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Conserved domains on  [gi|568815662|ref|NP_001275588|]
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protein-L-histidine N-pros-methyltransferase isoform 3 [Homo sapiens]

Protein Classification

methyltransferase-like protein 9( domain architecture ID 11155959)

methyltransferase-like protein 9 (METTL9) is a protein-histidine N-methyltransferase that specifically catalyzes the 1-methylhistidine (pros-methylhistidine) methylation of target proteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DREV pfam05219
DREV methyltransferase; This family contains DREV protein homologs from several eukaryotes. ...
 16-277 9.27e-170

DREV methyltransferase; This family contains DREV protein homologs from several eukaryotes. The function of this protein is unknown. However, these proteins appear to be related to other methyltransferases (Bateman A pers obs).


:

Pssm-ID: 253097  Cd Length: 265  Bit Score: 469.75  E-value: 9.27e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   16 WYVCNREkLCESLQAVFVQSYLDQGTQIFLNNSIEKSGWLFIQLYHSFVSSVFSLFMSRTSINGLLGRGSMFVFSPDQFQ 95
Cdd:pfam05219   1 WYCLNHE-LPPRFQSKFVPSEPDATTQSFLENSKALSANIFTQLWHALARSILSFFMSQTDINGFLGRGSMFIFSEEQFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   96 RLLKI-----NPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKKKYRVLGINEWQNTGFQYDVISCLN 170
Cdd:pfam05219  80 KLLVIggfqpASGQEPVTLLDLGAGDGEITLRMAPTFEEVYATELSWTMRDRLKKKNYNVLTEIEWQETDVNLDLILCLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  171 LLDRCDQPLTLLKDIRSVLEPtRGRVILALVLPFHPYVENVGGKWEKPSEILEIKGQNWEEQVNSLPEVFRKAGFVIEAF 250
Cdd:pfam05219 160 LLDRCFDPFKLLEDIHLALAP-NGRVIVALVLPYMHYVETNTGSHLPPRPLLENNGASFEEEVARFMEVFENAGFRVEAW 238

                         250       260
                  ....*....|....*....|....*..
gi 568815662  251 TRLPYLCEGDMYNDYYVLDDAVFVLKP 277
Cdd:pfam05219 239 TRLPYLCEGDMHNSFYWLIDAIFVLKP 265
 
Name Accession Description Interval E-value
DREV pfam05219
DREV methyltransferase; This family contains DREV protein homologs from several eukaryotes. ...
 16-277 9.27e-170

DREV methyltransferase; This family contains DREV protein homologs from several eukaryotes. The function of this protein is unknown. However, these proteins appear to be related to other methyltransferases (Bateman A pers obs).


Pssm-ID: 253097  Cd Length: 265  Bit Score: 469.75  E-value: 9.27e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   16 WYVCNREkLCESLQAVFVQSYLDQGTQIFLNNSIEKSGWLFIQLYHSFVSSVFSLFMSRTSINGLLGRGSMFVFSPDQFQ 95
Cdd:pfam05219   1 WYCLNHE-LPPRFQSKFVPSEPDATTQSFLENSKALSANIFTQLWHALARSILSFFMSQTDINGFLGRGSMFIFSEEQFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   96 RLLKI-----NPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKKKYRVLGINEWQNTGFQYDVISCLN 170
Cdd:pfam05219  80 KLLVIggfqpASGQEPVTLLDLGAGDGEITLRMAPTFEEVYATELSWTMRDRLKKKNYNVLTEIEWQETDVNLDLILCLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  171 LLDRCDQPLTLLKDIRSVLEPtRGRVILALVLPFHPYVENVGGKWEKPSEILEIKGQNWEEQVNSLPEVFRKAGFVIEAF 250
Cdd:pfam05219 160 LLDRCFDPFKLLEDIHLALAP-NGRVIVALVLPYMHYVETNTGSHLPPRPLLENNGASFEEEVARFMEVFENAGFRVEAW 238

                         250       260
                  ....*....|....*....|....*..
gi 568815662  251 TRLPYLCEGDMYNDYYVLDDAVFVLKP 277
Cdd:pfam05219 239 TRLPYLCEGDMHNSFYWLIDAIFVLKP 265
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 108-199 2.02e-12

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: 62.73  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 108 RLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKK------KYRVLGINEWQNTGFQYDVISCLNLLDRCDQPLTL 181
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaelnvDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDPAAL 106

