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Conserved domains on  [gi|226530884|ref|NP_032812|]
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protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform 2 [Mus musculus]

Protein Classification

AdoMet_MTases domain-containing protein (domain architecture ID 12014395)

AdoMet_MTases domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
66-274 2.07e-110

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


:

Pssm-ID: 250389  Cd Length: 205  Bit Score: 321.63  E-value: 2.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884   66 ASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYA----KSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKAL 141
Cdd:pfam01135   1 NRNEALIENLKNYGVIKSDKVAEAMLAVDREEFVpesfKSYAYEDIPLSIGYGQTISAPHMHAMMLELL--ELKPGMRVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  142 DVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDPMllssgRVRLVVGDGRMGYAEEAPYDAIHVGAAAP 221
Cdd:pfam01135  79 EIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE-----NVIVVVGDGRQGWPEFAPYDAIHVGAAAP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226530884  222 VVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPL 274
Cdd:pfam01135 154 EIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRFVPL 205
 
Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
66-274 2.07e-110

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


Pssm-ID: 250389  Cd Length: 205  Bit Score: 321.63  E-value: 2.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884   66 ASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYA----KSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKAL 141
Cdd:pfam01135   1 NRNEALIENLKNYGVIKSDKVAEAMLAVDREEFVpesfKSYAYEDIPLSIGYGQTISAPHMHAMMLELL--ELKPGMRVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  142 DVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDPMllssgRVRLVVGDGRMGYAEEAPYDAIHVGAAAP 221
Cdd:pfam01135  79 EIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE-----NVIVVVGDGRQGWPEFAPYDAIHVGAAAP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226530884  222 VVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPL 274
Cdd:pfam01135 154 EIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRFVPL 205
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
62-281 1.67e-71

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  Cd Length: 215  Bit Score: 222.78  E-value: 1.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884   62 KSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYA----KSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEG 137
Cdd:TIGR00080   1 MDLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVpehfKEYAYVDTPLEIGYGQTISAPHMVAMMTELL--ELKPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  138 AKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVG 217
Cdd:TIGR00080  79 MKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLDNVIVIVGDGTQGWEPLAPYDRIYVT 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226530884  218 AAAPVVPQALIDQLKPGGRLILPVGPagGNQMLEQYDKlQDGSVKMKPLMGVIYVPLTDKEKQW 281
Cdd:TIGR00080 154 AAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK-RGGEIIIKDVEPVAFVPLVGGEGFQ 214
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
75-278 7.11e-56

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


Pssm-ID: 225316  Cd Length: 209  Bit Score: 182.06  E-value: 7.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  75 LRKNGIIKtDKVFEVMLATDR--------SHYAksnpYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKALDVGSG 146
Cdd:COG2518   10 LRTEGITD-ERVLKAFLAVPRelfvpaayKHLA----YEDRALPIGCGQTISAPHMVARMLQLL--ELKPGDRVLEIGTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 147 SGILTACFARMVGnsgKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQA 226
Cdd:COG2518   83 SGYQAAVLARLVG---RVVSIERIEELAEQARRNLET-----LGYENVTVRHGDGSKGWPEEAPYDRIIVTAAAPEVPEA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226530884 227 LIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLTDKE 278
Cdd:COG2518  155 LLDQLKPGGRLVIPVGS-GPAQRLLRITKDGDGNFERRDLFNVRFVPLVGGD 205
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
70-278 1.05e-52

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 174.05  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  70 ELIHNLRKNGIIKTDKVFEVMLATDR----SHYAKSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKALDVGS 145
Cdd:PRK13942   8 RVIEELIREGYIKSKKVIDALLKVPRhlfvPEYLEEYAYVDTPLEIGYGQTISAIHMVAIMCELL--DLKEGMKVLEIGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 146 GSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQ 225
Cdd:PRK13942  86 GSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK-----LGYDNVEVIVGDGTLGYEENAPYDRIYVTAAGPDIPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226530884 226 ALIDQLKPGGRLILPVGPAggNQMLEQYDKlQDGSVKMKPLMGVIYVPLTDKE 278
Cdd:PRK13942 161 PLIEQLKDGGIMVIPVGSY--SQELIRVEK-DNGKIIKKKLGEVAFVPLIGKN 210
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
139-241 1.25e-06

