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Conserved domains on  [gi|1958642774|ref|XP_038957965|]
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protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform X1 [Rattus norvegicus]

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

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List of domain hits

Name Accession Description Interval E-value
PCMT super family cl30237
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
77-239 1.17e-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: 253.44  E-value: 1.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  77 SFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDPMllss 156
Cdd:pfam01135  51 GYGQTISAPHMHAMMLELL--ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 157 gRVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIY 236
Cdd:pfam01135 125 -NVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRF 202

                  ...
gi 1958642774 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 1.17e-85

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 253.44  E-value: 1.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  77 SFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDPMllss 156
Cdd:pfam01135  51 GYGQTISAPHMHAMMLELL--ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 157 gRVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIY 236
Cdd:pfam01135 125 -NVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRF 202

                  ...
gi 1958642774 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 1.07e-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: 185.42  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  78 FQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmlLSSG 157
Cdd:TIGR00080  56 YGQTISAPHMVAMMTELL--ELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 158 RVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPagGNQMLEQYDKlQDGSVKMKPLMGVIYV 237
Cdd:TIGR00080 129 NVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK-RGGEIIIKDVEPVAFV 205

                  ....*....
gi 1958642774 238 PLTDKEKQW 246
Cdd:TIGR00080 206 PLVGGEGFQ 214
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
81-240 2.13e-44

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 147.93  E-value: 2.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHsgkVIGIDHIKELVDDSITNVKKddpmlLSSGRVR 160
Cdd:COG2518    48 TISQPYIVARMLEAL--DLKPGDRVLEIGTGSGYQAAVLARLAGR---VYSVERDPELAERARERLAA-----LGYDNVT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 161 LVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGsVKMKPLMGVIYVPLT 240
Cdd:COG2518   118 VRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVAPVGE-GGVQRLVLITRTGDG-FERESLFEVRFVPLR 195
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
81-243 1.80e-41

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 140.92  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVR 160
Cdd:PRK13942   58 TISAIHMVAIMCELL--DLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK-----LGYDNVE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 161 LVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAggNQMLEQYDKlQDGSVKMKPLMGVIYVPLT 240
Cdd:PRK13942  131 VIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQLKDGGIMVIPVGSY--SQELIRVEK-DNGKIIKKKLGEVAFVPLI 207

                  ...
gi 1958642774 241 DKE 243
Cdd:PRK13942  208 GKN 210
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
104-206 9.26e-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: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 104 KALDVGSGSGILTACFARmvGHSGKVIGIDhikelVDDSITNVKKDDPMLLSSGRVRLVVGDGRMG-FAEEAPYDAIHVG 182
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVD-----ISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISD 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958642774 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 1.17e-85

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 253.44  E-value: 1.17e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  77 SFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDPMllss 156
Cdd:pfam01135  51 GYGQTISAPHMHAMMLELL--ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE---- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 157 gRVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIY 236
Cdd:pfam01135 125 -NVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRF 202

                  ...
gi 1958642774 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 1.07e-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: 185.42  E-value: 1.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  78 FQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmlLSSG 157
Cdd:TIGR00080  56 YGQTISAPHMVAMMTELL--ELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 158 RVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPagGNQMLEQYDKlQDGSVKMKPLMGVIYV 237
Cdd:TIGR00080 129 NVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK-RGGEIIIKDVEPVAFV 205

                  ....*....
gi 1958642774 238 PLTDKEKQW 246
Cdd:TIGR00080 206 PLVGGEGFQ 214
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
81-240 2.13e-44

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 147.93  E-value: 2.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHsgkVIGIDHIKELVDDSITNVKKddpmlLSSGRVR 160
Cdd:COG2518    48 TISQPYIVARMLEAL--DLKPGDRVLEIGTGSGYQAAVLARLAGR---VYSVERDPELAERARERLAA-----LGYDNVT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 161 LVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGsVKMKPLMGVIYVPLT 240
Cdd:COG2518   118 VRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVAPVGE-GGVQRLVLITRTGDG-FERESLFEVRFVPLR 195
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
81-243 1.80e-41

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 140.92  E-value: 1.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVR 160
Cdd:PRK13942   58 TISAIHMVAIMCELL--DLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK-----LGYDNVE 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 161 LVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAggNQMLEQYDKlQDGSVKMKPLMGVIYVPLT 240
Cdd:PRK13942  131 VIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQLKDGGIMVIPVGSY--SQELIRVEK-DNGKIIKKKLGEVAFVPLI 207

