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Conserved domains on  [gi|1595155924|gb|QBO43036|]
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class I SAM-dependent methyltransferase (plasmid) [Escherichia coli]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10116212)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens guanidinoacetate N-methyltransferase and Saccharomyces cerevisiae protein arginine N-methyltransferase 2

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HsdM super family cl33828
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
32-183 3.33e-14

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


The actual alignment was detected with superfamily member COG0286:

Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 68.29  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  32 FVTPAPVCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMCDA--------VEINSGLVR------YLReNFNGV 97
Cdd:COG0286    25 FYTPREVVRLMVELLDPKPGETVYDPACGSGGFLVEAAEYLKEHGGDErkklslygQEINPTTYRlakmnlLLH-GIGDP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  98 RVQCGDFM--EWQPVQYYSRIIMNPPFS---HGQDIRH--------------------ILRAFSLLRPGGVLVAVCLNGP 152
Cdd:COG0286   104 NIELGDTLsnDGDELEKFDVVLANPPFGgkwKKEELKDdllgrfgyglppksnadllfLQHILSLLKPGGRAAVVLPDGV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1595155924 153 --RQQEKllpfsDVREE------------LPRGTFAYTDVPTMII 183
Cdd:COG0286   184 lfRGAEK-----EIRKKllendlleaiigLPSNLFYNTGIPTCIL 223
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
32-183 3.33e-14

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 68.29  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  32 FVTPAPVCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMCDA--------VEINSGLVR------YLReNFNGV 97
Cdd:COG0286    25 FYTPREVVRLMVELLDPKPGETVYDPACGSGGFLVEAAEYLKEHGGDErkklslygQEINPTTYRlakmnlLLH-GIGDP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  98 RVQCGDFM--EWQPVQYYSRIIMNPPFS---HGQDIRH--------------------ILRAFSLLRPGGVLVAVCLNGP 152
Cdd:COG0286   104 NIELGDTLsnDGDELEKFDVVLANPPFGgkwKKEELKDdllgrfgyglppksnadllfLQHILSLLKPGGRAAVVLPDGV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1595155924 153 --RQQEKllpfsDVREE------------LPRGTFAYTDVPTMII 183
Cdd:COG0286   184 lfRGAEK-----EIRKKllendlleaiigLPSNLFYNTGIPTCIL 223
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-149 3.51e-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: 60.14  E-value: 3.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  54 ILEPSAGTGAILRAIRDtAPEAMCDAVEINSGLVRYLREN-----FNGVRVQCGDFMEWQ--PVQYYSRIIMNPPFSHG- 125
Cdd:cd02440     2 VLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAaaallADNVEVLKGDAEELPpeADESFDVIISDPPLHHLv 80

                          90       100
                  ....*....|....*....|....*
gi 1595155924 126 QDIRHILR-AFSLLRPGGVLVAVCL 149
Cdd:cd02440    81 EDLARFLEeARRLLKPGGVLVLTLV 105
rADc smart00650
Ribosomal RNA adenine dimethylases;
38-145 4.02e-07

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 47.51  E-value: 4.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924   38 VCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMcdAVEINSGLVRYLRENF---NGVRVQCGDFM--EWQPVQY 112
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVT--AIEIDPRLAPRLREKFaaaDNLTVIHGDALkfDLPKLQP 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1595155924  113 YsRIIMNPPFSHGQDI-RHILRAFSLLRPGGVLV 145
Cdd:smart00650  79 Y-KVVGNLPYNISTPIlFKLLEEPPAFRDAVLMV 111
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-142 7.50e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 7.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  54 ILEPSAGTGAILRAIRDtAPEAMCDAVEINSGLVRYLRENFNG----VRVQCGDFMEWQ-PVQYYSRIIMNPPFSH--GQ 126
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPfPDGSFDLVVSSGVLHHlpDP 79

                          90
                  ....*....|....*..
gi 1595155924 127 DIRHILR-AFSLLRPGG 142
Cdd:pfam13649  80 DLEAALReIARVLKPGG 96
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
38-95 2.68e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1595155924  38 VCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMcdAVEINSGLVRYLRENFN 95
Cdd:PRK14896   17 VVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVY--AIELDPRLAEFLRDDEI 72
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 6-178 2.07e-04

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924   6 RERI-RLMRARLDNAaPVAEIRAESQ-----LFVTPAPVCDRLVT--LAEISNRD--------HILEPSAGTGAILRAIR 69
Cdd:TIGR00536  55 KERIfRLVLRRVKGV-PVAYLLGSKEfygleFFVNEHVLIPRPETeeLVEKALASlisqppilHILDLGTGSGCIALALA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  70 DTAPEAMCDAVEINSGLVRYLRENF------NGVRVQCGDFMEWQPVQYYSRIIMNPPFSHGQD---------------- 127
Cdd:TIGR00536 134 YEFPNAEVIAVDISPDALAVAEENAeknqleHRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDladlpnvvrfepllal 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595155924 128 ---------IRHILR-AFSLLRPGGVLvaVCLNGPRQQEKLlpfsdvrEELPRGTFAYTDV 178
Cdd:TIGR00536 214 vggddglniLRQIIElAPDYLKPNGFL--VCEIGNWQQKSL-------KELLRIKFTWYDV 265
 
Name Accession Description Interval E-value
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
32-183 3.33e-14

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 68.29  E-value: 3.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  32 FVTPAPVCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMCDA--------VEINSGLVR------YLReNFNGV 97
Cdd:COG0286    25 FYTPREVVRLMVELLDPKPGETVYDPACGSGGFLVEAAEYLKEHGGDErkklslygQEINPTTYRlakmnlLLH-GIGDP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  98 RVQCGDFM--EWQPVQYYSRIIMNPPFS---HGQDIRH--------------------ILRAFSLLRPGGVLVAVCLNGP 152
Cdd:COG0286   104 NIELGDTLsnDGDELEKFDVVLANPPFGgkwKKEELKDdllgrfgyglppksnadllfLQHILSLLKPGGRAAVVLPDGV 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1595155924 153 --RQQEKllpfsDVREE------------LPRGTFAYTDVPTMII 183
Cdd:COG0286   184 lfRGAEK-----EIRKKllendlleaiigLPSNLFYNTGIPTCIL 223
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
53-148 5.60e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 61.76  E-value: 5.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  53 HILEPSAGTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENFNGVRVQCGDFMEWQPVQYYSRIIMNPPFSHGQDIRHIL 132
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPFDLVVSNAALHWLPDHAALL 83

                          90
                  ....*....|....*..
gi 1595155924 133 -RAFSLLRPGGVLVAVC 148
Cdd:COG4106    84 aRLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 54-149 3.51e-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: 60.14  E-value: 3.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  54 ILEPSAGTGAILRAIRDtAPEAMCDAVEINSGLVRYLREN-----FNGVRVQCGDFMEWQ--PVQYYSRIIMNPPFSHG- 125
Cdd:cd02440     2 VLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAaaallADNVEVLKGDAEELPpeADESFDVIISDPPLHHLv 80

                          90       100
                  ....*....|....*....|....*
gi 1595155924 126 QDIRHILR-AFSLLRPGGVLVAVCL 149
Cdd:cd02440    81 EDLARFLEeARRLLKPGGVLVLTLV 105
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
39-165 1.08e-11

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 60.61  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  39 CDRLVTLAEISNRDHILEPSAGTGAILRAIRDT-APEAMCDAVEINSGLVRYLRENFNGVRVQCGD------FMEWQPVQ 111
Cdd:COG3963    34 ARAMASEVDWSGAGPVVELGPGTGVFTRAILARgVPDARLLAVEINPEFAEHLRRRFPRVTVVNGDaedlaeLLAEHGIG 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924 112 YYSRIIMNPPFSH-GQDIRH-ILR-AFSLLRPGGVLVAVC--LNGPRQQEKLLP-FSDVR 165
Cdd:COG3963   114 KVDAVVSGLPLLSfPPELRRaILDaAFRVLAPGGVFVQFTysPRSPVPRKLLRRgFEAVR 173
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
10-137 1.61e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 60.30  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  10 RLMRARLDNAAPVAEIRAESQLFVTPAPVCDRLVTLAEISNR---DHILEPSAGTG--AILRAIRDtAPEAMCdaVEINS 84
Cdd:COG2263     2 RELEIILEKLPGFSNPKVELEQYPTPAELAAELLHLAYLRGDiegKTVLDLGCGTGmlAIGAALLG-AKKVVG--VDIDP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  85 GLVRYLRENFN--GVRVQ--CGDFMEWQPVQYYSRIIMNPPFS---HGQDIRHILRAFSL 137
Cdd:COG2263    79 EALEIARENAErlGVRVDfiRADVTRIPLGGSVDTVVMNPPFGaqrRHADRPFLEKALEI 138
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 45-147 3.87e-11

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: 59.77  E-value: 3.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  45 LAEISNRDHILEPSAGTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENF--NG----VRVQCGDFMEWQ---PVQYYSR 115
Cdd:COG4123    32 FAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNValNGledrITVIHGDLKEFAaelPPGSFDL 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1595155924 116 IIMNPP-FSHGQDI----------RH---------ILRAFSLLRPGGVLVAV 147
Cdd:COG4123   112 VVSNPPyFKAGSGRkspdearaiaRHedaltledlIRAAARLLKPGGRFALI 163
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-156 5.03e-08

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: 49.61  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  40 DRLVTLAEISNRDHILEPSAGTGAILRAIRDTApeAMCDAVEINSGLVRYLRENFN----GVRVQCGDFMEWQ-PVQYYS 114
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAeaglNVEFVVGDAEDLPfPDGSFD 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1595155924 115 RIIMNPPFSHGQDIRHILR-AFSLLRPGGVLVAVCLNGPRQQE 156
Cdd:COG2226    90 LVISSFVLHHLPDPERALAeIARVLKPGGRLVVVDFSPPDLAE 132
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 59-147 3.09e-07

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: 48.26  E-value: 3.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  59 AGTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENF--NG---VRVQCGDFMEWQPVQYYSRIIMNPPFSHGQDIRH--- 130
Cdd:COG2813    58 CGYGVIGLALAKRNPEARVTLVDVNARAVELARANAaaNGlenVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVDKeva 137

                          90       100
                  ....*....|....*....|
gi 1595155924 131 ---ILRAFSLLRPGGVLVAV 147
Cdd:COG2813   138 halIADAARHLRPGGELWLV 157
rADc smart00650
Ribosomal RNA adenine dimethylases;
38-145 4.02e-07

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 47.51  E-value: 4.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924   38 VCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMcdAVEINSGLVRYLRENF---NGVRVQCGDFM--EWQPVQY 112
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVT--AIEIDPRLAPRLREKFaaaDNLTVIHGDALkfDLPKLQP 78

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1595155924  113 YsRIIMNPPFSHGQDI-RHILRAFSLLRPGGVLV 145
Cdd:smart00650  79 Y-KVVGNLPYNISTPIlFKLLEEPPAFRDAVLMV 111
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 38-106 1.25e-06

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 47.04  E-value: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595155924  38 VCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEamCDAVEINSGLVRYLRENFNG---VRVQCGDFME 106
Cdd:COG0030    25 IIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAAR--VTAVEIDRRLAAILRETFAAypnLTVIEGDALK 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-142 7.50e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 42.55  E-value: 7.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  54 ILEPSAGTGAILRAIRDtAPEAMCDAVEINSGLVRYLRENFNG----VRVQCGDFMEWQ-PVQYYSRIIMNPPFSH--GQ 126
Cdd:pfam13649   1 VLDLGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEaglnVEFVQGDAEDLPfPDGSFDLVVSSGVLHHlpDP 79

                          90
                  ....*....|....*..
gi 1595155924 127 DIRHILR-AFSLLRPGG 142
Cdd:pfam13649  80 DLEAALReIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 53-150 2.15e-05

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: 42.31  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  53 HILEPSAGTGAILRAIRDTAPEAmcDAVEINSGLVRYLRENFN--GVRVQCGDFMEWQ-PVQYYSRIIMNPPFSHGQDIR 129
Cdd:COG2227    27 RVLDVGCGTGRLALALARRGADV--TGVDISPEALEIARERAAelNVDFVQGDLEDLPlEDGSFDLVICSEVLEHLPDPA 104

                          90       100
                  ....*....|....*....|..
gi 1595155924 130 HILRAF-SLLRPGGVLVAVCLN 150
Cdd:COG2227   105 ALLRELaRLLKPGGLLLLSTPN 126
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
38-95 2.68e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 2.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1595155924  38 VCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEAMcdAVEINSGLVRYLRENFN 95
Cdd:PRK14896   17 VVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVY--AIELDPRLAEFLRDDEI 72
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
27-145 5.91e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.91  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  27 AESQLFVTPAPVCDRLVTLAEISNRDHILEPSAGTGAILRAIRDTAPEamCDAVEINSGLVRYLRENFNGVRVQCGDFME 106
Cdd:COG4976    23 VEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR--LTGVDLSEEMLAKAREKGVYDRLLVADLAD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1595155924 107 W-QPVQYYSRIIMNPPFSHGQDIRHILR-AFSLLRPGGVLV 145
Cdd:COG4976   101 LaEPDGRFDLIVAADVLTYLGDLAAVFAgVARALKPGGLFI 141
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 53-147 9.31e-05

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: 41.04  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  53 HILEPSAGTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENF-----NGVRVQCGDFMEWQPVQYYSRIIMNPPFSHGQD 127
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLaanglENGEVVASDVYSGVEDGKFDLIISNPPFHAGLA 113

                          90       100
                  ....*....|....*....|....*.
gi 1595155924 128 I------RHILRAFSLLRPGGVLVAV 147
Cdd:pfam05175 114 TtynvaqRFIADAKRHLRPGGELWIV 139
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 55-144 1.08e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 39.66  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  55 LEPSAGTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENFNGVRVQCGDFMEW-------QPVQYYSRIIMNPPFSHGQD 127
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELfqldlgeLDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1595155924 128 IRHILRAFS-LLRPGGVL 144
Cdd:pfam08242  81 PRAVLRNIRrLLKPGGVL 98
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 6-178 2.07e-04

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924   6 RERI-RLMRARLDNAaPVAEIRAESQ-----LFVTPAPVCDRLVT--LAEISNRD--------HILEPSAGTGAILRAIR 69
Cdd:TIGR00536  55 KERIfRLVLRRVKGV-PVAYLLGSKEfygleFFVNEHVLIPRPETeeLVEKALASlisqppilHILDLGTGSGCIALALA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  70 DTAPEAMCDAVEINSGLVRYLRENF------NGVRVQCGDFMEWQPVQYYSRIIMNPPFSHGQD---------------- 127
Cdd:TIGR00536 134 YEFPNAEVIAVDISPDALAVAEENAeknqleHRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDladlpnvvrfepllal 213

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595155924 128 ---------IRHILR-AFSLLRPGGVLvaVCLNGPRQQEKLlpfsdvrEELPRGTFAYTDV 178
Cdd:TIGR00536 214 vggddglniLRQIIElAPDYLKPNGFL--VCEIGNWQQKSL-------KELLRIKFTWYDV 265
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 52-144 2.13e-04

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 40.62  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  52 DHILEPSAGTG--AILRAIRDTApeaMCDAVEINSGLVRYLRENF--NGVR----VQCGDFMEWQPVQY--YSRIIMN-P 120
Cdd:COG2520   182 ERVLDMFAGVGpfSIPIAKRSGA---KVVAIDINPDAVEYLKENIrlNKVEdrvtPILGDAREVAPELEgkADRIIMNlP 258

                          90       100
                  ....*....|....*....|....
gi 1595155924 121 PFSHgqdiRHILRAFSLLRPGGVL 144
Cdd:COG2520   259 HSAD----EFLDAALRALKPGGVI 278
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 60-145 5.25e-04

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: 5.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  60 GTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENF------NGVRVQCGDFmeWQPVQYYSR---IIMNPP--------- 121
Cdd:COG2890   122 GSGAIALALAKERPDARVTAVDISPDALAVARRNAerlgleDRVRFLQGDL--FEPLPGDGRfdlIVSNPPyipedeial 199

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1595155924 122 --------------FShGQD----IRHILR-AFSLLRPGGVLV 145
Cdd:COG2890   200 lppevrdheprlalDG-GEDgldfYRRIIAqAPRLLKPGGWLL 241
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 42-146 3.36e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 36.70  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  42 LVTLAEISNRDHILEPSAGTG----AILRAIRDtapEAMCDAVEINSGLVRYLRENF------NGVRVQCGDFMEWQPvq 111
Cdd:COG4122     8 LYLLARLLGAKRILEIGTGTGystlWLARALPD---DGRLTTIEIDPERAAIARENFaraglaDRIRLILGDALEVLP-- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1595155924 112 yysrIIMNPPF-------SHGQDIRHILRAFSLLRPGGVLVA 146
Cdd:COG4122    83 ----RLADGPFdlvfidaDKSNYPDYLELALPLLRPGGLIVA 120
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 79-143 3.57e-03

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 36.56  E-value: 3.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595155924  79 AVEINSGLVRYLRENF------NGVRVQCGDFMEWQPVQYYSRIIMNPPFShgqDIRHILRAFSLLRPGGV 143
Cdd:pfam02475 128 AIELNPESYKYLKENIklnkveDVVKPILGDVREVILEDVADRVVMNLPGS---AHEFLDKAFAAVRDGGV 195
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-145 4.34e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.06  E-value: 4.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  40 DRLVTLAEISNRDHILEPSAGTGA-ILRAIRDTapEAMCDAVEINSGLVRYLRENF------NGVRVQCGDFMEWQPVQY 112
Cdd:COG2230    41 DLILRKLGLKPGMRVLDIGCGWGGlALYLARRY--GVRVTGVTLSPEQLEYARERAaeaglaDRVEVRLADYRDLPADGQ 118

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1595155924 113 YSRIIMNPPFSH--GQDIRHILR-AFSLLRPGGVLV 145
Cdd:COG2230   119 FDAIVSIGMFEHvgPENYPAYFAkVARLLKPGGRLL 154
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 41-155 4.72e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 36.22  E-value: 4.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  41 RLVTLAEISNRDHILEPSAGTG---AILRAirdtapeaMCD---AVEINSGLVRYLRENF-----NGVRVQCGDFME-WQ 108
Cdd:COG2518    57 RMLEALDLKPGDRVLEIGTGSGyqaAVLAR--------LAGrvySVERDPELAERARERLaalgyDNVTVRVGDGALgWP 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1595155924 109 PVQYYSRIIMN--PPfshgqdirHILRA-FSLLRPGGVLVAVCLNGPRQQ 155
Cdd:COG2518   129 EHAPFDRIIVTaaAP--------EVPEAlLEQLAPGGRLVAPVGEGGVQR 170
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
29-122 6.32e-03

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 36.19  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  29 SQLFVTPAPVCDRLVTLAEISNRDHILEPSAGTGAILRAIRDtapeaMCD---AVEINSGLVRYLRENFNG---VRVQCG 102
Cdd:pfam00398   9 GQNFLKDPKVINEIVDKANLRESDTVLEIGPGKGALTVILAK-----RAKqvvAIEIDPRLAKLLQKKLSLdenLTVIHQ 83

                          90       100
                  ....*....|....*....|
gi 1595155924 103 DFMEWQPvqYYSRIIMNPPF 122
Cdd:pfam00398  84 DFLKFEF--PSLVTHIHQEF 101
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
60-146 7.33e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 35.96  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595155924  60 GTGAILRAIRDTAPEAMCDAVEINSGLVRYLRENF---------NGVRVQCGDFMEW--QPVQYYSRIIMNPPFSHGQDI 128
Cdd:COG0421    47 GDGGLARELLKHPPVERVDVVEIDPEVVELAREYFpllapafddPRLRVVIGDGRAFlrEAEESYDVIIVDLTDPVGPAE 126

                          90       100
                  ....*....|....*....|...
gi 1595155924 129 RHILRAF-----SLLRPGGVLVA 146
Cdd:COG0421   127 GLFTREFyedcrRALKPGGVLVV 149
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
 113-173 8.77e-03

S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.


Pssm-ID: 287624 [Multi-domain]  Cd Length: 286  Bit Score: 36.01  E-value: 8.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595155924 113 YSRIIMNPP------FSHGQDIRHILRAF-SLLRPGGVLVAvCLNGPRQQEKLLpFSDVREELPRGTF 173
Cdd:pfam10672 196 YDLVIIDPPsfqkgsFALTKDYKKILRRLpELLVEGGTVLA-CVNSPAVGPDFL-IEEMAEEAPSLHF 261
 
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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