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Conserved domains on  [gi|1720420954|ref|XP_030098018|]
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protein arginine N-methyltransferase 1 isoform X2 [Mus musculus]

Protein Classification

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];
34-207 3.06e-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: 159.43  E-value: 3.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  34 HEEMLKDEVRtltyrNSMFH---NRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS-SISDYAVKIVKANKLDHV 109
Cdd:COG4076    12 HHPMLNDVER-----NDAFKaaiERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954 110 VTIIKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWweN 189
Cdd:COG4076    87 ITVINADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--Q 163

                         170
                  ....*....|....*...
gi 1720420954 190 VYGFDMSCIKDVAIKEPL 207
Cdd:COG4076   164 FDGFDFRLFGFLLYAEPL 181
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
34-207 3.06e-47

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 159.43  E-value: 3.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  34 HEEMLKDEVRtltyrNSMFH---NRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS-SISDYAVKIVKANKLDHV 109
Cdd:COG4076    12 HHPMLNDVER-----NDAFKaaiERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954 110 VTIIKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWweN 189
Cdd:COG4076    87 ITVINADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--Q 163

                         170
                  ....*....|....*...
gi 1720420954 190 VYGFDMSCIKDVAIKEPL 207
Cdd:COG4076   164 FDGFDFRLFGFLLYAEPL 181
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-160 1.49e-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: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN--KLDHVVTIIKGKVEEVELPVEKVDIIISeWMGYCLF 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVD---LSPEMLERARERaaEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 1720420954 141 YESMLNTVLH--ARdkWLAPDG 160
Cdd:pfam13649  77 PDPDLEAALReiAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-163 5.41e-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: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVK---ANKLDHVVTIIKGKVEE-VELPVEKVDIIISeWMGYC 138
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVD---ISPVALELARkaaAALLADNVEVLKGDAEElPPEADESFDVIIS-DPPLH 77

                          90       100
                  ....*....|....*....|....*
gi 1720420954 139 LFYESMLNTVLHARDKwLAPDGLIF 163
Cdd:cd02440    78 HLVEDLARFLEEARRL-LKPGGVLV 101
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
55-131 2.61e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.00  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  55 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN-KLDHVvtiikgkVEEVELP--VEKVDIII 131
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAARENaELNGV-------ELNVYLPqgDLKADVIV 184
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
34-207 3.06e-47

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 159.43  E-value: 3.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  34 HEEMLKDEVRtltyrNSMFH---NRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECS-SISDYAVKIVKANKLDHV 109
Cdd:COG4076    12 HHPMLNDVER-----NDAFKaaiERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954 110 VTIIKGKVEEVELPvEKVDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWweN 189
Cdd:COG4076    87 ITVINADATDLDLP-EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAEGFEDW--Q 163

                         170
                  ....*....|....*...
gi 1720420954 190 VYGFDMSCIKDVAIKEPL 207
Cdd:COG4076   164 FDGFDFRLFGFLLYAEPL 181
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-163 3.64e-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: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  54 NRHLFKDKVVLDVGSGTGILCMFAAKAGARkVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISe 133
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGAD-VTGVD---ISPEALEIARERAAELNVDFVQGDLEDLPLEDGSFDLVIC- 93

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720420954 134 wmgyclfyesmLNTVLHARD---------KWLAPDGLIF 163
Cdd:COG2227    94 -----------SEVLEHLPDpaallrelaRLLKPGGLLL 121
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
55-131 1.21e-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: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  55 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKI----VKANKLDHVVTIIKGKVeeveLPVEKVDII 130
Cdd:COG2264   144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVD---IDPVAVEAarenAELNGVEDRIEVVLGDL----LEDGPYDLV 216


                  .
gi 1720420954 131 I 131
Cdd:COG2264   217 V 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-160 1.49e-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: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN--KLDHVVTIIKGKVEEVELPVEKVDIIISeWMGYCLF 140
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVD---LSPEMLERARERaaEAGLNVEFVQGDAEDLPFPDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 1720420954 141 YESMLNTVLH--ARdkWLAPDG 160
Cdd:pfam13649  77 PDPDLEAALReiAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 63-163 5.41e-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: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVK---ANKLDHVVTIIKGKVEE-VELPVEKVDIIISeWMGYC 138
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVD---ISPVALELARkaaAALLADNVEVLKGDAEElPPEADESFDVIIS-DPPLH 77

