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Conserved domains on  [gi|182507159|ref|NP_956797|]
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protein arginine N-methyltransferase 7 [Danio rerio]

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];
38-188 4.05e-40

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: 146.72  E-value: 4.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159  38 MLHDKDRNEKYYEGIRAAVRrvkargERPVVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAQAASCIVERNGFSDKIK 117
Cdd:COG4076   15 MLNDVERNDAFKAAIERVVK------PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRIT 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 182507159 118 IINKHSTEVtvgpdgDMQERANILVTELFDTELIGEGALPSYEHAHMHLVQTGCEAVPHRATIYAQLVESD 188
Cdd:COG4076   89 VINADATDL------DLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESP 153
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
377-527 3.45e-09

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: 57.74  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159 377 LNDEQRTESYVSALRSILKPDSVCLSVSDGS-LLPVFAHLLGSKKVFSLESSGMAKQVIEQVLHTNSLKDGVQLLG---- 451
Cdd:COG4076   16 LNDVERNDAFKAAIERVVKPGDVVLDIGTGSgLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINadat 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159 452 ----------IRAEQLSLADLDGNQISVLMgepyfstsllpwhslffwycrTAVAQLLQPDATILPRAATLYAVAVE--- 518
Cdd:COG4076   96 dldlpekadvIISEMLDTALLDEGQVPILN---------------------HARKRLLKPGGRIIPERITNAAQPVEspv 154

                 ....*....
gi 182507159 519 FQDLWRIRF 527
Cdd:COG4076  155 DAEGFEDWQ 163
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
38-188 4.05e-40

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 146.72  E-value: 4.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159  38 MLHDKDRNEKYYEGIRAAVRrvkargERPVVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAQAASCIVERNGFSDKIK 117
Cdd:COG4076   15 MLNDVERNDAFKAAIERVVK------PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRIT 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 182507159 118 IINKHSTEVtvgpdgDMQERANILVTELFDTELIGEGALPSYEHAHMHLVQTGCEAVPHRATIYAQLVESD 188
Cdd:COG4076   89 VINADATDL------DLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESP 153
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
377-527 3.45e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 57.74  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159 377 LNDEQRTESYVSALRSILKPDSVCLSVSDGS-LLPVFAHLLGSKKVFSLESSGMAKQVIEQVLHTNSLKDGVQLLG---- 451
Cdd:COG4076   16 LNDVERNDAFKAAIERVVKPGDVVLDIGTGSgLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINadat 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159 452 ----------IRAEQLSLADLDGNQISVLMgepyfstsllpwhslffwycrTAVAQLLQPDATILPRAATLYAVAVE--- 518
Cdd:COG4076   96 dldlpekadvIISEMLDTALLDEGQVPILN---------------------HARKRLLKPGGRIIPERITNAAQPVEspv 154

                 ....*....
gi 182507159 519 FQDLWRIRF 527
Cdd:COG4076  155 DAEGFEDWQ 163
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
52-142 1.97e-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: 40.71  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159   52 IRAAVRRVKARGErpvVLDIGTGTGLLSMMAVTAGADFCYAIEVfKPMA-QAASCIVERNGFSDKIKIINkhstevtvgP 130
Cdd:pfam06325 152 LEALERLVKPGES---VLDVGCGSGILAIAALKLGAKKVVGVDI-DPVAvRAAKENAELNGVEARLEVYL---------P 218
                          90
                  ....*....|..
gi 182507159  131 DGDMQERANILV 142
Cdd:pfam06325 219 GDLPKEKADVVV 230
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
68-120 5.31e-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: 37.02  E-value: 5.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 182507159  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAQAAScIVERNGFSDKIKIIN 120
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLK 53
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
38-188 4.05e-40

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 146.72  E-value: 4.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159  38 MLHDKDRNEKYYEGIRAAVRrvkargERPVVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAQAASCIVERNGFSDKIK 117
Cdd:COG4076   15 MLNDVERNDAFKAAIERVVK------PGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRIT 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 182507159 118 IINKHSTEVtvgpdgDMQERANILVTELFDTELIGEGALPSYEHAHMHLVQTGCEAVPHRATIYAQLVESD 188
Cdd:COG4076   89 VINADATDL------DLPEKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESP 153
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
377-527 3.45e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 57.74  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159 377 LNDEQRTESYVSALRSILKPDSVCLSVSDGS-LLPVFAHLLGSKKVFSLESSGMAKQVIEQVLHTNSLKDGVQLLG---- 451
Cdd:COG4076   16 LNDVERNDAFKAAIERVVKPGDVVLDIGTGSgLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINadat 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159 452 ----------IRAEQLSLADLDGNQISVLMgepyfstsllpwhslffwycrTAVAQLLQPDATILPRAATLYAVAVE--- 518
Cdd:COG4076   96 dldlpekadvIISEMLDTALLDEGQVPILN---------------------HARKRLLKPGGRIIPERITNAAQPVEspv 154

                 ....*....
gi 182507159 519 FQDLWRIRF 527
Cdd:COG4076  155 DAEGFEDWQ 163
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
68-147 2.30e-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: 52.45  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159  68 VLDIGTGTGLLSMMAV--TAGADFcYAIEVFKPMAQAASCIVERNGFSDKIKIINkhstevtvgpdGDMQERANILVTEL 145
Cdd:COG4123   41 VLDLGTGTGVIALMLAqrSPGARI-TGVEIQPEAAELARRNVALNGLEDRITVIH-----------GDLKEFAAELPPGS 108

                 ..
gi 182507159 146 FD 147
Cdd:COG4123  109 FD 110
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
68-141 3.12e-04

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.24  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVfKPMAQAASCI-VERNGFSDKIKIInkhstevtvGPDGDMQER-----ANIL 141
Cdd:COG2264  152 VLDVGCGSGILAIAAAKLGAKRVLAVDI-DPVAVEAAREnAELNGVEDRIEVV---------LGDLLEDGPydlvvANIL 221
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
43-103 3.73e-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: 41.13  E-value: 3.73e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 182507159  43 DRNEKYYEGIRAAVRRVKAR-GERpvVLDIGTGTGLLSMMAVTAGADfCYAIEVFKPMAQAA 103
Cdd:COG2226    2 DRVAARYDGREALLAALGLRpGAR--VLDLGCGTGRLALALAERGAR-VTGVDISPEMLELA 60
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
52-142 1.97e-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: 40.71  E-value: 1.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 182507159   52 IRAAVRRVKARGErpvVLDIGTGTGLLSMMAVTAGADFCYAIEVfKPMA-QAASCIVERNGFSDKIKIINkhstevtvgP 130
Cdd:pfam06325 152 LEALERLVKPGES---VLDVGCGSGILAIAALKLGAKKVVGVDI-DPVAvRAAKENAELNGVEARLEVYL---------P 218
                          90
                  ....*....|..
gi 182507159  131 DGDMQERANILV 142
Cdd:pfam06325 219 GDLPKEKADVVV 230
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
68-120 5.31e-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: 37.02  E-value: 5.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 182507159  68 VLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMAQAAScIVERNGFSDKIKIIN 120
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLK 53
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
41-103 6.72e-03

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: 37.30  E-value: 6.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 182507159  41 DKDRNEKYYEGIRAAVRRVKARGERpvVLDIGTGTGLLSMMAVTAGADfCYAIEVFKPMAQAA 103
Cdd:COG2227    3 DPDARDFWDRRLAALLARLLPAGGR--VLDVGCGTGRLALALARRGAD-VTGVDISPEALEIA 62
 
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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