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Conserved domains on  [gi|1232315491|gb|OYV96580|]
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MAG: hypothetical protein B7Z73_00475 [Planctomycetia bacterium 21-64-5]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10606006)

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 histamine N-methyltransferase

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
PubMed:  12826405|12504684

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-230 9.28e-29

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


:

Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 108.67  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  84 IRLLKRIAGDGR-GKRLLDVGCGDGGFLRAAQRLGWQVSGTELEPQQARSLGLDVRAEIDDFRA----SEKFDCVTFWHS 158
Cdd:pfam13489  10 ADLLLRLLPKLPsPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEaavpAGKFDVIVAREV 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315491 159 LEHLPRPHEALRQARERLQPGGVLLVSVPDAGGWQARLFgRHWLHLDVP-RHLFHFNRPSLARLLETTGFVLV 230
Cdd:pfam13489  90 LEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLL-LEWPYLRPRnGHISLFSARSLKRLLEEAGFEVV 161
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-230 9.28e-29

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 108.67  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  84 IRLLKRIAGDGR-GKRLLDVGCGDGGFLRAAQRLGWQVSGTELEPQQARSLGLDVRAEIDDFRA----SEKFDCVTFWHS 158
Cdd:pfam13489  10 ADLLLRLLPKLPsPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEaavpAGKFDVIVAREV 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315491 159 LEHLPRPHEALRQARERLQPGGVLLVSVPDAGGWQARLFgRHWLHLDVP-RHLFHFNRPSLARLLETTGFVLV 230
Cdd:pfam13489  90 LEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLL-LEWPYLRPRnGHISLFSARSLKRLLEEAGFEVV 161
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 75-188 5.02e-26

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: 100.09  E-value: 5.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  75 TAGYRIWRR--IRLLKRIAGdgRGKRLLDVGCGDGGFLRAAQRLGWQVSGTELEPQ-----QARSLGLDVRAEIDDFR-- 145
Cdd:COG2227     4 PDARDFWDRrlAALLARLLP--AGGRVLDVGCGTGRLALALARRGADVTGVDISPEaleiaRERAAELNVDFVQGDLEdl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1232315491 146 --ASEKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSVPD 188
Cdd:COG2227    82 plEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 98-186 5.33e-11

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: 58.60  E-value: 5.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  98 RLLDVGCGDGGF-LRAAQRLGWQVSGTELEP------QQARSLGLDVRAEI-------DDFRASEKFDCVTFWHSLEHLP 163
Cdd:cd02440     1 RVLDLGCGTGALaLALASGPGARVTGVDISPvalelaRKAAAALLADNVEVlkgdaeeLPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 1232315491 164 -RPHEALRQARERLQPGGVLLVSV 186
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 81-229 9.56e-11

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 60.77  E-value: 9.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  81 WRRIRLLKRIAGDGRGKRLLDVGCGdGGFLRAA-QRLGWQVSGTELEPQ---------QARSLGLDVRAE-IDDF--RAS 147
Cdd:TIGR01983  32 YIRDRIRKNFKNPLDGLRVLDVGCG-GGLLSEPlARLGANVTGIDASEEnievaklhaKKDPLQIDYRCTtVEDLaeKKA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 148 EKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSV--PDAGGWQARLFGRHWLHLDVPRHLFHFN---RPS-LARL 221
Cdd:TIGR01983 111 GSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTinRTPKSYLLAIVGAEYILRIVPKGTHDWEkfiKPSeLLSW 190


                  ....*...
gi 1232315491 222 LETTGFVL 229
Cdd:TIGR01983 191 LESAGLRV 198
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
95-184 1.01e-05

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 46.76  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  95 RGKRLLDVGCGDGGFLR-AAQRLGWQVSGTELEPQQA-----RSLGLDVRAEIDDFRA-SEKFDCVTFWHSLEHL-PRPH 166
Cdd:PRK11705  167 PGMRVLDIGCGWGGLARyAAEHYGVSVVGVTISAEQQklaqeRCAGLPVEIRLQDYRDlNGQFDRIVSVGMFEHVgPKNY 246

                          90
                  ....*....|....*....
gi 1232315491 167 EA-LRQARERLQPGGVLLV 184
Cdd:PRK11705  247 RTyFEVVRRCLKPDGLFLL 265
 
Name Accession Description Interval E-value
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 84-230 9.28e-29

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 108.67  E-value: 9.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  84 IRLLKRIAGDGR-GKRLLDVGCGDGGFLRAAQRLGWQVSGTELEPQQARSLGLDVRAEIDDFRA----SEKFDCVTFWHS 158
Cdd:pfam13489  10 ADLLLRLLPKLPsPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEaavpAGKFDVIVAREV 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315491 159 LEHLPRPHEALRQARERLQPGGVLLVSVPDAGGWQARLFgRHWLHLDVP-RHLFHFNRPSLARLLETTGFVLV 230
Cdd:pfam13489  90 LEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLL-LEWPYLRPRnGHISLFSARSLKRLLEEAGFEVV 161
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 75-188 5.02e-26

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: 100.09  E-value: 5.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  75 TAGYRIWRR--IRLLKRIAGdgRGKRLLDVGCGDGGFLRAAQRLGWQVSGTELEPQ-----QARSLGLDVRAEIDDFR-- 145
Cdd:COG2227     4 PDARDFWDRrlAALLARLLP--AGGRVLDVGCGTGRLALALARRGADVTGVDISPEaleiaRERAAELNVDFVQGDLEdl 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1232315491 146 --ASEKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSVPD 188
Cdd:COG2227    82 plEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 79-196 8.18e-19

