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Conserved domains on  [gi|357197158|ref|NP_001239405|]
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protein arginine N-methyltransferase 1 isoform 2 [Mus musculus]

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];
45-218 8.18e-47

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: 158.66  E-value: 8.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  45 HEEMLKDEVRtltyrNSMFH---NRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS-SISDYAVKIVKANKLDHV 120
Cdd:COG4076   12 HHPMLNDVER-----NDAFKaaiERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158 121 VTIIKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWweN 200
Cdd:COG4076   87 ITVINADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--Q 163

                        170
                 ....*....|....*...
gi 357197158 201 VYGFDMSCIKDVAIKEPL 218
Cdd:COG4076  164 FDGFDFRLFGFLLYAEPL 181
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
45-218 8.18e-47

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 158.66  E-value: 8.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  45 HEEMLKDEVRtltyrNSMFH---NRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS-SISDYAVKIVKANKLDHV 120
Cdd:COG4076   12 HHPMLNDVER-----NDAFKaaiERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158 121 VTIIKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWweN 200
Cdd:COG4076   87 ITVINADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--Q 163

                        170
                 ....*....|....*...
gi 357197158 201 VYGFDMSCIKDVAIKEPL 218
Cdd:COG4076  164 FDGFDFRLFGFLLYAEPL 181
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-171 1.57e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   74 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN--KLDHVVTIIKGKVEEVELPVEKVDIIISeWMGYCLF 151
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVD---LSPEMLERARERaaEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 357197158  152 YESMLNTVLH--ARdkWLAPDG 171
Cdd:pfam13649  77 PDPDLEAALReiAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-174 5.86e-11

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: 58.98  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  74 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVK---ANKLDHVVTIIKGKVEE-VELPVEKVDIIISeWMGYC 149
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVD---ISPVALELARkaaAALLADNVEVLKGDAEElPPEADESFDVIIS-DPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 357197158 150 LFYESMLNTVLHARDKwLAPDGLIF 174
Cdd:cd02440   78 HLVEDLARFLEEARRL-LKPGGVLV 101
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
66-142 3.00e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.00  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  66 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN-KLDHVvtiikgkVEEVELP--VEKVDIII 142
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAARENaELNGV-------ELNVYLPqgDLKADVIV 184
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
45-218 8.18e-47

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 158.66  E-value: 8.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  45 HEEMLKDEVRtltyrNSMFH---NRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS-SISDYAVKIVKANKLDHV 120
Cdd:COG4076   12 HHPMLNDVER-----NDAFKaaiERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158 121 VTIIKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWweN 200
Cdd:COG4076   87 ITVINADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--Q 163

                        170
                 ....*....|....*...
gi 357197158 201 VYGFDMSCIKDVAIKEPL 218
Cdd:COG4076  164 FDGFDFRLFGFLLYAEPL 181
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 65-174 3.92e-14

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: 68.12  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  65 NRHLFKDKVVLDVGSGTGILCMFAAKAGARkVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISe 144
Cdd:COG2227   19 ARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVIC- 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 357197158 145 wmgyclfyesmLNTVLHARD---------KWLAPDGLIF 174
Cdd:COG2227   94 -----------SEVLEHLPDpaallrelaRLLKPGGLLL 121
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
66-142 1.66e-12

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 67.12  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  66 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKI----VKANKLDHVVTIIKGKVeeveLPVEKVDII 141
Cdd:COG2264  144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVD---IDPVAVEAarenAELNGVEDRIEVVLGDL----LEDGPYDLV 216


                 .
gi 357197158 142 I 142
Cdd:COG2264  217 V 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-171 1.57e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   74 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN--KLDHVVTIIKGKVEEVELPVEKVDIIISeWMGYCLF 151
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVD---LSPEMLERARERaaEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 357197158  152 YESMLNTVLH--ARdkWLAPDG 171
Cdd:pfam13649  77 PDPDLEAALReiAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-174 5.86e-11

