|
Name |
Accession |
Description |
Interval |
E-value |
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
8-200 |
1.15e-97 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 281.95 E-value: 1.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 8 ANNEDLIRQLKDHGVIASDAVAQAMKETDRKHYSPR----NPYMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPGARIL 83
Cdd:pfam01135 1 NRNEALIENLKNYGVIKSDKVAEAMLAVDREEFVPEsfksYAYEDIPLSIGYGQTISAPHMHAMMLELLE--LKPGMRVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 84 DVGSGSGYLTACFYRYIKAKGvdadtRIVGIEHQAELVRRSKANLNTDDRSmldsgQLLIVEGDGRKGYPPNAPYNAIHV 163
Cdd:pfam01135 79 EIGSGSGYLTACFARMVGEVG-----RVVSIEHIPELVEIARRNLEKLGLE-----NVIVVVGDGRQGWPEFAPYDAIHV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 442617574 164 GAAAPDTPTELINQLASGGRLIVPVGPdGGSQYMQQV 200
Cdd:pfam01135 149 GAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQF 184
|
|
| pimt |
TIGR00080 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ... |
4-202 |
7.49e-59 |
|
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: 183.87 E-value: 7.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 4 RSVGANNEDLIRQLKDHGVIASDAVAQAMKETDRKHYSPRN----PYMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPG 79
Cdd:TIGR00080 1 MDLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVPEHfkeyAYVDTPLEIGYGQTISAPHMVAMMTELLE--LKPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 80 ARILDVGSGSGYLTACFyryikAKGVDADTRIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYN 159
Cdd:TIGR00080 79 MKVLEIGTGSGYQAAVL-----AEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLDNVIVIVGDGTQGWEPLAPYD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442617574 160 AIHVGAAAPDTPTELINQLASGGRLIVPVGPdgGSQYMQQVGR 202
Cdd:TIGR00080 149 RIYVTAAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK 189
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
14-200 |
3.86e-46 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 150.62 E-value: 3.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 14 IRQLKDHGvIASDAVAQAMKETDRKHYSPRNP----YMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPGARILDVGSGS 89
Cdd:COG2518 1 VQQLRPRG-VTDPRVLDAMRAVPRELFVPEALrelaYADRALPIGHGQTISQPYIVARMLEALD--LKPGDRVLEIGTGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 90 GYLTACFyryikAKGVDadtRIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYNAIHVGAAAPD 169
Cdd:COG2518 78 GYQAAVL-----ARLAG---RVYSVERDPELAERARERLAA-----LGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPE 144
|
170 180 190
....*....|....*....|....*....|.
gi 442617574 170 TPTELINQLASGGRLIVPVGpDGGSQYMQQV 200
Cdd:COG2518 145 VPEALLEQLAPGGRLVAPVG-EGGVQRLVLI 174
|
|
| pcm |
PRK00312 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; |
13-202 |
4.22e-43 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
Pssm-ID: 178974 [Multi-domain] Cd Length: 212 Bit Score: 143.42 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 13 LIRQLKDHGvIASDAVAQAMKETDR--------KHYSprnpYMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPGARILD 84
Cdd:PRK00312 12 LVLRLRAEG-ILDERVLEAIEATPRelfvpeafKHKA----YENRALPIGCGQTISQPYMVARMTELLE--LKPGDRVLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 85 VGSGSGYLTAcfyryIKAKGVDadtRIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYNAIHVG 164
Cdd:PRK00312 85 IGTGSGYQAA-----VLAHLVR---RVFSVERIKTLQWEAKRRLKQ-----LGLHNVSVRHGDGWKGWPAYAPFDRILVT 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 442617574 165 AAAPDTPTELINQLASGGRLIVPVGpDGGSQYMQQVGR 202
Cdd:PRK00312 152 AAAPEIPRALLEQLKEGGILVAPVG-GEEQQLLTRVRK 188
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
81-188 |
3.65e-03 |
|
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: 35.87 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 81 RILDVGSGSGYLTACFYRYIKAK--GVDADtrivgiEHQAELVRRSKANLNTDDRSmldsgqllIVEGDGRKG-YPPNAP 157
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARvtGVDIS------PVALELARKAAAALLADNVE--------VLKGDAEELpPEADES 66
|
90 100 110
....*....|....*....|....*....|....*...
