.64e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 70.62  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGQkGHITGIDMTKVQVEVAKAYLeyhtekfgfqtPNVTFLHGQIEMLAEAgiqkESYDIV 152
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARL-----------PNVRFVVADLRDLDPP----EPFDLV 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:COG4106    68 VSNAALHWLPDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 70-199 1.32e-13

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 68.79  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  70 ENCRILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAyleyHTEKFGFqtPNVTFLHGQIEMLAEagIQKESY 149
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARA----RAAKAGL--GNVEFLVADLAELDP--LPAESF 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2074188857 150 DIVISNCVINLVP--DKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKSH 199
Cdd:COG0500    96 DLVVAFGVLHHLPpeEREALLRELARALKPGGVLLLSASDAAAALSLARLLL 147
PRK08317 PRK08317
hypothetical protein; Provisional
 73-179 5.10e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 64.96  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLaeaGIQKESYDIV 152
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAK-------ERAAGLGPNVEFVRGDADGL---PFPDGSFDAV 91

                          90       100
                  ....*....|....*....|....*..
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGG 179
Cdd:PRK08317   92 RSDRVLQHLEDPARALAEIARVLRPGG 118
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
73-184 1.16e-11

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 62.71  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVgqkGHITGIDMTKVQVEVAKAYLEYhtekfgfqtpnVTFLHGQIEMLAEAGiqkESYDIV 152
Cdd:COG4976    49 RVLDLGCGTGLLGEALRPRG---YRLTGVDLSEEMLAKAREKGVY-----------DRLLVADLADLAEPD---GRFDLI 111

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2074188857 153 ISNCVINLVPDKQKVLREVYQVLKYGGELYFS 184
Cdd:COG4976   112 VAADVLTYLGDLAAVFAGVARALKPGGLFIFS 143
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-185 7.01e-11

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 61.53  E-value: 7.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  68 HLENCRILDLGSGSGrdcYVLSQLVGQ--KGHITGIDMTKVQVEVAKAYLeyhtekfgfqTPNVTFLHGQIEMLAeagIQ 145
Cdd:TIGR02072  32 IFIPASVLDIGCGTG---YLTRALLKRfpQAEFIALDISAGMLAQAKTKL----------SENVQFICGDAEKLP---LE 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2074188857 146 KESYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSD 185
Cdd:TIGR02072  96 DSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 73-181 8.73e-11

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 61.32  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKayleyhtEKF--GFQTPNVTFLHGQIEMLAeagIQKESYD 150
Cdd:PRK00216   54 KVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGR-------EKLrdLGLSGNVEFVQGDAEALP---FPDNSFD 123

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2074188857 151 IV-ISNCVINlVPDKQKVLREVYQVLKYGGEL 181
Cdd:PRK00216  124 AVtIAFGLRN-VPDIDKALREMYRVLKPGGRL 154
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
69-182 9.12e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 61.30  E-value: 9.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  69 LENCRILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLEyhteKFGFQtpNVTFLHGQIEMLAEagiQKES 148
Cdd:pfam01209  41 KRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAK----EEGKY--NIEFLQGNAEELPF---EDDS 111

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2074188857 149 YDIVISNCVINLVPDKQKVLREVYQVLKYGGELY 182
Cdd:pfam01209 112 FDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVV 145
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-181 2.53e-10

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.99  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  75 LDLGSGSGRDCYVLSQLVGQkGHITGIDMTKVQVEVAKayleyhtEKFGFQTPNVTFLHGQIEMLAEAGiQKESYDIVIS 154
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPG-LEYTGLDISPAALEAAR-------ERLAALGLLNAVRVELFQLDLGEL-DPGSFDVVVA 71

                          90       100
                  ....*....|....*....|....*..
gi 2074188857 155 NCVINLVPDKQKVLREVYQVLKYGGEL 181
Cdd:pfam08242  72 SNVLHHLADPRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 73-185 6.59e-08

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.47  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKAYLeyhtEKFGFqTPNVTFLHGQIEMLAEAGiqkeSYDIV 152
Cdd:COG2230    54 RVLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARERA----AEAGL-ADRVEVRLADYRDLPADG----QFDAI 122

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2074188857 153 ISNCVINLVPDKQ--KVLREVYQVLKYGGELYFSD 185
Cdd:COG2230   123 VSIGMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-225 2.65e-06

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 47.04  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  66 PEHLENCRILDLGSGSGRDCyvlsQLVGQKG-HITGIDMTKVQVEVAKAYleyhtekfgfqtpNVTFLHGQIEMLAEAGi 144
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFL----RLLRAQGfSVTGVDPSPIAIERALLN-------------VRFDQFDEQEAAVPAG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857 145 qkeSYDIVISNCVINLVPDKQKVLREVYQVLKYGGELYFSDVYASLEVSEDIKsHKVLWGECLGGALYW--KDLAVIAKK 222
Cdd:pfam13489  80 ---KFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLL-EWPYLRPRNGHISLFsaRSLKRLLEE 155


                  ...
gi 2074188857 223 IGF 225
Cdd:pfam13489 156 AGF 158
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 73-179 3.84e-06

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 47.46  E-value: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYLeyhtEKFGFqTPNVTFLHGQIemlaEAGIQKESYDIV 152
Cdd:COG2519    94 RVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNL----ERFGL-PDNVELKLGDI----REGIDEGDVDAV 164

