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Conserved domains on  [gi|1034594838|ref|XP_016878789|]
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protein arginine N-methyltransferase 7 isoform X11 [Homo sapiens]

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];
38-187 4.19e-43

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: 154.81  E-value: 4.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838  38 MLHDKDRNVKYYQGIRAAVSrvkdrgQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIK 117
Cdd:COG4076    15 MLNDVERNDAFKAAIERVVK------PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRIT 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838 118 VINKHSTEVtvgpegDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVES 187
Cdd:COG4076    89 VINADATDL------DLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVES 152
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
38-187 4.19e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 154.81  E-value: 4.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838  38 MLHDKDRNVKYYQGIRAAVSrvkdrgQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIK 117
Cdd:COG4076    15 MLNDVERNDAFKAAIERVVK------PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRIT 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838 118 VINKHSTEVtvgpegDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVES 187
Cdd:COG4076    89 VINADATDL------DLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVES 152
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 68-120 2.01e-03

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: 38.18  E-value: 2.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034594838  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAvKIVEKNGFSDKIKVIN 120
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLK 53
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-120 3.30e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 3.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034594838  52 IRAAVSRVKDRgqkalVLDIGTGTGLLSMMAVTAGADFcYAIEVfKPMA-DAAVKIVEKNGFSD-KIKVIN 120
Cdd:PRK14968   16 AENAVDKKGDR-----VLEVGTGSGIVAIVAAKNGKKV-VGVDI-NPYAvECAKCNAKLNNIRNnGVEVIR 79
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 68-141 4.49e-03

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: 39.56  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVfKPMA-DAAVKIVEKNGFSDKIKVINkhstevtvgpEGDMPCR------ANI 140
Cdd:pfam06325 165 VLDVGCGSGILAIAALKLGAKKVVGVDI-DPVAvRAAKENAELNGVEARLEVYL----------PGDLPKEkadvvvANI 233


                  .
gi 1034594838 141 L 141
Cdd:pfam06325 234 L 234
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
38-187 4.19e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 154.81  E-value: 4.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838  38 MLHDKDRNVKYYQGIRAAVSrvkdrgQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIK 117
Cdd:COG4076    15 MLNDVERNDAFKAAIERVVK------PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRIT 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838 118 VINKHSTEVtvgpegDMPCRANILVTELFDTELIGEGALPSYEHAHRHLVEENCEAVPHRATVYAQLVES 187
Cdd:COG4076    89 VINADATDL------DLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVES 152
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 37-120 1.21e-07

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: 53.22  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838  37 DMLHDKDrnVKYYQ-------GIR----AAVSRVKDRGQkalVLDIGTGTGLLSMMAV--TAGADFcYAIEVFKPMADAA 103
Cdd:COG4123     4 DGFLFKQ--FRIIQprcgyrfGTDavllAAFAPVKKGGR---VLDLGTGTGVIALMLAqrSPGARI-TGVEIQPEAAELA 77

                          90
                  ....*....|....*..
gi 1034594838 104 VKIVEKNGFSDKIKVIN 120
Cdd:COG4123    78 RRNVALNGLEDRITVIH 94
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
68-119 1.38e-04

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 44.01  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034594838  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVfkpmaDA-AVKI----VEKNGFSDKIKVI 119
Cdd:COG2264   152 VLDVGCGSGILAIAAAKLGAKRVLAVDI-----DPvAVEAarenAELNGVEDRIEVV 203
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 43-112 5.54e-04

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: 40.75  E-value: 5.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034594838  43 DRNVKYYQGIRAAVSRVKDR-GQKalVLDIGTGTGLLSMMAVTAGADfCYAIEVFKPMADAAVKIVEKNGF 112
Cdd:COG2226     2 DRVAARYDGREALLAALGLRpGAR--VLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAEAGL 69
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 68-120 2.01e-03

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: 38.18  E-value: 2.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034594838  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAvKIVEKNGFSDKIKVIN 120
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLK 53
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-120 3.30e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 3.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034594838  52 IRAAVSRVKDRgqkalVLDIGTGTGLLSMMAVTAGADFcYAIEVfKPMA-DAAVKIVEKNGFSD-KIKVIN 120
Cdd:PRK14968   16 AENAVDKKGDR-----VLEVGTGSGIVAIVAAKNGKKV-VGVDI-NPYAvECAKCNAKLNNIRNnGVEVIR 79
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 68-141 4.49e-03

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: 39.56  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594838  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVfKPMA-DAAVKIVEKNGFSDKIKVINkhstevtvgpEGDMPCR------ANI 140
Cdd:pfam06325 165 VLDVGCGSGILAIAALKLGAKKVVGVDI-DPVAvRAAKENAELNGVEARLEVYL----------PGDLPKEkadvvvANI 233


                  .
gi 1034594838 141 L 141
Cdd:pfam06325 234 L 234
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-112 7.12e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 36.39  E-value: 7.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034594838  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGF 112
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL 45
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 68-119 9.95e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 37.76  E-value: 9.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034594838  68 VLDIGTGTG----LLSMMA--VtagadfcYAIEVFKPMADAAVKIVEKNGFsDKIKVI 119
Cdd:COG2518    70 VLEIGTGSGyqaaVLARLAgrV-------YSVERDPELAERARERLAALGY-DNVTVR 119
 
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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