                          90       100
                  ....*....|....*....|....*
gi 1720420954 139 LFYESMLNTVLHARDKwLAPDGLIF 163
Cdd:cd02440    78 HLVEDLARFLEEARRL-LKPGGVLV 101
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
58-132 2.08e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 59.53  E-value: 2.08e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720420954  58 FKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN--KLDHVVTIIKGKVEEVELpVEKVDIIIS 132
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVD---IDPEALEIARENaeRLGVRVDFIRADVTRIPL-GGSVDTVVM 116
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 55-131 1.45e-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: 1.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420954  55 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN-KLDHVVTIIKGKVEEvELPVEKVDIII 131
Cdd:pfam06325 157 RLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENaELNGVEARLEVYLPG-DLPKEKADVVV 230
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-163 1.52e-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: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  64 LDVGSGTGILCMFAAKAGARkVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMgycLFYES 143
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR-VTGVD---ISPEMLELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV---LHHVE 73

                          90       100
                  ....*....|....*....|
gi 1720420954 144 MLNTVLHARDKWLAPDGLIF 163
Cdd:pfam08241  74 DPERALREIARVLKPGGILI 93
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
55-131 2.61e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.00  E-value: 2.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  55 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN-KLDHVvtiikgkVEEVELP--VEKVDIII 131
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAARENaELNGV-------ELNVYLPqgDLKADVIV 184
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 63-163 3.66e-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: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILCMFAAKAGARKVIGIecsSIS----DYAVKIVKANKLDHVVTIIKGKVEEVELPvEKVDIIIS----EW 134
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGV---TLSpeqlEYARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSigmfEH 130

                          90       100
                  ....*....|....*....|....*....
gi 1720420954 135 MGYcLFYESMLNTVlharDKWLAPDGLIF 163
Cdd:COG2230   131 VGP-ENYPAYFAKV----ARLLKPGGRLL 154
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 63-132 5.28e-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: 5.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720420954  63 VLDVGSGTGILC-MFAAKAGARKVIGIECSSIS-DYAVKIVKANKLDHVVTIIKGKVEEV--ELPVEKVDIIIS 132
Cdd:COG4123    41 VLDLGTGTGVIAlMLAQRSPGARITGVEIQPEAaELARRNVALNGLEDRITVIHGDLKEFaaELPPGSFDLVVS 114
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 59-132 1.52e-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: 1.52e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720420954  59 KDKVVLDVGSGTGILCMFAAKAGARkVIGIEcssISDYAVKIV--KANKLDHVVTIIKGKVEEVELPVEKVDIIIS 132
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGAR-VTGVD---ISPEMLELAreRAAEAGLNVEFVVGDAEDLPFPDGSFDLVIS 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
18-163 1.79e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.38  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  18 MTSKDY---YFDSYAHfgIHEEMLkdeVRTLTYRN------SMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARkVIGI 88
Cdd:COG4976     1 MALDAYveaLFDQYAD--SYDAAL---VEDLGYEApallaeELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR-LTGV 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720420954  89 EcssISDYAVKIVKANKLDhvVTIIKGKVEEVELPVEKVDIIISeWMGYClfYESMLNTVLHARDKWLAPDG-LIF 163
Cdd:COG4976    75 D---LSEEMLAKAREKGVY--DRLLVADLADLAEPDGRFDLIVA-ADVLT--YLGDLAAVFAGVARALKPGGlFIF 142
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 63-163 3.94e-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: 3.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILCMFAAKAGARKVIGIECSSIS-DYAVKIVKANKLDHvVTIIKGKVEE-VELPVEKVDIIISeWMGYCLF 140
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGN-VEFLVADLAElDPLPAESFDLVVA-FGVLHHL 107

                          90       100
                  ....*....|....*....|...
gi 1720420954 141 YESMLNTVLHARDKWLAPDGLIF 163
Cdd:COG0500   108 PPEEREALLRELARALKPGGVLL 130
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 48-188 2.94e-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: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  48 RNSMFhNR--HLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN----KLDHVVTIIKGKVEEV- 120
Cdd:COG0742    29 REALF-NIlgPDIEGARVLDLFAGSGALGLEALSRGAASVVFVE---KDRKAAAVIRKNleklGLEDRARVIRGDALRFl 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954 121 -ELPVEKVDIIIsewmgycL---FYESMLNTVLHA--RDKWLAPDGLI---------FPDRATLYvTAIEDRQYKDYKIH 185
Cdd:COG0742   105 kRLAGEPFDLVF-------LdppYAKGLLEKALELlaENGLLAPGGLIvvehskreeLPELPAGL-ELLKERKYGDTRLS 176


