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Conserved domains on  [gi|18390448|ref|NP_563720|]
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protein arginine methyltransferase 10 [Arabidopsis thaliana]

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];
42-192 3.16e-46

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: 157.89  E-value: 3.16e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  42 LYHQkDMLSDRVRMDAYFNAVfqNKHHFEGKTVLDVGTGSGILAIWSAQAGARKVYAVEA-TKMADHARALVKANNLDHI 120
Cdd:COG4076  10 RWHH-PMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVnPDIAAVARRIIAANGLSDR 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390448 121 VEVIEGSVEDISLPEKVDVIISEWMGYFLLRESMFDSVISARDRWLKPTGVMYPSHARMWLAPIKSNIADRK 192
Cdd:COG4076  87 ITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEG 158
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
42-192 3.16e-46

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 157.89  E-value: 3.16e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  42 LYHQkDMLSDRVRMDAYFNAVfqNKHHFEGKTVLDVGTGSGILAIWSAQAGARKVYAVEA-TKMADHARALVKANNLDHI 120
Cdd:COG4076  10 RWHH-PMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVnPDIAAVARRIIAANGLSDR 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390448 121 VEVIEGSVEDISLPEKVDVIISEWMGYFLLRESMFDSVISARDRWLKPTGVMYPSHARMWLAPIKSNIADRK 192
Cdd:COG4076  87 ITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEG 158
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-170 7.40e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 7.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    74 VLDVGTGSGILAIWSAQAGARKVYAVEAT-KMADHARALVKANNLDhiVEVIEGSVEDISLP-EKVDVIISeWMGYFLLR 151
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGLN--VEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 18390448   152 ESMFDSVISARDRWLKPTG 170
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-173 4.44e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.06  E-value: 4.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  73 TVLDVGTGSGILAIWSAQAGARKVYAVEAT-KMADHARALVKANNLDHiVEVIEGSVEDISL--PEKVDVIISEWMGYFL 149
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISpVALELARKAAAALLADN-VEVLKGDAEELPPeaDESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
gi 18390448 150 LREsmFDSVISARDRWLKPTGVMY 173
Cdd:cd02440  80 VED--LARFLEEARRLLKPGGVLV 101
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
69-141 5.64e-11

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 62.09  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448   69 FEGKTVLDVGTGSGILAIWSAQAGARKVY-------AVEATKmaDHARalvkANNLDHIVEVIEGSvedislpEKVDVII 141
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAAR--ENAE----LNGVELNVYLPQGD-------LKADVIV 184
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 73-121 2.00e-05

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: 44.22  E-value: 2.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18390448    73 TVLDVGTGSGILAIWSAQAGAR-KVYAVEAT-KMADHARALVKANNLDHIV 121
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLpDAYEILEENVKLNNLPNVV 51
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
42-192 3.16e-46

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 157.89  E-value: 3.16e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  42 LYHQkDMLSDRVRMDAYFNAVfqNKHHFEGKTVLDVGTGSGILAIWSAQAGARKVYAVEA-TKMADHARALVKANNLDHI 120
Cdd:COG4076  10 RWHH-PMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVnPDIAAVARRIIAANGLSDR 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390448 121 VEVIEGSVEDISLPEKVDVIISEWMGYFLLRESMFDSVISARDRWLKPTGVMYPSHARMWLAPIKSNIADRK 192
Cdd:COG4076  87 ITVINADATDLDLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEG 158
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
66-141 1.91e-15

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 75.98  E-value: 1.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  66 KHHFEGKTVLDVGTGSGILAIWSAQAGARKVY-------AVEAtkmadhARALVKANNLDHIVEVIEGSVEDislPEKVD 138
Cdd:COG2264 144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLavdidpvAVEA------ARENAELNGVEDRIEVVLGDLLE---DGPYD 214


