NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|42565060|ref|NP_188701|]
View 

mRNA capping enzyme family protein [Arabidopsis thaliana]

Protein Classification

mRNA cap guanine-N7 methyltransferase( domain architecture ID 10505544)

mRNA cap guanine-N7 methyltransferase is the catalytic subunit of the mRNA-capping methyltransferase RNMT:RAMAC complex that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 30-341 1.84e-141

mRNA capping enzyme; This family of enzymes are related to pfam03919.


:

Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 404.89  E-value: 1.84e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    30 FLEDETTKNFARKVADHYSRRTN--QTLEEREASPIIHLKKLNNWIKSVLIQLYARPDD------AVLDLACGKGGDLIK 101
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPEtgELLKPRQASPIIYLRNFNNWIKSLLISLYASKTFqnsnkrKVLDLGCGKGGDLEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   102 WDKARIGYYVGIDIAEGSIEDCRTRYNgdadhHQRRKKFS----FPSRLLCGDCFEVELDKILEE-DAPFDICSCQFAMH 176
Cdd:pfam03291  81 WFKGGISQLIGTDIAEVSIEQCRERYN-----KLRSGNKSkyykFDAEFITGDCFVSSLREVFEDpFGKFDIVSCQFAIH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   177 YSWTTEARARRALANVSALLRPGGVFIGTMPDANVI----IKKLREAE--GLEIGNSVYWIRFGEEYSQKKFkssspFGI 250
Cdd:pfam03291 156 YSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEEEPPQVPL-----FGI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   251 EYVFHLEDAV-DCPEWIVPFNVFKSLAEEYDLELVFVKNSHEFVHEYMKKpEFVELMRRLGAL-----------GDGSND 318
Cdd:pfam03291 231 KYDYNLEDAVdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKK-EFKKLIKRMSAMesrpstrnffgLQRSAG 309

                         330       340
                  ....*....|....*....|...
gi 42565060   319 QSTLSADEWEAAYLYLSFVLRKR 341
Cdd:pfam03291 310 KGTLGGDEWEAASFYLVFVFEKR 332
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 30-341 1.84e-141

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 404.89  E-value: 1.84e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    30 FLEDETTKNFARKVADHYSRRTN--QTLEEREASPIIHLKKLNNWIKSVLIQLYARPDD------AVLDLACGKGGDLIK 101
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPEtgELLKPRQASPIIYLRNFNNWIKSLLISLYASKTFqnsnkrKVLDLGCGKGGDLEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   102 WDKARIGYYVGIDIAEGSIEDCRTRYNgdadhHQRRKKFS----FPSRLLCGDCFEVELDKILEE-DAPFDICSCQFAMH 176
Cdd:pfam03291  81 WFKGGISQLIGTDIAEVSIEQCRERYN-----KLRSGNKSkyykFDAEFITGDCFVSSLREVFEDpFGKFDIVSCQFAIH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   177 YSWTTEARARRALANVSALLRPGGVFIGTMPDANVI----IKKLREAE--GLEIGNSVYWIRFGEEYSQKKFkssspFGI 250
Cdd:pfam03291 156 YSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEEEPPQVPL-----FGI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   251 EYVFHLEDAV-DCPEWIVPFNVFKSLAEEYDLELVFVKNSHEFVHEYMKKpEFVELMRRLGAL-----------GDGSND 318
Cdd:pfam03291 231 KYDYNLEDAVdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKK-EFKKLIKRMSAMesrpstrnffgLQRSAG 309

                         330       340
                  ....*....|....*....|...
gi 42565060   319 QSTLSADEWEAAYLYLSFVLRKR 341
Cdd:pfam03291 310 KGTLGGDEWEAASFYLVFVFEKR 332
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 74-219 1.44e-14

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: 70.02  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  74 KSVLIQLYARPDDAVLDLACGKGGDLIKWdkARIGY-YVGIDIAEGSIEDCRtryngdadhhQRRKKFSFPSRLLCGDCF 152
Cdd:COG2226  12 EALLAALGLRPGARVLDLGCGTGRLALAL--AERGArVTGVDISPEMLELAR----------ERAAEAGLNVEFVVGDAE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060 153 EVELdkileEDAPFDICSCQFAMHYSwtteARARRALANVSALLRPGGVFI---GTMPDANVIIKKLREA 219
Cdd:COG2226  80 DLPF-----PDGSFDLVISSFVLHHL----PDPERALAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 88-203 7.09e-10

