PRMT6 [Arabidopsis thaliana]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
COG4076 super family | cl44002 | Predicted RNA methylase [General function prediction only]; |
83-235 | 3.21e-45 | |||
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: 156.74 E-value: 3.21e-45
|
|||||||
Cupredoxin super family | cl19115 | Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ... |
272-337 | 9.54e-03 | |||
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II. The actual alignment was detected with superfamily member cd13896: Pssm-ID: 473140 [Multi-domain] Cd Length: 115 Bit Score: 36.08 E-value: 9.54e-03
|
|||||||
Name | Accession | Description | Interval | E-value | |||
COG4076 | COG4076 | Predicted RNA methylase [General function prediction only]; |
83-235 | 3.21e-45 | |||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 156.74 E-value: 3.21e-45
|
|||||||
AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
122-221 | 1.14e-16 | |||
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: 75.54 E-value: 1.14e-16
|
|||||||
Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
122-218 | 2.59e-15 | |||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 71.06 E-value: 2.59e-15
|
|||||||
prmA | PRK00517 | 50S ribosomal protein L11 methyltransferase; |
118-189 | 4.42e-15 | |||
50S ribosomal protein L11 methyltransferase; Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 74.80 E-value: 4.42e-15
|
|||||||
prmA | TIGR00406 | ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ... |
119-225 | 9.04e-11 | |||
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification] Pssm-ID: 273061 Cd Length: 288 Bit Score: 62.54 E-value: 9.04e-11
|
|||||||
CuRO_3_CopA | cd13896 | The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ... |
272-337 | 9.54e-03 | |||
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259963 [Multi-domain] Cd Length: 115 Bit Score: 36.08 E-value: 9.54e-03
|
|||||||
Name | Accession | Description | Interval | E-value | ||||
COG4076 | COG4076 | Predicted RNA methylase [General function prediction only]; |
83-235 | 3.21e-45 | ||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 443253 [Multi-domain] Cd Length: 230 Bit Score: 156.74 E-value: 3.21e-45
|
||||||||
PrmA | COG2264 | Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
108-189 | 8.22e-18 | ||||
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 83.30 E-value: 8.22e-18
|
||||||||
AdoMet_MTases | cd02440 | S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
122-221 | 1.14e-16 | ||||
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: 75.54 E-value: 1.14e-16
|
||||||||
Cfa | COG2230 | Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
116-221 | 3.81e-16 | ||||
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism]; Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 75.35 E-value: 3.81e-16
|
||||||||
Methyltransf_25 | pfam13649 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
122-218 | 2.59e-15 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 463945 [Multi-domain] Cd Length: 96 Bit Score: 71.06 E-value: 2.59e-15
|
||||||||
prmA | PRK00517 | 50S ribosomal protein L11 methyltransferase; |
118-189 | 4.42e-15 | ||||
50S ribosomal protein L11 methyltransferase; Pssm-ID: 234786 [Multi-domain] Cd Length: 250 Bit Score: 74.80 E-value: 4.42e-15
|
||||||||
UbiG | COG2227 | 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
98-221 | 5.98e-15 | ||||
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: 71.20 E-value: 5.98e-15
|
||||||||
COG2263 | COG2263 | Predicted RNA methylase [General function prediction only]; |
117-190 | 1.08e-14 | ||||
Predicted RNA methylase [General function prediction only]; Pssm-ID: 441864 [Multi-domain] Cd Length: 199 Bit Score: 72.24 E-value: 1.08e-14
|
||||||||
PrmA | pfam06325 | Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ... |
118-223 | 1.22e-12 | ||||
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: 68.06 E-value: 1.22e-12
|
||||||||
HemK | COG2890 | Methylase of polypeptide chain release factors [Translation, ribosomal structure and ... |
100-190 | 3.02e-12 | ||||
Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis]; Pssm-ID: 442135 [Multi-domain] Cd Length: 282 Bit Score: 66.71 E-value: 3.02e-12
|
||||||||
UbiE | COG2226 | Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
99-221 | 3.25e-12 | ||||
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: 63.86 E-value: 3.25e-12
|
||||||||
SmtA | COG0500 | SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ... |
110-221 | 8.41e-12 | ||||
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only]; Pssm-ID: 440266 [Multi-domain] Cd Length: 199 Bit Score: 64.17 E-value: 8.41e-12
|
||||||||
TrmN6 | COG4123 | tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
119-224 | 2.94e-11 | ||||
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: 63.24 E-value: 2.94e-11
|
||||||||