                  ...
gi 1958642774 241 DKE 243
Cdd:PRK13942  208 GKN 210
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
81-243 4.75e-36

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 126.86  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHsgkVIGIDHIKELVDDSITNVKKddpmlLSSGRVR 160
Cdd:PRK00312   60 TISQPYMVARMTELL--ELKPGDRVLEIGTGSGYQAAVLAHLVRR---VFSVERIKTLQWEAKRRLKQ-----LGLHNVS 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 161 LVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGpaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLT 240
Cdd:PRK00312  130 VRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLEQLKEGGILVAPVG--GEEQQLLTRVRKRGGRFEREVLEEVRFVPLV 207

                  ...
gi 1958642774 241 DKE 243
Cdd:PRK00312  208 KGE 210
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
78-239 1.82e-25

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 99.50  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  78 FQATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmLLSSG 157
Cdd:PRK13944   51 AGATISAPHMVAMMCELI--EPRPGMKILEVGTGSGYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIER----LGYWG 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 158 RVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGnQMLEQYDKLQDGsVKMKPLMGVIYV 237
Cdd:PRK13944  125 VVEVYHGDGKRGLEKHAPFDAIIVTAAASTIPSALVRQLKDGGVLVIPVEEGVG-QVLYKVVKRGEK-VEKRAITYVLFV 202

                  ..
gi 1958642774 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 4.07e-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: 85.50  E-value: 4.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  81 TISAPHMHAYALELLfdQLHEGAKALDVGSGsGILTACFARMVGHSGKVIGIDHIKELVDDSitnvkkdDPMLLSSG--R 158
Cdd:TIGR04364  64 SVSAPHIQAMMLEQA--GVEPGMRVLEIGSG-GYNAALLAELVGPSGEVTTVDIDEDVTDRA-------RACLAAAGypQ 133
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958642774 159 VRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPV 206
Cdd:TIGR04364 134 VTVVLADAEAGVPELAPYDRIIVTVGAWDIPPAWLDQLAPGGRLVVPL 181
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
80-206 1.60e-18

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 82.97  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  80 ATISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRV 159
Cdd:PRK13943   61 STSSQPSLMALFMEWV--GLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRR-----LGIENV 133
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958642774 160 RLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPV 206
Cdd:PRK13943  134 IFVCGDGYYGVPEFAPYDVIFVTVGVDEVPETWFTQLKEGGRVIVPI 180
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
99-203 3.47e-12

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: 64.03  E-value: 3.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  99 LHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmLLSSGRVRLVVGDGRMGFAEEaPYDA 178
Cdd:COG2519    89 IFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLER----FGLPDNVELKLGDIREGIDEG-DVDA 163
                          90       100
                  ....*....|....*....|....*..
gi 1958642774 179 IHVGAAAP--VVPQAlIDQLKPGGRLI 203
Cdd:COG2519   164 VFLDMPDPweALEAV-AKALKPGGVLV 189
methyltr_grsp TIGR04188
methyltransferase, ATP-grasp peptide maturase system; Members of this protein family are ...
99-211 9.19e-10

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: 58.14  E-value: 9.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  99 LHEGAKALDVGSGSGILTACFARMVGhsgkvigidhikelvDDSITNVKKDdPMLLSSGRVRL---------VVGDGRMG 169
Cdd:TIGR04188 105 VEDGHRVLEIGTGTGYSAALLCHRLG---------------DDNVTSVEVD-PGLAARAASALaaagyaptvVTGDGLLG 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958642774 170 FAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVG---PAGG 211
Cdd:TIGR04188 169 HPPRAPYDRIIATCAVRRVPPAWLRQTRPGGVILTTLSgwlYGGG 213
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
93-204 1.35e-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: 54.64  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  93 ELLFDQLHEGAKALDVGSGSGILTACFARMvGHsgKVIGIDhikeLVDDSITNVKKddpmLLSSGRVRLVVGDGRMGFAE 172
Cdd:COG2227    16 ALLARLLPAGGRVLDVGCGTGRLALALARR-GA--DVTGVD----ISPEALEIARE----RAAELNVDFVQGDLEDLPLE 84
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958642774 173 EAPYDAI-------HVGAAAPVVpQALIDQLKPGGRLIL 204
Cdd:COG2227    85 DGSFDLVicsevleHLPDPAALL-RELARLLKPGGLLLL 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
91-204 4.61e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.78  E-value: 4.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  91 ALELLFD--QLHEGAKALDVGSGSGILTACFARMVGHsgKVIGID-------HIKELVDDsitnvkkddpmLLSSGRVRL 161
Cdd:COG2230    39 KLDLILRklGLKPGMRVLDIGCGWGGLALYLARRYGV--RVTGVTlspeqleYARERAAE-----------AGLADRVEV 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958642774 162 VVGDGRmGFAEEAPYDAI-------HVGAAA-PVVPQALIDQLKPGGRLIL 204
Cdd:COG2230   106 RLADYR-DLPADGQFDAIvsigmfeHVGPENyPAYFAKVARLLKPGGRLLL 155
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
92-204 5.01e-09