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: 55.90  E-value: 7.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  88 VLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRyngdadhhqRRKKFSFPSRLLCGDCFEVELDkileEDAPFD 167
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKA---------AAALLADNVEVLKGDAEELPPE----ADESFD 68

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 42565060 168 ICSCQFAMHYSwttEARARRALANVSALLRPGGVFI 203
Cdd:cd02440  69 VIISDPPLHHL---VEDLARFLEEARRLLKPGGVLV 101
PRK08317 PRK08317
hypothetical protein; Provisional
 76-200 3.37e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.54  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   76 VLIQLYARPDDAVLDLACGKGGDL--IKWDKARIGYYVGIDIAEGSIEDCRTRYNGDADhhqrrkkfsfPSRLLCGDCFE 153
Cdd:PRK08317  11 TFELLAVQPGDRVLDVGCGPGNDAreLARRVGPEGRVVGIDRSEAMLALAKERAAGLGP----------NVEFVRGDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 42565060  154 VELdkileEDAPFDIC-SCQFAMHYswtteARARRALANVSALLRPGG 200
Cdd:PRK08317  81 LPF-----PDGSFDAVrSDRVLQHL-----EDPARALAEIARVLRPGG 118
 
Name Accession Description Interval E-value
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 30-341 1.84e-141

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 404.89  E-value: 1.84e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    30 FLEDETTKNFARKVADHYSRRTN--QTLEEREASPIIHLKKLNNWIKSVLIQLYARPDD------AVLDLACGKGGDLIK 101
Cdd:pfam03291   1 EGPFETNSNITDIVATHYNERPEtgELLKPRQASPIIYLRNFNNWIKSLLISLYASKTFqnsnkrKVLDLGCGKGGDLEK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   102 WDKARIGYYVGIDIAEGSIEDCRTRYNgdadhHQRRKKFS----FPSRLLCGDCFEVELDKILEE-DAPFDICSCQFAMH 176
Cdd:pfam03291  81 WFKGGISQLIGTDIAEVSIEQCRERYN-----KLRSGNKSkyykFDAEFITGDCFVSSLREVFEDpFGKFDIVSCQFAIH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   177 YSWTTEARARRALANVSALLRPGGVFIGTMPDANVI----IKKLREAE--GLEIGNSVYWIRFGEEYSQKKFkssspFGI 250
Cdd:pfam03291 156 YSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFIsaltIKRLFAIEkdLPSFGNSIYSVKFEEEPPQVPL-----FGI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   251 EYVFHLEDAV-DCPEWIVPFNVFKSLAEEYDLELVFVKNSHEFVHEYMKKpEFVELMRRLGAL-----------GDGSND 318
Cdd:pfam03291 231 KYDYNLEDAVdDVPEYIVPFETLVSLAEEYGLELVDKKTFADIFEEEIKK-EFKKLIKRMSAMesrpstrnffgLQRSAG 309

                         330       340
                  ....*....|....*....|...
gi 42565060   319 QSTLSADEWEAAYLYLSFVLRKR 341
Cdd:pfam03291 310 KGTLGGDEWEAASFYLVFVFEKR 332
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 88-200 1.10e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.83  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    88 VLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRYngdadhhqrrKKFSFPSRLLCGDCFEVELdkileEDAPFD 167
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERA----------AEAGLNVEFVQGDAEDLPF-----PDGSFD 65

                          90       100       110
                  ....*....|....*....|....*....|...
gi 42565060   168 ICSCQFAMHYswTTEARARRALANVSALLRPGG 200
Cdd:pfam13649  66 LVVSSGVLHH--LPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 74-219 1.44e-14