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  Cd Length: 107  Bit Score: 46.27  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 139 KALDVGSGSGILTACFARmvGNSGKVIGIDhikelVDDSITNVKKDDPMLLSSGRVRLVVGDGRMG-YAEEAPYDAIHVG 217
Cdd:cd02440    1 RVLDLGCGTGALALALAS--GPGARVTGVD-----ISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISD 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 226530884 218 AAAPVV---PQALIDQ----LKPGGRLILPV 241
Cdd:cd02440   74 PPLHHLvedLARFLEEarrlLKPGGVLVLTL 104
 
Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
66-274 2.07e-110

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


Pssm-ID: 250389  Cd Length: 205  Bit Score: 321.63  E-value: 2.07e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884   66 ASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYA----KSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKAL 141
Cdd:pfam01135   1 NRNEALIENLKNYGVIKSDKVAEAMLAVDREEFVpesfKSYAYEDIPLSIGYGQTISAPHMHAMMLELL--ELKPGMRVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  142 DVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDPMllssgRVRLVVGDGRMGYAEEAPYDAIHVGAAAP 221
Cdd:pfam01135  79 EIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLE-----NVIVVVGDGRQGWPEFAPYDAIHVGAAAP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 226530884  222 VVPQALIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPL 274
Cdd:pfam01135 154 EIPEALIDQLKEGGRLVIPVGP-NGNQVLQQFDKRNDGSVVIKDLEGVRFVPL 205
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
62-281 1.67e-71

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  Cd Length: 215  Bit Score: 222.78  E-value: 1.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884   62 KSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYA----KSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEG 137
Cdd:TIGR00080   1 MDLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVpehfKEYAYVDTPLEIGYGQTISAPHMVAMMTELL--ELKPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  138 AKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVG 217
Cdd:TIGR00080  79 MKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLDNVIVIVGDGTQGWEPLAPYDRIYVT 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226530884  218 AAAPVVPQALIDQLKPGGRLILPVGPagGNQMLEQYDKlQDGSVKMKPLMGVIYVPLTDKEKQW 281
Cdd:TIGR00080 154 AAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK-RGGEIIIKDVEPVAFVPLVGGEGFQ 214
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
75-278 7.11e-56

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


Pssm-ID: 225316  Cd Length: 209  Bit Score: 182.06  E-value: 7.11e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  75 LRKNGIIKtDKVFEVMLATDR--------SHYAksnpYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKALDVGSG 146
Cdd:COG2518   10 LRTEGITD-ERVLKAFLAVPRelfvpaayKHLA----YEDRALPIGCGQTISAPHMVARMLQLL--ELKPGDRVLEIGTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 147 SGILTACFARMVGnsgKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQA 226
Cdd:COG2518   83 SGYQAAVLARLVG---RVVSIERIEELAEQARRNLET-----LGYENVTVRHGDGSKGWPEEAPYDRIIVTAAAPEVPEA 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 226530884 227 LIDQLKPGGRLILPVGPaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLTDKE 278
Cdd:COG2518  155 LLDQLKPGGRLVIPVGS-GPAQRLLRITKDGDGNFERRDLFNVRFVPLVGGD 205
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
70-278 1.05e-52

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 174.05  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  70 ELIHNLRKNGIIKTDKVFEVMLATDR----SHYAKSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKALDVGS 145
Cdd:PRK13942   8 RVIEELIREGYIKSKKVIDALLKVPRhlfvPEYLEEYAYVDTPLEIGYGQTISAIHMVAIMCELL--DLKEGMKVLEIGT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 146 GSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQ 225
Cdd:PRK13942  86 GSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKK-----LGYDNVEVIVGDGTLGYEENAPYDRIYVTAAGPDIPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 226530884 226 ALIDQLKPGGRLILPVGPAggNQMLEQYDKlQDGSVKMKPLMGVIYVPLTDKE 278
Cdd:PRK13942 161 PLIEQLKDGGIMVIPVGSY--SQELIRVEK-DNGKIIKKKLGEVAFVPLIGKN 210
pcm PRK00312
protein-L-isoaspartate O-methyltransferase; Reviewed
71-278 3.26e-44

