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Conserved domains on  [gi|15600308|ref|NP_253802|]
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hypothetical protein PA5115 [Pseudomonas aeruginosa PAO1]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11454891)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.-.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 17-130 4.30e-17

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


:

Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 74.58  E-value: 4.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  17 PNAFLKEHAQRLAGP----VLSVAEGEGRNAVFLAS-LGLEVLGVDGSTVGLAKARRLAEAKGVSiDTLVVDLADYE--P 89
Cdd:COG2230  36 QEAKLDLILRKLGLKpgmrVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRdlP 114

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600308  90 PAAAFGAVVSI--FAHLPSRVRGRLNRLLERSLRPGGLFLLEA 130
Cdd:COG2230 115 ADGQFDAIVSIgmFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 17-130 4.30e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 74.58  E-value: 4.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  17 PNAFLKEHAQRLAGP----VLSVAEGEGRNAVFLAS-LGLEVLGVDGSTVGLAKARRLAEAKGVSiDTLVVDLADYE--P 89
Cdd:COG2230  36 QEAKLDLILRKLGLKpgmrVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRdlP 114

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600308  90 PAAAFGAVVSI--FAHLPSRVRGRLNRLLERSLRPGGLFLLEA 130
Cdd:COG2230 115 ADGQFDAIVSIgmFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-124 4.56e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.89  E-value: 4.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308    32 VLSVAEGEGRNAVFLAS-LGLEVLGVDGSTVGLAKARRLAEAKGVSIDTLVVDLADYEPPAAAFGAVVSIFA--HLPSRV 108
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVlhHLPDPD 80

                          90
                  ....*....|....*.
gi 15600308   109 RGRLNRLLERSLRPGG 124
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 4-84 1.41e-05

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 44.16  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308    4 ERYAAEEYVYgTEPNAFLKEHAQRL-AGPVLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAKGVSIDTLVV 82
Cdd:PRK12335  96 EDYFHKKYNL-TATHSEVLEAVQTVkPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLY 174


                 ..
gi 15600308   83 DL 84
Cdd:PRK12335 175 DI 176
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 32-132 2.51e-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: 38.95  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  32 VLSVAEGEGRNAVFLASL-GLEVLGVDGSTVGLAKARR-LAEAKGVSIDTLVVDLADYEPPA-AAFGAVVSIFA-HLPSR 107
Cdd:cd02440   2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEELPPEAdESFDVIISDPPlHHLVE 81

                        90       100
                ....*....|....*....|....*
gi 15600308 108 VRGRLNRLLERSLRPGGLFLLEAYR 132
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 17-130 4.30e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 74.58  E-value: 4.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  17 PNAFLKEHAQRLAGP----VLSVAEGEGRNAVFLAS-LGLEVLGVDGSTVGLAKARRLAEAKGVSiDTLVVDLADYE--P 89
Cdd:COG2230  36 QEAKLDLILRKLGLKpgmrVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAGLA-DRVEVRLADYRdlP 114

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15600308  90 PAAAFGAVVSI--FAHLPSRVRGRLNRLLERSLRPGGLFLLEA 130
Cdd:COG2230 115 ADGQFDAIVSIgmFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 2-180 6.14e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 69.56  E-value: 6.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308   2 WDERYAAEeyvyGTEPNAFLKEHAQRLAGP--VLSVAEGEGRNAVFLASL-GLEVLGVDGSTVGLAKARRLAEAKGVS-I 77
Cdd:COG0500   2 WDSYYSDE----LLPGLAALLALLERLPKGgrVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLGnV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  78 DTLVVDLADYEP-PAAAFGAVVSIFA--HLPSRVRGRLNRLLERSLRPGGLFLLEAYRPEQLGRGTG-GPADVDMLVSRA 153
Cdd:COG0500  78 EFLVADLAELDPlPAESFDLVVAFGVlhHLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARlLLLATASLLELL 157

                       170       180
                ....*....|....*....|....*..
gi 15600308 154 ALEAELPECEVLLAREIEREVVEGRFH 180
Cdd:COG0500 158 LLLRLLALELYLRALLAAAATEDLRSD 184
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-124 4.56e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.89  E-value: 4.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308    32 VLSVAEGEGRNAVFLAS-LGLEVLGVDGSTVGLAKARRLAEAKGVSIDTLVVDLADYEPPAAAFGAVVSIFA--HLPSRV 108
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVlhHLPDPD 80

                          90
                  ....*....|....*.
gi 15600308   109 RGRLNRLLERSLRPGG 124
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 2-129 6.21e-14

