NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|354983497|ref|NP_001238980|]
View 

protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform 4 [Homo sapiens]

Protein Classification

protein-L-isoaspartate O-methyltransferase family protein( domain architecture ID 1000299)

protein-L-isoaspartate O-methyltransferase (PIMT) family protein catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues

Gene Ontology:  GO:0051998|GO:0036211

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PCMT super family cl30237
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
77-239 2.35e-85

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


The actual alignment was detected with superfamily member pfam01135:

Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 252.67  E-value: 2.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   77 SFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTllss 156
Cdd:pfam01135  51 GYGQTISAPHMHAMMLELL--ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  157 gRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSIKMKPLMGVIY 236
Cdd:pfam01135 125 -NVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRF 202

                  ...
gi 354983497  237 VPL 239
Cdd:pfam01135 203 VPL 205
 
Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
77-239 2.35e-85

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 252.67  E-value: 2.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   77 SFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTllss 156
Cdd:pfam01135  51 GYGQTISAPHMHAMMLELL--ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  157 gRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSIKMKPLMGVIY 236
Cdd:pfam01135 125 -NVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRF 202

                  ...
gi 354983497  237 VPL 239
Cdd:pfam01135 203 VPL 205
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
78-246 3.11e-58

protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]


Pssm-ID: 272896 [Multi-domain]  Cd Length: 215  Bit Score: 184.26  E-value: 3.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   78 FQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptlLSSG 157
Cdd:TIGR00080  56 YGQTISAPHMVAMMTELL--ELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  158 RVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPagGNQMLEQYDKlQDGSIKMKPLMGVIYV 237
Cdd:TIGR00080 129 NVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK-RGGEIIIKDVEPVAFV 205

                  ....*....
gi 354983497  238 PLTDKEKQW 246
Cdd:TIGR00080 206 PLVGGEGFQ 214
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
81-240 6.44e-45

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 149.47  E-value: 6.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGctgKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQ 160
Cdd:COG2518   48 TISQPYIVARMLEAL--DLKPGDRVLEIGTGSGYQAAVLARLAG---RVYSVERDPELAERARERLAA-----LGYDNVT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 161 LVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGsIKMKPLMGVIYVPLT 240
Cdd:COG2518  118 VRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVAPVGE-GGVQRLVLITRTGDG-FERESLFEVRFVPLR 195
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
81-243 8.73e-43

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 144.39  E-value: 8.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQ 160
Cdd:PRK13942  58 TISAIHMVAIMCELL--DLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK-----LGYDNVE 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 161 LVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAggNQMLEQYDKlQDGSIKMKPLMGVIYVPLT 240
Cdd:PRK13942 131 VIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQLKDGGIMVIPVGSY--SQELIRVEK-DNGKIIKKKLGEVAFVPLI 207

                 ...
gi 354983497 241 DKE 243
Cdd:PRK13942 208 GKN 210
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
104-206 8.33e-07

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: 46.27  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 104 KALDVGSGSGILTACFARMVGCtgKVIGIDhikelVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMG-YAEEAPYDAIHVG 182
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA--RVTGVD-----ISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISD 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 354983497 183 AAAPVV---PQALIDQ----LKPGGRLILPV 206
Cdd:cd02440   74 PPLHHLvedLARFLEEarrlLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
77-239 2.35e-85

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 252.67  E-value: 2.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   77 SFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDPTllss 156
Cdd:pfam01135  51 GYGQTISAPHMHAMMLELL--ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  157 gRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSIKMKPLMGVIY 236
Cdd:pfam01135 125 -NVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRF 202

                  ...
gi 354983497  237 VPL 239
Cdd:pfam01135 203 VPL 205
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
78-246 3.11e-58

protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]