                         90
                 ....*....|....*...
gi 568815662 182 LKDIRSVLEPtRGRVILA 199
Cdd:COG2227  107 LRELARLLKP-GGLLLLS 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 108-202 7.21e-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: 38.18  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 108 RLLDLGAGDGEVT-KIMSPHFEEIYATELSETMIWQLQKKKYRVLG---------INEWQNTGF-QYD-VISCLNLLDRC 175
Cdd:cd02440    1 RVLDLGCGTGALAlALASGPGARVTGVDISPVALELARKAAAALLAdnvevlkgdAEELPPEADeSFDvIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 568815662 176 DQPLTLLKDIRSVLEPtRGRVILALVL 202
Cdd:cd02440   81 EDLARFLEEARRLLKP-GGVLVLTLVL 106
 
Name Accession Description Interval E-value
DREV pfam05219
DREV methyltransferase; This family contains DREV protein homologs from several eukaryotes. ...
 16-277 9.27e-170

DREV methyltransferase; This family contains DREV protein homologs from several eukaryotes. The function of this protein is unknown. However, these proteins appear to be related to other methyltransferases (Bateman A pers obs).


Pssm-ID: 253097  Cd Length: 265  Bit Score: 469.75  E-value: 9.27e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   16 WYVCNREkLCESLQAVFVQSYLDQGTQIFLNNSIEKSGWLFIQLYHSFVSSVFSLFMSRTSINGLLGRGSMFVFSPDQFQ 95
Cdd:pfam05219   1 WYCLNHE-LPPRFQSKFVPSEPDATTQSFLENSKALSANIFTQLWHALARSILSFFMSQTDINGFLGRGSMFIFSEEQFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   96 RLLKI-----NPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKKKYRVLGINEWQNTGFQYDVISCLN 170
Cdd:pfam05219  80 KLLVIggfqpASGQEPVTLLDLGAGDGEITLRMAPTFEEVYATELSWTMRDRLKKKNYNVLTEIEWQETDVNLDLILCLN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  171 LLDRCDQPLTLLKDIRSVLEPtRGRVILALVLPFHPYVENVGGKWEKPSEILEIKGQNWEEQVNSLPEVFRKAGFVIEAF 250
Cdd:pfam05219 160 LLDRCFDPFKLLEDIHLALAP-NGRVIVALVLPYMHYVETNTGSHLPPRPLLENNGASFEEEVARFMEVFENAGFRVEAW 238

                         250       260
                  ....*....|....*....|....*..
gi 568815662  251 TRLPYLCEGDMYNDYYVLDDAVFVLKP 277
Cdd:pfam05219 239 TRLPYLCEGDMHNSFYWLIDAIFVLKP 265
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 108-199 2.02e-12

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: 62.73  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 108 RLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKK------KYRVLGINEWQNTGFQYDVISCLNLLDRCDQPLTL 181
Cdd:COG2227   27 RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERaaelnvDFVQGDLEDLPLEDGSFDLVICSEVLEHLPDPAAL 106

                         90
                 ....*....|....*...
gi 568815662 182 LKDIRSVLEPtRGRVILA 199
Cdd:COG2227  107 LRELARLLKP-GGLLLLS 123
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 92-199 8.18e-10

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: 56.16  E-value: 8.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  92 DQFQRLLKINPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIwQLQKKKYRVLGIN------EWQNTGF---Q 162
Cdd:COG2226    9 DGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEML-ELARERAAEAGLNvefvvgDAEDLPFpdgS 87