Methyltransf_11 | pfam08241 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
123-221 | 3.58e-11 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 462406 [Multi-domain] Cd Length: 94 Bit Score: 59.22 E-value: 3.58e-11
|
||||||||
prmA | TIGR00406 | ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ... |
119-225 | 9.04e-11 | ||||
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification] Pssm-ID: 273061 Cd Length: 288 Bit Score: 62.54 E-value: 9.04e-11
|
||||||||
COG4976 | COG4976 | Predicted methyltransferase, contains TPR repeat [General function prediction only]; |
77-270 | 1.21e-10 | ||||
Predicted methyltransferase, contains TPR repeat [General function prediction only]; Pssm-ID: 444001 [Multi-domain] Cd Length: 181 Bit Score: 60.40 E-value: 1.21e-10
|
||||||||
PRK09328 | PRK09328 | N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional |
100-221 | 4.89e-10 | ||||
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional Pssm-ID: 236467 [Multi-domain] Cd Length: 275 Bit Score: 60.18 E-value: 4.89e-10
|
||||||||
RsmC | COG2813 | 16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
118-190 | 6.23e-10 | ||||
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: 58.28 E-value: 6.23e-10
|
||||||||
Tam | COG4106 | Trans-aconitate methyltransferase [Energy production and conversion]; |
118-221 | 1.06e-09 | ||||
Trans-aconitate methyltransferase [Energy production and conversion]; Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 55.21 E-value: 1.06e-09
|
||||||||
PRK14968 | PRK14968 | putative methyltransferase; Provisional |
118-221 | 1.02e-08 | ||||
putative methyltransferase; Provisional Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 54.90 E-value: 1.02e-08
|
||||||||
MTS | pfam05175 | Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
112-190 | 1.93e-08 | ||||
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: 53.75 E-value: 1.93e-08
|
||||||||
TrmA | COG2265 | tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ... |
103-189 | 4.38e-08 | ||||
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 441866 [Multi-domain] Cd Length: 377 Bit Score: 54.80 E-value: 4.38e-08
|
||||||||
RlmK | COG1092 | 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ... |
107-189 | 9.09e-08 | ||||
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification Pssm-ID: 440709 [Multi-domain] Cd Length: 392 Bit Score: 54.03 E-value: 9.09e-08
|
||||||||
Trm5 | COG2520 | tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ... |
118-220 | 2.67e-07 | ||||
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 442010 [Multi-domain] Cd Length: 333 Bit Score: 52.17 E-value: 2.67e-07
|
||||||||
RsmG | COG0357 | 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ... |
118-221 | 1.03e-06 | ||||
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification Pssm-ID: 440126 Cd Length: 211 Bit Score: 49.38 E-value: 1.03e-06
|
||||||||
Gcd14 | COG2519 | tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
119-189 | 1.03e-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: 49.77 E-value: 1.03e-06
|
||||||||
Cons_hypoth95 | pfam03602 | Conserved hypothetical protein 95; |
114-231 | 1.80e-06 | ||||
Conserved hypothetical protein 95; Pssm-ID: 427391 [Multi-domain] Cd Length: 179 Bit Score: 48.00 E-value: 1.80e-06
|
||||||||
PRK14967 | PRK14967 | putative methyltransferase; Provisional |
110-190 | 2.82e-06 | ||||
putative methyltransferase; Provisional Pssm-ID: 184931 [Multi-domain] Cd Length: 223 Bit Score: 48.13 E-value: 2.82e-06
|
||||||||
PRK07580 | PRK07580 | Mg-protoporphyrin IX methyl transferase; Validated |
119-169 | 2.93e-06 | ||||
Mg-protoporphyrin IX methyl transferase; Validated Pssm-ID: 236059 [Multi-domain] Cd Length: 230 Bit Score: 48.29 E-value: 2.93e-06
|
||||||||
FtsJ | pfam01728 | FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ... |
108-190 | 4.27e-06 | ||||
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping. Pssm-ID: 426399 Cd Length: 179 Bit Score: 46.81 E-value: 4.27e-06
|
||||||||
hemK_fam | TIGR00536 | HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ... |
35-190 | 4.42e-06 | ||||
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair] Pssm-ID: 273125 [Multi-domain] Cd Length: 284 Bit Score: 48.12 E-value: 4.42e-06
|
||||||||
Methyltransf_12 | pfam08242 | Methyltransferase domain; Members of this family are SAM dependent methyltransferases. |
123-220 | 5.34e-06 | ||||
Methyltransferase domain; Members of this family are SAM dependent methyltransferases. Pssm-ID: 400515 [Multi-domain] Cd Length: 98 Bit Score: 44.67 E-value: 5.34e-06
|
||||||||
Methyltransf_9 | pfam08003 | Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ... |
84-265 | 5.77e-06 | ||||
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: 47.78 E-value: 5.77e-06
|
||||||||
PLN02585 | PLN02585 | magnesium protoporphyrin IX methyltransferase |
117-162 | 9.49e-06 | ||||