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: 65.42  E-value: 6.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308   2 WDERYAAeeyvygtepnaFLKEHAQRlAGPVLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAkgVSIDTLV 81
Cdd:COG2227  10 WDRRLAA-----------LLARLLPA-GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAE--LNVDFVQ 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15600308  82 VDLADYEPPAAAFGAVVSI--FAHLPSRVRGrLNRLLeRSLRPGGLFLLE 129
Cdd:COG2227  76 GDLEDLPLEDGSFDLVICSevLEHLPDPAAL-LRELA-RLLKPGGLLLLS 123
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 19-134 2.63e-12

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: 61.55  E-value: 2.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  19 AFLKEHAQRLAGPVLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAKGVSIDTLVVDLADYEPPAAAFGAVV 98
Cdd:COG2226  13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVI 92

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15600308  99 SIFA--HLPSRVRGrLNRLLeRSLRPGGLFLL-EAYRPE 134
Cdd:COG2226  93 SSFVlhHLPDPERA-LAEIA-RVLKPGGRLVVvDFSPPD 129
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
19-167 7.00e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.47  E-value: 7.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  19 AFLKEHAQRLAGPVLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARrlaeAKGVSIDTLVVDLADYEPPAAAFGAVV 98
Cdd:COG4976  37 ELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAR----EKGVYDRLLVADLADLAEPDGRFDLIV 112

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600308  99 S--IFAHLpsrvrGRLNRLLE---RSLRPGGLFLLEAYRPEQLGRGTGGPADVdmlvsRAALEAELPECEVLLA 167
Cdd:COG4976 113 AadVLTYL-----GDLAAVFAgvaRALKPGGLFIFSVEDADGSGRYAHSLDYV-----RDLLAAAGFEVPGLLV 176
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
38-129 3.77e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.36  E-value: 3.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  38 GEGRNAVFLASL--GLEVLGVDGSTVGLAKARRLAEAkgvsIDTLVVDLADYEPPaAAFGAVVSIFA--HLPSRVRgRLN 113
Cdd:COG4106  11 GTGRLTALLAERfpGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLDPP-EPFDLVVSNAAlhWLPDHAA-LLA 84

                        90
                ....*....|....*.
gi 15600308 114 RLLeRSLRPGGLFLLE 129
Cdd:COG4106  85 RLA-AALAPGGVLAVQ 99
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 38-128 6.30e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 45.73  E-value: 6.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308    38 GEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAKGVSIdtLVVDLADYEPPAAAFGAVVSIFA--HLPSRVrgRLNRL 115
Cdd:pfam08241   6 GTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTF--VVGDAEDLPFPDNSFDLVLSSEVlhHVEDPE--RALRE 81

                          90
                  ....*....|...
gi 15600308   116 LERSLRPGGLFLL 128
Cdd:pfam08241  82 IARVLKPGGILII 94
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 4-84 1.41e-05

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 44.16  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308    4 ERYAAEEYVYgTEPNAFLKEHAQRL-AGPVLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAKGVSIDTLVV 82
Cdd:PRK12335  96 EDYFHKKYNL-TATHSEVLEAVQTVkPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLY 174


                 ..
gi 15600308   83 DL 84
Cdd:PRK12335 175 DI 176
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
3-84 9.60e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 41.26  E-value: 9.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308    3 DERYAAEEYVYgTEPNAFLKEHAQRLA-GPVLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAKGVS-IDTL 80
Cdd:PRK11207   5 DENYFTDKYGL-TRTHSEVLEAVKVVKpGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDnLHTA 83


                 ....
gi 15600308   81 VVDL 84
Cdd:PRK11207  84 VVDL 87
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 32-132 2.51e-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: 38.95  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308  32 VLSVAEGEGRNAVFLASL-GLEVLGVDGSTVGLAKARR-LAEAKGVSIDTLVVDLADYEPPA-AAFGAVVSIFA-HLPSR 107
Cdd:cd02440   2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKaAAALLADNVEVLKGDAEELPPEAdESFDVIISDPPlHHLVE 81

                        90       100
                ....*....|....*....|....*
gi 15600308 108 VRGRLNRLLERSLRPGGLFLLEAYR 132
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLTLVL 106
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
32-124 9.35e-03

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 35.71  E-value: 9.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600308   32 VLSVAEGEGRNAVFLASLGLEVLGVDGSTVGLAKARRLAEAKGVS-----IDTLVVDLADY-EPPA--AAFGAVVSIFAH 103
Cdd:PRK11036  48 VLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSdnmqfIHCAAQDIAQHlETPVdlILFHAVLEWVAD 127

                         90       100
                 ....*....|....*....|.
gi 15600308  104 lPSRVrgrLNRLLErSLRPGG 124
Cdd:PRK11036 128 -PKSV---LQTLWS-VLRPGG 143
 
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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