protein-L-isoaspartate O-methyltransferase; Reviewed


Pssm-ID: 178974  Cd Length: 212  Bit Score: 151.90  E-value: 3.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  71 LIHNLRKNGIiKTDKVFEVMLATDRS--------HYAksnpYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKALD 142
Cdd:PRK00312  12 LVLRLRAEGI-LDERVLEAIEATPRElfvpeafkHKA----YENRALPIGCGQTISQPYMVARMTELL--ELKPGDRVLE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 143 VGSGSGILTACFARMVGnsgKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPV 222
Cdd:PRK00312  85 IGTGSGYQAAVLAHLVR---RVFSVERIKTLQWEAKRRLKQ-----LGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPE 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226530884 223 VPQALIDQLKPGGRLILPVGpaGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLTDKE 278
Cdd:PRK00312 157 IPRALLEQLKEGGILVAPVG--GEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGE 210
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
71-274 4.73e-32

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 119.53  E-value: 4.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  71 LIHNLRKNGIIKTDKVFEVMLATDRSHYA----KSNPYMDSPQSIGFQATISAPHMHAYALELLfdQLHEGAKALDVGSG 146
Cdd:PRK13944   5 LVEELVREGIIKSERVKKAMLSVPREEFVmpeyRMMAYEDRPLPLFAGATISAPHMVAMMCELI--EPRPGMKILEVGTG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 147 SGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmLLSSGRVRLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQA 226
Cdd:PRK13944  83 SGYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIER----LGYWGVVEVYHGDGKRGLEKHAPFDAIIVTAAASTIPSA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 226530884 227 LIDQLKPGGRLILPVGPAGGnQMLEQYDKLQDGsVKMKPLMGVIYVPL 274
Cdd:PRK13944 159 LVRQLKDGGVLVIPVEEGVG-QVLYKVVKRGEK-VEKRAITYVLFVPL 204
methyltran_FxLD TIGR04364
methyltransferase, FxLD system; Members of this family resemble occur regularly in the ...
69-241 5.42e-21

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: 91.27  E-value: 5.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884   69 SELIHNLRKNGIIKTDKVFEVMLATDRSHYAKSNP----YM----------DSPQSIgfqATISAPHMHAYALELLfdQL 134
Cdd:TIGR04364   6 AALVDELREDGVIRSPRVEAAFRTVPRHLFAPGAPlekaYAanravvtkrdEDGRAL---SSVSAPHIQAMMLEQA--GV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  135 HEGAKALDVGSGsGILTACFARMVGNSGKVIGIDHIKELVDdsitnvkKDDPMLLSSG--RVRLVVGDGRMGYAEEAPYD 212
Cdd:TIGR04364  81 EPGMRVLEIGSG-GYNAALLAELVGPSGEVTTVDIDEDVTD-------RARACLAAAGypQVTVVLADAEAGVPELAPYD 152
                         170       180
                  ....*....|....*....|....*....
gi 226530884  213 AIHVGAAAPVVPQALIDQLKPGGRLILPV 241
Cdd:TIGR04364 153 RIIVTVGAWDIPPAWLDQLAPGGRLVVPL 181
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
64-241 1.52e-19