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 55.56  E-value: 5.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  92 LELLFDQLHEGAKALDVGSGSGILtACFARMVGHsGKVIGIDhIKEL-VDDSITNVKKDDpmllSSGRVRLVVGDGRmgf 170
Cdd:COG2264   139 LEALEKLLKPGKTVLDVGCGSGIL-AIAAAKLGA-KRVLAVD-IDPVaVEAARENAELNG----VEDRIEVVLGDLL--- 208
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958642774 171 aEEAPYDAIhVgA---AAPVVPQA--LIDQLKPGGRLIL 204
Cdd:COG2264   209 -EDGPYDLV-V-AnilANPLIELApdLAALLKPGGYLIL 244
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
101-204 5.17e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 52.52  E-value: 5.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 101 EGAKALDVGSGSGILTACFARMVGHsGKVIGIDhikeLVDDSITNVKKDDPmllssgRVRLVVGDGRmGFAEEAPYDAIH 180
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPG-ARVTGVD----LSPEMLARARARLP------NVRFVVADLR-DLDPPEPFDLVV 68
                          90       100       110
                  ....*....|....*....|....*....|
gi 1958642774 181 VGAA------APVVPQALIDQLKPGGRLIL 204
Cdd:COG4106    69 SNAAlhwlpdHAALLARLAAALAPGGVLAV 98
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
99-204 1.33e-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: 52.30  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  99 LHEGAKALDVGSGSGILTACFARmvgHSGKVIGIDHIKELVDDSITNVKKDDPmllssgRVRLVVGDG-RMGFAEEApYD 177
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERAAEAGL------NVEFVVGDAeDLPFPDGS-FD 89
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958642774 178 AIHVGAAAPVVP--QALIDQ----LKPGGRLIL 204
Cdd:COG2226    90 LVISSFVLHHLPdpERALAEiarvLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
106-200 1.65e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.03  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 106 LDVGSGSGILTACFARMVGHsgKVIGIDHIKELVDDSITNVKKDDPmllssgRVRLVVGDGR-MGFAEEaPYDAIHVGAA 184
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGA--RVTGVDLSPEMLERARERAAEAGL------NVEFVQGDAEdLPFPDG-SFDLVVSSGV 72
                          90       100
                  ....*....|....*....|....
gi 1958642774 185 APVVPQALIDQ--------LKPGG 200
Cdd:pfam13649  73 LHHLPDPDLEAalreiarvLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
91-234 5.53e-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: 5.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  91 ALELLFDQLHEGAKALDVGSGSGILTACFARMVGHsgKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGD-GRMG 169
Cdd:COG0500    16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFGG--RVIGIDLSPEAIALARARAAK-----AGLGNVEFLVADlAELD 88
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958642774 170 FAEEAPYDAI-------HVgaaAPVVPQALID----QLKPGGRLILPVGPAGGNQMLEQYDKLQDGSVKMKPLMGV 234
Cdd:COG0500    89 PLPAESFDLVvafgvlhHL---PPEEREALLRelarALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLR 161
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
82-206 6.38e-07