magnesium protoporphyrin IX methyltransferase Pssm-ID: 215319 [Multi-domain] Cd Length: 315 Bit Score: 47.16 E-value: 9.49e-06
|
||||||||
cbiT | PRK00377 | cobalt-precorrin-6Y C(15)-methyltransferase; Provisional |
116-188 | 9.51e-06 | ||||
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional Pssm-ID: 234740 Cd Length: 198 Bit Score: 46.33 E-value: 9.51e-06
|
||||||||
TrmR | COG4122 | tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
116-221 | 1.62e-05 | ||||
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 443298 Cd Length: 173 Bit Score: 45.18 E-value: 1.62e-05
|
||||||||
CbiT | TIGR02469 | precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ... |
119-221 | 1.96e-05 | ||||
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: 43.86 E-value: 1.96e-05
|
||||||||
Methyltransf_31 | pfam13847 | Methyltransferase domain; This family appears to have methyltransferase activity. |
118-221 | 2.10e-05 | ||||
Methyltransferase domain; This family appears to have methyltransferase activity. Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 44.33 E-value: 2.10e-05
|
||||||||
Methyltransf_23 | pfam13489 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
118-221 | 5.86e-05 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 404385 [Multi-domain] Cd Length: 162 Bit Score: 43.19 E-value: 5.86e-05
|
||||||||
YqxC | COG1189 | Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ... |
117-221 | 1.15e-04 | ||||
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis]; Pssm-ID: 440802 [Multi-domain] Cd Length: 248 Bit Score: 43.51 E-value: 1.15e-04
|
||||||||
fkbM_fam | TIGR01444 | methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ... |
121-190 | 1.53e-04 | ||||
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: 41.53 E-value: 1.53e-04
|
||||||||
BioC | TIGR02072 | malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ... |
109-228 | 2.10e-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: 42.66 E-value: 2.10e-04
|
||||||||
CobL | COG2242 | Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ... |
116-179 | 3.86e-04 | ||||
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441843 [Multi-domain] Cd Length: 403 Bit Score: 42.46 E-value: 3.86e-04
|
||||||||
Methyltransf_24 | pfam13578 | Methyltransferase domain; This family appears to be a methyltransferase domain. |
123-221 | 5.14e-04 | ||||
Methyltransferase domain; This family appears to be a methyltransferase domain. Pssm-ID: 433324 [Multi-domain] Cd Length: 106 Bit Score: 39.21 E-value: 5.14e-04
|
||||||||
sugar_DH | cd08236 | NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ... |
119-246 | 6.72e-04 | ||||
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex. Pssm-ID: 176198 [Multi-domain] Cd Length: 343 Bit Score: 41.44 E-value: 6.72e-04
|
||||||||
PLN02336 | PLN02336 | phosphoethanolamine N-methyltransferase |
94-220 | 1.80e-03 | ||||
phosphoethanolamine N-methyltransferase Pssm-ID: 177970 [Multi-domain] Cd Length: 475 Bit Score: 40.50 E-value: 1.80e-03
|
||||||||
PRK08317 | PRK08317 | hypothetical protein; Provisional |
106-236 | 1.97e-03 | ||||
hypothetical protein; Provisional Pssm-ID: 181382 [Multi-domain] Cd Length: 241 Bit Score: 39.53 E-value: 1.97e-03
|
||||||||
rsmC | PRK09489 | 16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC; |
117-190 | 2.05e-03 | ||||
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC; Pssm-ID: 181902 [Multi-domain] Cd Length: 342 Bit Score: 39.92 E-value: 2.05e-03
|
||||||||
CMAS | pfam02353 | Mycolic acid cyclopropane synthetase; This family consist of ... |
116-190 | 2.43e-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: 39.62 E-value: 2.43e-03
|
||||||||
arsM | PRK11873 | arsenite methyltransferase; |
112-190 | 2.82e-03 | ||||
arsenite methyltransferase; Pssm-ID: 237007 [Multi-domain] Cd Length: 272 Bit Score: 39.55 E-value: 2.82e-03
|
||||||||
Rsm22 | COG5459 | Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ... |
122-221 | 3.64e-03 | ||||
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins Pssm-ID: 444210 [Multi-domain] Cd Length: 306 Bit Score: 39.17 E-value: 3.64e-03
|
||||||||
CuRO_3_CopA | cd13896 | The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper ... |
272-337 | 9.54e-03 | ||||
The third cupredoxin domain of CopA copper resistance protein family; CopA is a multicopper oxidase (MCO) related to laccase and L-ascorbate oxidase, both copper-containing enzymes. It is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CopA is a copper efflux P-type ATPase that is located in the inner cell membrane and is is involved in copper resistance in bacteria. CopA mutant causes a loss of function including copper tolerance and oxidase activity and copA transcription is inducible in the presence of copper. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. Pssm-ID: 259963 [Multi-domain] Cd Length: 115 Bit Score: 36.08 E-value: 9.54e-03
|
||||||||
Blast search parameters | ||||
|