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568  Cd Length: 322  Bit Score: 86.44  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  64 GGASHSELIHNLRKNGIikTDKVFEVMLATDRS-----HYAKSNPYMD----SPQSIGFQATISAPHMHAYALELLfdQL 134
Cdd:PRK13943   3 EFFMREKLFWILKKYGI--SDHIAKAFLEVPREefltkSYPLSYVYEDivlvSYDDGEEYSTSSQPSLMALFMEWV--GL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 135 HEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRMGYAEEAPYDAI 214
Cdd:PRK13943  79 DKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRR-----LGIENVIFVCGDGYYGVPEFAPYDVI 153
                        170       180
                 ....*....|....*....|....*..
gi 226530884 215 HVGAAAPVVPQALIDQLKPGGRLILPV 241
Cdd:PRK13943 154 FVTVGVDEVPETWFTQLKEGGRVIVPI 180
methyltr_grsp TIGR04188
methyltransferase, ATP-grasp peptide maturase system; Members of this protein family are ...
134-246 1.52e-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: 60.84  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  134 LHEGAKALDVGSGSGILTACFARMVGnsgkvigidhikelvDDSITNVKKDdPMLLSSGRVRL---------VVGDGRMG 204
Cdd:TIGR04188 105 VEDGHRVLEIGTGTGYSAALLCHRLG---------------DDNVTSVEVD-PGLAARAASALaaagyaptvVTGDGLLG 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 226530884  205 YAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVG---PAGG 246
Cdd:TIGR04188 169 HPPRAPYDRIIATCAVRRVPPAWLRQTRPGGVILTTLSgwlYGGG 213
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism];
117-239 1.66e-09

Precorrin-6B methylase 2 [Coenzyme transport and metabolism];


Pssm-ID: 225151  Cd Length: 187  Bit Score: 56.10  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 117 ISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTaCFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRL 196
Cdd:COG2242   17 MTKEEIRALTLSKL--RPRPGDRLWDIGAGTGSIT-IEWALAGPSGRVIAIERDEEALELIERNAAR-----FGVDNLEV 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 226530884 197 VVGDGRMGYAEEAPYDAIHVGAAAPV--VPQALIDQLKPGGRLIL 239
Cdd:COG2242   89 VEGDAPEALPDLPSPDAIFIGGGGNIeeILEAAWERLKPGGRLVA 133
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis];
134-238 4.63e-08

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 225317  Cd Length: 256  Bit Score: 52.68  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 134 LHEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmLLSSGRVRLVVGDGRmGYAEEAPYDA 213
Cdd:COG2519   92 ISPGSRVLEAGTGSGALTAYLARAVGPEGHVTTYEIREDFAKTARENLSE----FGLGDRVTLKLGDVR-EGIDEEDVDA 166
                         90       100
                 ....*....|....*....|....*.
gi 226530884 214 IHVGAAAPV-VPQALIDQLKPGGRLI 238
Cdd:COG2519  167 VFLDLPDPWnVLEHVSDALKPGGVVV 192
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
141-235 5.73e-08

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


Pssm-ID: 316196  Cd Length: 96  Bit Score: 50.26  E-value: 5.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  141 LDVGSGSGILTACFARMVGnsGKVIGIDHIKELVDDSITNVKKDDPmllssgRVRLVVGDGRMGYAEEAPYDAIHVGAAA 220
Cdd:pfam13649   2 LDLGCGTGRLALALARRGG--ARVTGVDLSPEMLERARERAAEAGL------NVEFVQGDAEDLPFPDGSFDLVVSSGVL 73
                          90       100
                  ....*....|....*....|...
gi 226530884  221 PVVPQALIDQ--------LKPGG 235
Cdd:pfam13649  74 HHLPDPDLEAalreiarvLKPGG 96
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
117-241 1.75e-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  Cd Length: 124  Bit Score: 49.25  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  117 ISAPHMHAYALELLfdQLHEGAKALDVGSGSGILTACFARMVGNsGKVIGIDHIKELVDdsitnvkkddpmLLSSGRVRL 196
Cdd:TIGR02469   2 MTKREVRALTLAKL--RLRPGDVLWDIGAGTGSVTIEAARLVPN-GRVYAIERNPEALD------------LIERNLRRF 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 226530884  197 VVGDGR--MGYAEEAPY------DAIHVGAAA---PVVPQALIDQLKPGGRLILPV 241
Cdd:TIGR02469  67 GVSNIVivEGDAPEAPEallpdpDAVFVGGSGgllQEILEAVERRLRPGGRIVLNA 122
PRK08317 PRK08317
hypothetical protein; Provisional
124-239 2.87e-07

