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Conserved domains on  [gi|568920233|ref|XP_006500685|]
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protein-L-isoaspartate O-methyltransferase domain-containing protein 2 isoform X3 [Mus musculus]

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);
11-219 9.25e-26

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: 100.91  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   11 NDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHG-NIHLSAPCIYSEVMEALDLQPGLSFLNLGS 89
Cdd:pfam01135   3 NEALIENLKNYGVIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGyGQTISAPHMHAMMLELLELKPGMRVLEIGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   90 GTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLdvfiRTSDSFDKfdfcepSFVTGNCLEIAPDCCQYDRVYCGAGV 169
Cdd:pfam01135  83 GSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNL----EKLGLENV------IVVVGDGRQGWPEFAPYDAIHVGAAA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920233  170 QKEHEEYMkNLLKVGGILVMPLEEK----LTKITRTGPSAWETKKILAVSFAPL 219
Cdd:pfam01135 153 PEIPEALI-DQLKEGGRLVIPVGPNgnqvLQQFDKRNDGSVVIKDLEGVRFVPL 205
 
Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
11-219 9.25e-26

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 100.91  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   11 NDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHG-NIHLSAPCIYSEVMEALDLQPGLSFLNLGS 89
Cdd:pfam01135   3 NEALIENLKNYGVIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGyGQTISAPHMHAMMLELLELKPGMRVLEIGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   90 GTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLdvfiRTSDSFDKfdfcepSFVTGNCLEIAPDCCQYDRVYCGAGV 169
Cdd:pfam01135  83 GSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNL----EKLGLENV------IVVVGDGRQGWPEFAPYDAIHVGAAA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920233  170 QKEHEEYMkNLLKVGGILVMPLEEK----LTKITRTGPSAWETKKILAVSFAPL 219
Cdd:pfam01135 153 PEIPEALI-DQLKEGGRLVIPVGPNgnqvLQQFDKRNDGSVVIKDLEGVRFVPL 205
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
 6-220 1.33e-21

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: 89.89  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233    6 SAGEDNDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHG-NIHLSAPCIYSEVMEALDLQPGLSF 84
Cdd:TIGR00080   2 DLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGyGQTISAPHMVAMMTELLELKPGMKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   85 LNLGSGTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKL------DVFIRTSDSFDKFDfcepsfvtgnclEIAPdcc 158
Cdd:TIGR00080  82 LEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLrklgldNVIVIVGDGTQGWE------------PLAP--- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568920233  159 qYDRVYCGAGVQKEHEEYMKNlLKVGGILVMPLEEKLTKITRTGP--SAWETKKILAVSFAPLV 220
Cdd:TIGR00080 147 -YDRIYVTAAGPKIPEALIDQ-LKEGGILVMPVGEYLQVLKRAEKrgGEIIIKDVEPVAFVPLV 208
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 24-220 3.24e-21

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 88.61  E-value: 3.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  24 IRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHGN-IHLSAPCIYSEVMEALDLQPGLSFLNLGSGTGY----LSSMV 98
Cdd:COG2518    9 VTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHgQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYqaavLARLA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  99 GLIlgpfgvnHGVELHSDVTEYAKQKLdvfirtsdsfDKFDFCEPSFVTGNCLEIAPDCCQYDRVYCGAGVQKEHEEYmK 178
Cdd:COG2518   89 GRV-------YSVERDPELAERARERL----------AALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEAL-L 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568920233 179 NLLKVGGILVMPLEE----KLTKITRTGpSAWETKKILAVSFAPLV 220
Cdd:COG2518  151 EQLAPGGRLVAPVGEggvqRLVLITRTG-DGFERESLFEVRFVPLR 195
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 9-220 6.23e-17

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 77.36  E-value: 6.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   9 EDNDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKD--LAWKHGNIhLSAPCIYSEVMEALDLQPGLSFLN 86
Cdd:PRK13942   4 EEKRRVIEELIREGYIKSKKVIDALLKVPRHLFVPEYLEEYAYVDtpLEIGYGQT-ISAIHMVAIMCELLDLKEGMKVLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  87 LGSGTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLdvfirtsdsfDKFDFCEPSFVTGNCLEIAPDCCQYDRVYCG 166
Cdd:PRK13942  83 IGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTL----------KKLGYDNVEVIVGDGTLGYEENAPYDRIYVT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568920233 167 AGVQKEHEEYMKNlLKVGGILVMPL---EEKLTKITRTGPSAWEtKKILAVSFAPLV 220
Cdd:PRK13942 153 AAGPDIPKPLIEQ-LKDGGIMVIPVgsySQELIRVEKDNGKIIK-KKLGEVAFVPLI 207
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-193 1.89e-04

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: 40.11  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  84 FLNLGSGTGYLSSmvGLILGPFGVNHGVELHSDVTEYAKQKLDVFIRTSDSFDKFDFCEPSFVTGNcleiapdccQYDRV 163
Cdd:cd02440    2 VLDLGCGTGALAL--ALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADE---------SFDVI 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568920233 164 YCGAGVQKEHEEY------MKNLLKVGGILVMPLEE 193
Cdd:cd02440   71 ISDPPLHHLVEDLarfleeARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
11-219 9.25e-26