                  ...
gi 1720420954 186 WWE 188
Cdd:COG0742   177 FYR 179
arsM PRK11873
arsenite methyltransferase;
62-132 3.75e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 47.64  E-value: 3.75e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720420954  62 VVLDVGSGTGILCMFAAKA-GAR-KVIGIEcssISDYAVKIVKAN--KLDHV-VTIIKGKVEEVELPVEKVDIIIS 132
Cdd:PRK11873   80 TVLDLGSGGGFDCFLAARRvGPTgKVIGVD---MTPEMLAKARANarKAGYTnVEFRLGEIEALPVADNSVDVIIS 152
PRK14968 PRK14968
putative methyltransferase; Provisional
 59-109 8.04e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.66  E-value: 8.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720420954  59 KDKVVLDVGSGTGILCMFAAKAGArKVIGIEcssISDYAVKIVKAN-KLDHV 109
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNGK-KVVGVD---INPYAVECAKCNaKLNNI 70
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 57-131 4.40e-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: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  57 LFKDKVVLDVGSGTGILCMFAAKAgARKVIGIECS--SISDyAVKIVKANKLDHvVTIIKGKVEEV---ELPVEKVDIII 131
Cdd:COG2265   231 LTGGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpeAVED-ARENARLNGLKN-VEFVAGDLEEVlpeLLWGGRPDVVV 307
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-163 2.08e-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: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  57 LFKDKVVLDVGSGTGILCMFAAKAGArKVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEvelpvEKVDIIISeWMG 136
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGF-SVTGVD---PSPIAIERALLNVRFDQFDEQEAAVPA-----GKFDVIVA-REV 89

                          90       100
                  ....*....|....*....|....*..
gi 1720420954 137 YCLFyESMLNTVLHARdKWLAPDGLIF 163
Cdd:pfam13489  90 LEHV-PDPPALLRQIA-ALLKPGGLLL 114
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 59-132 5.12e-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: 5.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720420954  59 KDKVVLDVGSGTGILCMFAAKAGARkvIGIECSSISDYAVKIVKANKLDH---VVTIIKGKVEEvELPVEKVDIIIS 132
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPD--AELTMVDINARALESARENLAANgleNGEVVASDVYS-GVEDGKFDLIIS 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-132 5.62e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.71  E-value: 5.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  57 LFKDKVVLDVGSGTGILCMFAA-KAGAR-KVIGIEcssISDYAVKIVKANKLDH---VVTIIKGKVEEVELPVE--KVDI 129
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAeELGPNaEVVGID---ISEEAIEKARENAQKLgfdNVEFEQGDIEELPELLEddKFDV 77


                  ...
gi 1720420954 130 IIS 132
Cdd:pfam13847  78 VIS 80
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
63-163 8.41e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  63 VLDVGSGTGILC-MFAAKAGARKVIGIEcssISDYAVKIVKANkLDHvVTIIKGKVEEVELPvEKVDIIISewmGYCLFY 141
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVD---LSPEMLARARAR-LPN-VRFVVADLRDLDPP-EPFDLVVS---NAALHW 75

                          90       100
                  ....*....|....*....|...
gi 1720420954 142 ESMLNTVLHARDKWLAPDG-LIF 163
Cdd:COG4106    76 LPDHAALLARLAAALAPGGvLAV 98
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 59-132 1.31e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.76  E-value: 1.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420954  59 KDKVVLDVGSGTG-ILCMFAAKAGARKVIGIEcssISDYAVKIVKANKLDHV---VTIIKGKVEEvELPVEKVDIIIS 132
Cdd:PRK09328  108 EPLRVLDLGTGSGaIALALAKERPDAEVTAVD---ISPEALAVARRNAKHGLgarVEFLQGDWFE-PLPGGRFDLIVS 181
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 26-123 2.02e-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: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  26 DSYAHFGIHeeMLKDEVRTLTYRNSmfhnrHLFKDKVVLDVGSGTG---ILCMFAAKAGarKVIGIECSSIsdyAVKIVK 102
Cdd:COG2242   221 EAFERDKGP--ITKREVRALTLAKL-----ALRPGDVLWDIGAGSGsvsIEAARLAPGG--RVYAIERDPE---RAALIR 288