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: 58.98  E-value: 5.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  74 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVK---ANKLDHVVTIIKGKVEE-VELPVEKVDIIISeWMGYC 149
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVD---ISPVALELARkaaAALLADNVEVLKGDAEElPPEADESFDVIIS-DPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 357197158 150 LFYESMLNTVLHARDKwLAPDGLIF 174
Cdd:cd02440   78 HLVEDLARFLEEARRL-LKPGGVLV 101
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
69-143 2.50e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 59.15  E-value: 2.50e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357197158  69 FKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN--KLDHVVTIIKGKVEEVELpVEKVDIIIS 143
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVD---IDPEALEIARENaeRLGVRVDFIRADVTRIPL-GGSVDTVVM 116
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-174 1.66e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.21  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   75 LDVGSGTGILCMFAAKAGARkVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMgycLFYES 154
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV---LHHVE 73

                          90       100
                  ....*....|....*....|
gi 357197158  155 MLNTVLHARDKWLAPDGLIF 174
Cdd:pfam08241  74 DPERALREIARVLKPGGILI 93
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 66-142 1.87e-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: 58.05  E-value: 1.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357197158   66 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN-KLDHVVTIIKGKVEEvELPVEKVDIII 142
Cdd:pfam06325 157 RLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENaELNGVEARLEVYLPG-DLPKEKADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
66-142 3.00e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.00  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  66 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN-KLDHVvtiikgkVEEVELP--VEKVDIII 142
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAARENaELNGV-------ELNVYLPqgDLKADVIV 184
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 74-174 3.83e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.24  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  74 VLDVGSGTGILCMFAAKAGARKVIGIecsSIS----DYAVKIVKANKLDHVVTIIKGKVEEVELPvEKVDIIIS----EW 145
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYGVRVTGV---TLSpeqlEYARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSigmfEH 130

                         90       100
                 ....*....|....*....|....*....
gi 357197158 146 MGYcLFYESMLNTVlharDKWLAPDGLIF 174
Cdd:COG2230  131 VGP-ENYPAYFAKV----ARLLKPGGRLL 154
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 74-143 5.58e-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: 5.58e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 357197158  74 VLDVGSGTGILC-MFAAKAGARKVIGIECSSIS-DYAVKIVKANKLDHVVTIIKGKVEEV--ELPVEKVDIIIS 143
Cdd:COG4123   41 VLDLGTGTGVIAlMLAQRSPGARITGVEIQPEAaELARRNVALNGLEDRITVIHGDLKEFaaELPPGSFDLVVS 114
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 70-143 1.59e-07

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: 49.99  E-value: 1.59e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357197158  70 KDKVVLDVGSGTGILCMFAAKAGARkVIGIEcssISDYAVKIV--KANKLDHVVTIIKGKVEEVELPVEKVDIIIS 143
Cdd:COG2226   22 PGARVLDLGCGTGRLALALAERGAR-VTGVD---ISPEMLELAreRAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
29-174 2.76e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.00  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  29 MTSKDY---YFDSYAHfgIHEEMLkdeVRTLTYRN------SMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARkVIGI 99
Cdd:COG4976    1 MALDAYveaLFDQYAD--SYDAAL---VEDLGYEApallaeELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGV 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357197158 100 EcssISDYAVKIVKANKLDhvVTIIKGKVEEVELPVEKVDIIISeWMGYClfYESMLNTVLHARDKWLAPDG-LIF 174
Cdd:COG4976   75 D---LSEEMLAKAREKGVY--DRLLVADLADLAEPDGRFDLIVA-ADVLT--YLGDLAAVFAGVARALKPGGlFIF 142
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 74-174 4.13e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 4.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  74 VLDVGSGTGILCMFAAKAGARKVIGIECSSIS-DYAVKIVKANKLDHvVTIIKGKVEE-VELPVEKVDIIISeWMGYCLF 151
Cdd:COG0500   30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGN-VEFLVADLAElDPLPAESFDLVVA-FGVLHHL 107

                         90       100
                 ....*....|....*....|...
gi 357197158 152 YESMLNTVLHARDKWLAPDGLIF 174
Cdd:COG0500  108 PPEEREALLRELARALKPGGVLL 130
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 59-199 3.08e-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: 47.00  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  59 RNSMFhNR--HLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN----KLDHVVTIIKGKVEEV- 131
Cdd:COG0742   29 REALF-NIlgPDIEGARVLDLFAGSGALGLEALSRGAASVVFVE---KDRKAAAVIRKNleklGLEDRARVIRGDALRFl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158 132 -ELPVEKVDIIIsewmgycL---FYESMLNTVLHA--RDKWLAPDGLI---------FPDRATLYvTAIEDRQYKDYKIH 196
Cdd:COG0742  105 kRLAGEPFDLVF-------LdppYAKGLLEKALELlaENGLLAPGGLIvvehskreeLPELPAGL-ELLKERKYGDTRLS 176