gi 442617574 158 YNAIHVGAAAPDTPT-------ELINQLASGGRLIVPV 188
Cdd:cd02440 67 FDVIISDPPLHHLVEdlarfleEARRLLKPGGVLVLTL 104
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PCMT |
pfam01135 |
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT); |
8-200 |
1.15e-97 |
|
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
Pssm-ID: 395902 [Multi-domain] Cd Length: 205 Bit Score: 281.95 E-value: 1.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 8 ANNEDLIRQLKDHGVIASDAVAQAMKETDRKHYSPR----NPYMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPGARIL 83
Cdd:pfam01135 1 NRNEALIENLKNYGVIKSDKVAEAMLAVDREEFVPEsfksYAYEDIPLSIGYGQTISAPHMHAMMLELLE--LKPGMRVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 84 DVGSGSGYLTACFYRYIKAKGvdadtRIVGIEHQAELVRRSKANLNTDDRSmldsgQLLIVEGDGRKGYPPNAPYNAIHV 163
Cdd:pfam01135 79 EIGSGSGYLTACFARMVGEVG-----RVVSIEHIPELVEIARRNLEKLGLE-----NVIVVVGDGRQGWPEFAPYDAIHV 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 442617574 164 GAAAPDTPTELINQLASGGRLIVPVGPdGGSQYMQQV 200
Cdd:pfam01135 149 GAAAPEIPEALIDQLKEGGRLVIPVGP-NGNQVLQQF 184
|
|
| pimt |
TIGR00080 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ... |
4-202 |
7.49e-59 |
|
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: 183.87 E-value: 7.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 4 RSVGANNEDLIRQLKDHGVIASDAVAQAMKETDRKHYSPRN----PYMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPG 79
Cdd:TIGR00080 1 MDLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVPEHfkeyAYVDTPLEIGYGQTISAPHMVAMMTELLE--LKPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 80 ARILDVGSGSGYLTACFyryikAKGVDADTRIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYN 159
Cdd:TIGR00080 79 MKVLEIGTGSGYQAAVL-----AEIVGRDGLVVSIERIPELAEKAERRLRK-----LGLDNVIVIVGDGTQGWEPLAPYD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442617574 160 AIHVGAAAPDTPTELINQLASGGRLIVPVGPdgGSQYMQQVGR 202
Cdd:TIGR00080 149 RIYVTAAGPKIPEALIDQLKEGGILVMPVGE--YLQVLKRAEK 189
|
|
| Pcm |
COG2518 |
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ... |
14-200 |
3.86e-46 |
|
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442008 [Multi-domain] Cd Length: 197 Bit Score: 150.62 E-value: 3.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 14 IRQLKDHGvIASDAVAQAMKETDRKHYSPRNP----YMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPGARILDVGSGS 89
Cdd:COG2518 1 VQQLRPRG-VTDPRVLDAMRAVPRELFVPEALrelaYADRALPIGHGQTISQPYIVARMLEALD--LKPGDRVLEIGTGS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 90 GYLTACFyryikAKGVDadtRIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYNAIHVGAAAPD 169
Cdd:COG2518 78 GYQAAVL-----ARLAG---RVYSVERDPELAERARERLAA-----LGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPE 144
|
170 180 190
....*....|....*....|....*....|.
gi 442617574 170 TPTELINQLASGGRLIVPVGpDGGSQYMQQV 200
Cdd:COG2518 145 VPEALLEQLAPGGRLVAPVG-EGGVQRLVLI 174
|
|
| pcm |
PRK00312 |
protein-L-isoaspartate(D-aspartate) O-methyltransferase; |
13-202 |
4.22e-43 |
|
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
