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Conserved domains on  [gi|749395227|gb|AJF18554|]
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prmt6, partial [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];
1-175 6.27e-42

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: 140.94  E-value: 6.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   1 HEEMIADTVRTNGYKQAILHNrcALQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLASHVVTLNGMDNKVKV 79
Cdd:COG4076   12 HHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARRIIAANGLSDRITV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  80 LNSPVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGIILPSAADLFIAPINDRVVEsrlDFWnEVKGLY 159
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDA---EGF-EDWQFD 165
                        170
                 ....*....|....*...
gi 749395227 160 GVDMSC--MRPFAHSCIM 175
Cdd:COG4076  166 GFDFRLfgFLLYAEPLLH 183
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
1-175 6.27e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 140.94  E-value: 6.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   1 HEEMIADTVRTNGYKQAILHNrcALQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLASHVVTLNGMDNKVKV 79
Cdd:COG4076   12 HHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARRIIAANGLSDRITV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  80 LNSPVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGIILPSAADLFIAPINDRVVEsrlDFWnEVKGLY 159
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDA---EGF-EDWQFD 165
                        170
                 ....*....|....*...
gi 749395227 160 GVDMSC--MRPFAHSCIM 175
Cdd:COG4076  166 GFDFRLfgFLLYAEPLLH 183
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
25-131 3.37e-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: 54.96  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   25 LQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQLAS-HVVTLNGMDNKVKVLNspveSAEIP-EQVDAIVSEWMG 102
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAkENAELNGVEARLEVYL----PGDLPkEKADVVVANILA 235
                          90       100
                  ....*....|....*....|....*....
gi 749395227  103 YALMyesMLPSVIYARdkwLKPGGIILPS 131
Cdd:pfam06325 236 DPLI---ELAPDIYAL---VKPGGYLILS 258
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
29-129 8.84e-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: 51.28  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  29 TVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESA--EIPEQVDAIVSEWMGYAL 105
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEELppEADESFDVIISDPPLHHL 79
                         90       100
                 ....*....|....*....|....
gi 749395227 106 MyESMLPSVIYARDKwLKPGGIIL 129
Cdd:cd02440   80 V-EDLARFLEEARRL-LKPGGVLV 101
PRK14968 PRK14968
putative methyltransferase; Provisional
27-129 2.79e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  27 GHTVLDVGAGTGILSVFCVQAGAtRVYAVEAS--AVsQLASHVVTLNGMDN-KVKVLNS----PVESAE----------I 89
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINpyAV-ECAKCNAKLNNIRNnGVEVIRSdlfePFRGDKfdvilfnppyL 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 749395227  90 PEQVDAIVSEWMGYAL--------MYESMLPSViyarDKWLKPGGIIL 129
Cdd:PRK14968 102 PTEEEEEWDDWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
29-81 3.49e-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: 39.22  E-value: 3.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 749395227   29 TVLDVGAGTGILSVFCVQAGA-TRVYAVEAS--AVSQLASHvVTLNGMDNkVKVLN 81
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpdAYEILEEN-VKLNNLPN-VVLLN 54
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
1-175 6.27e-42