Pssm-ID: 272896 [Multi-domain]  Cd Length: 215  Bit Score: 184.26  E-value: 3.11e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   78 FQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptlLSSG 157
Cdd:TIGR00080  56 YGQTISAPHMVAMMTELL--ELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  158 RVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPagGNQMLEQYDKlQDGSIKMKPLMGVIYV 237
Cdd:TIGR00080 129 NVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK-RGGEIIIKDVEPVAFV 205

                  ....*....
gi 354983497  238 PLTDKEKQW 246
Cdd:TIGR00080 206 PLVGGEGFQ 214
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
81-240 6.44e-45

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 149.47  E-value: 6.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGctgKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQ 160
Cdd:COG2518   48 TISQPYIVARMLEAL--DLKPGDRVLEIGTGSGYQAAVLARLAG---RVYSVERDPELAERARERLAA-----LGYDNVT 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 161 LVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGsIKMKPLMGVIYVPLT 240
Cdd:COG2518  118 VRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVAPVGE-GGVQRLVLITRTGDG-FERESLFEVRFVPLR 195
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
81-243 8.73e-43

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 144.39  E-value: 8.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQ 160
Cdd:PRK13942  58 TISAIHMVAIMCELL--DLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK-----LGYDNVE 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 161 LVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAggNQMLEQYDKlQDGSIKMKPLMGVIYVPLT 240
Cdd:PRK13942 131 VIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQLKDGGIMVIPVGSY--SQELIRVEK-DNGKIIKKKLGEVAFVPLI 207

                 ...
gi 354983497 241 DKE 243
Cdd:PRK13942 208 GKN 210
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
81-243 1.58e-35

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 125.70  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGctgKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQ 160
Cdd:PRK00312  60 TISQPYMVARMTELL--ELKPGDRVLEIGTGSGYQAAVLAHLVR---RVFSVERIKTLQWEAKRRLKQ-----LGLHNVS 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 161 LVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGpaGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLT 240
Cdd:PRK00312 130 VRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLEQLKEGGILVAPVG--GEEQQLLTRVRKRGGRFEREVLEEVRFVPLV 207

                 ...
gi 354983497 241 DKE 243
Cdd:PRK00312 208 KGE 210
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
78-239 2.33e-25

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 99.12  E-value: 2.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  78 FQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptLLSSG 157
Cdd:PRK13944  51 AGATISAPHMVAMMCELI--EPRPGMKILEVGTGSGYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIER----LGYWG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 158 RVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGnQMLEQYDKLQDGsIKMKPLMGVIYV 237
Cdd:PRK13944 125 VVEVYHGDGKRGLEKHAPFDAIIVTAAASTIPSALVRQLKDGGVLVIPVEEGVG-QVLYKVVKRGEK-VEKRAITYVLFV 202

                 ..
gi 354983497 238 PL 239
Cdd:PRK13944 203 PL 204
methyltran_FxLD TIGR04364
methyltransferase, FxLD system; Members of this family resemble occur regularly in the ...
81-206 9.59e-19

methyltransferase, FxLD system; Members of this family resemble occur regularly in the vicinity of lantibiotic biosynthesis enzymes and their probable target, the FxLD family of putative ribosomal natural product precursor (TIGR04363). Members resemble protein-L-isoaspartate O-methyltransferase (TIGR00080) and a predicted methyltranserase, TIGR04188, of another putative peptide modification system.


Pssm-ID: 275158  Cd Length: 394  Bit Score: 84.34  E-value: 9.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   81 TISAPHMHAYALELLfdQLHEGAKALDVGSGsGILTACFARMVGCTGKVIGIDHIKELVDDSvnnvRKddptLLSS---G 157
Cdd:TIGR04364  64 SVSAPHIQAMMLEQA--GVEPGMRVLEIGSG-GYNAALLAELVGPSGEVTTVDIDEDVTDRA----RA----CLAAagyP 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 354983497  158 RVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPV 206
Cdd:TIGR04364 133 QVTVVLADAEAGVPELAPYDRIIVTVGAWDIPPAWLDQLAPGGRLVVPL 181
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
80-206 1.00e-18