                ...
gi 18390448 139 VII 141
Cdd:COG2264 215 LVV 217
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 71-173 6.26e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 68.80  E-value: 6.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  71 GKTVLDVGTGSGILAIWSAQAGARKVYAVE-ATKMADHARALVKANNLDHIVEVIEGSVEDISLPEKVDVIIS----EWM 145
Cdd:COG2230  52 GMRVLDIGCGWGGLALYLARRYGVRVTGVTlSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSigmfEHV 131

                        90       100
                ....*....|....*....|....*...
gi 18390448 146 GYfLLRESMFDSVisarDRWLKPTGVMY 173
Cdd:COG2230 132 GP-ENYPAYFAKV----ARLLKPGGRLL 154
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-170 7.40e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 7.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    74 VLDVGTGSGILAIWSAQAGARKVYAVEAT-KMADHARALVKANNLDhiVEVIEGSVEDISLP-EKVDVIISeWMGYFLLR 151
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGLN--VEFVQGDAEDLPFPdGSFDLVVS-SGVLHHLP 77

                          90
                  ....*....|....*....
gi 18390448   152 ESMFDSVISARDRWLKPTG 170
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 65-173 1.04e-12

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 64.65  E-value: 1.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  65 NKHHFEGKTVLDVGTGSGILAIWSAQAGARkVYAVE-ATKMADHARALVKANNldhiVEVIEGSVEDISLP-EKVDVIIS 142
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVDiSPEALEIARERAAELN----VDFVQGDLEDLPLEdGSFDLVIC 93

                        90       100       110
                ....*....|....*....|....*....|...
gi 18390448 143 ewMGYFllrESMFD--SVISARDRWLKPTGVMY 173
Cdd:COG2227  94 --SEVL---EHLPDpaALLRELARLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
69-142 1.59e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 65.70  E-value: 1.59e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390448  69 FEGKTVLDVGTGSGILAIWSAQAGARKVYAVE-ATKMADHARALvkANNLDHIVEVIEGSVEDISLPEKVDVIIS 142
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDiDPEALEIAREN--AERLGVRVDFIRADVTRIPLGGSVDTVVM 116
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 73-173 4.44e-12

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


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 62.06  E-value: 4.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  73 TVLDVGTGSGILAIWSAQAGARKVYAVEAT-KMADHARALVKANNLDHiVEVIEGSVEDISL--PEKVDVIISEWMGYFL 149
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISpVALELARKAAAALLADN-VEVLKGDAEELPPeaDESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....
gi 18390448 150 LREsmFDSVISARDRWLKPTGVMY 173
Cdd:cd02440  80 VED--LARFLEEARRLLKPGGVLV 101
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 70-173 1.28e-11

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: 61.93  E-value: 1.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  70 EGKTVLDVGTGSGILAIWSAQAGARkVYAVE-ATKMADHARALVKANNLDhiVEVIEGSVEDISLP-EKVDVIISEWMGY 147
Cdd:COG2226  22 PGARVLDLGCGTGRLALALAERGAR-VTGVDiSPEMLELARERAAEAGLN--VEFVVGDAEDLPFPdGSFDLVISSFVLH 98

                        90       100       110
                ....*....|....*....|....*....|..
gi 18390448 148 FL------LREsMFdsvisardRWLKPTGVMY 173
Cdd:COG2226  99 HLpdperaLAE-IA--------RVLKPGGRLV 121
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
69-141 5.64e-11

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 62.09  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448   69 FEGKTVLDVGTGSGILAIWSAQAGARKVY-------AVEATKmaDHARalvkANNLDHIVEVIEGSvedislpEKVDVII 141
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAKLGAKKVLavdidpqAVEAAR--ENAE----LNGVELNVYLPQGD-------LKADVIV 184
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 71-142 7.43e-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: 61.70  E-value: 7.43e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390448  71 GKTVLDVGTGSGILAI-WSAQAGARKVYAVEA-TKMADHARALVKANNLDHIVEVIEGSVEDIS---LPEKVDVIIS 142
Cdd:COG4123  38 GGRVLDLGTGTGVIALmLAQRSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLKEFAaelPPGSFDLVVS 114
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 70-179 4.08e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.77  E-value: 4.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  70 EGKTVLDVGTGSGILAIWSAQAGARKVYAVEATK-MADHARALVKANNLDHiVEVIEGSVEDI--SLPEKVDVIISewMG 146
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPeAIALARARAAKAGLGN-VEFLVADLAELdpLPAESFDLVVA--FG 102

                        90       100       110
                ....*....|....*....|....*....|....
gi 18390448 147 YF-LLRESMFDSVISARDRWLKPTGVMYPSHARM 179
Cdd:COG0500 103 VLhHLPPEEREALLRELARALKPGGVLLLSASDA 136
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 70-141 9.21e-10

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: 59.20  E-value: 9.21e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390448    70 EGKTVLDVGTGSGILAIWSAQAGARKVYAVEATKMA-DHARALVKANNLDHIVEVIegsVEDISLPEKVDVII 141
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVY---LPGDLPKEKADVVV 230
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-173 3.45e-09

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 56.06  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448   70 EGKTVLDVGTGSGILAIWSAQAGARKV------YAVEATKMAdharalVKANNLDHI-VEVIEGS-VEDISlPEKVDVII 141
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVECAKCN------AKLNNIRNNgVEVIRSDlFEPFR-GDKFDVIL 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18390448  142 --------------SEWMGYFLL-----REsMFDSVISARDRWLKPTGVMY 173
Cdd:PRK14968  96 fnppylpteeeeewDDWLNYALSggkdgRE-VIDRFLDEVGRYLKPGGRIL 145
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 69-141 8.99e-09

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


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 55.55  E-value: 8.99e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390448  69 FEGKTVLDVGTGSGILAIWSAQA----GarKVYAVEA-TKMADHARALVKANNLDHIVEVIEGSVEDISLPEKVDVII 141
Cdd:COG2519  90 FPGARVLEAGTGSGALTLALARAvgpeG--KVYSYERrEDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDVDAVF 165
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 70-142 1.09e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 55.93  E-value: 1.09e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390448  70 EGKTVLDVGTGSGILAI--WSAQAGARkVYAVEATKMA-DHARALVKANNLDHIVEVIEGSV-EDISLPEKVDVIIS 142
Cdd:COG2890 112 APPRVLDLGTGSGAIALalAKERPDAR-VTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLfEPLPGDGRFDLIVS 187
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-173 1.56e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 51.51  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    75 LDVGTGSGILAIWSAQAGARkVYAVE-ATKMADHARALVKANNLDHIVevieGSVEDISLPEK-VDVIISEWMGYFL--- 149
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVDiSPEMLELAREKAPREGLTFVV----GDAEDLPFPDNsFDLVLSSEVLHHVedp 75

                          90       100
                  ....*....|....*....|....*..
gi 18390448   150 ---LRESMfdsvisardRWLKPTGVMY 173
Cdd:pfam08241  76 eraLREIA---------RVLKPGGILI 93
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 69-141 5.05e-08

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: 52.96  E-value: 5.05e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390448  69 FEGKTVLDVGTGSGILAIWSAQAGARKVYAVEATKMA-DHARALVKANNLDhiVEVIEGSVEDISLPEKVDVII 141
Cdd:COG3897  69 VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEAlAALRLNAALNGVA--ITTRLGDWRDPPAAGGFDLIL 140
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
70-172 1.74e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.67  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  70 EGKTVLDVGTGSGILAIW-SAQAGARKVYAVEAT-KMADHARAlvkanNLDHiVEVIEGSVEDISLPEKVDVIISEWMGY 147
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALlAERFPGARVTGVDLSpEMLARARA-----RLPN-VRFVVADLRDLDPPEPFDLVVSNAALH 74