Pssm-ID: 178974 [Multi-domain] Cd Length: 212 Bit Score: 143.42 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 13 LIRQLKDHGvIASDAVAQAMKETDR--------KHYSprnpYMDAPQPIGGGVTISAPHMHAFALEYLRdhLKPGARILD 84
Cdd:PRK00312 12 LVLRLRAEG-ILDERVLEAIEATPRelfvpeafKHKA----YENRALPIGCGQTISQPYMVARMTELLE--LKPGDRVLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 85 VGSGSGYLTAcfyryIKAKGVDadtRIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYNAIHVG 164
Cdd:PRK00312 85 IGTGSGYQAA-----VLAHLVR---RVFSVERIKTLQWEAKRRLKQ-----LGLHNVSVRHGDGWKGWPAYAPFDRILVT 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 442617574 165 AAAPDTPTELINQLASGGRLIVPVGpDGGSQYMQQVGR 202
Cdd:PRK00312 152 AAAPEIPRALLEQLKEGGILVAPVG-GEEQQLLTRVRK 188
|
|
| PRK13942 |
PRK13942 |
protein-L-isoaspartate O-methyltransferase; Provisional |
13-198 |
2.82e-40 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 184409 Cd Length: 212 Bit Score: 136.30 E-value: 2.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 13 LIRQLKDHGVIASDAVAQAMKETDRKHYSP----RNPYMDAPQPIGGGVTISAPHMHAFALEYLrdHLKPGARILDVGSG 88
Cdd:PRK13942 9 VIEELIREGYIKSKKVIDALLKVPRHLFVPeyleEYAYVDTPLEIGYGQTISAIHMVAIMCELL--DLKEGMKVLEIGTG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 89 SGYLTAcfyryIKAKGVDADTRIVGIEHQAELVRRSKANLntddrSMLDSGQLLIVEGDGRKGYPPNAPYNAIHVGAAAP 168
Cdd:PRK13942 87 SGYHAA-----VVAEIVGKSGKVVTIERIPELAEKAKKTL-----KKLGYDNVEVIVGDGTLGYEENAPYDRIYVTAAGP 156
|
170 180 190
....*....|....*....|....*....|
gi 442617574 169 DTPTELINQLASGGRLIVPVGpdggsQYMQ 198
Cdd:PRK13942 157 DIPKPLIEQLKDGGIMVIPVG-----SYSQ 181
|
|
| PRK13944 |
PRK13944 |
protein-L-isoaspartate O-methyltransferase; Provisional |
13-193 |
1.84e-28 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 140001 Cd Length: 205 Bit Score: 105.67 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 13 LIRQLKDHGVIASDAVAQAMKETDRKHYSPRN----PYMDAPQPIGGGVTISAPHMHAFALEYLRDhlKPGARILDVGSG 88
Cdd:PRK13944 5 LVEELVREGIIKSERVKKAMLSVPREEFVMPEyrmmAYEDRPLPLFAGATISAPHMVAMMCELIEP--RPGMKILEVGTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 89 SGYLTACFYRYIKAKGvdadtRIVGIEHQAELVRRSKANLntddRSMLDSGQLLIVEGDGRKGYPPNAPYNAIHVGAAAP 168
Cdd:PRK13944 83 SGYQAAVCAEAIERRG-----KVYTVEIVKELAIYAAQNI----ERLGYWGVVEVYHGDGKRGLEKHAPFDAIIVTAAAS 153
|
170 180
....*....|....*....|....*
gi 442617574 169 DTPTELINQLASGGRLIVPVGPDGG 193
Cdd:PRK13944 154 TIPSALVRQLKDGGVLVIPVEEGVG 178
|
|
| methyltran_FxLD |
TIGR04364 |
methyltransferase, FxLD system; Members of this family resemble occur regularly in the ... |
11-188 |
2.39e-23 |
|
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: 95.90 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 11 EDLIRQLKDHGVIASDAVAQAMKETDRKHYSPRNP----YmDAPQPI-----GGGVTIS---APHMHAFALEYLRdhLKP 78
Cdd:TIGR04364 6 AALVDELREDGVIRSPRVEAAFRTVPRHLFAPGAPlekaY-AANRAVvtkrdEDGRALSsvsAPHIQAMMLEQAG--VEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 79 GARILDVGSGsGYLTAcfyrYIkAKGVDADTRIVGIEHQAELVRRSKANLNtddrsmlDSG--QLLIVEGDGRKGYPPNA 156
Cdd:TIGR04364 83 GMRVLEIGSG-GYNAA----LL-AELVGPSGEVTTVDIDEDVTDRARACLA-------AAGypQVTVVLADAEAGVPELA 149
|
170 180 190
....*....|....*....|....*....|..
gi 442617574 157 PYNAIHVGAAAPDTPTELINQLASGGRLIVPV 188
Cdd:TIGR04364 150 PYDRIIVTVGAWDIPPAWLDQLAPGGRLVVPL 181
|
|
| PRK13943 |
PRK13943 |
protein-L-isoaspartate O-methyltransferase; Provisional |
11-188 |
1.27e-18 |
|
protein-L-isoaspartate O-methyltransferase; Provisional
Pssm-ID: 237568 [Multi-domain] Cd Length: 322 Bit Score: 81.82 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 11 EDLIRQLKDHGViaSDAVAQAMKETDR-----KHYSPRNPYMDapQPI----GGGV--TISAPHMHAFALEYLrdHLKPG 79
Cdd:PRK13943 8 EKLFWILKKYGI--SDHIAKAFLEVPReefltKSYPLSYVYED--IVLvsydDGEEysTSSQPSLMALFMEWV--GLDKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 80 ARILDVGSGSGYLTACFYRYIKAKGVdadtrIVGIEHQAELVRRSKANLNTddrsmLDSGQLLIVEGDGRKGYPPNAPYN 159
Cdd:PRK13943 82 MRVLEIGGGTGYNAAVMSRVVGEKGL-----VVSVEYSRKICEIAKRNVRR-----LGIENVIFVCGDGYYGVPEFAPYD 151
|
170 180
....*....|....*....|....*....
gi 442617574 160 AIHVGAAAPDTPTELINQLASGGRLIVPV 188
Cdd:PRK13943 152 VIFVTVGVDEVPETWFTQLKEGGRVIVPI 180
|
|
| Tam |
COG4106 |
Trans-aconitate methyltransferase [Energy production and conversion]; |
78-186 |
8.00e-10 |
|
Trans-aconitate methyltransferase [Energy production and conversion];
Pssm-ID: 443282 [Multi-domain] Cd Length: 100 Bit Score: 53.67 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 78 PGARILDVGSGSGYLTacfyRYIKAKGVDAdtRIVGIEHQAELVRRSKANLntddrsmldsGQLLIVEGDGRkGYPPNAP 157
Cdd:COG4106 1 PPRRVLDLGCGTGRLT----ALLAERFPGA--RVTGVDLSPEMLARARARL----------PNVRFVVADLR-DLDPPEP 63
|
90 100 110
....*....|....*....|....*....|....*
gi 442617574 158 YNAIHVGAA---APDTPT---ELINQLASGGRLIV 186
Cdd:COG4106 64 FDLVVSNAAlhwLPDHAAllaRLAAALAPGGVLAV 98
|
|
| UbiG |
COG2227 |
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ... |
70-186 |
3.51e-07 |
|
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: 47.32 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 70 EYLRDHLKPGARILDVGSGSGYLTacfyRYIKAKGVDadtrIVGIEHQAELVRRSKANLNTDDrsmldsgqLLIVEGDGR 149
Cdd:COG2227 16 ALLARLLPAGGRVLDVGCGTGRLA----LALARRGAD----VTGVDISPEALEIARERAAELN--------VDFVQGDLE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 442617574 150 KGYPPNAPYNAI-------HVgaaaPDTPT---ELINQLASGGRLIV 186
Cdd:COG2227 80 DLPLEDGSFDLVicsevleHL----PDPAAllrELARLLKPGGLLLL 122
|
|
| TrmR |
COG4122 |
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ... |
75-186 |
2.74e-06 |
|
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443298 Cd Length: 173 Bit Score: 45.56 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 75 HLKPGARILDVGSGSGYLTACFyryikAKGVDADTRIVGIEHQAELVRRSKANLntdDRSMLDSgQLLIVEGDGRKGYP- 153
Cdd:COG4122 13 RLLGAKRILEIGTGTGYSTLWL-----ARALPDDGRLTTIEIDPERAAIARENF---ARAGLAD-RIRLILGDALEVLPr 83
|
90 100 110
....*....|....*....|....*....|....*..