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568815662 163 YDVISCLNLLDRCDQPLTLLKDIRSVLEPtRGRVILA 199
Cdd:COG2226   88 FDLVISSFVLHHLPDPERALAEIARVLKP-GGRLVVV 123
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 110-191 5.69e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.37  E-value: 5.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  110 LDLGAGDGEVTKIMSPHFE--EIYATELSETMIWQLQKK----------KYRVLGINEWQNTGFQYDVISCLNLLDRCDQ 177
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPglEYTGLDISPAALEAARERlaalgllnavRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....
gi 568815662  178 PLTLLKDIRSVLEP 191
Cdd:pfam08242  81 PRAVLRNIRRLLKP 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 95-249 8.83e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 53.59  E-value: 8.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662   95 QRLLKINPDWKthRLLDLGAGDGEVTKIMSPHFEEIYATELSETMI-WQLQKKKYRVLGINEWQNTGFQYDVISCLNLLD 173
Cdd:pfam13489  14 LRLLPKLPSPG--RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIeRALLNVRFDQFDEQEAAVPAGKFDVIVAREVLE 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568815662  174 RCDQPLTLLKDIRSVLEPtRGRVILALVLPFHpYVENVGGKWEKPSEILEiKGQNWEEQvnSLPEVFRKAGFVIEA 249
Cdd:pfam13489  92 HVPDPPALLRQIAALLKP-GGLLLLSTPLASD-EADRLLLEWPYLRPRNG-HISLFSAR--SLKRLLEEAGFEVVS 162
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
94-191 4.28e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.92  E-value: 4.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  94 FQRLLKINPDWKTHRLLDLGAGDGEVTKIMSPHFEEIYATELSETMIWQLQKK----KYRVLGINEWQNTGFQYDVISCL 169
Cdd:COG4976   35 AEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKgvydRLLVADLADLAEPDGRFDLIVAA 114

                         90       100
                 ....*....|....*....|..
gi 568815662 170 NLLDRCDQPLTLLKDIRSVLEP 191
Cdd:COG4976  115 DVLTYLGDLAAVFAGVARALKP 136
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 110-198 1.23e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.43  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  110 LDLGAGDGEVTKIMSPHFEEIYATELSETMIwQLQKKKYRVLGINEWQNTGFQ-------YDVISCLNLLDRCDQPLTLL 182
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEML-ELAREKAPREGLTFVVGDAEDlpfpdnsFDLVLSSEVLHHVEDPERAL 79

                          90
                  ....*....|....*.
gi 568815662  183 KDIRSVLEPtRGRVIL 198
Cdd:pfam08241  80 REIARVLKP-GGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
108-198 1.65e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 48.28  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 108 RLLDLGAGDGEVTKIMSPHFE--EIYATELSETMIWQLQKK----KYRVLGINEWQNTGfQYDVISCLNLLDRCDQPLTL 181
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPgaRVTGVDLSPEMLARARARlpnvRFVVADLRDLDPPE-PFDLVVSNAALHWLPDHAAL 82

                         90
                 ....*....|....*..
gi 568815662 182 LKDIRSVLEPtRGRVIL 198
Cdd:COG4106   83 LARLAAALAP-GGVLAV 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 110-191 2.15e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 45.25  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662  110 LDLGAGDGEVTKIMSPHFE-EIYATELSETMIWQLQKK--------KYRVLGINEWQNTGFQYDVISCLNLLDRCDQP-- 178
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERaaeaglnvEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPdl 81

                          90
                  ....*....|...
gi 568815662  179 LTLLKDIRSVLEP 191
Cdd:pfam13649  82 EAALREIARVLKP 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 108-202 7.21e-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: 38.18  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 108 RLLDLGAGDGEVT-KIMSPHFEEIYATELSETMIWQLQKKKYRVLG---------INEWQNTGF-QYD-VISCLNLLDRC 175
Cdd:cd02440    1 RVLDLGCGTGALAlALASGPGARVTGVDISPVALELARKAAAALLAdnvevlkgdAEELPPEADeSFDvIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 568815662 176 DQPLTLLKDIRSVLEPtRGRVILALVL 202
Cdd:cd02440   81 EDLARFLEEARRLLKP-GGVLVLTLVL 106
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 108-255 7.51e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 36.82  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 108 RLLDLGAGDGEVTKIMSPHF-EEIYATELSETMIWQLQKK---------KYRVLGINEWQNTGFQ-YDVISCLNLLDRCD 176
Cdd:COG0500   29 RVLDLGCGTGRNLLALAARFgGRVIGIDLSPEAIALARARaakaglgnvEFLVADLAELDPLPAEsFDLVVAFGVLHHLP 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568815662 177 --QPLTLLKDIRSVLEPTrGRVILALVLPFHPYVENVGGKWEKPSEILEIKGQNWeEQVNSLPEVFRKAGFVIEAFTRLP 254
Cdd:COG0500  109 peEREALLRELARALKPG-GVLLLSASDAAAALSLARLLLLATASLLELLLLLRL-LALELYLRALLAAAATEDLRSDAL 186


                 .
gi 568815662 255 Y 255
Cdd:COG0500  187 L 187
 
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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