hypothetical protein; Provisional


Pssm-ID: 181382  Cd Length: 241  Bit Score: 50.32  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 124 AYALELLfdQLHEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDPmllssgRVRLVVGDG-R 202
Cdd:PRK08317   9 ARTFELL--AVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGP------NVEFVRGDAdG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 226530884 203 MGYAEEApYDAI-------HVGAaapvvPQALIDQ----LKPGGRLIL 239
Cdd:PRK08317  81 LPFPDGS-FDAVrsdrvlqHLED-----PARALAEiarvLRPGGRVVV 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
134-239 3.65e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 316372  Cd Length: 150  Bit Score: 48.57  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  134 LHEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDgrmgyAEEAP--- 210
Cdd:pfam13847   1 LKKGLRVLDLGCGTGYLTFELAEELGPNAEVVGIDISEEAIEKARENAQK-----LGFDNVEFEQGD-----IEELPell 70
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226530884  211 ----YD------AIHVGAAAPVVPQALIDQLKPGGRLIL 239
Cdd:pfam13847  71 eddsFDviisncVLNLIADPDKVLEEILRVLKPGGRLLI 109
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
136-277 1.03e-06

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 48.44  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  136 EGAKALDVGSGSGILTACFARMVGNsgkVIGIDHIKELVDDSiTNVKKDDPMLLSSgrvrlvvgdgRMGYAEEAP----- 210
Cdd:TIGR01983  46 DGLRVLDVGCGGGLLSEPLARLGAN---VTGIDASEENIEVA-KLHAKKDPLQIDY----------RCTTVEDLAekkag 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  211 -YDAI-------HVgAAAPVVPQALIDQLKPGGRL------------------------ILPVG---------PAggnqm 249
Cdd:TIGR01983 112 sFDVVtcmevleHV-PDPQAFIRACAQLLKPGGILffstinrtpksyllaivgaeyilrIVPKGthdwekfikPS----- 185
                         170       180
                  ....*....|....*....|....*...
gi 226530884  250 lEQYDKLQDGSVKMKPLMGVIYVPLTDK 277
Cdd:TIGR01983 186 -ELLSWLESAGLRVKDIKGLVYNPIKNT 212
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
139-241 1.25e-06

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  Cd Length: 107  Bit Score: 46.27  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 139 KALDVGSGSGILTACFARmvGNSGKVIGIDhikelVDDSITNVKKDDPMLLSSGRVRLVVGDGRMG-YAEEAPYDAIHVG 217
Cdd:cd02440    1 RVLDLGCGTGALALALAS--GPGARVTGVD-----ISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISD 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 226530884 218 AAAPVV---PQALIDQ----LKPGGRLILPV 241
Cdd:cd02440   74 PPLHHLvedLARFLEEarrlLKPGGVLVLTL 104
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
124-239 1.97e-06

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


Pssm-ID: 225173  Cd Length: 300  Bit Score: 48.07  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 124 AYALELLFDQLHEGAKALDVGSGSGILtACFARMVGnSGKVIGIDhIKEL-VDDSITNVKKDDPMLlssgRVRLVVGDGR 202
Cdd:COG2264  150 SLCLEALEKLLKKGKTVLDVGCGSGIL-AIAAAKLG-AKKVVGVD-IDPQaVEAARENARLNGVEL----LVQAKGFLLL 222
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 226530884 203 MGyAEEAPYDAIhVgA---AAPVV---PQALIdQLKPGGRLIL 239
Cdd:COG2264  223 EV-PENGPFDVI-V-AnilAEVLVelaPDIKR-LLKPGGRLIL 261
ubiE PRK00216
ubiquinone/menaquinone biosynthesis methyltransferase; Reviewed
137-239 4.32e-06