                          90       100
                  ....*....|....*....|....*.
gi 1720420954 103 ANKLDH-V--VTIIKGKVEEV--ELP 123
Cdd:COG2242   289 ANARRFgVpnVEVVEGEAPEAlaDLP 314
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
57-132 2.20e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.11  E-value: 2.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720420954  57 LFKDKVVLDVGSGTGILCMFAAKAgARKVIGIEC-SSISDYAVKIVKANKLdhvVTIIKGKVEEVELPveKVDIIIS 132
Cdd:PRK14896   27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAAGN---VEIIEGDALKVDLP--EFNKVVS 97
PRMT5 pfam05185
PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ...
 62-136 2.37e-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: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  62 VVLDVGSGTGIL--CMF--AAKAGAR-KVIGIEcssISDYAV----KIVKANKLDHVVTIIKGKVEEVELPvEKVDIIIS 132
Cdd:pfam05185  66 VILVVGAGRGPLvdRALraAEETGTKvKIYAVE---KNPNAYvtlqKRINFEKWGDKVTIISSDMREWQGP-EKADILVS 141


                  ....
gi 1720420954 133 EWMG 136
Cdd:pfam05185 142 ELLG 145
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
61-131 3.04e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 38.74  E-value: 3.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720420954  61 KVVLDVGSGTGILCMFAAKAGARKVIGIEcssISDYAVKIVKAN----KL-DHVVTIIKGKVEEV--ELPVEKVDIII 131
Cdd:COG2521   134 DRVLDTCTGLGYTAIEALKRGAREVITVE---KDPNVLELAELNpwsrELaNERIKIILGDASEVikTFPDESFDAII 208
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
56-89 3.67e-03

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


Pssm-ID: 237898  Cd Length: 322  Bit Score: 38.69  E-value: 3.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720420954  56 HLF--KDKVVLDVGSGTGILCMFAAKAGARKVIGIE 89
Cdd:PRK15068  117 HLSplKGRTVLDVGCGNGYHMWRMLGAGAKLVVGID 152
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-162 4.04e-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: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  64 LDVGSGTGILCMFAAKAGAR-KVIGIEcssISDYAVKI----VKANKLDHVVTIIKGKVEEVELPVEKVDIIIsewMGYC 138
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLD---ISPAALEAarerLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNV 74

                          90       100
                  ....*....|....*....|....
gi 1720420954 139 LFYESMLNTVLHARDKWLAPDGLI 162
Cdd:pfam08242  75 LHHLADPRAVLRNIRRLLKPGGVL 98
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 55-132 5.69e-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: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  55 RHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGI------ECSSISDYAVKIVKANkldhvVTIIKGKVEEVELPVEKVD 128
Cdd:pfam01728  17 GLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVdlgpmqLWKPRNDPGVTFIQGD-----IRDPETLDLLEELLGRKVD 91


                  ....
gi 1720420954 129 IIIS 132
Cdd:pfam01728  92 LVLS 95
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 62-132 9.14e-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: 9.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720420954  62 VVLDVGSGTGILCMFAAKA--GARkVIGIEcssISDYAVKIVKAN----KLDHVVTIIKGKVEEVELPVEKVDIIIS 132
Cdd:COG2890   115 RVLDLGTGSGAIALALAKErpDAR-VTAVD---ISPDALAVARRNaerlGLEDRVRFLQGDLFEPLPGDGRFDLIVS 187
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 49-131 9.23e-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: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720420954  49 NSMFHNRHLFKDKVVLDVGSGT-GILCMFAAKAGARKVIGIEcssISDYAVKIVKANKLDHVVTIIKGKVEEVELP--VE 125
Cdd:cd05188   124 HALRRAGVLKPGDTVLVLGAGGvGLLAAQLAKAAGARVIVTD---RSDEKLELAKELGADHVIDYKEEDLEEELRLtgGG 200


                  ....*.
gi 1720420954 126 KVDIII 131
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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