                        90       100
                ....*....|....*....|....*.
gi 18390448 148 FLL-RESMFDSVIsardRWLKPTGVM 172
Cdd:COG4106  75 WLPdHAALLARLA----AALAPGGVL 96
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 71-142 3.26e-07

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: 49.90  E-value: 3.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390448    71 GKTVLDVGTGSGILAIWSAQAGAR-KVYAVEATKMA-DHARALVKANNLDHiVEVIEGSVEDISLPEKVDVIIS 142
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDaELTMVDINARAlESARENLAANGLEN-GEVVASDVYSGVEDGKFDLIIS 104
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 70-142 6.48e-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: 49.42  E-value: 6.48e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390448  70 EGKTVLDVGTGSGILAIWSAQAGA-RKVYAVEATKMA-DHARALVKANNLDHiVEVIEGSV-EDISlPEKVDVIIS 142
Cdd:COG2813  49 LGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLEN-VEVLWSDGlSGVP-DGSFDLILS 122
arsM PRK11873
arsenite methyltransferase;
70-142 2.68e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 48.41  E-value: 2.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390448   70 EGKTVLDVGTGSGILAIWSAQA-GAR-KVYAVEAT-KMADHARALVKANNLDHiVEVIEGSVEDISLPEK-VDVIIS 142
Cdd:PRK11873  77 PGETVLDLGSGGGFDCFLAARRvGPTgKVIGVDMTpEMLAKARANARKAGYTN-VEFRLGEIEALPVADNsVDVIIS 152
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 50-173 2.81e-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: 47.38  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  50 SDRVRmDAYFNAVfqnKHHFEGKTVLDVGTGSGILAIWSAQAGARKVYAVEAtkmADHARALVKAN----NLDHIVEVIE 125
Cdd:COG0742  25 TDRVR-EALFNIL---GPDIEGARVLDLFAGSGALGLEALSRGAASVVFVEK---DRKAAAVIRKNleklGLEDRARVIR 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18390448 126 GSVEDI---SLPEKVDVIisewmgyFL---LRESMFDSVISA--RDRWLKPTGVMY 173
Cdd:COG0742  98 GDALRFlkrLAGEPFDLV-------FLdppYAKGLLEKALELlaENGLLAPGGLIV 146
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
50-180 3.53e-06

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 46.85  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    50 SDRVRmDAYFNAVfqnKHHFEGKTVLDVGTGSGILAIWSAQAGARKVYAVEATKMAdhARALVKanNLDHI----VEVIE 125
Cdd:pfam03602  25 TDRVR-EALFNWL---APYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRA--VQILKE--NLQLLglpgAVLVM 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390448   126 GSVEDI----SLPEKVDVIisewmgyFL---LRESMFDSVIS--ARDRWLKPTGVMYPSHARMW 180
Cdd:pfam03602  97 DALLALlrlaGKGPVFDIV-------FLdppYAKGLIEEVLDllAEKGWLKPNALIYVETEKRG 153
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 70-142 1.06e-05

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 45.91  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  70 EGKTVLDVGTGSG----ILAIwsaqagAR---KVYAVEAT-KMADHARALVKANNLDHiVEVIEGSVEDISLPEKVDVII 141
Cdd:COG0357  67 EGARVLDVGSGAGfpgiPLAI------ARpdlQVTLVDSLgKKIAFLREVVRELGLKN-VTVVHGRAEELAPREKFDVVT 139


                .
gi 18390448 142 S 142
Cdd:COG0357 140 A 140
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 73-121 2.00e-05

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: 44.22  E-value: 2.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18390448    73 TVLDVGTGSGILAIWSAQAGAR-KVYAVEAT-KMADHARALVKANNLDHIV 121
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAEgRVIAFEPLpDAYEILEENVKLNNLPNVV 51
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 70-141 2.07e-05

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: 46.31  E-value: 2.07e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390448  70 EGKTVLDVGTGSGILAI-WSAQAGARKVYAVEATKMadhARALVKAN----NLDHiVEVIEGSVEDI--SLPEkVDVII 141
Cdd:COG2242 247 PGDVLWDIGAGSGSVSIeAARLAPGGRVYAIERDPE---RAALIRANarrfGVPN-VEVVEGEAPEAlaDLPD-PDAVF 320
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 70-141 2.42e-05

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 45.94  E-value: 2.42e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390448  70 EGKTVLDVGTGSGILAIWSAQAgARKVYAVEATK-MADHARALVKANNLDHiVEVIEGSVEDI----SLPEKVDVII 141
Cdd:COG2265 233 GGERVLDLYCGVGTFALPLARR-AKKVIGVEIVPeAVEDARENARLNGLKN-VEFVAGDLEEVlpelLWGGRPDVVV 307
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 57-171 3.13e-05

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: 45.62  E-value: 3.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  57 AYFNAVFQNKHH------FEGKTVLDVGTGSGILAIWSAQAGARKVYAVE----ATKMadhARALVKANNLDHIVEVIEG 126
Cdd:COG2520 161 VYFSPRLATERLriaelvKPGERVLDMFAGVGPFSIPIAKRSGAKVVAIDinpdAVEY---LKENIRLNKVEDRVTPILG 237

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 18390448 127 SVEDI--SLPEKVDVIIsewMGYFLLRESMFDSVISArdrwLKPTGV 171
Cdd:COG2520 238 DAREVapELEGKADRII---MNLPHSADEFLDAALRA----LKPGGV 277
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 70-143 3.15e-05

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 44.17  E-value: 3.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  70 EGKTVLD--VGTGsGILAiwSAQAGARKVYAVEA-TKMADHARAlvkanNLDH----IVEVIEGSVEDISLP-EKVDVII 141
Cdd:COG1041  26 EGDTVLDpfCGTG-TILI--EAGLLGRRVIGSDIdPKMVEGARE-----NLEHygyeDADVIRGDARDLPLAdESVDAIV 97


                ..
gi 18390448 142 SE 143
Cdd:COG1041  98 TD 99
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 61-142 3.74e-05

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 44.77  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448   61 AVFQNKHHFEGKTVLDVGTGSGILAIwsAQAGAR---KVYAV----EATKMADH-ARALVKANnldhiVEVIEGSVEDIS 132
Cdd:PRK09328  99 WALEALLLKEPLRVLDLGTGSGAIAL--ALAKERpdaEVTAVdispEALAVARRnAKHGLGAR-----VEFLQGDWFEPL 171

                         90
                 ....*....|
gi 18390448  133 LPEKVDVIIS 142
Cdd:PRK09328 172 PGGRFDLIVS 181
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 72-140 3.93e-05

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: 43.63  E-value: 3.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390448  72 KTVLDVGTGSGILAIWSAQAGAR--KVYAVE-ATKMADHARALVKANNLDHIVEVIEGSVEDIsLP----EKVDVI 140
Cdd:COG4122  18 KRILEIGTGTGYSTLWLARALPDdgRLTTIEiDPERAAIARENFARAGLADRIRLILGDALEV-LPrladGPFDLV 92
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
70-100 4.05e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.90  E-value: 4.05e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 18390448  70 EGKTVLDVGTGSGILAIWSAQAGARKVYAVE 100
Cdd:COG2521 132 RGDRVLDTCTGLGYTAIEALKRGAREVITVE 162
PRK14967 PRK14967
putative methyltransferase; Provisional
 71-142 4.80e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 44.27  E-value: 4.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390448   71 GKTVLDVGTGSGILAIWSAQAGARKVYAVEATKMAdHARALVKANNLDHIVEVIEGSVEDISLPEKVDVIIS 142
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRA-VRSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVS 107
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 59-141 1.28e-04

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 43.08  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  59 FNAVFQNKHHFEGKTVLDVGTGS-GILAIWSAQAGARKVYAVEatkMADHARALVKANNLDHIVEVIEGSVED---ISLP 134
Cdd:cd05188 123 YHALRRAGVLKPGDTVLVLGAGGvGLLAAQLAKAAGARVIVTD---RSDEKLELAKELGADHVIDYKEEDLEEelrLTGG 199


                ....*..
gi 18390448 135 EKVDVII 141
Cdd:cd05188 200 GGADVVI 206
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 70-141 1.46e-04

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 42.38  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  70 EGKTVLDVGTGSG----ILAiwsaqAGARKVYAVEATK-MADHARALVKANNLDHiVEVIEGsveDIS--LPEK--VDVI 140
Cdd:COG2518  66 PGDRVLEIGTGSGyqaaVLA-----RLAGRVYSVERDPeLAERARERLAALGYDN-VTVRVG---DGAlgWPEHapFDRI 136


                .
gi 18390448 141 I 141
Cdd:COG2518 137 I 137
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 51-172 2.20e-04

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: 41.42  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    51 DRVRMDAYFNAVFQ--------NKHHFEGKTVLDVGTGSGILAIWSAQAGAR-----KVYAVEATKMA-DHARALVKANN 116
Cdd:pfam05185  36 DPVKYDLYERAIEKalsdrvpeKKKTSKLLVILVVGAGRGPLVDRALRAAEEtgtkvKIYAVEKNPNAyVTLQKRINFEK 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448   117 LDHIVEVIEGSVEDISLPEKVDVIISEWMGYF----LLRESMfDSVisarDRWLKPTGVM 172
Cdd:pfam05185 116 WGDKVTIISSDMREWQGPEKADILVSELLGSFgdneLSPECL-DGA----QKFLKPDGIS 170
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-171 4.69e-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: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    75 LDVGTGSGILAIWSAQAGAR-KVYAVEATK-MADHARALVKANNLDHIVEViEGSVEDIS--LPEKVDVIIsewMGYFLL 150
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPaALEAARERLAALGLLNAVRV-ELFQLDLGelDPGSFDVVV---ASNVLH 76

                          90       100
                  ....*....|....*....|.
gi 18390448   151 RESMFDSVISARDRWLKPTGV 171
Cdd:pfam08242  77 HLADPRAVLRNIRRLLKPGGV 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 63-171 6.68e-04

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.73  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    63 FQNKHHFEGKTVLDVGTGSGIL-AIWSAQAGARKVYAVE-ATKMADHARALVKANnldhiVEVIEGSVEDISLPE-KVDV 139
Cdd:TIGR02072  27 LKEKGIFIPASVLDIGCGTGYLtRALLKRFPQAEFIALDiSAGMLAQAKTKLSEN-----VQFICGDAEKLPLEDsSFDL 101

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18390448   140 IIS----EWMGyfllresMFDSVISARDRWLKPTGV 171
Cdd:TIGR02072 102 IVSnlalQWCD-------DLSQALSELARVLKPGGL 130
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 71-132 1.13e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 40.21  E-value: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390448   71 GKTVLDVGTGSGILAIWSAQAGARkVYAVE-ATKMADHARALVKANNLDHIVEVIEGSVEDIS 132
Cdd:PRK07580  64 GLRILDAGCGVGSLSIPLARRGAK-VVASDiSPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 69-171 1.15e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.14  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448   69 FEGKTVLDVGTGSGILAI-WSAQAGAR-KVYAVE-ATKMADHARALVKANNLDHIVEVIEGSVEDISLPEKVDVIISewM 145
Cdd:PRK00216  50 RPGDKVLDLACGTGDLAIaLAKAVGKTgEVVGLDfSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVT--I 127