                          90       100
                  ....*....|....*....|....*...
gi 2074188857 153 IsncvinL-VPDKQKVLREVYQVLKYGG 179
Cdd:COG2519   165 F------LdMPDPWEALEAVAKALKPGG 186
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 69-184 2.04e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 42.64  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  69 LENCRILDLGSGSGrdcyVLS---QLVGQKgHITGIDMTKVQVEVAKAYLEYHtekfgfqtpNVtflHGQIEMLAEAGIQ 145
Cdd:pfam06325 160 KPGESVLDVGCGSG----ILAiaaLKLGAK-KVVGVDIDPVAVRAAKENAELN---------GV---EARLEVYLPGDLP 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2074188857 146 KESYDIVISNC----VINLVPDkqkvlreVYQVLKYGGELYFS 184
Cdd:pfam06325 223 KEKADVVVANIladpLIELAPD-------IYALVKPGGYLILS 258
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 73-178 2.93e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 42.19  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGRDCYVLSQLVGQKGHITGIDMTKVQVEVAKAYleyhtekfgfQTPNVTFLHGQIEMlaeagIQKESYDIV 152
Cdd:PLN02233   76 RVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAASR----------QELKAKSCYKNIEW-----IEGDATDLP 140

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2074188857 153 ISNCVINLVP---------DKQKVLREVYQVLKYG 178
Cdd:PLN02233  141 FDDCYFDAITmgyglrnvvDRLKAMQEMYRVLKPG 175
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 65-183 4.66e-04

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 40.94  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  65 VPEHLENcRILDLGSGSGrdcyVLS---QLVGQKGHITGIDMTKVQVEVAKAYLEYHtekfgfQTPNVTFLHGQiemlAE 141
Cdd:COG2813    45 LPEPLGG-RVLDLGCGYG----VIGlalAKRNPEARVTLVDVNARAVELARANAAAN------GLENVEVLWSD----GL 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2074188857 142 AGIQKESYDIVISNCVI--NLVPDK---QKVLREVYQVLKYGGELYF 183
Cdd:COG2813   110 SGVPDGSFDLILSNPPFhaGRAVDKevaHALIADAARHLRPGGELWL 156
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 73-183 7.22e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 40.51  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  73 RILDLGSGSGrdcyVLSQLVGQK---GHITGidmtkvqVEVAKAYLEYHTEKF---GFQtPNVTFLHGQIEMLAEAgIQK 146
Cdd:COG4123    40 RVLDLGTGTG----VIALMLAQRspgARITG-------VEIQPEAAELARRNValnGLE-DRITVIHGDLKEFAAE-LPP 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2074188857 147 ESYDIVISN--------CVINlvPDKQK-------------VLREVYQVLKYGGELYF 183
Cdd:COG4123   107 GSFDLVVSNppyfkagsGRKS--PDEARaiarhedaltledLIRAAARLLKPGGRFAL 162
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 63-155 2.06e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.37  E-value: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  63 LVVPEHLENCRILDLGSGSG----------RDCYVlsqlvgqkghiTGIDMTKVQVEVAKAYLEYHTEKfgfqtpNVTFL 132
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGaialalakerPDAEV-----------TAVDISPEALAVARRNAKHGLGA------RVEFL 163

                          90       100
                  ....*....|....*....|...
gi 2074188857 133 HGqiEMLaeAGIQKESYDIVISN 155
Cdd:PRK09328  164 QG--DWF--EPLPGGRFDLIVSN 182
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 70-189 2.59e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.18  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  70 ENCRILDLGSGSGRDCYVLSQLVGqkGHITGIDMTKVQVEVAKaylEYHTEKfgfqtpnvtflhGQIEMLAEAGIQKE-- 147
Cdd:PTZ00098   52 ENSKVLDIGSGLGGGCKYINEKYG--AHVHGVDICEKMVNIAK---LRNSDK------------NKIEFEANDILKKDfp 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2074188857 148 --SYDIVISNCVINLVP--DKQKVLREVYQVLKYGGELYFSDVYAS 189
Cdd:PTZ00098  115 enTFDMIYSRDAILHLSyaDKKKLFEKCYKWLKPNGILLITDYCAD 160
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 67-155 3.80e-03

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 38.60  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  67 EHLENC-RILDLGSGSGrdCYVLSQLVGQKG-HITGIDMTKVQVEVAKAYLEYHtekfgfQTPNVTFLHGQiemLAEAgI 144
Cdd:TIGR03534  82 ERLKKGpRVLDLGTGSG--AIALALAKERPDaRVTAVDISPEALAVARKNARRL------GLENVEFLQGD---WFEP-L 149

                          90
                  ....*....|.
gi 2074188857 145 QKESYDIVISN 155
Cdd:TIGR03534 150 PSGKFDLIVSN 160
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
69-184 3.87e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 38.62  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  69 LENCRILDLGSGSGrdcyVLS---QLVGQKgHITGIDMTKVQVEVAKAyleyhtekfgfqtpNVTF--LHGQIEMLAEAG 143
Cdd:COG2264   147 KPGKTVLDVGCGSG----ILAiaaAKLGAK-RVLAVDIDPVAVEAARE--------------NAELngVEDRIEVVLGDL 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2074188857 144 IQKESYDIVISNcvIN------LVPDkqkvlreVYQVLKYGGELYFS 184
Cdd:COG2264   208 LEDGPYDLVVAN--ILanplieLAPD-------LAALLKPGGYLILS 245
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 50-157 6.15e-03

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 38.00  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2074188857  50 VHEEVtsryygcgLVVPEHLENCRILDLGSGSGRDCYVLSqlvgQKGH-ITGIDmtkvQVEVAKAYLEYHTEKFGFQTPn 128
Cdd:PRK12335  108 THSEV--------LEAVQTVKPGKALDLGCGQGRNSLYLA----LLGFdVTAVD----INQQSLENLQEIAEKENLNIR- 170

                          90       100
                  ....*....|....*....|....*....
gi 2074188857 129 vTFLHGqiemLAEAGIQkESYDIVISNCV 157
Cdd:PRK12335  171 -TGLYD----INSASIQ-EEYDFILSTVV 193
 
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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