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: 47.32  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  82 ISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGhSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRL 161
Cdd:TIGR02469   2 MTKREVRALTLAKL--RLRPGDVLWDIGAGTGSVTIEAARLVP-NGRVYAIERNPEALDLIERNLRR-----FGVSNIVI 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958642774 162 VVGDgrmgfAEEAPY------DAIHVGAAA---PVVPQALIDQLKPGGRLILPV 206
Cdd:TIGR02469  74 VEGD-----APEAPEallpdpDAVFVGGSGgllQEILEAVERRLRPGGRIVLNA 122
PRK08317 PRK08317
hypothetical protein; Provisional
89-204 7.26e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 48.78  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  89 AYALELLfdQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDPmllssgRVRLVVGDG-R 167
Cdd:PRK08317    9 ARTFELL--AVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGP------NVEFVRGDAdG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958642774 168 MGFAEEApYDAIHVGAAAPVV--PQALIDQ----LKPGGRLIL 204
Cdd:PRK08317   81 LPFPDGS-FDAVRSDRVLQHLedPARALAEiarvLRPGGRVVV 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
104-206 9.26e-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: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 104 KALDVGSGSGILTACFARmvGHSGKVIGIDhikelVDDSITNVKKDDPMLLSSGRVRLVVGDGRMG-FAEEAPYDAIHVG 182
Cdd:cd02440     1 RVLDLGCGTGALALALAS--GPGARVTGVD-----ISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISD 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958642774 183 AAAPVV---PQALIDQ----LKPGGRLILPV 206
Cdd:cd02440    74 PPLHHLvedLARFLEEarrlLKPGGVLVLTL 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
99-204 1.77e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.64  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  99 LHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDgrmgfAEEAP--- 175
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQK-----LGFDNVEFEQGD-----IEELPell 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1958642774 176 ----YD------AIHVGAAAPVVPQALIDQLKPGGRLIL 204
Cdd:pfam13847  71 eddkFDvvisncVLNHIPDPDKVLQEILRVLKPGGRLII 109
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
102-204 4.73e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 46.30  E-value: 4.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 102 GAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDdsitNVKKDDPMLLSSGRVRLVVGDgrmgfAEEAPY----- 176
Cdd:PRK00216   52 GDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLA----VGREKLRDLGLSGNVEFVQGD-----AEALPFpdnsf 122
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958642774 177 DAIHVGAAAPVVPQalIDQ--------LKPGGRL-IL 204
Cdd:PRK00216  123 DAVTIAFGLRNVPD--IDKalremyrvLKPGGRLvIL 157
arsM PRK11873
arsenite methyltransferase;
96-139 9.85e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 45.71  E-value: 9.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958642774  96 FDQLHEGAKALDVGSGSGIltACF--ARMVGHSGKVIGIDHIKELV 139
Cdd:PRK11873   72 LAELKPGETVLDLGSGGGF--DCFlaARRVGPTGKVIGVDMTPEML 115
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
91-206 1.50e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 44.40  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  91 ALELLFDQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDPMllssGRVRLVVGDGRMGF 170
Cdd:PRK00377   30 ALALSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVL----NNIVLIKGEAPEIL 105
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958642774 171 AEEAP-YDAIHVGAAA---PVVPQALIDQLKPGGRLILPV 206
Cdd:PRK00377  106 FTINEkFDRIFIGGGSeklKEIISASWEIIKKGGRIVIDA 145
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
106-204 2.33e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.88  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 106 LDVGSGSGILTACFARMVGHsgkVIGIDHIKELVDDSITNVKKDDpmllssgrVRLVVGDG-RMGFAEEApYDAIHVGAA 184
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKAPREG--------LTFVVGDAeDLPFPDNS-FDLVLSSEV 68
                          90       100
                  ....*....|....*....|....*.
gi 1958642774 185 A---PVVPQAL--IDQ-LKPGGRLIL 204
Cdd:pfam08241  69 LhhvEDPERALreIARvLKPGGILII 94
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
101-203 3.23e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 43.97  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774 101 EGAKALDVGSGSGILTACFARMVGHSGKVIGIDhikelVDDSITNVKKDDPMLLSSGRVRLVVGDGRMGFAEEAPYDAIH 180
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLD-----INENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVT 116
                          90       100
                  ....*....|....*....|....*....
gi 1958642774 181 VGAA---APVVPQALIDQ---LKPGGRLI 203
Cdd:pfam01209 117 ISFGlrnFPDYLKVLKEAfrvLKPGGRVV 145
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
92-204 8.13e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 42.83  E-value: 8.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  92 LELLFDQLHEGAKALDVGSGSGILtACFARMVGHsGKVIGIDhIKEL-VDDSITNVKKDDpmllssgrVRLVVGDGrmgf 170
Cdd:PRK00517  110 LEALEKLVLPGKTVLDVGCGSGIL-AIAAAKLGA-KKVLAVD-IDPQaVEAARENAELNG--------VELNVYLP---- 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958642774 171 AEEAPYDAIhVgA---AAPVVpqALIDQ----LKPGGRLIL 204
Cdd:PRK00517  175 QGDLKADVI-V-AnilANPLL--ELAPDlarlLKPGGRLIL 211
PRK14968 PRK14968
putative methyltransferase; Provisional
93-133 1.33e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 1.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958642774  93 ELLFDQLHE--GAKALDVGSGSGILTACFARMvghSGKVIGID 133
Cdd:PRK14968   13 FLLAENAVDkkGDRVLEVGTGSGIVAIVAAKN---GKKVVGVD 52
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
93-204 2.88e-04

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: 40.56  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  93 ELLFDQL--HEGAKALDVGSGSGILTACFARMVGHSgKVIGIDhIKEL-VDDSITNVKKDDPmllssGRVRLVVGDGRMG 169
Cdd:COG2813    39 RLLLEHLpePLGGRVLDLGCGYGVIGLALAKRNPEA-RVTLVD-VNARaVELARANAAANGL-----ENVEVLWSDGLSG 111
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958642774 170 FAEEaPYDAI------HVGAAAPV-VPQALIDQ----LKPGGRLIL 204
Cdd:COG2813   112 VPDG-SFDLIlsnppfHAGRAVDKeVAHALIADaarhLRPGGELWL 156
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
98-200 4.27e-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: 39.78  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  98 QLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDpmllSSGRVRLVVGDGR--MGFAEEAP 175
Cdd:COG4122    13 RLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAG----LADRIRLILGDALevLPRLADGP 88
                          90       100
                  ....*....|....*....|....*...
gi 1958642774 176 YDAIHVGAAAPVVP---QALIDQLKPGG 200
Cdd:COG4122    89 FDLVFIDADKSNYPdylELALPLLRPGG 116
PLN02366 PLN02366
spermidine synthase
149-200 5.29e-04

spermidine synthase


Pssm-ID: 215208 [Multi-domain]  Cd Length: 308  Bit Score: 40.40  E-value: 5.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958642774 149 DDPmllssgRVRLVVGDGR--MGFAEEAPYDAIHVGAAAPVVP-QALIDQ---------LKPGG 200
Cdd:PLN02366  143 DDP------RVNLHIGDGVefLKNAPEGTYDAIIVDSSDPVGPaQELFEKpffesvaraLRPGG 200
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
86-204 1.04e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.83  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  86 HMHAYALELLFDQlhEGAKALDVGSGSGILTACFARMVGHsgkVIGIDHIKELVDdsITNVKKDDpmllssgrVRLVVGD 165
Cdd:COG4976    33 LLAEELLARLPPG--PFGRVLDLGCGTGLLGEALRPRGYR---LTGVDLSEEMLA--KAREKGVY--------DRLLVAD 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958642774 166 GRMGFAEEAPYDAI-------HVGAAAPVVpQALIDQLKPGGRLIL 204
Cdd:COG4976    98 LADLAEPDGRFDLIvaadvltYLGDLAAVF-AGVARALKPGGLFIF 142
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
75-204 5.75e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 36.90  E-value: 5.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  75 LRSFQATISAPHMHAYALELLfdQLHEGAKALDVGSGSG---ILTAC-FARMvghsgKVIGIDHIKELVDDSITNVKKdd 150
Cdd:PRK08287    7 LRGEKVPMTKEEVRALALSKL--ELHRAKHLIDVGAGTGsvsIEAALqFPSL-----QVTAIERNPDALRLIKENRQR-- 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958642774 151 pmlLSSGRVRLVVGDGRMGFAEEApyDAIHVGAAAPVVpQALID----QLKPGGRLIL 204
Cdd:PRK08287   78 ---FGCGNIDIIPGEAPIELPGKA--DAIFIGGSGGNL-TAIIDwslaHLHPGGRLVL 129
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
96-204 7.28e-03

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: 36.41  E-value: 7.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958642774  96 FDQLHEGaKALDVGSGSGILTACFARMVGHsGKVIGIDHIKELVDDSITNVKKDDPMllssgRVRLVVGDGRMGFaEEAP 175
Cdd:pfam05175  27 LPKDLSG-KVLDLGCGAGVLGAALAKESPD-AELTMVDINARALESARENLAANGLE-----NGEVVASDVYSGV-EDGK 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958642774 176 YDAI------HVG-AAAPVVPQALI----DQLKPGGRLIL 204
Cdd:pfam05175  99 FDLIisnppfHAGlATTYNVAQRFIadakRHLRPGGELWI 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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