                 ...
gi 357197158 197 WWE 199
Cdd:COG0742  177 FYR 179
arsM PRK11873
arsenite methyltransferase;
73-143 3.96e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 47.64  E-value: 3.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357197158  73 VVLDVGSGTGILCMFAAKA-GAR-KVIGIEcssISDYAVKIVKAN--KLDHV-VTIIKGKVEEVELPVEKVDIIIS 143
Cdd:PRK11873  80 TVLDLGSGGGFDCFLAARRvGPTgKVIGVD---MTPEMLAKARANarKAGYTnVEFRLGEIEALPVADNSVDVIIS 152
PRK14968 PRK14968
putative methyltransferase; Provisional
 70-120 8.34e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.66  E-value: 8.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357197158  70 KDKVVLDVGSGTGILCMFAAKAGArKVIGIEcssISDYAVKIVKAN-KLDHV 120
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGK-KVVGVD---INPYAVECAKCNaKLNNI 70
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 68-142 4.66e-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: 44.78  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  68 LFKDKVVLDVGSGTGILCMFAAKAgARKVIGIECS--SISDyAVKIVKANKLDHvVTIIKGKVEEV---ELPVEKVDIII 142
Cdd:COG2265  231 LTGGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpeAVED-ARENARLNGLKN-VEFVAGDLEEVlpeLLWGGRPDVVV 307
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-174 1.97e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.26  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   68 LFKDKVVLDVGSGTGILCMFAAKAGArKVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEvelpvEKVDIIISeWMG 147
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVD---PSPIAIERALLNVRFDQFDEQEAAVPA-----GKFDVIVA-REV 89

                          90       100
                  ....*....|....*....|....*..
gi 357197158  148 YCLFyESMLNTVLHARdKWLAPDGLIF 174
Cdd:pfam13489  90 LEHV-PDPPALLRQIA-ALLKPGGLLL 114
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 70-143 5.35e-04

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: 40.27  E-value: 5.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357197158   70 KDKVVLDVGSGTGILCMFAAKAGARkvIGIECSSISDYAVKIVKANKLDH---VVTIIKGKVEEvELPVEKVDIIIS 143
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPD--AELTMVDINARALESARENLAANgleNGEVVASDVYS-GVEDGKFDLIIS 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 68-143 6.43e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.71  E-value: 6.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   68 LFKDKVVLDVGSGTGILCMFAA-KAGAR-KVIGIEcssISDYAVKIVKANKLDH---VVTIIKGKVEEVELPVE--KVDI 140
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAeELGPNaEVVGID---ISEEAIEKARENAQKLgfdNVEFEQGDIEELPELLEddKFDV 77


                  ...
gi 357197158  141 IIS 143
Cdd:pfam13847  78 VIS 80
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
74-174 8.72e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  74 VLDVGSGTGILC-MFAAKAGARKVIGIEcssISDYAVKIVKANkLDHvVTIIKGKVEEVELPvEKVDIIISewmGYCLFY 152
Cdd:COG4106    5 VLDLGCGTGRLTaLLAERFPGARVTGVD---LSPEMLARARAR-LPN-VRFVVADLRDLDPP-EPFDLVVS---NAALHW 75