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 100.91  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   11 NDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHG-NIHLSAPCIYSEVMEALDLQPGLSFLNLGS 89
Cdd:pfam01135   3 NEALIENLKNYGVIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGyGQTISAPHMHAMMLELLELKPGMRVLEIGS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   90 GTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLdvfiRTSDSFDKfdfcepSFVTGNCLEIAPDCCQYDRVYCGAGV 169
Cdd:pfam01135  83 GSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNL----EKLGLENV------IVVVGDGRQGWPEFAPYDAIHVGAAA 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568920233  170 QKEHEEYMkNLLKVGGILVMPLEEK----LTKITRTGPSAWETKKILAVSFAPL 219
Cdd:pfam01135 153 PEIPEALI-DQLKEGGRLVIPVGPNgnqvLQQFDKRNDGSVVIKDLEGVRFVPL 205
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
 6-220 1.33e-21

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: 89.89  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233    6 SAGEDNDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHG-NIHLSAPCIYSEVMEALDLQPGLSF 84
Cdd:TIGR00080   2 DLESQKKALIDKLINEGYIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGyGQTISAPHMVAMMTELLELKPGMKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   85 LNLGSGTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKL------DVFIRTSDSFDKFDfcepsfvtgnclEIAPdcc 158
Cdd:TIGR00080  82 LEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLrklgldNVIVIVGDGTQGWE------------PLAP--- 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568920233  159 qYDRVYCGAGVQKEHEEYMKNlLKVGGILVMPLEEKLTKITRTGP--SAWETKKILAVSFAPLV 220
Cdd:TIGR00080 147 -YDRIYVTAAGPKIPEALIDQ-LKEGGILVMPVGEYLQVLKRAEKrgGEIIIKDVEPVAFVPLV 208
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 24-220 3.24e-21

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 88.61  E-value: 3.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  24 IRTDLVEQAFRAIDRADYYLEEFKENAYKDLAWKHGN-IHLSAPCIYSEVMEALDLQPGLSFLNLGSGTGY----LSSMV 98
Cdd:COG2518    9 VTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHgQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYqaavLARLA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  99 GLIlgpfgvnHGVELHSDVTEYAKQKLdvfirtsdsfDKFDFCEPSFVTGNCLEIAPDCCQYDRVYCGAGVQKEHEEYmK 178
Cdd:COG2518   89 GRV-------YSVERDPELAERARERL----------AALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEAL-L 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568920233 179 NLLKVGGILVMPLEE----KLTKITRTGpSAWETKKILAVSFAPLV 220
Cdd:COG2518  151 EQLAPGGRLVAPVGEggvqRLVLITRTG-DGFERESLFEVRFVPLR 195
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 9-220 6.23e-17

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 77.36  E-value: 6.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233   9 EDNDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKD--LAWKHGNIhLSAPCIYSEVMEALDLQPGLSFLN 86
Cdd:PRK13942   4 EEKRRVIEELIREGYIKSKKVIDALLKVPRHLFVPEYLEEYAYVDtpLEIGYGQT-ISAIHMVAIMCELLDLKEGMKVLE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  87 LGSGTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLdvfirtsdsfDKFDFCEPSFVTGNCLEIAPDCCQYDRVYCG 166
Cdd:PRK13942  83 IGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTL----------KKLGYDNVEVIVGDGTLGYEENAPYDRIYVT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568920233 167 AGVQKEHEEYMKNlLKVGGILVMPL---EEKLTKITRTGPSAWEtKKILAVSFAPLV 220
Cdd:PRK13942 153 AAGPDIPKPLIEQ-LKDGGIMVIPVgsySQELIRVEKDNGKIIK-KKLGEVAFVPLI 207
methyltran_FxLD TIGR04364
methyltransferase, FxLD system; Members of this family resemble occur regularly in the ...
 7-126 7.60e-12

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: 64.70  E-value: 7.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233    7 AGEDNDELIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAY---KDLAWK---HGNI--HLSAPCIYSEVMEALDL 78
Cdd:TIGR04364   1 AARLRAALVDELREDGVIRSPRVEAAFRTVPRHLFAPGAPLEKAYaanRAVVTKrdeDGRAlsSVSAPHIQAMMLEQAGV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 568920233   79 QPGLSFLNLGSGtGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLD 126
Cdd:TIGR04364  81 EPGMRVLEIGSG-GYNAALLAELVGPSGEVTTVDIDEDVTDRARACLA 127
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
14-221 1.61e-11

