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Conserved domains on  [gi|25188199|ref|NP_055608|]
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tRNA wybutosine-synthesizing protein 4 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10007192)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Streptomyces glaucescens tetracenomycin polyketide synthesis O-methyltransferase TcmP, which catalyzes the methylation of the C-9 carboxy group of tetracenomycin E

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
26-280 1.45e-16

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442544  Cd Length: 246  Bit Score: 79.62  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199  26 SLAARGYVQDPFAALLVPGAAR------RAPLIHRGYYVRARAVRHCVRAFLeqigapqAALRAQILSLGAGFDSLYFRL 99
Cdd:COG3315   2 SRRPDPLFRDPYAARLVGAIGYdfsrllAGRGLRLGVAARTRFFDDLLRAAL-------AAGIAQVVILGAGLDTRAYRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199 100 ktaGRLARAAVWEVDFPDVARRKAERIGEtpelcaltgpfergepasalCFESADYCILGLDLRQ---LQRVEEALGAAG 176
Cdd:COG3315  75 ---DNPGGVRWFEVDLPEVIALKRRLLPE--------------------LGPPARLRLVAVDLRDpdwPDALPAAGFDPS 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199 177 LdaasPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRP----QDAFGQFMLQHFRQLNSPLHGLERFPDVE 252
Cdd:COG3315 132 R----PTLFIAEGVLMYLTEEAVRALLRRIAALFPPGSELAFDYVPPlalkGSKKHPAVRKLRRDLGAPFKFGIDPDDPA 207
                       250       260
                ....*....|....*....|....*...
gi 25188199 253 AQrrrFLQAGWTACGAVDMNEFYHCFLP 280
Cdd:COG3315 208 EL---LEEPGWRLVEELSPLELLARYLP 232
 
Name Accession Description Interval E-value
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
26-280 1.45e-16

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 79.62  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199  26 SLAARGYVQDPFAALLVPGAAR------RAPLIHRGYYVRARAVRHCVRAFLeqigapqAALRAQILSLGAGFDSLYFRL 99
Cdd:COG3315   2 SRRPDPLFRDPYAARLVGAIGYdfsrllAGRGLRLGVAARTRFFDDLLRAAL-------AAGIAQVVILGAGLDTRAYRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199 100 ktaGRLARAAVWEVDFPDVARRKAERIGEtpelcaltgpfergepasalCFESADYCILGLDLRQ---LQRVEEALGAAG 176
Cdd:COG3315  75 ---DNPGGVRWFEVDLPEVIALKRRLLPE--------------------LGPPARLRLVAVDLRDpdwPDALPAAGFDPS 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199 177 LdaasPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRP----QDAFGQFMLQHFRQLNSPLHGLERFPDVE 252
Cdd:COG3315 132 R----PTLFIAEGVLMYLTEEAVRALLRRIAALFPPGSELAFDYVPPlalkGSKKHPAVRKLRRDLGAPFKFGIDPDDPA 207
                       250       260
                ....*....|....*....|....*...
gi 25188199 253 AQrrrFLQAGWTACGAVDMNEFYHCFLP 280
Cdd:COG3315 208 EL---LEEPGWRLVEELSPLELLARYLP 232
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
28-197 5.02e-15

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


Pssm-ID: 427692  Cd Length: 188  Bit Score: 73.81  E-value: 5.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199    28 AARGYVQDPFAALLV----------------------PGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGApqaalrAQI 85
Cdd:pfam04072  15 PADPLIDDPFAEPLVraagldlltrradgeldpakddPGKWARFPGLNDGIAVRTRFFDDFLLAALAAAGI------RQV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199    86 LSLGAGFDSLYFRLKtagRLARAAVWEVDFPDVARRKAERIGE-----TPELCALTGPFERGEPASALcfESAdycilGL 160
Cdd:pfam04072  89 VILGAGLDTRAYRLP---WPAGTRVFEVDQPDVLEFKRETLAElgalpPAHRRYVPVDLRDDDWPEAL--RAA-----GF 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 25188199   161 DLRQlqrveealgaagldaasPTLLLAEAVLTYLEPE 197
Cdd:pfam04072 159 DPEQ-----------------PTAWLAEGLLYYLPPE 178
mthyl_TIGR00027 TIGR00027
methyltransferase, TIGR00027 family; This model represents a set of probable ...
33-197 2.09e-07

methyltransferase, TIGR00027 family; This model represents a set of probable methyltransferases, about 300 amino acids long, with essentially full length homology. Members share an N-terminal region described by Pfam model pfam02409. Included are a paralogous family of 12 proteins in Mycobacterium tuberculosis, plus close homologs in related species, a family of 8 in the archaeon Methanosarcina acetivorans, and small numbers of members in other species, including plants. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272862  Cd Length: 260  Bit Score: 52.70  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199    33 VQDPFAALLVPGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGAPQ--------AALRA---QILSLGAGFDSLYFRLKt 101
Cdd:TIGR00027  22 FRDPYAAAFLGAAGRAAMPLDGLLRADAGAYDGLLRGFADFIAVRTrffddfllAAVAAgirQVVILGAGLDTRAYRLP- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199   102 agRLARAAVWEVDFPDVARRKAERIGEtpelcaltgpfERGEPASALCFesadyciLGLDLRQlqRVEEALGAAGLDAAS 181
Cdd:TIGR00027 101 --WPDGTRVFEVDQPAVLAFKEKVLAE-----------LGAEPPAHRRA-------VPVDLRQ--DWPAALAAAGFDPTA 158
                         170
                  ....*....|....*.
gi 25188199   182 PTLLLAEAVLTYLEPE 197
Cdd:TIGR00027 159 PTAWLWEGLLMYLTEE 174
 