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 83.36  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  80 ATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptlLSSGRV 159
Cdd:PRK13943  61 STSSQPSLMALFMEWV--GLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRR-----LGIENV 133
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 354983497 160 QLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPV 206
Cdd:PRK13943 134 IFVCGDGYYGVPEFAPYDVIFVTVGVDEVPETWFTQLKEGGRVIVPI 180
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
99-203 3.08e-11

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: 61.33  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  99 LHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptLLSSGRVQLVVGDGRMGYAEEaPYDA 178
Cdd:COG2519   89 IFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLER----FGLPDNVELKLGDIREGIDEG-DVDA 163
                         90       100
                 ....*....|....*....|....*..
gi 354983497 179 IHVGAAAP--VVPQAlIDQLKPGGRLI 203
Cdd:COG2519  164 VFLDMPDPweALEAV-AKALKPGGVLV 189
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
93-204 1.60e-09

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: 54.25  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  93 ELLFDQLHEGAKALDVGSGSGILTACFARMvGCtgKVIGIDhikeLVDDSVNNVRKddptLLSSGRVQLVVGDGRMGYAE 172
Cdd:COG2227   16 ALLARLLPAGGRVLDVGCGTGRLALALARR-GA--DVTGVD----ISPEALEIARE----RAAELNVDFVQGDLEDLPLE 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 354983497 173 EAPYDAI-------HVGAAAPVVpQALIDQLKPGGRLIL 204
Cdd:COG2227   85 DGSFDLVicsevleHLPDPAALL-RELARLLKPGGLLLL 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
91-204 1.73e-09

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.94  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  91 ALELLFD--QLHEGAKALDVGSGSGILTACFARMVGCtgKVIGIDhikeLVDDSVNNVRKDDPTLLSSGRVQLVVGDGRm 168
Cdd:COG2230   39 KLDLILRklGLKPGMRVLDIGCGWGGLALYLARRYGV--RVTGVT----LSPEQLEYARERAAEAGLADRVEVRLADYR- 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 354983497 169 GYAEEAPYDAI-------HVGAAA-PVVPQALIDQLKPGGRLIL 204
Cdd:COG2230  112 DLPADGQFDAIvsigmfeHVGPENyPAYFAKVARLLKPGGRLLL 155
methyltr_grsp TIGR04188
methyltransferase, ATP-grasp peptide maturase system; Members of this protein family are ...
99-211 5.11e-09

methyltransferase, ATP-grasp peptide maturase system; Members of this protein family are predicted SAM-dependent methyltransferases that regularly occur in the context of a putative peptide modification ATP-grasp enzyme (TIGR04187, related to enzymes of microviridin maturation) and a putative ribosomal peptide modification target (TIGR04186).


Pssm-ID: 275041  Cd Length: 363  Bit Score: 55.83  E-value: 5.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   99 LHEGAKALDVGSGSGILTACFARMVGcTGKVIGIDhikelVDDSVnnVRKDDPTLLSSG-RVQLVVGDGRMGYAEEAPYD 177
Cdd:TIGR04188 105 VEDGHRVLEIGTGTGYSAALLCHRLG-DDNVTSVE-----VDPGL--AARAASALAAAGyAPTVVTGDGLLGHPPRAPYD 176
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 354983497  178 AIHVGAAAPVVPQALIDQLKPGGRLILPVG---PAGG 211
Cdd:TIGR04188 177 RIIATCAVRRVPPAWLRQTRPGGVILTTLSgwlYGGG 213
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
92-204 1.07e-08