ubiquinone/menaquinone biosynthesis methyltransferase; Reviewed


Pssm-ID: 234689  Cd Length: 239  Bit Score: 46.68  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 137 GAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDdsitNVKKDDPMLLSSGRVRLVVGDgrmgyAEEAPY----- 211
Cdd:PRK00216  52 GDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLA----VGREKLRDLGLSGNVEFVQGD-----AEALPFpdnsf 122
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226530884 212 DAIHVGAAAPVVPQalIDQ--------LKPGGRL-IL 239
Cdd:PRK00216 123 DAVTIAFGLRNVPD--IDKalremyrvLKPGGRLvIL 157
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
126-241 1.23e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 44.79  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 126 ALELLFDQLHEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDPMllssGRVRLVVGDGRMGY 205
Cdd:PRK00377  30 ALALSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVL----NNIVLIKGEAPEIL 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226530884 206 AEEAP-YDAIHVGAAA---PVVPQALIDQLKPGGRLILPV 241
Cdd:PRK00377 106 FTINEkFDRIFIGGGSeklKEIISASWEIIKKGGRIVIDA 145
arsM PRK11873
arsenite S-adenosylmethyltransferase; Reviewed
131-174 1.44e-05

arsenite S-adenosylmethyltransferase; Reviewed


Pssm-ID: 237007  Cd Length: 272  Bit Score: 45.32  E-value: 1.44e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 226530884 131 FDQLHEGAKALDVGSGSGIltACF--ARMVGNSGKVIGIDHIKELV 174
Cdd:PRK11873  72 LAELKPGETVLDLGSGGGF--DCFlaARRVGPTGKVIGVDMTPEML 115
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
141-239 1.51e-05

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


Pssm-ID: 311935  Cd Length: 96  Bit Score: 43.07  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  141 LDVGSGSGILTACFARMVGNsgkVIGIDHIKELVDDSITNVKKDDPMllssgrVRLVVGDG-RMGYAEEApYDAIHVGAA 219
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKAPRAGLT------IEFVVGDAeDLPFPDNS-FDLVLSSEV 70
                          90       100
                  ....*....|....*....|....*.
gi 226530884  220 A---PVVPQAL--IDQ-LKPGGRLIL 239
Cdd:pfam08241  71 LhhvEDPERALreIARvLKPGGILII 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];
133-238 2.76e-05

Ubiquinone/menaquinone biosynthesis C-methylase UbiE [Coenzyme transport and metabolism];


Pssm-ID: 225136  Cd Length: 238  Bit Score: 44.18  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 133 QLHEGAKALDVGSGSGILTACFARMVGNsGKVIGIDHIKELVDdsiTNVKKDDPmlLSSGRVRLVVGDgrmgyAEEAPY- 211
Cdd:COG2226   48 GIKPGDKVLDVACGTGDMALLLAKSVGT-GEVVGLDISESMLE---VAREKLKK--KGVQNVEFVVGD-----AENLPFp 116
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 226530884 212 ----DAIHVGAAAPVVPQalIDQ--------LKPGGRLI 238
Cdd:COG2226  117 dnsfDAVTISFGLRNVTD--IDKalkemyrvLKPGGRLL 153
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
136-238 3.06e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 279542  Cd Length: 228  Bit Score: 43.97  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  136 EGAKALDVGSGSGILTACFARMVGNSGKVIGIDhikelVDDSITNVKKDDPMLLSSGRVRLVVGDGRMGYAEEAPYDAIH 215
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLD-----INENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVT 116
                          90       100
                  ....*....|....*....|....*....
gi 226530884  216 VGAA---APVVPQALIDQ---LKPGGRLI 238
Cdd:pfam01209 117 ISFGlrnFPDYLKVLKEAfrvLKPGGRVV 145
prmA PRK00517
ribosomal protein L11 methyltransferase; Reviewed
127-239 4.29e-05