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 140.94  E-value: 6.27e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   1 HEEMIADTVRTNGYKQAILHNrcALQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLASHVVTLNGMDNKVKV 79
Cdd:COG4076   12 HHPMLNDVERNDAFKAAIERV--VKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPdIAAVARRIIAANGLSDRITV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  80 LNSPVESAEIPEQVDAIVSEWMGYALMYESMLPSVIYARDKWLKPGGIILPSAADLFIAPINDRVVEsrlDFWnEVKGLY 159
Cdd:COG4076   90 INADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDA---EGF-EDWQFD 165
                        170
                 ....*....|....*...
gi 749395227 160 GVDMSC--MRPFAHSCIM 175
Cdd:COG4076  166 GFDFRLfgFLLYAEPLLH 183
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
27-129 2.24e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.86  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  27 GHTVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDNKVKVLNSPVESAEIPEQVDAIVS----EWM 101
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQlEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSigmfEHV 131
                         90       100
                 ....*....|....*....|....*...
gi 749395227 102 GYALmYESMLPSViyarDKWLKPGGIIL 129
Cdd:COG2230  132 GPEN-YPAYFAKV----ARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
21-129 2.17e-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: 53.48  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  21 NRCALQGHTVLDVGAGTGILSVFCVQAGAtRVYAVEAS--AVSQLASHVVTLNgmdnkVKVLNSPVESAEIP-EQVDAIV 97
Cdd:COG2227   19 ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISpeALEIARERAAELN-----VDFVQGDLEDLPLEdGSFDLVI 92
                         90       100       110
                 ....*....|....*....|....*....|..
gi 749395227  98 SewmGYALMYESMLPSVIYARDKWLKPGGIIL 129
Cdd:COG2227   93 C---SEVLEHLPDPAALLRELARLLKPGGLLL 121
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
25-131 3.37e-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: 54.96  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   25 LQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQLAS-HVVTLNGMDNKVKVLNspveSAEIP-EQVDAIVSEWMG 102
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAkENAELNGVEARLEVYL----PGDLPkEKADVVVANILA 235
                          90       100
                  ....*....|....*....|....*....
gi 749395227  103 YALMyesMLPSVIYARdkwLKPGGIILPS 131
Cdd:pfam06325 236 DPLI---ELAPDIYAL---VKPGGYLILS 258
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
29-129 8.84e-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: 51.28  E-value: 8.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  29 TVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESA--EIPEQVDAIVSEWMGYAL 105
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEELppEADESFDVIISDPPLHHL 79
                         90       100
                 ....*....|....*....|....
gi 749395227 106 MyESMLPSVIYARDKwLKPGGIIL 129
Cdd:cd02440   80 V-EDLARFLEEARRL-LKPGGVLV 101
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
26-138 1.46e-08

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: 52.84  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  26 QGHTVLDVGAGTGILSVFCVQ-AGATRVYAVEA-SAVSQLASHVVTLNGMDNKVKVLNSPV---ESAEIPEQVDAIVS-- 98
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMLAQrSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLkefAAELPPGSFDLVVSnp 116
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 749395227  99 ----EWMGY-------AL-MYESMLP--SVIYARDKWLKPGG----IILPSAADLFIA 138
Cdd:COG4123  117 pyfkAGSGRkspdearAIaRHEDALTleDLIRAAARLLKPGGrfalIHPAERLAEILA 174
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
22-97 3.18e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 52.10  E-value: 3.18e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749395227  22 RCALQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQLASHV-VTLNGMDNKVKVLNSPVESaeiPEQVDAIV 97
Cdd:COG2264  144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAAREnAELNGVEDRIEVVLGDLLE---DGPYDLVV 217
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
25-98 9.41e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 50.29  E-value: 9.41e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749395227  25 LQGHTVLDVGAGTGILSVFCVQAGATRVYAVEA--SAVSQLASHvvtLNGMDNKVKVLNSPVESAEIPEQVDAIVS 98
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIdpEALEIAREN---AERLGVRVDFIRADVTRIPLGGSVDTVVM 116
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
30-126 3.69e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 46.40  E-value: 3.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   30 VLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMdnKVKVLNSPVESAEIP-EQVDAIVSeWMGYALMY 107
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMlERARERAAEAGL--NVEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77
                          90       100
                  ....*....|....*....|.
gi 749395227  108 ESMLPSVI--YARdkWLKPGG 126
Cdd:pfam13649  78 DPDLEAALreIAR--VLKPGG 96
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
29-98 1.98e-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: 46.34  E-value: 1.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749395227  29 TVLDVGAGTGILSVFCVQAGA-TRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESAEIPEQVDAIVS 98
Cdd:COG2813   52 RVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILS 122
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
7-102 3.33e-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: 45.27  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227    7 DTVRTNGYKQAIlhnRCALQ-----------GHTVLDVGAGTGILsVFCV-QAGAT-----RVYAVE--ASAVSQLaSHV 67
Cdd:pfam05185  36 DPVKYDLYERAI---EKALSdrvpekkktskLLVILVVGAGRGPL-VDRAlRAAEEtgtkvKIYAVEknPNAYVTL-QKR 110
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 749395227   68 VTLNGMDNKVKVLNSPVESAEIPEQVDAIVSEWMG 102
Cdd:pfam05185 111 INFEKWGDKVTIISSDMREWQGPEKADILVSELLG 145
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
18-148 4.46e-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: 45.07  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  18 ILHNRcaLQGHTVLDVGAGTGILSvfcVQA---GATRVYAVEAS--AVSQLASHVVTLnGMDNKVKVLNSPVESA---EI 89
Cdd:COG0742   35 ILGPD--IEGARVLDLFAGSGALG---LEAlsrGAASVVFVEKDrkAAAVIRKNLEKL-GLEDRARVIRGDALRFlkrLA 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749395227  90 PEQVDAIvseWMG--YAL-MYESMLPSViyARDKWLKPGGIIL---PSAADLFIAPINDRVVESR 148
Cdd:COG0742  109 GEPFDLV---FLDppYAKgLLEKALELL--AENGLLAPGGLIVvehSKREELPELPAGLELLKER 168
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
19-79 5.98e-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: 45.26  E-value: 5.98e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749395227  19 LHNRCALQGHTVLDVGAGTGILSVFCVQAGATRVYAVEasaVSQLASHVVTLNGMDNKVKV 79
Cdd:COG3897   63 LLDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATD---YDPEALAALRLNAALNGVAI 120
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
27-129 1.01e-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: 43.44  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  27 GHTVLDVGAGTGILSVFCVQAGAtRVYAVEASA--VSQLASHvvtLNGMDNKVKVLNSPVESAEIP-EQVDAIVSewmGY 103
Cdd:COG2226   23 GARVLDLGCGTGRLALALAERGA-RVTGVDISPemLELARER---AAEAGLNVEFVVGDAEDLPFPdGSFDLVIS---SF 95
                         90       100
                 ....*....|....*....|....*...
gi 749395227 104 ALMYESMLPSVIY--ARdkWLKPGGIIL 129
Cdd:COG2226   96 VLHHLPDPERALAeiAR--VLKPGGRLV 121
PRK14968 PRK14968
putative methyltransferase; Provisional
27-129 2.79e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  27 GHTVLDVGAGTGILSVFCVQAGAtRVYAVEAS--AVsQLASHVVTLNGMDN-KVKVLNS----PVESAE----------I 89
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINpyAV-ECAKCNAKLNNIRNnGVEVIRSdlfePFRGDKfdvilfnppyL 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 749395227  90 PEQVDAIVSEWMGYAL--------MYESMLPSViyarDKWLKPGGIIL 129
Cdd:PRK14968 102 PTEEEEEWDDWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
26-129 3.01e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 41.35  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  26 QGHTVLDVGAGTGILSVFCVQA--GAtRVYAVEASA--VSQLASHVvtlngmdNKVKVLNSPVESAEIPEQVDAIVSewm 101
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGA-RVTGVDLSPemLARARARL-------PNVRFVVADLRDLDPPEPFDLVVS--- 69
                         90       100       110
                 ....*....|....*....|....*....|..
gi 749395227 102 GYALMY----ESMLPSVIyardKWLKPGGIIL 129
Cdd:COG4106   70 NAALHWlpdhAALLARLA----AALAPGGVLA 97
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
31-129 9.39e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 39.96  E-value: 9.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   31 LDVGAGTGILSVFCVQAGAtRVYAVEASAVsqlASHVVTLNGMDNKVKVLNSPVESAEIP-EQVDAIVSEWmgyALMYES 109
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPE---MLELAREKAPREGLTFVVGDAEDLPFPdNSFDLVLSSE---VLHHVE 73
                          90       100
                  ....*....|....*....|
gi 749395227  110 MLPSVIYARDKWLKPGGIIL 129
Cdd:pfam08241  74 DPERALREIARVLKPGGILI 93
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
25-129 1.19e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 41.68  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  25 LQGHTVLDVGAGTGILSVFCVQAGATRVY-------AVEASAvsqlasHVVTLNGMDNKVKVlnspvesAEIPEQVDAIV 97
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAAR------ENAELNGVELNVYL-------PQGDLKADVIV 184
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 749395227  98 sewmgyA------LMyesMLPSVIYARdkwLKPGGIIL 129
Cdd:PRK00517 185 ------AnilanpLL---ELAPDLARL---LKPGGRLI 210
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
25-97 1.50e-04