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: 70.02  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  74 KSVLIQLYARPDDAVLDLACGKGGDLIKWdkARIGY-YVGIDIAEGSIEDCRtryngdadhhQRRKKFSFPSRLLCGDCF 152
Cdd:COG2226  12 EALLAALGLRPGARVLDLGCGTGRLALAL--AERGArVTGVDISPEMLELAR----------ERAAEAGLNVEFVVGDAE 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060 153 EVELdkileEDAPFDICSCQFAMHYSwtteARARRALANVSALLRPGGVFI---GTMPDANVIIKKLREA 219
Cdd:COG2226  80 DLPF-----PDGSFDLVISSFVLHHL----PDPERALAEIARVLKPGGRLVvvdFSPPDLAELEELLAEA 140
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 77-208 1.16e-11

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: 61.57  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  77 LIQLYARPDDAVLDLACGKGGDLIKWdkARIGY-YVGIDIAEGSIEDCRTRYNGdadhhqrrkkfsFPSRLLCGDCFEVE 155
Cdd:COG2227  17 LLARLLPAGGRVLDVGCGTGRLALAL--ARRGAdVTGVDISPEALEIARERAAE------------LNVDFVQGDLEDLP 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 42565060 156 LdkileEDAPFDICSCQFAMHYswttEARARRALANVSALLRPGGVFIGTMPD 208
Cdd:COG2227  83 L-----EDGSFDLVICSEVLEH----LPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 89-202 4.72e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.92  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    89 LDLACGKGGDLIKWDKARIGY-YVGIDIAEGSIEDCRTRYNGDADHHQRRKKFsfpsrllcgdcfeVELDKILEEDAPFD 167
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeYTGLDISPAALEAARERLAALGLLNAVRVEL-------------FQLDLGELDPGSFD 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 42565060   168 ICSCQFAMHYSwtteARARRALANVSALLRPGGVF 202
Cdd:pfam08242  68 VVVASNVLHHL----ADPRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 88-203 5.59e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.39  E-value: 5.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  88 VLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRYNGDADHHQrrkkfsfpsRLLCGDCFEVEldkiLEEDAPFD 167
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNV---------EFLVADLAELD----PLPAESFD 96

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 42565060 168 ICSCQFAMHysWTTEARARRALANVSALLRPGGVFI 203
Cdd:COG0500  97 LVVAFGVLH--HLPPEEREALLRELARALKPGGVLL 130
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 88-203 7.09e-10

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: 55.90  E-value: 7.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  88 VLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRyngdadhhqRRKKFSFPSRLLCGDCFEVELDkileEDAPFD 167
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKA---------AAALLADNVEVLKGDAEELPPE----ADESFD 68

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 42565060 168 ICSCQFAMHYSwttEARARRALANVSALLRPGGVFI 203
Cdd:cd02440  69 VIISDPPLHHL---VEDLARFLEEARRLLKPGGVLV 101
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 89-203 1.32e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.59  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    89 LDLACGKGGdLIKWDKARIGYYVGIDIAEGSIEDCRTRYNGDadhhqrrkkfsfPSRLLCGDCFEVELdkileEDAPFDI 168
Cdd:pfam08241   1 LDVGCGTGL-LTELLARLGARVTGVDISPEMLELAREKAPRE------------GLTFVVGDAEDLPF-----PDNSFDL 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 42565060   169 CSCQFAMHYSwtteARARRALANVSALLRPGGVFI 203
Cdd:pfam08241  63 VLSSEVLHHV----EDPERALREIARVLKPGGILI 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
72-210 1.12e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 54.23  E-value: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  72 WIKSVLIQLYARPDDAVLDLACGKG--GDLIKwdkARIGYYVGIDIAEGSIEDCRTRYNGDadhhqrrkkfsfpsRLLCG 149
Cdd:COG4976  34 LAEELLARLPPGPFGRVLDLGCGTGllGEALR---PRGYRLTGVDLSEEMLAKAREKGVYD--------------RLLVA 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42565060 150 DcfeveLDKILEEDAPFDICSCQFAMHYswttEARARRALANVSALLRPGGVFIGTMPDAN 210
Cdd:COG4976  97 D-----LADLAEPDGRFDLIVAADVLTY----LGDLAAVFAGVARALKPGGLFIFSVEDAD 148
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
84-206 1.78e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 51.75  E-value: 1.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  84 PDDAVLDLACGKGGDLIK----WDKARIgyyVGIDIAEGSIEDCRTRYNGdadhhqrrkkfsfpSRLLCGDCFEVELDki 159
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALlaerFPGARV---TGVDLSPEMLARARARLPN--------------VRFVVADLRDLDPP-- 61

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42565060 160 leedAPFDICSCQFAMHysWTTEARArrALANVSALLRPGGVFIGTM 206
Cdd:COG4106  62 ----EPFDLVVSNAALH--WLPDHAA--LLARLAAALAPGGVLAVQV 100
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 79-203 1.16e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.70  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  79 QLYARPDDAVLDLACGKGGDLIKWDKaRIGYYV-GIDIAEGSIEDCRTRyngdadhhQRRKKFSFPSRLLCGDCFEveld 157
Cdd:COG2230  46 KLGLKPGMRVLDIGCGWGGLALYLAR-RYGVRVtGVTLSPEQLEYARER--------AAEAGLADRVEVRLADYRD---- 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 42565060 158 kiLEEDAPFD-ICSCQFAMHYSwttEARARRALANVSALLRPGGVFI 203
Cdd:COG2230 113 --LPADGQFDaIVSIGMFEHVG---PENYPAYFAKVARLLKPGGRLL 154
PRK08317 PRK08317
hypothetical protein; Provisional
 76-200 3.37e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.54  E-value: 3.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   76 VLIQLYARPDDAVLDLACGKGGDL--IKWDKARIGYYVGIDIAEGSIEDCRTRYNGDADhhqrrkkfsfPSRLLCGDCFE 153
Cdd:PRK08317  11 TFELLAVQPGDRVLDVGCGPGNDAreLARRVGPEGRVVGIDRSEAMLALAKERAAGLGP----------NVEFVRGDADG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 42565060  154 VELdkileEDAPFDIC-SCQFAMHYswtteARARRALANVSALLRPGG 200
Cdd:PRK08317  81 LPF-----PDGSFDAVrSDRVLQHL-----EDPARALAEIARVLRPGG 118
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 83-203 5.28e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.79  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060    83 RPDDAVLDLACGKGGDLIKWdkARI----GYYVGIDIAEGSIEDCRTRyngdadhhqRRKKFSFPSRLLCGDCFEVELdk 158
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFEL--AEElgpnAEVVGIDISEEAIEKAREN---------AQKLGFDNVEFEQGDIEELPE-- 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 42565060   159 iLEEDAPFDICSCQFAMHYSwtteARARRALANVSALLRPGGVFI 203
Cdd:pfam13847  69 -LLEDDKFDVVISNCVLNHI----PDPDKVLQEILRVLKPGGRLI 108
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 42-118 5.82e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.91  E-value: 5.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060   42 KVADHYSRrTNQTLeereaSPIIHLKklnnWIKSVLIQLYARPDDAVLDLACGKgGDL-IKWDKA--RIGYYVGIDIAEG 118
Cdd:PRK00216  19 SIAPKYDL-MNDLL-----SFGLHRV----WRRKTIKWLGVRPGDKVLDLACGT-GDLaIALAKAvgKTGEVVGLDFSEG 87
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 76-224 3.41e-03

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 38.01  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060  76 VLIQLY-ARPDDAVLDLACGKGGDLIkwDKARIGYYV-GIDIAEGSIEDCRT--RYNGDADHHqrrkkfsfpsrLLCGDC 151
Cdd:COG1041  17 ALVNLAgAKEGDTVLDPFCGTGTILI--EAGLLGRRViGSDIDPKMVEGAREnlEHYGYEDAD-----------VIRGDA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42565060 152 FEVELdkiLEE-------DAPFDICScqfamhySWTTEARA---RRALANVSALLRPGGVFIGTMPDanvIIKKLREAEG 221
Cdd:COG1041  84 RDLPL---ADEsvdaivtDPPYGRSS-------KISGEELLelyEKALEEAARVLKPGGRVVIVTPR---DIDELLEEAG 150


                ...
gi 42565060 222 LEI 224
Cdd:COG1041 151 FKV 153
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH