histone-arginine methyltransferase CARMER isoform X2 [Bombus terrestris]
histone-arginine methyltransferase( domain architecture ID 10351171)
histone-arginine methyltransferase is a type I arginine methyltransferase belonging to the class I SAM-dependent methyltransferase superfamily, similar to Drosophila histone-arginine methyltransferase CARMER that methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in proteins, using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
COG4076 super family | cl44002 | Predicted RNA methylase [General function prediction only]; |
134-321 | 3.49e-39 | ||||
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: 143.25 E-value: 3.49e-39
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PH-like super family | cl17171 | Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ... |
4-114 | 5.69e-06 | ||||
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins. The actual alignment was detected with superfamily member cd13330: Pssm-ID: 473070 Cd Length: 107 Bit Score: 45.47 E-value: 5.69e-06
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Name | Accession | Description | Interval | E-value | ||||
COG4076 | COG4076 | Predicted RNA methylase [General function prediction only]; |
134-321 | 3.49e-39 | ||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 143.25 E-value: 3.49e-39
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
163-264 | 2.86e-13 | ||||
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: 66.30 E-value: 2.86e-13
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Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
163-258 | 1.93e-10 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 57.57 E-value: 1.93e-10
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prmA | PRK00517 | 50S ribosomal protein L11 methyltransferase; |
157-214 | 4.25e-07 | ||||
50S ribosomal protein L11 methyltransferase; Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 51.31 E-value: 4.25e-07
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PH_CARM1 | cd13330 | Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ... |
4-114 | 5.69e-06 | ||||
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 241484 Cd Length: 107 Bit Score: 45.47 E-value: 5.69e-06
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CARM1 | pfam11531 | Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ... |
48-102 | 3.06e-05 | ||||
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine methyltransferase which methylates a variety of different proteins and plays a role in gene expression. This is the N terminal domain of the protein which has a PH domain, normally present to regulate protein-protein interactions.A molecular switch is also present on the N terminal domain. Pssm-ID: 402914 Cd Length: 105 Bit Score: 43.29 E-value: 3.06e-05
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fkbM_fam | TIGR01444 | methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ... |
162-208 | 8.44e-05 | ||||
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548. Pssm-ID: 273628 Cd Length: 143 Bit Score: 43.07 E-value: 8.44e-05
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Name | Accession | Description | Interval | E-value | ||||
COG4076 | COG4076 | Predicted RNA methylase [General function prediction only]; |
134-321 | 3.49e-39 | ||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 143.25 E-value: 3.49e-39
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AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
163-264 | 2.86e-13 | ||||
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: 66.30 E-value: 2.86e-13
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Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
163-261 | 4.57e-12 | ||||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 64.18 E-value: 4.57e-12
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UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
138-261 | 7.08e-12 | ||||
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: 62.73 E-value: 7.08e-12
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PrmA | COG2264 | Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
157-230 | 7.79e-11 | ||||
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 63.27 E-value: 7.79e-11
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Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
163-258 | 1.93e-10 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 57.57 E-value: 1.93e-10
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COG2263 | COG2263 | Predicted RNA methylase [General function prediction only]; |
157-233 | 1.33e-09 | ||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 57.99 E-value: 1.33e-09
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UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
149-268 | 6.70e-09 | ||||
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: 54.61 E-value: 6.70e-09
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TrmN6 | COG4123 | tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
151-261 | 1.43e-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: 55.54 E-value: 1.43e-08
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Nnt1 | COG3897 | Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ... |
149-245 | 1.63e-07 | ||||
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: 52.19 E-value: 1.63e-07
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PrmA | pfam06325 | Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
159-259 | 3.85e-07 | ||||
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: 51.88 E-value: 3.85e-07
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prmA | PRK00517 | 50S ribosomal protein L11 methyltransferase; |
157-214 | 4.25e-07 | ||||
50S ribosomal protein L11 methyltransferase; Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 51.31 E-value: 4.25e-07
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Tam | COG4106 | Trans-aconitate methyltransferase [Energy production and conversion]; |
163-261 | 1.75e-06 | ||||
Trans-aconitate methyltransferase [Energy production and conversion]; Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 46.74 E-value: 1.75e-06
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MTS | pfam05175 | Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
149-261 | 1.91e-06 | ||||
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: 48.36 E-value: 1.91e-06
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Gcd14 | COG2519 | tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
150-259 | 3.07e-06 | ||||
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 49.00 E-value: 3.07e-06
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ksgA | PRK14896 | 16S ribosomal RNA methyltransferase A; |
151-231 | 5.27e-06 | ||||
16S ribosomal RNA methyltransferase A; Pssm-ID: 237852 [Multi-domain] Cd Length: 258 Bit Score: 48.36 E-value: 5.27e-06
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PH_CARM1 | cd13330 | Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known ... |
4-114 | 5.69e-06 | ||||
Coactivator-Associated Methyltransferase 1 Pleckstrin homology (PH) domain; CARM1 (also known as protein arginine methyltransferase 4/PRMT4) is a protein arginine methyltransferase recruited by several transcription factors. It methylates a variety of proteins and plays a role in gene expression. The N-terminal domain of CARM1 contains a N-terminal PH domain, a catalytic core module composed of two parts (a Rossmann fold topology (RF) and a beta-barrel), and a C-terminal domain. The N-terminal and the C-terminal end of CARM1 catalytic module contain molecular switches that may explain how CARM1 regulates its biological activities by protein-protein interactions. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes. Pssm-ID: 241484 Cd Length: 107 Bit Score: 45.47 E-value: 5.69e-06
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RsmC | COG2813 | 16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
149-261 | 6.64e-06 | ||||
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification Pssm-ID: 442062 [Multi-domain] Cd Length: 191 Bit Score: 47.11 E-value: 6.64e-06
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CARM1 | pfam11531 | Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine ... |
48-102 | 3.06e-05 | ||||
Coactivator-associated arginine methyltransferase 1 N terminal; CARM1 is an arginine methyltransferase which methylates a variety of different proteins and plays a role in gene expression. This is the N terminal domain of the protein which has a PH domain, normally present to regulate protein-protein interactions.A molecular switch is also present on the N terminal domain. Pssm-ID: 402914 Cd Length: 105 Bit Score: 43.29 E-value: 3.06e-05
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Methyltransf_11 | pfam08241 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
164-261 | 5.78e-05 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 42.27 E-value: 5.78e-05
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fkbM_fam | TIGR01444 | methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ... |
162-208 | 8.44e-05 | ||||
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548. Pssm-ID: 273628 Cd Length: 143 Bit Score: 43.07 E-value: 8.44e-05
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HemK | COG2890 | Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
149-261 | 1.25e-04 | ||||
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis]; Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 44.37 E-value: 1.25e-04
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RsmD | COG0742 | 16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
151-258 | 1.28e-04 | ||||
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: 43.15 E-value: 1.28e-04
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PRMT5 | pfam05185 | PRMT5 arginine-N-methyltransferase; The human homolog of yeast Skb1 (Shk1 kinase-binding ... |
139-241 | 1.48e-04 | ||||
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: 42.58 E-value: 1.48e-04
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Methyltransf_9 | pfam08003 | Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ... |
147-258 | 1.84e-04 | ||||
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8. Pssm-ID: 429781 [Multi-domain] Cd Length: 315 Bit Score: 43.93 E-value: 1.84e-04
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PRK15068 | PRK15068 | tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB; |
147-258 | 4.09e-04 | ||||
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB; Pssm-ID: 237898 Cd Length: 322 Bit Score: 42.92 E-value: 4.09e-04
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BioC | TIGR02072 | malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
150-231 | 4.74e-04 | ||||
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin] Pssm-ID: 273953 [Multi-domain] Cd Length: 240 Bit Score: 42.27 E-value: 4.74e-04
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COG4976 | COG4976 | Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
140-259 | 1.78e-03 | ||||
Predicted methyltransferase, contains TPR repeat [General function prediction only]; Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 39.60 E-value: 1.78e-03
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Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
164-259 | 2.72e-03 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 37.35 E-value: 2.72e-03
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YqxC | COG1189 | Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ... |
157-231 | 2.90e-03 | ||||
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440802 [Multi-domain] Cd Length: 248 Bit Score: 39.66 E-value: 2.90e-03
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CbiT | TIGR02469 | precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ... |
159-260 | 4.18e-03 | ||||
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 274148 [Multi-domain] Cd Length: 124 Bit Score: 37.69 E-value: 4.18e-03
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PRK14968 | PRK14968 | putative methyltransferase; Provisional |
142-190 | 5.70e-03 | ||||
putative methyltransferase; Provisional Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 38.34 E-value: 5.70e-03
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CMAS | pfam02353 | Mycolic acid cyclopropane synthetase; This family consist of ... |
163-260 | 6.49e-03 | ||||
Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid. Pssm-ID: 396777 [Multi-domain] Cd Length: 272 Bit Score: 38.85 E-value: 6.49e-03
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PRK07580 | PRK07580 | Mg-protoporphyrin IX methyl transferase; Validated |
152-220 | 7.82e-03 | ||||
Mg-protoporphyrin IX methyl transferase; Validated Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 38.28 E-value: 7.82e-03
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Blast search parameters | ||||
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