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Conserved domains on  [gi|2462533029|ref|XP_054228540|]
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protein arginine N-methyltransferase 8 isoform X3 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 17570124)

class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
86-259 9.76e-45

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.11  E-value: 9.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029  86 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 164
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 165 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWweNVYG 244
Cdd:COG4076    90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--QFDG 166

                         170
                  ....*....|....*
gi 2462533029 245 FDMTCIRDVAMKEPL 259
Cdd:COG4076   167 FDFRLFGFLLYAEPL 181
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
86-259 9.76e-45

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.11  E-value: 9.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029  86 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 164
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 165 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWweNVYG 244
Cdd:COG4076    90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--QFDG 166

                         170
                  ....*....|....*
gi 2462533029 245 FDMTCIRDVAMKEPL 259
Cdd:COG4076   167 FDFRLFGFLLYAEPL 181
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 115-215 2.02e-12

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: 62.45  E-value: 2.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIISeWMGYCLF 192
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEElPPEADESFDVIIS-DPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 2462533029 193 YESMLNTVIFARDKwLKPGGLMF 215
Cdd:cd02440    80 VEDLARFLEEARRL-LKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 115-212 1.72e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIISeWMGY 189
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGV------DLSPEMLerareRAAEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVL 73

                          90       100
                  ....*....|....*....|....*
gi 2462533029 190 CLFYESMLNTVI--FARdkWLKPGG 212
Cdd:pfam13649  74 HHLPDPDLEAALreIAR--VLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
107-183 1.16e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 107 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKIIKA-------NHLDNIITIFKGKveevelpvEKV 179
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV------DIDPQAVEAarenaelNGVELNVYLPQGD--------LKA 180


                  ....
gi 2462533029 180 DIII 183
Cdd:PRK00517  181 DVIV 184
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 89-214 1.30e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029  89 MLKDEVRTLTYRNSMYHnkhvfKDKVVLDVGSGTGILSMFAAKA-GAKKVFGIE-----CSSIsdysEKIIKANHLDNII 162
Cdd:TIGR02469   2 MTKREVRALTLAKLRLR-----PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLI----ERNLRRFGVSNIV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462533029 163 TIFKGKVEEVELPVEKVDIIIsewMGYClfyESMLNTVIFARDKWLKPGGLM 214
Cdd:TIGR02469  73 IVEGDAPEAPEALLPDPDAVF---VGGS---GGLLQEILEAVERRLRPGGRI 118
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
86-259 9.76e-45

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 152.11  E-value: 9.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029  86 HEEMLKDEVRTLTYRNSMYHnkHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIECS-SISDYSEKIIKANHLDNIITI 164
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 165 FKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVIFARDKWLKPGGLMFPDRAALYVVAIEDRQYKDFKIHWweNVYG 244
Cdd:COG4076    90 INADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--QFDG 166

                         170
                  ....*....|....*
gi 2462533029 245 FDMTCIRDVAMKEPL 259
Cdd:COG4076   167 FDFRLFGFLLYAEPL 181
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
107-183 6.24e-13

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 67.51  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 107 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKI----IKANHLDNIITIFKGKVeeveLPVEKVDII 182
Cdd:COG2264   144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVD---IDPVAVEAarenAELNGVEDRIEVVLGDL----LEDGPYDLV 216


                  .
gi 2462533029 183 I 183
Cdd:COG2264   217 V 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 115-215 2.02e-12

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: 62.45  E-value: 2.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIISeWMGYCLF 192
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEElPPEADESFDVIIS-DPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 2462533029 193 YESMLNTVIFARDKwLKPGGLMF 215
Cdd:cd02440    80 VEDLARFLEEARRL-LKPGGVLV 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 106-215 7.08e-12

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: 61.57  E-value: 7.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 106 NKHVFKDKVVLDVGSGTGILSMFAAKAGAkKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISe 185
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVIC- 93

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462533029 186 wmGYCLFY----ESMLNTVIfardKWLKPGGLMF 215
Cdd:COG2227    94 --SEVLEHlpdpAALLRELA----RLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 115-212 1.72e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.50  E-value: 1.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIISeWMGY 189
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGV------DLSPEMLerareRAAEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVL 73

                          90       100
                  ....*....|....*....|....*
gi 2462533029 190 CLFYESMLNTVI--FARdkWLKPGG 212
Cdd:pfam13649  74 HHLPDPDLEAALreIAR--VLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
107-183 1.16e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 107 KHVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIecssisDYSEKIIKA-------NHLDNIITIFKGKveevelpvEKV 179
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV------DIDPQAVEAarenaelNGVELNVYLPQGD--------LKA 180


                  ....
gi 2462533029 180 DIII 183
Cdd:PRK00517  181 DVIV 184
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 115-215 4.15e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.55  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILSMFAAKAGAKKVFGIecsSIS----DYSEKIIKANHLDNIITIFKGKVEEVELPvEKVDIIIS----EW 186
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGV---TLSpeqlEYARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSigmfEH 130

                          90       100
                  ....*....|....*....|....*....
gi 2462533029 187 MGYcLFYESMLNTVifarDKWLKPGGLMF 215
Cdd:COG2230   131 VGP-ENYPAYFAKV----ARLLKPGGRLL 154
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 108-183 6.42e-09

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: 56.12  E-value: 6.42e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533029 108 HVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKAN-HLDNIITIFKGKVEEvELPVEKVDIII 183
Cdd:pfam06325 158 LVKPGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENaELNGVEARLEVYLPG-DLPKEKADVVV 230
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 116-215 8.36e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.20  E-value: 8.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 116 LDVGSGTGILSMFAAKAGAkKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVELPVEKVDIIISEWMgycLFYES 195
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV---LHHVE 73

                          90       100
                  ....*....|....*....|..
gi 2462533029 196 MLNTVI--FARdkWLKPGGLMF 215
Cdd:pfam08241  74 DPERALreIAR--VLKPGGILI 93
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 115-184 1.57e-07

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: 51.30  E-value: 1.57e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462533029 115 VLDVGSGTGILS-MFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNIITIFKGKVEEV--ELPVEKVDIIIS 184
Cdd:COG4123    41 VLDLGTGTGVIAlMLAQRSPGARITGVEIQPEAaELARRNVALNGLEDRITVIHGDLKEFaaELPPGSFDLVVS 114
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
110-184 3.73e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 3.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533029 110 FKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKANH--LDNIITIFKGKVEEVELpVEKVDIIIS 184
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVD---IDPEALEIARENAerLGVRVDFIRADVTRIPL-GGSVDTVVM 116
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 111-215 1.09e-06

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: 47.30  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 111 KDKVVLDVGSGTGILSMFAAKAGAkKVFGIecssisDYSEKII-----KANHLDNIITIFKGKVEEVELPVEKVDIIISe 185
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGA-RVTGV------DISPEMLelareRAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS- 93

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462533029 186 wmGYCLFYESMLNTVI--FARdkWLKPGGLMF 215
Cdd:COG2226    94 --SFVLHHLPDPERALaeIAR--VLKPGGRLV 121
PRK14968 PRK14968
putative methyltransferase; Provisional
 111-191 1.19e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.27  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 111 KDKVVLDVGSGTGILSMFAAKAGaKKVFGIEcssISDYSEKIIKANHLDNIITIFKGKVEEVEL--PV--EKVDIII--- 183
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNG-KKVVGVD---INPYAVECAKCNAKLNNIRNNGVEVIRSDLfePFrgDKFDVILfnp 98

                          90
                  ....*....|....*....
gi 2462533029 184 -----------SEWMGYCL 191
Cdd:PRK14968   99 pylpteeeeewDDWLNYAL 117
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 111-183 1.75e-05

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 45.94  E-value: 1.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462533029 111 KDKVVLDVGSGTGILSMFAAKAgAKKVFGIECS--SISDySEKIIKANHLDNiITIFKGKVEEV---ELPVEKVDIII 183
Cdd:COG2265   233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpeAVED-ARENARLNGLKN-VEFVAGDLEEVlpeLLWGGRPDVVV 307
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 115-213 4.10e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.75  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILSMFAAKAGAKKVFGIECSSIS-DYSEKIIKANHLDNiITIFKGKVEE-VELPVEKVDIIISEwmgYCLF 192
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGN-VEFLVADLAElDPLPAESFDLVVAF---GVLH 105

                          90       100
                  ....*....|....*....|...
gi 2462533029 193 YESMLNTVIFARD--KWLKPGGL 213
Cdd:COG0500   106 HLPPEEREALLRElaRALKPGGV 128
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 108-240 1.70e-04

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 41.61  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 108 HVFKDKVVLDVGSGTGILSMFAAKAGAKKVFGIEcssISDYSEKIIKAN----HLDNIITIFKGKVEEV--ELPVEKVDI 181
Cdd:COG0742    38 PDIEGARVLDLFAGSGALGLEALSRGAASVVFVE---KDRKAAAVIRKNleklGLEDRARVIRGDALRFlkRLAGEPFDL 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533029 182 IisewmgyclF---------YESMLNTVifARDKWLKPGGLM---------FPDRAALYVVaIEDRQYKDFKIHWWE 240
Cdd:COG0742   115 V---------FldppyakglLEKALELL--AENGLLAPGGLIvvehskreeLPELPAGLEL-LKERKYGDTRLSFYR 179
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
70-213 9.14e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.60  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029  70 MTSRDY---YFDSYAHfgIHEEMLkdeVRTLTYRNSMYHNKHVF------KDKVVLDVGSGTGILSMFAAKAGaKKVFGI 140
Cdd:COG4976     1 MALDAYveaLFDQYAD--SYDAAL---VEDLGYEAPALLAEELLarlppgPFGRVLDLGCGTGLLGEALRPRG-YRLTGV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462533029 141 ecssisDYSEKII---KANHLDniITIFKGKVEEVELPVEKVDIIISeWMGYClfYESMLNTVIFARDKWLKPGGL 213
Cdd:COG4976    75 ------DLSEEMLakaREKGVY--DRLLVADLADLAEPDGRFDLIVA-ADVLT--YLGDLAAVFAGVARALKPGGL 139
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 111-184 1.22e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 39.11  E-value: 1.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533029 111 KDKVVLDVGSGTGILSMFAAKAGAKKVFGIecSSISDYSEKIIKANHLDNIIT-IFKGKVEE--VELPVEKVDIIIS 184
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGV--DLGPMQLWKPRNDPGVTFIQGdIRDPETLDllEELLGRKVDLVLS 95
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 89-214 1.30e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 38.08  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029  89 MLKDEVRTLTYRNSMYHnkhvfKDKVVLDVGSGTGILSMFAAKA-GAKKVFGIE-----CSSIsdysEKIIKANHLDNII 162
Cdd:TIGR02469   2 MTKREVRALTLAKLRLR-----PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLI----ERNLRRFGVSNIV 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462533029 163 TIFKGKVEEVELPVEKVDIIIsewMGYClfyESMLNTVIFARDKWLKPGGLM 214
Cdd:TIGR02469  73 IVEGDAPEAPEALLPDPDAVF---VGGS---GGLLQEILEAVERRLRPGGRI 118
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
109-184 1.85e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.11  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462533029 109 VFKDKVVLDVGSGTGILSMFAAKAgAKKVFGIEC-SSISDYSEKIIKAnhlDNIITIFKGKVEEVELPveKVDIIIS 184
Cdd:PRK14896   27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIA---AGNVEIIEGDALKVDLP--EFNKVVS 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 106-213 1.88e-03

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: 39.19  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 106 NKHVFKDKVVLDVGSGTGILSmfaaKAGAKKVFGIECSS--ISDYSEKIIKaNHLDNIITIFKGKVEEVELPVEKVDIII 183
Cdd:TIGR02072  29 EKGIFIPASVLDIGCGTGYLT----RALLKRFPQAEFIAldISAGMLAQAK-TKLSENVQFICGDAEKLPLEDSSFDLIV 103

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462533029 184 S----EWMGyclfyesMLNTVIFARDKWLKPGGL 213
Cdd:TIGR02072 104 SnlalQWCD-------DLSQALSELARVLKPGGL 130
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 111-184 2.27e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 111 KDKVVLDVGSGTGILSMFAAK--AGAKKVFGIE--CSSISdYSEKIIKANHLDNiITIFKGKVEEVELPVE--KVDIIIS 184
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDisEEAIE-KARENAQKLGFDN-VEFEQGDIEELPELLEddKFDVVIS 80
arsM PRK11873
arsenite methyltransferase;
114-212 3.15e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 38.39  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 114 VVLDVGSGTGILSMFAAKA-GAK-KVFGIecssisDYSEKII---KANH----LDNiITIFKGKVEEVELPVEKVDIIIS 184
Cdd:PRK11873   80 TVLDLGSGGGFDCFLAARRvGPTgKVIGV------DMTPEMLakaRANArkagYTN-VEFRLGEIEALPVADNSVDVIIS 152

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462533029 185 ewmgyclfyesmlNTVI-FARDK---------WLKPGG 212
Cdd:PRK11873  153 -------------NCVInLSPDKervfkeafrVLKPGG 177
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
115-215 3.32e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 36.34  E-value: 3.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462533029 115 VLDVGSGTGILS-MFAAKAGAKKVFGIecssisDYSEKIIKA--NHLDNiITIFKGKVEEVELPvEKVDIIISewmGYCL 191
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGV------DLSPEMLARarARLPN-VRFVVADLRDLDPP-EPFDLVVS---NAAL 73

                          90       100
                  ....*....|....*....|....*...
gi 2462533029 192 FY----ESMLNTVIfardKWLKPGGLMF 215
Cdd:COG4106    74 HWlpdhAALLARLA----AALAPGGVLA 97
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
115-165 4.19e-03

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 37.73  E-value: 4.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462533029 115 VLDVGSGTGILS-MFAAKAGAK-KVFGIECS-SISDYSEKIIKANHLDNIITIF 165
Cdd:pfam01135  77 VLEIGSGSGYLTaCFARMVGEVgRVVSIEHIpELVEIARRNLEKLGLENVIVVV 130
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 111-184 6.78e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 36.80  E-value: 6.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462533029 111 KDKVVLDVGSGTGILSMFAAKAGAKKVfgIECSSISDY----SEKIIKANHLDNiITIFKGKVEEvELPVEKVDIIIS 184
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPDAE--LTMVDINARalesARENLAANGLEN-GEVVASDVYS-GVEDGKFDLIIS 104
 
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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