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 18390448  146 GYFL---------LREsMFdsvisardRWLKPTGV 171
Cdd:PRK00216 128 AFGLrnvpdidkaLRE-MY--------RVLKPGGR 153
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
70-135 1.79e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.50  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390448   70 EGKTVLDVGTGSGILAIWSAQAgARKVYAVEATK-MADHAR-ALVKANNldhiVEVIEGSVEDISLPE 135
Cdd:PRK14896  29 DGDPVLEIGPGKGALTDELAKR-AKKVYAIELDPrLAEFLRdDEIAAGN----VEIIEGDALKVDLPE 91
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
 51-184 1.95e-03

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 38.93  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    51 DRVRmDAYFNAVFQNKHHFEGktvLDVGTGSGILAIWSAQAGARKVYAVEATKMAdhARALVKanNLD------HIVEVI 124
Cdd:TIGR00095  35 DRVR-ESLFNILRPDIVGAHF---LDLFAGSGALGLEALSRGAASAVFVEQDRKV--AQTLKE--NLStlkksgEQATVL 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390448   125 EGSVEDIS-LPEK---VDVIisewmgyFL---LRESMFDSVISARD--RWLKPTGVMYPSHARMWLAPI 184
Cdd:TIGR00095 107 NDAVRALLfLAKKqtpFDII-------YLdppFNRGLLEALLELLGenKWLNPKGLIVVEYDRENELPT 168
GidB pfam02527
rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited ...
 68-142 2.12e-03

rRNA small subunit methyltransferase G; This is a family of bacterial glucose inhibited division proteins these are probably involved in the regulation of cell devision. GidB has been shown to be a methyltransferase G specific to the rRNA small subunit. Previously identified as a glucose-inhibited division protein B that appears to be present and in a single copy in all complete eubacterial genomes so far sequenced. GidB specifically methylates the N7 position of a guanosine in 16S rRNA.


Pssm-ID: 396880  Cd Length: 184  Bit Score: 38.80  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    68 HFEGKTVLDVGTGSG----ILAIWSAQagaRKVYAVEAT-KMADHARALVKANNLDHiVEVIEGSVEDISLPEKVDVIIS 142
Cdd:pfam02527  46 DNDRDHVLDVGSGAGfpgiPLAIARPD---KKVTLLESLlKKINFLEEVKSELGLDN-VTIVHARAEEYQPEEQYDVITS 121
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 69-140 2.40e-03

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 39.27  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448  69 FEGKTVLDVG--TGsG----ILaiwsaQAGARKVYAVE------ATKMADHARalvkannldhiVEVIEG----SVEDIS 132
Cdd:COG1189  76 VAGKVCLDIGasTG-GftdcLL-----QRGAAKVYAVDvgygqlAWKLRQDPR-----------VVVLERtnarYLTPED 138


                ....*...
gi 18390448 133 LPEKVDVI 140
Cdd:COG1189 139 LPEPPDLV 146
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 70-142 2.65e-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: 39.23  E-value: 2.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390448    70 EGKTVLDVGTGSGILAIWSAQAGARKVYAVEATK-MADHARALVKANNLDHIVEVIEGSVEDisLPEKVDVIIS 142
Cdd:pfam02353  61 PGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKnQYKLARKRVAAEGLARKVEVLLQDYRD--FDEPFDRIVS 132
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 59-142 7.91e-03

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: 37.72  E-value: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390448    59 FNAVFQNKHHFEgktVLDVGTGSGILAIWSAQAGAR-KVYAVEATKmadHARALVKAN----NLDHIVEVIEGSVEDISL 133
Cdd:TIGR00536 106 LASLISQPPILH---ILDLGTGSGCIALALAYEFPNaEVIAVDISP---DALAVAEENaeknQLEHRVEFIQSNLFEPLA 179


                  ....*....
gi 18390448   134 PEKVDVIIS 142
Cdd:TIGR00536 180 GQKIDIIVS 188
 
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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