ribosomal protein L11 methyltransferase; Reviewed


Pssm-ID: 234786  Cd Length: 250  Bit Score: 43.60  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 127 LELLFDQLHEGAKALDVGSGSGILtACFARMVGNsGKVIGIDhIKEL-VDDSITNVKKDDpmllssgrVRLVVGDGrmgy 205
Cdd:PRK00517 110 LEALEKLVLPGKTVLDVGCGSGIL-AIAAAKLGA-KKVLAVD-IDPQaVEAARENAELNG--------VELNVYLP---- 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226530884 206 AEEAPYDAIhVgA---AAPVVpqALIDQ----LKPGGRLIL 239
Cdd:PRK00517 175 QGDLKADVI-V-AnilANPLL--ELAPDlarlLKPGGRLIL 211
PRK14968 PRK14968
putative methyltransferase; Provisional
128-168 1.10e-04

putative methyltransferase; Provisional


Pssm-ID: 237872  Cd Length: 188  Bit Score: 41.81  E-value: 1.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 226530884 128 ELLFDQLHE--GAKALDVGSGSGILTACFARmvgNSGKVIGID 168
Cdd:PRK14968  13 FLLAENAVDkkGDRVLEVGTGSGIVAIVAAK---NGKKVVGVD 52
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
90-239 1.24e-04

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


Pssm-ID: 223574  Cd Length: 257  Bit Score: 42.58  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  90 MLATDRSHYAKSNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAK-ALDVGSGSGILTAcFARMVGNSGKVIGID 168
Cdd:COG0500    1 DSLLSAELLSRILELYDRLAELLDAFLLLAEELLDLLLVLRLLRLLPGGLgVLDIGCGTGRLAL-LARLGGRGAYVVGVD 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226530884 169 HIKELVDDSITNVKKDDpmllsSGRVRLVVGD---GRMGYAEEAPYDAIHVGAAAPVVPQA-----LIDQLKPGGRLIL 239
Cdd:COG0500   80 LSPEMLALARARAEGAG-----LGLVDFVVADalgGVLPFEDSASFDLVISLLVLHLLPPAkalreLLRVLKPGGRLVL 153
MenG_heptapren TIGR02752
demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that ...
136-238 3.52e-04

demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that catalyzes the last step in menaquinone biosynthesis; the exact enzymatic activity differs for different MenG because the menaquinone differ in their prenoid side chains in different species. Members of this MenG protein family are 2-heptaprenyl-1,4-naphthoquinone methyltransferase, and are found together in operons with the two subunits of the heptaprenyl diphosphate synthase in Bacillus subtilis and related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131799  Cd Length: 231  Bit Score: 40.94  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  136 EGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVddSITNVKKDDPMLlssGRVRLVVGDgrmgyAEEAPY---- 211
Cdd:TIGR02752  45 AGTSALDVCCGTADWSIALAEAVGPEGHVIGLDFSENML--SVGRQKVKDAGL---HNVELVHGN-----AMELPFddns 114
                          90       100       110
                  ....*....|....*....|....*....|....
gi 226530884  212 -DAIHVGAAAPVVP------QALIDQLKPGGRLI 238
Cdd:TIGR02752 115 fDYVTIGFGLRNVPdymqvlREMYRVVKPGGKVV 148
PLN02366 PLN02366
spermidine synthase
184-235 3.87e-04

spermidine synthase


Pssm-ID: 215208  Cd Length: 308  Bit Score: 41.17  E-value: 3.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226530884 184 DDPmllssgRVRLVVGDGR--MGYAEEAPYDAIHVGAAAPVVP-QALIDQ---------LKPGG 235
Cdd:PLN02366 143 DDP------RVNLHIGDGVefLKNAPEGTYDAIIVDSSDPVGPaQELFEKpffesvaraLRPGG 200
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
112-214 4.27e-04

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930  Cd Length: 219  Bit Score: 40.55  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  112 GFQATISAPH--MHAYALELLFDQLHEGAKALDVGSGSGILTACFARmvgNSGKVIGIDHIKELVddSITNvkKDDPMLL 189
Cdd:TIGR02021  29 RVRQTVREGRaaMRRKLLDWLPKDPLKGKRVLDAGCGTGLLSIELAK---RGAIVKAVDISEQMV--QMAR--NRAQGRD 101
                          90       100
                  ....*....|....*....|....*
gi 226530884  190 SSGRVRLVVGDGRmgyAEEAPYDAI 214
Cdd:TIGR02021 102 VAGNVEFEVNDLL---SLCGEFDIV 123
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
133-237 5.01e-04