                         90       100
                 ....*....|....*....|...
gi 357197158 153 ESMLNTVLHARDKWLAPDG-LIF 174
Cdd:COG4106   76 LPDHAALLARLAAALAPGGvLAV 98
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 70-143 1.38e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.76  E-value: 1.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357197158  70 KDKVVLDVGSGTG-ILCMFAAKAGARKVIGIEcssISDYAVKIVKANKLDHV---VTIIKGKVEEvELPVEKVDIIIS 143
Cdd:PRK09328 108 EPLRVLDLGTGSGaIALALAKERPDAEVTAVD---ISPEALAVARRNAKHGLgarVEFLQGDWFE-PLPGGRFDLIVS 181
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
68-143 2.13e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.11  E-value: 2.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357197158  68 LFKDKVVLDVGSGTGILCMFAAKAgARKVIGIEC-SSISDYAVKIVKANKLdhvVTIIKGKVEEVELPveKVDIIIS 143
Cdd:PRK14896  27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAAGN---VEIIEGDALKVDLP--EFNKVVS 97
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 37-134 2.13e-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: 39.76  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  37 DSYAHFGIHeeMLKDEVRTLTYRNSmfhnrHLFKDKVVLDVGSGTG---ILCMFAAKAGarKVIGIECSSIsdyAVKIVK 113
Cdd:COG2242  221 EAFERDKGP--ITKREVRALTLAKL-----ALRPGDVLWDIGAGSGsvsIEAARLAPGG--RVYAIERDPE---RAALIR 288

                         90       100
                 ....*....|....*....|....*.
gi 357197158 114 ANKLDH-V--VTIIKGKVEEV--ELP 134
Cdd:COG2242  289 ANARRFgVpnVEVVEGEAPEAlaDLP 314
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 73-147 2.34e-03

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: 38.34  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   73 VVLDVGSGTGIL--CMF--AAKAGAR-KVIGIEcssISDYAV----KIVKANKLDHVVTIIKGKVEEVELPvEKVDIIIS 143
Cdd:pfam05185  66 VILVVGAGRGPLvdRALraAEETGTKvKIYAVE---KNPNAYvtlqKRINFEKWGDKVTIISSDMREWQGP-EKADILVS 141


                  ....
gi 357197158  144 EWMG 147
Cdd:pfam05185 142 ELLG 145
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
72-142 3.19e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 38.74  E-value: 3.19e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357197158  72 KVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN----KL-DHVVTIIKGKVEEV--ELPVEKVDIII 142
Cdd:COG2521  134 DRVLDTCTGLGYTAIEALKRGAREVITVE---KDPNVLELAELNpwsrELaNERIKIILGDASEVikTFPDESFDAII 208
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
67-100 3.86e-03

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 38.69  E-value: 3.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 357197158  67 HLF--KDKVVLDVGSGTGILCMFAAKAGARKVIGIE 100
Cdd:PRK15068 117 HLSplKGRTVLDVGCGNGYHMWRMLGAGAKLVVGID 152
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-173 4.19e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 36.19  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   75 LDVGSGTGILCMFAAKAGAR-KVIGIEcssISDYAVKI----VKANKLDHVVTIIKGKVEEVELPVEKVDIIIsewMGYC 149
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLD---ISPAALEAarerLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNV 74

                          90       100
                  ....*....|....*....|....
gi 357197158  150 LFYESMLNTVLHARDKWLAPDGLI 173
Cdd:pfam08242  75 LHHLADPRAVLRNIRRLLKPGGVL 98
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 66-143 5.56e-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: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158   66 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGI------ECSSISDYAVKIVKANkldhvVTIIKGKVEEVELPVEKVD 139
Cdd:pfam01728  17 GLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVdlgpmqLWKPRNDPGVTFIQGD-----IRDPETLDLLEELLGRKVD 91


                  ....
gi 357197158  140 IIIS 143
Cdd:pfam01728  92 LVLS 95
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 73-143 9.60e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 37.44  E-value: 9.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 357197158  73 VVLDVGSGTGILCMFAAKA--GARkVIGIEcssISDYAVKIVKAN----KLDHVVTIIKGKVEEVELPVEKVDIIIS 143
Cdd:COG2890  115 RVLDLGTGSGAIALALAKErpDAR-VTAVD---ISPDALAVARRNaerlGLEDRVRFLQGDLFEPLPGDGRFDLIVS 187
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 60-142 9.68e-03

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: 37.30  E-value: 9.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357197158  60 NSMFHNRHLFKDKVVLDVGSGT-GILCMFAAKAGARKVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEVELP--VE 136
Cdd:cd05188  124 HALRRAGVLKPGDTVLVLGAGGvGLLAAQLAKAAGARVIVTD---RSDEKLELAKELGADHVIDYKEEDLEEELRLtgGG 200


                 ....*.
gi 357197158 137 KVDIII 142
Cdd:cd05188  201 GADVVI 206
 
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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