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Conserved domains on  [gi|2312042238|ref|XP_050764268|]
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histone-arginine methyltransferase METTL23 isoform X1 [Gymnogyps californianus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 2-129 1.10e-19

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 82.62  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312042238   2 YVWPCAVVLAQYLWvHRSSLPGKRVLEVGAGVSLPGVVAAKCGA-EVILSDSEelPQCLHNCRRSCLMNDLPrVPVIGLT 80
Cdd:COG3897    51 FLWPSGQALARYLL-DHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYD--PEALAALRLNAALNGVA-ITTRLGD 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2312042238  81 WGRVSPEllslAPVDIILGSDVFFDPKDFEDILTtiyfLLER--NPHAQFW 129
Cdd:COG3897   127 WRDPPAA----GGFDLILGGDVLYERDLAEPLLP----FLDRlaAPGGEVL 169
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 2-129 1.10e-19

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 82.62  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312042238   2 YVWPCAVVLAQYLWvHRSSLPGKRVLEVGAGVSLPGVVAAKCGA-EVILSDSEelPQCLHNCRRSCLMNDLPrVPVIGLT 80
Cdd:COG3897    51 FLWPSGQALARYLL-DHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYD--PEALAALRLNAALNGVA-ITTRLGD 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2312042238  81 WGRVSPEllslAPVDIILGSDVFFDPKDFEDILTtiyfLLER--NPHAQFW 129
Cdd:COG3897   127 WRDPPAA----GGFDLILGGDVLYERDLAEPLLP----FLDRlaAPGGEVL 169
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 3-125 6.40e-17

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 74.29  E-value: 6.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312042238   3 VWPCAVVLAQYL------WVHRSSLPGKRVLEVGAGVSLPGVVAAK--CGAEVILSDSEELpqcLHNCRRSCLMNDL-PR 73
Cdd:pfam10294  21 VWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEA---LELLKKNIELNALsSK 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2312042238  74 VPVIGLTWG-RVSPELLSLAPVDIILGSDVFFDPKDFEDILTTIYFLLERNPH 125
Cdd:pfam10294  98 VVVKVLDWGeNLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV 150
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 2-129 1.10e-19

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 82.62  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312042238   2 YVWPCAVVLAQYLWvHRSSLPGKRVLEVGAGVSLPGVVAAKCGA-EVILSDSEelPQCLHNCRRSCLMNDLPrVPVIGLT 80
Cdd:COG3897    51 FLWPSGQALARYLL-DHPEVAGKRVLELGCGLGLVGIAAAKAGAaDVTATDYD--PEALAALRLNAALNGVA-ITTRLGD 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2312042238  81 WGRVSPEllslAPVDIILGSDVFFDPKDFEDILTtiyfLLER--NPHAQFW 129
Cdd:COG3897   127 WRDPPAA----GGFDLILGGDVLYERDLAEPLLP----FLDRlaAPGGEVL 169
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 3-125 6.40e-17

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 74.29  E-value: 6.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312042238   3 VWPCAVVLAQYL------WVHRSSLPGKRVLEVGAGVSLPGVVAAK--CGAEVILSDSEELpqcLHNCRRSCLMNDL-PR 73
Cdd:pfam10294  21 VWDAAVVLSKYLemkifkELGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITDLEEA---LELLKKNIELNALsSK 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2312042238  74 VPVIGLTWG-RVSPELLSLAPVDIILGSDVFFDPKDFEDILTTIYFLLERNPH 125
Cdd:pfam10294  98 VVVKVLDWGeNLPPDLFDGHPVDLILAADCVYNEDSFPLLEKTLKDLLGKESV 150
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 15-109 7.51e-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: 34.99  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2312042238  15 WVHRSSLPGKRVLEVGAGvslPGVVA---AKCGAEVILSD-SEELpqcLHNCRRsclmndlpRVPVIGLTWGRVSPELLS 90
Cdd:COG2227    17 LLARLLPAGGRVLDVGCG---TGRLAlalARRGADVTGVDiSPEA---LEIARE--------RAAELNVDFVQGDLEDLP 82

                          90       100
                  ....*....|....*....|....
gi 2312042238  91 LAP--VDIILGSDVF---FDPKDF 109
Cdd:COG2227    83 LEDgsFDLVICSEVLehlPDPAAL 106
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 21-57 8.98e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 36.21  E-value: 8.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2312042238  21 LPGKRVLEVGAGVSlpGVVAA----KCGAEVILSDSEELPQ 57
Cdd:COG0771     2 LKGKKVLVLGLGKS--GLAAArllaKLGAEVTVSDDRPAPE 40
 
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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