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Conserved domains on  [gi|442617574|ref|NP_001262287|]
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Protein-L-isoaspartate (D-aspartate) O-methyltransferase, isoform C [Drosophila melanogaster]

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);
8-200 1.15e-97

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: 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
 
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
                         10        20
                 ....*....|....*....|..
gi 442617574  69 LEYLRDHLKPGARILDVGSGSG 90
Cdd:COG2264  139 LEALEKLLKPGKTVLDVGCGSG 160
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
 
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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