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 54.41  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  92 LELLFDQLHEGAKALDVGSGSGILtACFARMVGCtGKVIGIDhIKEL-VDDSVNNVRKDDptllSSGRVQLVVGDGRmgy 170
Cdd:COG2264  139 LEALEKLLKPGKTVLDVGCGSGIL-AIAAAKLGA-KRVLAVD-IDPVaVEAARENAELNG----VEDRIEVVLGDLL--- 208
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 354983497 171 aEEAPYDAIhVgA---AAPVVPQA--LIDQLKPGGRLIL 204
Cdd:COG2264  209 -EDGPYDLV-V-AnilANPLIELApdLAALLKPGGYLIL 244
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
106-200 1.77e-08

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 50.64  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  106 LDVGSGSGILTACFARMVGCtgKVIGIDHIKELVDDSVNNVRKDDPtllssgRVQLVVGDGRMGYAEEAPYDAIHVGAAA 185
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA--RVTGVDLSPEMLERARERAAEAGL------NVEFVQGDAEDLPFPDGSFDLVVSSGVL 73
                          90       100
                  ....*....|....*....|...
gi 354983497  186 PVVPQALIDQ--------LKPGG 200
Cdd:pfam13649  74 HHLPDPDLEAalreiarvLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
101-204 2.55e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 50.59  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 101 EGAKALDVGSGSGILTACFARMVGCtGKVIGIDhikeLVDDSVNNVRKDDPtllssgRVQLVVGDGRmGYAEEAPYDAIH 180
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPG-ARVTGVD----LSPEMLARARARLP------NVRFVVADLR-DLDPPEPFDLVV 68
                         90       100       110
                 ....*....|....*....|....*....|
gi 354983497 181 VGAA------APVVPQALIDQLKPGGRLIL 204
Cdd:COG4106   69 SNAAlhwlpdHAALLARLAAALAPGGVLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
91-234 6.33e-08

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.46  E-value: 6.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  91 ALELLFDQLHEGAKALDVGSGSGILTACFARMVGctGKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQLVVGD-GRMG 169
Cdd:COG0500   16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAK-----AGLGNVEFLVADlAELD 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 354983497 170 YAEEAPYDAI-------HVgaaAPVVPQALID----QLKPGGRLILPVGPAGGNQMLEQYDKLQDGSIKMKPLMGV 234
Cdd:COG0500   89 PLPAESFDLVvafgvlhHL---PPEEREALLRelarALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLR 161
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
88-204 6.45e-08

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: 50.38  E-value: 6.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  88 HAYALELLfdQLHEGAKALDVGSGSGILTACFARMvgcTGKVIGIDHIKELVDDSVNNVRKDDPtllssgRVQLVVGDG- 166
Cdd:COG2226   11 REALLAAL--GLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGL------NVEFVVGDAe 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 354983497 167 RMGYAEEApYDAIHVGAAAPVVP--QALIDQ----LKPGGRLIL 204
Cdd:COG2226   80 DLPFPDGS-FDLVISSFVLHHLPdpERALAEiarvLKPGGRLVV 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
104-206 8.33e-07

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: 46.27  E-value: 8.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 104 KALDVGSGSGILTACFARMVGCtgKVIGIDhikelVDDSVNNVRKDDPTLLSSGRVQLVVGDGRMG-YAEEAPYDAIHVG 182
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGA--RVTGVD-----ISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISD 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 354983497 183 AAAPVV---PQALIDQ----LKPGGRLILPV 206
Cdd:cd02440   74 PPLHHLvedLARFLEEarrlLKPGGVLVLTL 104
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
102-204 1.10e-06

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 48.23  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497 102 GAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDdsvnNVRKDDPTLLSSGRVQLVVGDgrmgyAEEAPY----- 176
Cdd:PRK00216  52 GDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLA----VGREKLRDLGLSGNVEFVQGD-----AEALPFpdnsf 122
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 354983497 177 DAIHVGAAAPVVPQalIDQ--------LKPGGRL-IL 204
Cdd:PRK00216 123 DAVTIAFGLRNVPD--IDKalremyrvLKPGGRLvIL 157
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
82-206 1.46e-06

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: 46.17  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   82 ISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGcTGKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQL 161
Cdd:TIGR02469   2 MTKREVRALTLAKL--RLRPGDVLWDIGAGTGSVTIEAARLVP-NGRVYAIERNPEALDLIERNLRR-----FGVSNIVI 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 354983497  162 VVGDgrmgyAEEAPY------DAIHVGAAA---PVVPQALIDQLKPGGRLILPV 206
Cdd:TIGR02469  74 VEGD-----APEAPEallpdpDAVFVGGSGgllQEILEAVERRLRPGGRIVLNA 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
99-204 2.47e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.87  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   99 LHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptlLSSGRVQLVVGDgrmgyAEEAP--- 175
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQK-----LGFDNVEFEQGD-----IEELPell 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 354983497  176 ----YD------AIHVGAAAPVVPQALIDQLKPGGRLIL 204
Cdd:pfam13847  71 eddkFDvvisncVLNHIPDPDKVLQEILRVLKPGGRLII 109
PRK08317 PRK08317
hypothetical protein; Provisional
89-204 2.50e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 47.24  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  89 AYALELLfdQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVdDSVNNVRKDDptllsSGRVQLVVGDG-R 167
Cdd:PRK08317   9 ARTFELL--AVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAML-ALAKERAAGL-----GPNVEFVRGDAdG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 354983497 168 MGYAEEApYDAIHVGAAAPVV--PQALIDQ----LKPGGRLIL 204
Cdd:PRK08317  81 LPFPDGS-FDAVRSDRVLQHLedPARALAEiarvLRPGGRVVV 122
arsM PRK11873
arsenite methyltransferase;
96-148 4.36e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 46.48  E-value: 4.36e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 354983497  96 FDQLHEGAKALDVGSGSGIltACF--ARMVGCTGKVIGIDHIKELVDDSVNNVRK 148
Cdd:PRK11873  72 LAELKPGETVLDLGSGGGF--DCFlaARRVGPTGKVIGVDMTPEMLAKARANARK 124
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
91-206 3.49e-05

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 43.25  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  91 ALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKddptLLSSGRVQLVVGDGRMGY 170
Cdd:PRK00377  30 ALALSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEK----FGVLNNIVLIKGEAPEIL 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 354983497 171 AEEAP-YDAIHVGAAA---PVVPQALIDQLKPGGRLILPV 206
Cdd:PRK00377 106 FTINEkFDRIFIGGGSeklKEIISASWEIIKKGGRIVIDA 145
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
92-204 3.88e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.60  E-value: 3.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  92 LELLFDQLHEGAKALDVGSGSGILtACFARMVGCTgKVIGIDhIKEL-VDDSVNNVRkddptlLSSGRVQLVVGDGrmgy 170
Cdd:PRK00517 110 LEALEKLVLPGKTVLDVGCGSGIL-AIAAAKLGAK-KVLAVD-IDPQaVEAARENAE------LNGVELNVYLPQG---- 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 354983497 171 aeEAPYDAIhVgA---AAPVVpqALIDQ----LKPGGRLIL 204
Cdd:PRK00517 177 --DLKADVI-V-AnilANPLL--ELAPDlarlLKPGGRLIL 211
PRK14968 PRK14968
putative methyltransferase; Provisional
93-133 7.04e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.19  E-value: 7.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 354983497  93 ELLFDQLHE--GAKALDVGSGSGILTACFARMvgcTGKVIGID 133
Cdd:PRK14968  13 FLLAENAVDkkGDRVLEVGTGSGIVAIVAAKN---GKKVVGVD 52
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
106-204 9.28e-05

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 40.34  E-value: 9.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  106 LDVGSGSGILTACFARMVgctGKVIGIDHIKELVDDSVNNVRKDDptllssgrVQLVVGDG-RMGYAEEApYDAIHVGAA 184
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG---ARVTGVDISPEMLELAREKAPREG--------LTFVVGDAeDLPFPDNS-FDLVLSSEV 68
                          90       100
                  ....*....|....*....|....*.
gi 354983497  185 A---PVVPQAL--IDQ-LKPGGRLIL 204
Cdd:pfam08241  69 LhhvEDPERALreIARvLKPGGILII 94
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
101-203 3.67e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 40.50  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  101 EGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDdptllSSGRVQLVVGDGRMGYAEEAPYDAIH 180
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEE-----GKYNIEFLQGNAEELPFEDDSFDIVT 116
                          90       100
                  ....*....|....*....|....*....
gi 354983497  181 VGAA---APVVPQALIDQ---LKPGGRLI 203
Cdd:pfam01209 117 ISFGlrnFPDYLKVLKEAfrvLKPGGRVV 145
PLN02366 PLN02366
spermidine synthase
146-200 4.66e-04

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 40.78  E-value: 4.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 354983497 146 VRKDDPtllssgRVQLVVGDGR--MGYAEEAPYDAIHVGAAAPVVP-QALIDQ---------LKPGG 200
Cdd:PLN02366 140 VGFDDP------RVNLHIGDGVefLKNAPEGTYDAIIVDSSDPVGPaQELFEKpffesvaraLRPGG 200
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
98-200 6.62e-04

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: 39.40  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  98 QLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSVNNVRKDDptllSSGRVQLVVGDGR--MGYAEEAP 175
Cdd:COG4122   13 RLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAG----LADRIRLILGDALevLPRLADGP 88
                         90       100
                 ....*....|....*....|....*...
gi 354983497 176 YDAIHVGAAAPVVP---QALIDQLKPGG 200
Cdd:COG4122   89 FDLVFIDADKSNYPdylELALPLLRPGG 116
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
96-204 7.82e-04

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: 39.11  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497   96 FDQLHEGaKALDVGSGSGILTACFARMVGctgkvigiDHIKELVDDSVNNVRKDDPTLLSSG--RVQLVVGDGRMGyAEE 173
Cdd:pfam05175  27 LPKDLSG-KVLDLGCGAGVLGAALAKESP--------DAELTMVDINARALESARENLAANGleNGEVVASDVYSG-VED 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 354983497  174 APYDAI------HVG-AAAPVVPQALI----DQLKPGGRLIL 204
Cdd:pfam05175  97 GKFDLIisnppfHAGlATTYNVAQRFIadakRHLRPGGELWI 138
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
86-204 1.28e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.44  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  86 HMHAYALELLFDQlhEGAKALDVGSGSGILTACFARMVgctGKVIGIDhikeLVDDSVNNVRKddptllSSGRVQLVVGD 165
Cdd:COG4976   33 LLAEELLARLPPG--PFGRVLDLGCGTGLLGEALRPRG---YRLTGVD----LSEEMLAKARE------KGVYDRLLVAD 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 354983497 166 GRMGYAEEAPYDAI-------HVGAAAPVVpQALIDQLKPGGRLIL 204
Cdd:COG4976   98 LADLAEPDGRFDLIvaadvltYLGDLAAVF-AGVARALKPGGLFIF 142
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
93-204 2.70e-03

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: 37.86  E-value: 2.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354983497  93 ELLFDQL--HEGAKALDVGSGSGILTACFARMVGcTGKVIGIDhikelvddsVN---------NVRKDDPTllssgRVQL 161
Cdd:COG2813   39 RLLLEHLpePLGGRVLDLGCGYGVIGLALAKRNP-EARVTLVD---------VNaravelaraNAAANGLE-----NVEV 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 354983497 162 VVGDGRMGYAEEaPYDAI------HVGAAAPV-VPQALIDQ----LKPGGRLIL 204
Cdd:COG2813  104 LWSDGLSGVPDG-SFDLIlsnppfHAGRAVDKeVAHALIADaarhLRPGGELWL 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH