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Conserved domains on  [gi|51258689|gb|AAH80055|]
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MGC83989 protein [Xenopus laevis]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 1905023)

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

EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12826405|12504684
SCOP:  3000118

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];
22-237 1.60e-41

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: 144.41  E-value: 1.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  22 YSDVSIHEEMIADTVRTNGYKQAILHNhcALQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLASHVVTLNGM 100
Cdd:COG4076   6 FFVPRWHHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARRIIAANGL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689 101 DNKVKVLNSPVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGIILPSAADLFIAPINDRVVEsrlDFWn 180
Cdd:COG4076  84 SDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDA---EGF- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51258689 181 EVKGLYGVDMSC--MRPFAHSCIMnKEMAVNLLSPEDVLSFPVRFASLDLNVCTQEEVR 237
Cdd:COG4076 160 EDWQFDGFDFRLfgFLLYAEPLLH-LTRLVRTPLLLLLLPTAFDEFPFDLASQRATSAQ 217
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
22-237 1.60e-41

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 144.41  E-value: 1.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  22 YSDVSIHEEMIADTVRTNGYKQAILHNhcALQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLASHVVTLNGM 100
Cdd:COG4076   6 FFVPRWHHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARRIIAANGL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689 101 DNKVKVLNSPVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGIILPSAADLFIAPINDRVVEsrlDFWn 180
Cdd:COG4076  84 SDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDA---EGF- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51258689 181 EVKGLYGVDMSC--MRPFAHSCIMnKEMAVNLLSPEDVLSFPVRFASLDLNVCTQEEVR 237
Cdd:COG4076 160 EDWQFDGFDFRLfgFLLYAEPLLH-LTRLVRTPLLLLLLPTAFDEFPFDLASQRATSAQ 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-156 3.63e-09

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: 53.59  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  56 TVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESA--EIPEQVDAIVSEWMGYAL 132
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEELppEADESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
gi 51258689 133 MyESMLPSVIYARDKwLKPGGIIL 156
Cdd:cd02440  80 V-EDLARFLEEARRL-LKPGGVLV 101
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 52-158 7.17e-08

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: 53.04  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    52 LQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQLAS-HVVTLNGMDNKVKVLNspveSAEIP-EQVDAIVSEWMG 129
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAkENAELNGVEARLEVYL----PGDLPkEKADVVVANILA 235

                          90       100
                  ....*....|....*....|....*....
gi 51258689   130 YALMyesMLPSVIYARdkwLKPGGIILPS 158
Cdd:pfam06325 236 DPLI---ELAPDIYAL---VKPGGYLILS 258
PRK14968 PRK14968
putative methyltransferase; Provisional
 54-156 3.75e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 43.73  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689   54 GLTVLDVGAGTGILSVFCVQAGAtRVYAVEAS--AVsQLASHVVTLNGMDN-KVKVLNS----PVESAE----------I 116
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINpyAV-ECAKCNAKLNNIRNnGVEVIRSdlfePFRGDKfdvilfnppyL 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 51258689  117 PEQVDAIVSEWMGYAL--------MYESMLPSViyarDKWLKPGGIIL 156
Cdd:PRK14968 102 PTEEEEEWDDWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 56-108 1.81e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 41.14  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51258689    56 TVLDVGAGTGILSVFCVQAGA-TRVYAVEAS--AVSQLASHvVTLNGMDNkVKVLN 108
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpdAYEILEEN-VKLNNLPN-VVLLN 54
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
22-237 1.60e-41

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 144.41  E-value: 1.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  22 YSDVSIHEEMIADTVRTNGYKQAILHNhcALQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLASHVVTLNGM 100
Cdd:COG4076   6 FFVPRWHHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARRIIAANGL 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689 101 DNKVKVLNSPVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGIILPSAADLFIAPINDRVVEsrlDFWn 180
Cdd:COG4076  84 SDRITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDA---EGF- 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 51258689 181 EVKGLYGVDMSC--MRPFAHSCIMnKEMAVNLLSPEDVLSFPVRFASLDLNVCTQEEVR 237
Cdd:COG4076 160 EDWQFDGFDFRLfgFLLYAEPLLH-LTRLVRTPLLLLLLPTAFDEFPFDLASQRATSAQ 217
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 51-156 1.27e-09

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: 55.41  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  51 ALQGLTVLDVGAGTGILSVFCVQAGAtRVYAVEAS--AVSQLASHVVTLNgmdnkVKVLNSPVESAEIP-EQVDAIVSew 127
Cdd:COG2227  22 LPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISpeALEIARERAAELN-----VDFVQGDLEDLPLEdGSFDLVIC-- 93

                        90       100
                ....*....|....*....|....*....
gi 51258689 128 mGYALMYESMLPSVIYARDKWLKPGGIIL 156
Cdd:COG2227  94 -SEVLEHLPDPAALLRELARLLKPGGLLL 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-156 3.63e-09

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: 53.59  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  56 TVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESA--EIPEQVDAIVSEWMGYAL 132
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEELppEADESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
gi 51258689 133 MyESMLPSVIYARDKwLKPGGIIL 156
Cdd:cd02440  80 V-EDLARFLEEARRL-LKPGGVLV 101
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 54-156 4.16e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.94  E-value: 4.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  54 GLTVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDNKVKVLNSPVESAEIPEQVDAIVS----EWM 128
Cdd:COG2230  52 GMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQlEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSigmfEHV 131

                        90       100
                ....*....|....*....|....*...
gi 51258689 129 GYALmYESMLPSViyarDKWLKPGGIIL 156
Cdd:COG2230 132 GPEN-YPAYFAKV----ARLLKPGGRLL 154
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
51-165 5.69e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 53.25  E-value: 5.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  51 ALQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQLASHV-VTLNGMDNKVKVLNSPVESaeiPEQVDAIVsewmg 129
Cdd:COG2264 146 LKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAAREnAELNGVEDRIEVVLGDLLE---DGPYDLVV----- 217

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 51258689 130 yA------LMyeSMLPsVIYARdkwLKPGGI-----ILPSAADLFIA 165
Cdd:COG2264 218 -AnilanpLI--ELAP-DLAAL---LKPGGYlilsgILEEQADEVLA 257
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 52-158 7.17e-08

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: 53.04  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    52 LQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQLAS-HVVTLNGMDNKVKVLNspveSAEIP-EQVDAIVSEWMG 129
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAkENAELNGVEARLEVYL----PGDLPkEKADVVVANILA 235

                          90       100
                  ....*....|....*....|....*....
gi 51258689   130 YALMyesMLPSVIYARdkwLKPGGIILPS 158
Cdd:pfam06325 236 DPLI---ELAPDIYAL---VKPGGYLILS 258
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
52-125 8.49e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.83  E-value: 8.49e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51258689  52 LQGLTVLDVGAGTGILSVFCVQAGATRVYAVEA--SAVSQLASHvvtLNGMDNKVKVLNSPVESAEIPEQVDAIVS 125
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIdpEALEIAREN---AERLGVRVDFIRADVTRIPLGGSVDTVVM 116
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 53-165 1.13e-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: 52.07  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  53 QGLTVLDVGAGTGILSVFCVQ-AGATRVYAVEA-SAVSQLASHVVTLNGMDNKVKVLNSPV---ESAEIPEQVDAIVS-- 125
Cdd:COG4123  37 KGGRVLDLGTGTGVIALMLAQrSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLkefAAELPPGSFDLVVSnp 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51258689 126 ----EWMGY-------AL-MYESMLP--SVIYARDKWLKPGG----IILPSAADLFIA 165
Cdd:COG4123 117 pyfkAGSGRkspdearAIaRHEDALTleDLIRAAARLLKPGGrfalIHPAERLAEILA 174
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-153 2.03e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.33  E-value: 2.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    57 VLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMdnKVKVLNSPVESAEIP-EQVDAIVSeWMGYALMY 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMlERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90       100
                  ....*....|....*....|.
gi 51258689   135 ESMLPSVI--YARdkWLKPGG 153
Cdd:pfam13649  78 DPDLEAALreIAR--VLKPGG 96
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 46-156 1.07e-06

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 48.73  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  46 LHNHCALQGLTVLDVGAGTGILSVFCVQAGATRVYAVEasaVSQLASHVVTLNGMDNKVKV--LNSPVESAEIPEQVDAI 123
Cdd:COG3897  63 LLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATD---YDPEALAALRLNAALNGVAIttRLGDWRDPPAAGGFDLI 139

                        90       100       110
                ....*....|....*....|....*....|....*
gi 51258689 124 V-SEwmgyaLMYESMLPSVIYAR-DKWLKPGGIIL 156
Cdd:COG3897 140 LgGD-----VLYERDLAEPLLPFlDRLAAPGGEVL 169
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 34-129 1.82e-06

PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding protein 1) is PRMT5, an arginine-N-methyltransferase. These proteins appear to be key mitotic regulators. They play a role in Jak signalling in higher eukaryotes.


Pssm-ID: 428356  Cd Length: 171  Bit Score: 47.58  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    34 DTVRTNGYKQAIlhnHCALQ-----------GLTVLDVGAGTGILsVFCV-QAGAT-----RVYAVEA--SAVSQLaSHV 94
Cdd:pfam05185  36 DPVKYDLYERAI---EKALSdrvpekkktskLLVILVVGAGRGPL-VDRAlRAAEEtgtkvKIYAVEKnpNAYVTL-QKR 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 51258689    95 VTLNGMDNKVKVLNSPVESAEIPEQVDAIVSEWMG 129
Cdd:pfam05185 111 INFEKWGDKVTIISSDMREWQGPEKADILVSELLG 145
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 56-125 3.05e-06

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: 47.11  E-value: 3.05e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51258689  56 TVLDVGAGTGILSVFCVQAGA-TRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESAEIPEQVDAIVS 125
Cdd:COG2813  52 RVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILS 122
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 45-175 4.81e-06

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: 46.23  E-value: 4.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  45 ILHNHcaLQGLTVLDVGAGTGILSvfcVQA---GATRVYAVEAS--AVSQLASHVVTLnGMDNKVKVLNSPVESA---EI 116
Cdd:COG0742  35 ILGPD--IEGARVLDLFAGSGALG---LEAlsrGAASVVFVEKDrkAAAVIRKNLEKL-GLEDRARVIRGDALRFlkrLA 108

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51258689 117 PEQVDAIvseWMG--YAL-MYESMLPSViyARDKWLKPGGIIL---PSAADLFIAPINDRVVESR 175
Cdd:COG0742 109 GEPFDLV---FLDppYAKgLLEKALELL--AENGLLAPGGLIVvehSKREELPELPAGLELLKER 168
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 54-156 1.16e-05

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: 44.60  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  54 GLTVLDVGAGTGILSVFCVQAGAtRVYAVEASA--VSQLASHvvtLNGMDNKVKVLNSPVESAEIP-EQVDAIVSewmGY 130
Cdd:COG2226  23 GARVLDLGCGTGRLALALAERGA-RVTGVDISPemLELARER---AAEAGLNVEFVVGDAEDLPFPdGSFDLVIS---SF 95

                        90       100
                ....*....|....*....|....*...
gi 51258689 131 ALMYESMLPSVIY--ARdkWLKPGGIIL 156
Cdd:COG2226  96 VLHHLPDPERALAeiAR--VLKPGGRLV 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
53-156 1.89e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.89  E-value: 1.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  53 QGLTVLDVGAGTGILSVFCVQA--GAtRVYAVEASA--VSQLASHVvtlngmdNKVKVLNSPVESAEIPEQVDAIVSewm 128
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERfpGA-RVTGVDLSPemLARARARL-------PNVRFVVADLRDLDPPEPFDLVVS--- 69

                        90       100       110
                ....*....|....*....|....*....|..
gi 51258689 129 GYALMY----ESMLPSVIyardKWLKPGGIIL 156
Cdd:COG4106  70 NAALHWlpdhAALLARLA----AALAPGGVLA 97
PRK14968 PRK14968
putative methyltransferase; Provisional
 54-156 3.75e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 43.73  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689   54 GLTVLDVGAGTGILSVFCVQAGAtRVYAVEAS--AVsQLASHVVTLNGMDN-KVKVLNS----PVESAE----------I 116
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINpyAV-ECAKCNAKLNNIRNnGVEVIRSdlfePFRGDKfdvilfnppyL 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 51258689  117 PEQVDAIVSEWMGYAL--------MYESMLPSViyarDKWLKPGGIIL 156
Cdd:PRK14968 102 PTEEEEEWDDWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
52-156 4.48e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 44.37  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689   52 LQGLTVLDVGAGTGILSVFCVQAGATRVY-------AVEASAvsqlasHVVTLNGMDNKVKVlnspvesAEIPEQVDAIV 124
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAAR------ENAELNGVELNVYL-------PQGDLKADVIV 184

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 51258689  125 sewmgyA------LMyesMLPSVIYARdkwLKPGGIIL 156
Cdd:PRK00517 185 ------AnilanpLL---ELAPDLARL---LKPGGRLI 210
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 53-162 5.66e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.37  E-value: 5.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  53 QGLTVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDN-KVKVLNSPVESAEIPEQVDAIVS----E 126
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVAfgvlH 105

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 51258689 127 WMGyalmyESMLPSVIYARDKWLKPGGIILPSAADL 162
Cdd:COG0500 106 HLP-----PEEREALLRELARALKPGGVLLLSASDA 136
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 58-156 6.26e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.11  E-value: 6.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    58 LDVGAGTGILSVFCVQAGAtRVYAVEASAVsqlASHVVTLNGMDNKVKVLNSPVESAEIP-EQVDAIVSEWmgyALMYES 136
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPE---MLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSE---VLHHVE 73

                          90       100
                  ....*....|....*....|
gi 51258689   137 MLPSVIYARDKWLKPGGIIL 156
Cdd:pfam08241  74 DPERALREIARVLKPGGILI 93
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 56-108 1.81e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 41.14  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 51258689    56 TVLDVGAGTGILSVFCVQAGA-TRVYAVEAS--AVSQLASHvVTLNGMDNkVKVLN 108
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpdAYEILEEN-VKLNNLPN-VVLLN 54
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
33-156 2.11e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.52  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  33 ADTVRTNGYK------QAILHNHCALQGLTVLDVGAGTGILSVFCVQAGaTRVYAVEASA--VSQLASHvvtlnGMDNKV 104
Cdd:COG4976  20 AALVEDLGYEapallaEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEemLAKAREK-----GVYDRL 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 51258689 105 KVLNsPVESAEIPEQVDAIVSewmGYALMYESMLPSVIYARDKWLKPGGIIL 156
Cdd:COG4976  94 LVAD-LADLAEPDGRFDLIVA---ADVLTYLGDLAAVFAGVARALKPGGLFI 141
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 58-155 5.44e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.89  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    58 LDVGAGTGILSVFCVQAGA-TRVYAVEAS--AVSQLASHVVTLNGMDNKVKVLNSPVESAEIPEQVDAIVsewMGYALMY 134
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISpaALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 51258689   135 ESMLPSVIYARDKWLKPGGII 155
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 43-156 7.25e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.53  E-value: 7.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689   43 QAILHNHCALQGLTVLDVGAGTGILSV----FCVQAgatRVYAVEAS--AVSQLASHVVTLNGmdNKVKVLNSPVESAEI 116
Cdd:PRK09328  98 EWALEALLLKEPLRVLDLGTGSGAIALalakERPDA---EVTAVDISpeALAVARRNAKHGLG--ARVEFLQGDWFEPLP 172

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51258689  117 PEQVDAIVS--------EW---MGYALMYEsmlPSV----------IYAR-----DKWLKPGGIIL 156
Cdd:PRK09328 173 GGRFDLIVSnppyipeaDIhllQPEVRDHE---PHLalfggedgldFYRRiieqaPRYLKPGGWLL 235
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
52-124 1.51e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.89  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  52 LQGLTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLAshvvTLNG-----MDNKVKVLNSPVeSAEIP----EQVD 121
Cdd:COG2521 131 RRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDPnVLELA----ELNPwsrelANERIKIILGDA-SEVIKtfpdESFD 205


                ...
gi 51258689 122 AIV 124
Cdd:COG2521 206 AII 208
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 53-156 1.72e-03

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 39.62  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689    53 QGLTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQ-LASHVVTLNGMDNKVKVLNSPVEsaEIPEQVDAIVSEWMGYA 131
Cdd:pfam02353  61 PGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYkLARKRVAAEGLARKVEVLLQDYR--DFDEPFDRIVSVGMFEH 138

                          90       100
                  ....*....|....*....|....*
gi 51258689   132 LMYESmLPSVIYARDKWLKPGGIIL 156
Cdd:pfam02353 139 VGHEN-YDTFFKKLYNLLPPGGLML 162
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 43-125 2.28e-03

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.36  E-value: 2.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689  43 QAILHNHCALQGLTVLDVGAGTGILSVFCVQA-GATRVYAVEAS--AVsQLASHVVTLNGMDNKVKVLNS----PVESAe 115
Cdd:COG2890 102 ELALALLPAGAPPRVLDLGTGSGAIALALAKErPDARVTAVDISpdAL-AVARRNAERLGLEDRVRFLQGdlfePLPGD- 179

                        90
                ....*....|
gi 51258689 116 ipEQVDAIVS 125
Cdd:COG2890 180 --GRFDLIVS 187
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 28-86 3.78e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 38.28  E-value: 3.78e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 51258689   28 HEEMIADTVrtngykqAILHNHCALQGLTVLDVGAGTGILSVFCVQAGAtRVYAVEASA 86
Cdd:PRK07580  45 HQRMRDTVL-------SWLPADGDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISP 95
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 52-155 5.68e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.19  E-value: 5.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51258689   52 LQGLTVLDVGAGTGILSVFCVQAgATRVYAVE--ASAVSQLAShvvtLNGMDNKVKVLNSPVESAEI---PEQVDAIVSE 126
Cdd:PLN02336  36 YEGKSVLELGAGIGRFTGELAKK-AGQVIALDfiESVIKKNES----INGHYKNVKFMCADVTSPDLnisDGSVDLIFSN 110

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 51258689  127 WMgyaLMY------ESMLPSVIyardKWLKPGGII 155
Cdd:PLN02336 111 WL---LMYlsdkevENLAERMV----KWLKVGGYI 138
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 53-82 7.60e-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: 36.80  E-value: 7.60e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 51258689    53 QGLTVLDVGAGTGILSVFCVQAGATRVYAV 82
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGV 50
 
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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