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884  Cd Length: 223  Bit Score: 40.32  E-value: 5.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  133 QLHEGAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDdsiTNVKKDDPMLlssgRVRLVVGDgrmgyAEEAP-- 210
Cdd:TIGR01934  36 GVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLE---VAKKKSELPL----NIEFIQAD-----AEALPfe 103
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 226530884  211 ---YDAIHVGAA---APVVPQAL---IDQLKPGGRL 237
Cdd:TIGR01934 104 dnsFDAVTIAFGlrnVTDIQKALremYRVLKPGGRL 139
YrrM COG4122
Predicted O-methyltransferase YrrM [General function prediction only];
137-239 1.51e-03

Predicted O-methyltransferase YrrM [General function prediction only];


Pssm-ID: 226607  Cd Length: 219  Bit Score: 38.84  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 137 GAKALDVGSGSGILTACFARMVGNSGKVIGIDHIKELVDDSITNVKKDDpmlLSSGRVRLVVGDGRMGYAEEA--PYDAI 214
Cdd:COG4122   60 PKRILEIGTAIGYSALWMALALPDDGRLTTIERDEERAEIARENLAEAG---VDDRIELLLGGDALDVLSRLLdgSFDLV 136
                         90       100
                 ....*....|....*....|....*...
gi 226530884 215 HVGAAAPVVPQAL---IDQLKPGGRLIL 239
Cdd:COG4122  137 FIDADKADYPEYLeraLPLLRPGGLIVA 164
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
127-241 1.93e-03

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: 307718  Cd Length: 178  Bit Score: 38.33  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  127 LELL--FDQLHEGAKALDVGSGSGILTACFARMVGNsGKVIGID--HIKELVDDSI-----TNVKKDDP----MLLSSGR 193
Cdd:pfam01728  10 LEIDekFGLLKPGKTVLDLGAAPGGWSQVALQRVGA-GKVVGVDlgPMQKPRNDPGvtfiqGDIRDPETldllEELLGRK 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 226530884  194 VRLVVGDGR--MGYAEEAPydaiHVGAAAPVVPQALI--DQLKPGGRLILPV 241
Cdd:pfam01728  89 VDLVLSDGSpnISGNKVLD----HLRSLDLVKAALEValEVLRKGGNFVCKV 136
PRK08287 PRK08287
cobalt-precorrin-6Y C(15)-methyltransferase; Validated
124-239 4.99e-03

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 36.90  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884 124 AYALELLfdQLHEGAKALDVGSGSGILTACFARMVGNSgKVIGIDHIKELVDDSITNVKKddpmlLSSGRVRLVVGDGRM 203
Cdd:PRK08287  21 ALALSKL--ELHRAKHLIDVGAGTGSVSIEAALQFPSL-QVTAIERNPDALRLIKENRQR-----FGCGNIDIIPGEAPI 92
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 226530884 204 GYAEEApyDAIHVGAAAPVVpQALID----QLKPGGRLIL 239
Cdd:PRK08287  93 ELPGKA--DAIFIGGSGGNL-TAIIDwslaHLHPGGRLVL 129
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
127-239 9.76e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 283886  Cd Length: 295  Bit Score: 36.85  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226530884  127 LELLFDQLHEGAKALDVGSGSGILtACFARMVGnSGKVIGIDhIKEL-VDDSITNVKkddpmlLSSGRVRLVV---GDGr 202
Cdd:pfam06325 152 LEALEQLVKPGETVLDVGCGSGIL-AIAALKLG-AKKVVGVD-IDPVaVRAAKENAE------LNGVEARLEVylpGDL- 221
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 226530884  203 mgyAEEAPYDAIhVG--AAAPVVpqALIDQ----LKPGGRLIL 239
Cdd:pfam06325 222 ---PKEEKADVV-VAniLADPLI--ELAPDiyalVKPGGYLIL 258
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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