5DX0
Crystal structure of CARM1, sinefungin, and H3 peptide (R17)
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
A | SCOP2B Superfamily | S-adenosyl-L-methionine-dependent methyltransferases | 8046582 | 3000118 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Arginine methyltransferase C-terminal oligomerisation domain-like | 8053427 | 3002184 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | S-adenosyl-L-methionine-dependent methyltransferases | 8046582 | 3000118 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Arginine methyltransferase C-terminal oligomerisation domain-like | 8053427 | 3002184 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Arginine methyltransferase C-terminal oligomerisation domain-like | 8053427 | 3002184 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | S-adenosyl-L-methionine-dependent methyltransferases | 8046582 | 3000118 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | Arginine methyltransferase C-terminal oligomerisation domain-like | 8053427 | 3002184 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | S-adenosyl-L-methionine-dependent methyltransferases | 8046582 | 3000118 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
A | PRMT5_C_1 | e5dx0A1 | A: beta sandwiches | X: Arginine methyltransferase oligomerization subdomain (From Topology) | H: Arginine methyltransferase oligomerization subdomain (From Topology) | T: Arginine methyltransferase oligomerization subdomain | F: PRMT5_C_1 | ECOD (1.6) |
A | PrmA | e5dx0A2 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: PrmA | ECOD (1.6) |
B | PRMT5_C_1 | e5dx0B2 | A: beta sandwiches | X: Arginine methyltransferase oligomerization subdomain (From Topology) | H: Arginine methyltransferase oligomerization subdomain (From Topology) | T: Arginine methyltransferase oligomerization subdomain | F: PRMT5_C_1 | ECOD (1.6) |
B | PrmA | e5dx0B1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: PrmA | ECOD (1.6) |
C | PRMT5_C_1 | e5dx0C2 | A: beta sandwiches | X: Arginine methyltransferase oligomerization subdomain (From Topology) | H: Arginine methyltransferase oligomerization subdomain (From Topology) | T: Arginine methyltransferase oligomerization subdomain | F: PRMT5_C_1 | ECOD (1.6) |
C | PrmA | e5dx0C1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: PrmA | ECOD (1.6) |
D | PRMT5_C_1 | e5dx0D2 | A: beta sandwiches | X: Arginine methyltransferase oligomerization subdomain (From Topology) | H: Arginine methyltransferase oligomerization subdomain (From Topology) | T: Arginine methyltransferase oligomerization subdomain | F: PRMT5_C_1 | ECOD (1.6) |
D | PrmA | e5dx0D1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: S-adenosyl-L-methionine-dependent methyltransferases | F: PrmA | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
A | 3.40.50.150 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Vaccinia Virus protein VP39 | CATH (4.3.0) |
A | 2.70.160.11 | Mainly Beta | Distorted Sandwich | Hnrnp arginine n-methyltransferase1 | Hnrnp arginine n-methyltransferase1 | CATH (4.3.0) |
B | 3.40.50.150 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Vaccinia Virus protein VP39 | CATH (4.3.0) |
B | 2.70.160.11 | Mainly Beta | Distorted Sandwich | Hnrnp arginine n-methyltransferase1 | Hnrnp arginine n-methyltransferase1 | CATH (4.3.0) |
C | 3.40.50.150 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Vaccinia Virus protein VP39 | CATH (4.3.0) |
C | 2.70.160.11 | Mainly Beta | Distorted Sandwich | Hnrnp arginine n-methyltransferase1 | Hnrnp arginine n-methyltransferase1 | CATH (4.3.0) |
D | 3.40.50.150 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | Vaccinia Virus protein VP39 | CATH (4.3.0) |
D | 2.70.160.11 | Mainly Beta | Distorted Sandwich | Hnrnp arginine n-methyltransferase1 | Hnrnp arginine n-methyltransferase1 | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF22528 | Arginine methyltransferase oligomerization subdomain (PRMT_C) | Arginine methyltransferase oligomerization subdomain | This entry represents a domain found C-terminal in protein arginine methyltransferases. This domain is involved in oligomerisation. | Domain | |
PF06325 | Ribosomal protein L11 methyltransferase (PrmA) (PrmA) | Ribosomal protein L11 methyltransferase (PrmA) | - | Family | |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR020989 | Histone-arginine methyltransferase CARM1, N-terminal | Domain | |
IPR011993 | PH-like domain superfamily | Homologous Superfamily | |
IPR025799 | Protein arginine N-methyltransferase | Family | |
IPR029063 | S-adenosyl-L-methionine-dependent methyltransferase superfamily | Homologous Superfamily | |
E [auth F], F [auth G], G [auth H], H [auth I] | IPR000164 | Histone H3/CENP-A | Family |
E [auth F], F [auth G], G [auth H], H [auth I] | IPR009072 | Histone-fold | Homologous Superfamily |
E [auth F], F [auth G], G [auth H], H [auth I] | IPR007125 | Histone H2A/H2B/H3 | Domain |
Pharos: Disease Associations Pharos Homepage Annotation
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
E [auth F], F [auth G], G [auth H], H [auth I] | ACE | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 | : 
E [auth F], F [auth G], G [auth H], H [auth I] | NH2 | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 , L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109 | :