gi 442617574 154 -PNAPYNAIHVGAAAPDTPT---ELINQLASGGrLIV 186
Cdd:COG4122 84 lADGPFDLVFIDADKSNYPDyleLALPLLRPGG-LIV 119
|
|
| Gcd14 |
COG2519 |
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ... |
76-186 |
4.16e-06 |
|
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442009 [Multi-domain] Cd Length: 249 Bit Score: 45.92 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 76 LKPGARILDVGSGSGYLTACFYRYIKAKGvdadtRIVGIEHQAELVRRSKANLntddRSMLDSGQLLIVEGDGRKGYPPN 155
Cdd:COG2519 89 IFPGARVLEAGTGSGALTLALARAVGPEG-----KVYSYERREDFAEIARKNL----ERFGLPDNVELKLGDIREGIDEG 159
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442617574 156 ----------APYNAI-HVGAAapdtptelinqLASGGRLIV 186
Cdd:COG2519 160 dvdavfldmpDPWEALeAVAKA-----------LKPGGVLVA 190
|
|
| Cfa |
COG2230 |
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ... |
63-186 |
6.97e-06 |
|
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];
Pssm-ID: 441831 [Multi-domain] Cd Length: 158 Bit Score: 44.15 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 63 HMHAFALEYLRdhLKPGARILDVGSGSGYLTacfyRYI-KAKGVdadtRIVGI---EHQAELVRRSKANLNTDDRsmlds 138
Cdd:COG2230 38 AKLDLILRKLG--LKPGMRVLDIGCGWGGLA----LYLaRRYGV----RVTGVtlsPEQLEYARERAAEAGLADR----- 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 442617574 139 gqLLIVEGDGRKgYPPNAPYNAI-------HVGAAAPDTPTELINQ-LASGGRLIV 186
Cdd:COG2230 103 --VEVRLADYRD-LPADGQFDAIvsigmfeHVGPENYPAYFAKVARlLKPGGRLLL 155
|
|
| UbiE |
COG2226 |
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ... |
76-186 |
1.76e-05 |
|
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: 43.06 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 76 LKPGARILDVGSGSGYLTACFYRyikakgvdADTRIVGIEHQAELVRRSKANLNTDDRsmldsgQLLIVEGDGRKGYPPN 155
Cdd:COG2226 20 LRPGARVLDLGCGTGRLALALAE--------RGARVTGVDISPEMLELARERAAEAGL------NVEFVVGDAEDLPFPD 85
|
90 100 110
....*....|....*....|....*....|....*..
gi 442617574 156 APYNAIHVGAA---APDTP---TELINQLASGGRLIV 186
Cdd:COG2226 86 GSFDLVISSFVlhhLPDPEralAEIARVLKPGGRLVV 122
|
|
| CbiT |
TIGR02469 |
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ... |
59-188 |
2.02e-05 |
|
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274148 [Multi-domain] Cd Length: 124 Bit Score: 42.32 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 59 ISAPHMHAFALEYLRdhLKPGARILDVGSGSGYLTacfyryIKAKGVDADTRIVGIEHQAELVRRSKANLntdDRsmLDS 138
Cdd:TIGR02469 2 MTKREVRALTLAKLR--LRPGDVLWDIGAGTGSVT------IEAARLVPNGRVYAIERNPEALDLIERNL---RR--FGV 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 139 GQLLIVEGDGrkgypPNAPYN------AIHVGAAAPDTpTELIN----QLASGGRLIVPV 188
Cdd:TIGR02469 69 SNIVIVEGDA-----PEAPEAllpdpdAVFVGGSGGLL-QEILEaverRLRPGGRIVLNA 122
|
|
| MTS |
pfam05175 |
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ... |
66-186 |
2.14e-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: 40.27 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 66 AFALEYLRDHLkpGARILDVGSGSGYLTAcfyrYIKAKGVDADTRIVGIEHQAelVRRSKANLNTDDrsmLDSGQllIVE 145
Cdd:pfam05175 21 RLLLEHLPKDL--SGKVLDLGCGAGVLGA----ALAKESPDAELTMVDINARA--LESARENLAANG---LENGE--VVA 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 442617574 146 GDGRKGYPPnAPYNAI------HVG-AAAPDTPTELINQ----LASGGRLIV 186
Cdd:pfam05175 88 SDVYSGVED-GKFDLIisnppfHAGlATTYNVAQRFIADakrhLRPGGELWI 138
|
|
| Methyltransf_31 |
pfam13847 |
Methyltransferase domain; This family appears to have methyltransferase activity. |
76-127 |
1.01e-03 |
|
Methyltransferase domain; This family appears to have methyltransferase activity.
Pssm-ID: 463998 [Multi-domain] Cd Length: 150 Bit Score: 38.17 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 442617574 76 LKPGARILDVGSGSGYLTacfyrYIKAKGVDADTRIVGIEHQAELVRRSKAN 127
Cdd:pfam13847 1 IDKGMRVLDLGCGTGHLS-----FELAEELGPNAEVVGIDISEEAIEKAREN 47
|
|
| RsmC |
COG2813 |
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ... |
69-186 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 69 LEYLRDHLkpGARILDVGSGSGYLTAcfyrYIKAKGVDAdtRIVGIEHQAELVRRSKANLntdDRSMLDSGQllIVEGDG 148
Cdd:COG2813 42 LEHLPEPL--GGRVLDLGCGYGVIGL----ALAKRNPEA--RVTLVDVNARAVELARANA---AANGLENVE--VLWSDG 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 442617574 149 RKGyPPNAPYNAI------HVGAAAPDTPTE-LINQ----LASGGRLIV 186
Cdd:COG2813 109 LSG-VPDGSFDLIlsnppfHAGRAVDKEVAHaLIADaarhLRPGGELWL 156
|
|
| PrmA |
COG2264 |
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis]; |
69-90 |
1.68e-03 |
|
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 441865 [Multi-domain] Cd Length: 284 Bit Score: 38.23 E-value: 1.68e-03
|
| Methyltransf_32 |
pfam13679 |
Methyltransferase domain; This family appears to be a methyltransferase domain. |
77-126 |
2.14e-03 |
|
Methyltransferase domain; This family appears to be a methyltransferase domain.
Pssm-ID: 379330 [Multi-domain] Cd Length: 138 Bit Score: 36.78 E-value: 2.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 442617574 77 KPGARILDVGSGSGYLTacFYRYIKAKGVdadtRIVGIEHQAELVRRSKA 126
Cdd:pfam13679 24 NGPITIVDHGAGKGYLG--FILYYLKYGV----RVYGIDTRAELVEKANA 67
|
|
| CobL |
COG2242 |
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ... |
66-186 |
3.35e-03 |
|
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441843 [Multi-domain] Cd Length: 403 Bit Score: 37.45 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 66 AFALEYLRdhLKPGARILDVGSGSGYLTacfyryIKAKGVDADTRIVGIEHQAELVRRSKAN---LNTDDrsmldsgqLL 142
Cdd:COG2242 237 ALTLAKLA--LRPGDVLWDIGAGSGSVS------IEAARLAPGGRVYAIERDPERAALIRANarrFGVPN--------VE 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 442617574 143 IVEGDGRKGYPPNAPYNAIHVGAAAPDTPtELINQ----LASGGRLIV 186
Cdd:COG2242 301 VVEGEAPEALADLPDPDAVFIGGSGGNLP-EILEAcwarLRPGGRLVA 347
|
|
| AdoMet_MTases |
cd02440 |
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ... |
81-188 |
3.65e-03 |
|
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: 35.87 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442617574 81 RILDVGSGSGYLTACFYRYIKAK--GVDADtrivgiEHQAELVRRSKANLNTDDRSmldsgqllIVEGDGRKG-YPPNAP 157
Cdd:cd02440 1 RVLDLGCGTGALALALASGPGARvtGVDIS------PVALELARKAAAALLADNVE--------VLKGDAEELpPEADES 66
|
90 100 110
....*....|....*....|....*....|....*...
gi 442617574 158 YNAIHVGAAAPDTPT-------ELINQLASGGRLIVPV 188
Cdd:cd02440 67 FDVIISDPPLHHLVEdlarfleEARRLLKPGGVLVLTL 104
|
|
| PRK14968 |
PRK14968 |
putative methyltransferase; Provisional |
69-129 |
3.98e-03 |
|
putative methyltransferase; Provisional
Pssm-ID: 237872 [Multi-domain] Cd Length: 188 Bit Score: 36.80 E-value: 3.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442617574 69 LEYLRDhlKPGARILDVGSGSGYLTACFyryikakgVDADTRIVGIE---HQAELVRRSkANLN 129
Cdd:PRK14968 16 AENAVD--KKGDRVLEVGTGSGIVAIVA--------AKNGKKVVGVDinpYAVECAKCN-AKLN 68
|
|
| CMAS |
pfam02353 |
Mycolic acid cyclopropane synthetase; This family consist of ... |
68-133 |
6.16e-03 |
|
Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Pssm-ID: 396777 [Multi-domain] Cd Length: 272 Bit Score: 36.54 E-value: 6.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442617574 68 ALEYLrdHLKPGARILDVGSGSGYLTacfyRYIKAKgvdADTRIVGI---EHQAELVRRSKANLNTDDR 133
Cdd:pfam02353 53 ILDKL--GLKPGMTLLDIGCGWGGLM----RRAAER---YDVNVVGLtlsKNQYKLARKRVAAEGLARK 112
|
|
| TrmN6 |
COG4123 |
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ... |
76-128 |
6.88e-03 |
|
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 443299 [Multi-domain] Cd Length: 238 Bit Score: 36.28 E-value: 6.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 442617574 76 LKPGARILDVGSGSGYLTACF-YRYikakgvdADTRIVGIEHQAELVRRSKANL 128
Cdd:COG4123 35 VKKGGRVLDLGTGTGVIALMLaQRS-------PGARITGVEIQPEAAELARRNV 81
|
|
|