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 41.43  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  25 LQGHTVLDVGAGTGILSVFCVQAGATRVYAVEASA-VSQLAshvvTLNG-----MDNKVKVLNSPVeSAEIP----EQVD 94
Cdd:COG2521  131 RRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDPnVLELA----ELNPwsrelANERIKIILGDA-SEVIKtfpdESFD 205

                 ...
gi 749395227  95 AIV 97
Cdd:COG2521  206 AII 208
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
29-135 2.15e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 40.67  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  29 TVLDVGAGTGILSVFCVQAGATRVYAVEASAVS-QLASHVVTLNGMDN-KVKVLNSPVESAEIPEQVDAIVS----EWMG 102
Cdd:COG0500   29 RVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGNvEFLVADLAELDPLPAESFDLVVAfgvlHHLP 108
                         90       100       110
                 ....*....|....*....|....*....|...
gi 749395227 103 yalmyESMLPSVIYARDKWLKPGGIILPSAADL 135
Cdd:COG0500  109 -----PEEREALLRELARALKPGGVLLLSASDA 136
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
29-81 3.49e-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: 39.22  E-value: 3.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 749395227   29 TVLDVGAGTGILSVFCVQAGA-TRVYAVEAS--AVSQLASHvVTLNGMDNkVKVLN 81
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpdAYEILEEN-VKLNNLPN-VVLLN 54
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
31-128 3.52e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.50  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   31 LDVGAGTGILSVFCVQAGA-TRVYAVEAS--AVSQLASHVVTLNGMDNKVKVLNSPVESAEIPEQVDAIVsewMGYALMY 107
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISpaALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNVLHH 77
                          90       100
                  ....*....|....*....|.
gi 749395227  108 ESMLPSVIYARDKWLKPGGII 128
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
26-129 9.62e-04

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: 38.85  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   26 QGHTVLDVGAGTGILSVFCVQAGATRVYAVEASAVSQ-LASHVVTLNGMDNKVKVLNSPVEsaEIPEQVDAIVSEWMGYA 104
Cdd:pfam02353  61 PGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYkLARKRVAAEGLARKVEVLLQDYR--DFDEPFDRIVSVGMFEH 138
                          90       100
                  ....*....|....*....|....*
gi 749395227  105 LMYESmLPSVIYARDKWLKPGGIIL 129
Cdd:pfam02353 139 VGHEN-YDTFFKKLYNLLPPGGLML 162
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
25-128 1.38e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.96  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  25 LQGHTVLDVGAGTGILSVFCVQAgATRVYAVE--ASAVSQLAShvvtLNGMDNKVKVLNSPVESAEI---PEQVDAIVSE 99
Cdd:PLN02336  36 YEGKSVLELGAGIGRFTGELAKK-AGQVIALDfiESVIKKNES----INGHYKNVKFMCADVTSPDLnisDGSVDLIFSN 110
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 749395227 100 WMgyaLMY------ESMLPSVIyardKWLKPGGII 128
Cdd:PLN02336 111 WL---LMYlsdkevENLAERMV----KWLKVGGYI 138
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
6-129 2.13e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 37.67  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   6 ADTVRTNGYK------QAILHNRCALQGHTVLDVGAGTGILSVFCVQAGaTRVYAVEASA--VSQLASHvvtlnGMDNKV 77
Cdd:COG4976   20 AALVEDLGYEapallaEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEemLAKAREK-----GVYDRL 93
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 749395227  78 KVLNsPVESAEIPEQVDAIVSewmGYALMYESMLPSVIYARDKWLKPGGIIL 129
Cdd:COG4976   94 LVAD-LADLAEPDGRFDLIVA---ADVLTYLGDLAAVFAGVARALKPGGLFI 141
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
27-98 2.44e-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: 37.18  E-value: 2.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749395227   27 GHTVLDVGAGTGILSVFCVQAGA-TRVYAVEASAVS-QLASHVVTLNGMDNkVKVLNSPVESAEIPEQVDAIVS 98
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPdAELTMVDINARAlESARENLAANGLEN-GEVVASDVYSGVEDGKFDLIIS 104
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
26-55 2.48e-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: 37.18  E-value: 2.48e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 749395227   26 QGHTVLDVGAGTGILSVFCVQAGATRVYAV 55
Cdd:pfam01728  21 PGKTVLDLGAAPGGWSQVALQRGAGKVVGV 50
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
16-129 4.30e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 37.06  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  16 QAILHNRCALQGHTVLDVGAGTGILSV----FCVQAgatRVYAVEAS--AVSQLASHVVTLNGmdNKVKVLNSPVESAEI 89
Cdd:PRK09328  98 EWALEALLLKEPLRVLDLGTGSGAIALalakERPDA---EVTAVDISpeALAVARRNAKHGLG--ARVEFLQGDWFEPLP 172
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749395227  90 PEQVDAIVS--------EW---MGYALMYEsmlPSV----------IYAR-----DKWLKPGGIIL 129
Cdd:PRK09328 173 GGRFDLIVSnppyipeaDIhllQPEVRDHE---PHLalfggedgldFYRRiieqaPRYLKPGGWLL 235
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
24-98 6.42e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 36.67  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  24 ALQGHTVLDVGAGTGILSVFCVQA-GATRVYAVEAS--AVsQLASHVVTLNGMDNKVKVLNS----PVESAeipEQVDAI 96
Cdd:COG2890  110 AGAPPRVLDLGTGSGAIALALAKErPDARVTAVDISpdAL-AVARRNAERLGLEDRVRFLQGdlfePLPGD---GRFDLI 185

                 ..
gi 749395227  97 VS 98
Cdd:COG2890  186 VS 187
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
1-59 7.44e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 36.35  E-value: 7.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 749395227   1 HEEMIADTVrtngykqAILHNRCALQGHTVLDVGAGTGILSVFCVQAGAtRVYAVEASA 59
Cdd:PRK07580  45 HQRMRDTVL-------SWLPADGDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISP 95
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
26-132 7.56e-03

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 35.93  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227  26 QGHTVLDVGAGTGILSvfcVQAG-----ATRVYAVEAsavSQLASHVVTLNGmdNKVKVLNSPV-ESAEIPEQVDAIVSE 99
Cdd:PRK00377  40 KGDMILDIGCGTGSVT---VEASllvgeTGKVYAVDK---DEKAINLTRRNA--EKFGVLNNIVlIKGEAPEILFTINEK 111
                         90       100       110
                 ....*....|....*....|....*....|....
gi 749395227 100 WMGYALMYESM-LPSVIYARDKWLKPGGIILPSA 132
Cdd:PRK00377 112 FDRIFIGGGSEkLKEIISASWEIIKKGGRIVIDA 145
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
27-134 8.71e-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: 35.00  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749395227   27 GHTVLDVGAGTGILSV-FCVQAGATRVYAVEAS--AVSQLASHVVTLnGMDNKVKVLNSPVESAE-IPEQVDAIVSEWMG 102
Cdd:TIGR02469  20 GDVLWDIGAGTGSVTIeAARLVPNGRVYAIERNpeALDLIERNLRRF-GVSNIVIVEGDAPEAPEaLLPDPDAVFVGGSG 98
                          90       100       110
                  ....*....|....*....|....*....|..
gi 749395227  103 yalmyeSMLPSVIYARDKWLKPGGIILPSAAD 134
Cdd:TIGR02469  99 ------GLLQEILEAVERRLRPGGRIVLNAIT 124
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
27-59 9.46e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 36.30  E-value: 9.46e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 749395227  27 GHTVLDVGAGTGILSV-FCVQAGATRVYAVEASA 59
Cdd:COG2242  248 GDVLWDIGAGSGSVSIeAARLAPGGRVYAIERDP 281
 
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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