Name Accession Description Interval E-value
YktD COG3315
O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, ...
26-280 1.45e-16

O-Methyltransferase involved in polyketide biosynthesis [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442544  Cd Length: 246  Bit Score: 79.62  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199  26 SLAARGYVQDPFAALLVPGAAR------RAPLIHRGYYVRARAVRHCVRAFLeqigapqAALRAQILSLGAGFDSLYFRL 99
Cdd:COG3315   2 SRRPDPLFRDPYAARLVGAIGYdfsrllAGRGLRLGVAARTRFFDDLLRAAL-------AAGIAQVVILGAGLDTRAYRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199 100 ktaGRLARAAVWEVDFPDVARRKAERIGEtpelcaltgpfergepasalCFESADYCILGLDLRQ---LQRVEEALGAAG 176
Cdd:COG3315  75 ---DNPGGVRWFEVDLPEVIALKRRLLPE--------------------LGPPARLRLVAVDLRDpdwPDALPAAGFDPS 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199 177 LdaasPTLLLAEAVLTYLEPESAAALIAWAAQRFPNALFVVYEQMRP----QDAFGQFMLQHFRQLNSPLHGLERFPDVE 252
Cdd:COG3315 132 R----PTLFIAEGVLMYLTEEAVRALLRRIAALFPPGSELAFDYVPPlalkGSKKHPAVRKLRRDLGAPFKFGIDPDDPA 207
                       250       260
                ....*....|....*....|....*...
gi 25188199 253 AQrrrFLQAGWTACGAVDMNEFYHCFLP 280
Cdd:COG3315 208 EL---LEEPGWRLVEELSPLELLARYLP 232
LCM pfam04072
Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. ...
28-197 5.02e-15

Leucine carboxyl methyltransferase; Family of leucine carboxyl methyltransferases EC:2.1.1.-. This family may need divides a the full alignment contains a significantly shorter mouse sequence.


Pssm-ID: 427692  Cd Length: 188  Bit Score: 73.81  E-value: 5.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199    28 AARGYVQDPFAALLV----------------------PGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGApqaalrAQI 85
Cdd:pfam04072  15 PADPLIDDPFAEPLVraagldlltrradgeldpakddPGKWARFPGLNDGIAVRTRFFDDFLLAALAAAGI------RQV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199    86 LSLGAGFDSLYFRLKtagRLARAAVWEVDFPDVARRKAERIGE-----TPELCALTGPFERGEPASALcfESAdycilGL 160
Cdd:pfam04072  89 VILGAGLDTRAYRLP---WPAGTRVFEVDQPDVLEFKRETLAElgalpPAHRRYVPVDLRDDDWPEAL--RAA-----GF 158
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 25188199   161 DLRQlqrveealgaagldaasPTLLLAEAVLTYLEPE 197
Cdd:pfam04072 159 DPEQ-----------------PTAWLAEGLLYYLPPE 178
mthyl_TIGR00027 TIGR00027
methyltransferase, TIGR00027 family; This model represents a set of probable ...
33-197 2.09e-07

methyltransferase, TIGR00027 family; This model represents a set of probable methyltransferases, about 300 amino acids long, with essentially full length homology. Members share an N-terminal region described by Pfam model pfam02409. Included are a paralogous family of 12 proteins in Mycobacterium tuberculosis, plus close homologs in related species, a family of 8 in the archaeon Methanosarcina acetivorans, and small numbers of members in other species, including plants. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272862  Cd Length: 260  Bit Score: 52.70  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199    33 VQDPFAALLVPGAARRAPLIHRGYYVRARAVRHCVRAFLEQIGAPQ--------AALRA---QILSLGAGFDSLYFRLKt 101
Cdd:TIGR00027  22 FRDPYAAAFLGAAGRAAMPLDGLLRADAGAYDGLLRGFADFIAVRTrffddfllAAVAAgirQVVILGAGLDTRAYRLP- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25188199   102 agRLARAAVWEVDFPDVARRKAERIGEtpelcaltgpfERGEPASALCFesadyciLGLDLRQlqRVEEALGAAGLDAAS 181
Cdd:TIGR00027 101 --WPDGTRVFEVDQPAVLAFKEKVLAE-----------LGAEPPAHRRA-------VPVDLRQ--DWPAALAAAGFDPTA 158
                         170
                  ....*....|....*.
gi 25188199   182 PTLLLAEAVLTYLEPE 197
Cdd:TIGR00027 159 PTAWLWEGLLMYLTEE 174
 
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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