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 62.14  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  14 LIDNLKeAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKDLA-------WkhgnihLSAPCIYSEVMEALDLQPGLSFLN 86
Cdd:PRK00312  12 LVLRLR-AEGILDERVLEAIEATPRELFVPEAFKHKAYENRAlpigcgqT------ISQPYMVARMTELLELKPGDRVLE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  87 LGSGTGY----LSSMVGLILgpfgvnhGVELHSDVTEYAKQKL------DVFIRTSDSFDKFdfcePSFvtgncleiAPd 156
Cdd:PRK00312  85 IGTGSGYqaavLAHLVRRVF-------SVERIKTLQWEAKRRLkqlglhNVSVRHGDGWKGW----PAY--------AP- 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568920233 157 ccqYDRVYCGAGVQKEHEEYMkNLLKVGGILVMPL----EEKLTKITRTGpSAWETKKILAVSFAPLVQ 221
Cdd:PRK00312 145 ---FDRILVTAAAPEIPRALL-EQLKEGGILVAPVggeeQQLLTRVRKRG-GRFEREVLEEVRFVPLVK 208
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
 14-219 4.07e-10

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 58.29  E-value: 4.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  14 LIDNLKEAQYIRTDLVEQAFRAIDRADYYLEEFKENAYKD--LAWKHGNIhLSAPCIYSEVMEALDLQPGLSFLNLGSGT 91
Cdd:PRK13944   5 LVEELVREGIIKSERVKKAMLSVPREEFVMPEYRMMAYEDrpLPLFAGAT-ISAPHMVAMMCELIEPRPGMKILEVGTGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  92 GYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLD-------VFIRTSD---SFDKFDFCEPSFVTGNCLEIAPDccqyd 161
Cdd:PRK13944  84 GYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIErlgywgvVEVYHGDgkrGLEKHAPFDAIIVTAAASTIPSA----- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568920233 162 rvycgagvqkeheeyMKNLLKVGGILVMPLEE----KLTKITRTGpSAWETKKILAVSFAPL 219
Cdd:PRK13944 159 ---------------LVRQLKDGGVLVIPVEEgvgqVLYKVVKRG-EKVEKRAITYVLFVPL 204
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 64-197 7.84e-06

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 46.38  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  64 SAPCIYSEVMEALDLQPGLSFLNLGSGTGYLSSMVGLILGPFGVNHGVELHSDVTEYAKQKLdvfirtsdsfDKFDFCEP 143
Cdd:PRK13943  64 SQPSLMALFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNV----------RRLGIENV 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568920233 144 SFVTGNCLEIAPDCCQYDRVYCGAGVQKEHEEYMKNlLKVGGILVMPLEEKLTK 197
Cdd:PRK13943 134 IFVCGDGYYGVPEFAPYDVIFVTVGVDEVPETWFTQ-LKEGGRVIVPINLKLSR 186
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-213 6.35e-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: 41.90  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  69 YSEVMEALDLQPGLSFLNLGSGTGYLSsmvgLILGPFGVN-HGVELHSDVTEYAKQKLdvfirtsdsfdKFDFCEPSFVT 147
Cdd:COG2226   11 REALLAALGLRPGARVLDLGCGTGRLA----LALAERGARvTGVDISPEMLELARERA-----------AEAGLNVEFVV 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568920233 148 GNCLEIAPDCCQYDRVYCGAGVQ--KEHEEYMKNL---LKVGGILVMpleekltkITRTGPSAWETKKILA 213
Cdd:COG2226   76 GDAEDLPFPDGSFDLVISSFVLHhlPDPERALAEIarvLKPGGRLVV--------VDFSPPDLAELEELLA 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 84-193 1.89e-04

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: 40.11  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  84 FLNLGSGTGYLSSmvGLILGPFGVNHGVELHSDVTEYAKQKLDVFIRTSDSFDKFDFCEPSFVTGNcleiapdccQYDRV 163
Cdd:cd02440    2 VLDLGCGTGALAL--ALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADE---------SFDVI 70

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568920233 164 YCGAGVQKEHEEY------MKNLLKVGGILVMPLEE 193
Cdd:cd02440   71 ISDPPLHHLVEDLarfleeARRLLKPGGVLVLTLVL 106
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 78-189 2.04e-03

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: 37.30  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  78 LQPGLSFLNLGSGTGYLSSMvgliLGPFGVN-HGVELHSDVTEYAKQKLDVFirtsdsfdkfdfcEPSFVTGNCLEIAPD 156
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALA----LARRGADvTGVDISPEALEIARERAAEL-------------NVDFVQGDLEDLPLE 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 568920233 157 CCQYDRVYCGAGVqkEH----EEYMKNL---LKVGGILVM 189
Cdd:COG2227   85 DGSFDLVICSEVL--EHlpdpAALLRELarlLKPGGLLLL 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 69-189 6.26e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.45  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568920233  69 YSEVMEALDLQPGLSFLNLGSGTGYLSSMvglILGPFGVN-HGVELHSDVTEYAKQKldvfIRTSDSFDKFDfcepsFVT 147
Cdd:COG2230   40 LDLILRKLGLKPGMRVLDIGCGWGGLALY---LARRYGVRvTGVTLSPEQLEYARER----AAEAGLADRVE-----VRL 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 568920233 148 GNCLEIAPDcCQYDRVYCgAGV-----QKEHEEYMKN---LLKVGGILVM 189
Cdd:COG2230  108 ADYRDLPAD-GQFDAIVS-IGMfehvgPENYPAYFAKvarLLKPGGRLLL 155
 
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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