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: 81.58  E-value: 8.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  79 RIWRRIRLLKRIAGDGRGKRLLDVGCGDGGFLRAAQRLGWQVSGTELEP-------QQARSLGLDVRAEIDDFR----AS 147
Cdd:COG2226     6 ARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPemlelarERAAEAGLNVEFVVGDAEdlpfPD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1232315491 148 EKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSV---PDAGGWQARL 196
Cdd:COG2226    86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDfspPDLAELEELL 137
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 59-187 9.88e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 81.51  E-value: 9.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  59 DLGRFYRSYHGNRHGITAGYRIWRRIRLLKRIAGDGRGKRLLDVGCGDGGF-LRAAQRLGWQVSGTELEPQQ-------A 130
Cdd:COG2230    15 DPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLaLYLARRYGVRVTGVTLSPEQleyarerA 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232315491 131 RSLGLDVRAEI-----DDFRASEKFDCVTFWHSLEHLPRPH--EALRQARERLQPGGVLLVSVP 187
Cdd:COG2230    95 AEAGLADRVEVrladyRDLPADGQFDAIVSIGMFEHVGPENypAYFAKVARLLKPGGRLLLHTP 158
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
75-233 7.32e-18

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 80.04  E-value: 7.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  75 TAGYRIWRRI--RLLKRIAGdGRGKRLLDVGCGDGGFLRAAQRLGWQVSGTELEP---QQARSLGLDVRAEIDDFRA--- 146
Cdd:COG4976    25 DLGYEAPALLaeELLARLPP-GPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEemlAKAREKGVYDRLLVADLADlae 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 147 -SEKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSVPDAGGwqarlfgrhwlhldvpRHLFHFNRPSLARLLETT 225
Cdd:COG4976   104 pDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADG----------------SGRYAHSLDYVRDLLAAA 167


                  ....*...
gi 1232315491 226 GFVLVGHW 233
Cdd:COG4976   168 GFEVPGLL 175
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
95-186 3.06e-16

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 72.93  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  95 RGKRLLDVGCGDGGFLRA-AQRL-GWQVSGTELEP---QQARSLGLDVR---AEIDDFRASEKFDCVTFWHSLEHLPRPH 166
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALlAERFpGARVTGVDLSPemlARARARLPNVRfvvADLRDLDPPEPFDLVVSNAALHWLPDHA 80

                          90       100
                  ....*....|....*....|
gi 1232315491 167 EALRQARERLQPGGVLLVSV 186
Cdd:COG4106    81 ALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 100-180 3.69e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 67.20  E-value: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 100 LDVGCGDGGFLRA-AQRLGWQVSGTELEP-------QQARSLGLDVRAEIDDFR----ASEKFDCVTFWHSLEHLPRP-- 165
Cdd:pfam13649   2 LDLGCGTGRLTLAlARRGGARVTGVDLSPemlerarERAAEAGLNVEFVQGDAEdlpfPDGSFDLVVSSGVLHHLPDPdl 81

                          90
                  ....*....|....*
gi 1232315491 166 HEALRQARERLQPGG 180
Cdd:pfam13649  82 EAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 95-189 1.29e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.71  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  95 RGKRLLDVGCGDGGFLRA-AQRLGWQVSGTELEP-------QQARSLGLD-VRAEIDDFRAS-----EKFDCVTFWHSLE 160
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLAlAARFGGRVIGIDLSPeaialarARAAKAGLGnVEFLVADLAELdplpaESFDLVVAFGVLH 105

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315491 161 HLP--RPHEALRQARERLQPGGVLLVSVPDA 189
Cdd:COG0500   106 HLPpeEREALLRELARALKPGGVLLLSASDA 136
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-184 1.20e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 59.99  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 100 LDVGCGDGGFLRAAQRLGWQVSGTELEPQQARSLGLDVRAEIDDFR---------ASEKFDCVTFWHSLEHLPRPHEALR 170
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLTFVvgdaedlpfPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 1232315491 171 QARERLQPGGVLLV 184
Cdd:pfam08241  81 EIARVLKPGGILII 94
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 100-182 1.36e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.07  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 100 LDVGCGDGGFLR--AAQRLGWQVSGTELEP-------QQARSLG------LDVRAEIDDFRASEKFDCVTFWHSLEHLPR 164
Cdd:pfam08242   1 LEIGCGTGTLLRalLEALPGLEYTGLDISPaaleaarERLAALGllnavrVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1232315491 165 PHEALRQARERLQPGGVL 182
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 98-186 5.33e-11

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: 58.60  E-value: 5.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  98 RLLDVGCGDGGF-LRAAQRLGWQVSGTELEP------QQARSLGLDVRAEI-------DDFRASEKFDCVTFWHSLEHLP 163
Cdd:cd02440     1 RVLDLGCGTGALaLALASGPGARVTGVDISPvalelaRKAAAALLADNVEVlkgdaeeLPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 1232315491 164 -RPHEALRQARERLQPGGVLLVSV 186
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 81-229 9.56e-11

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 60.77  E-value: 9.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  81 WRRIRLLKRIAGDGRGKRLLDVGCGdGGFLRAA-QRLGWQVSGTELEPQ---------QARSLGLDVRAE-IDDF--RAS 147
Cdd:TIGR01983  32 YIRDRIRKNFKNPLDGLRVLDVGCG-GGLLSEPlARLGANVTGIDASEEnievaklhaKKDPLQIDYRCTtVEDLaeKKA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 148 EKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSV--PDAGGWQARLFGRHWLHLDVPRHLFHFN---RPS-LARL 221
Cdd:TIGR01983 111 GSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTinRTPKSYLLAIVGAEYILRIVPKGTHDWEkfiKPSeLLSW 190


                  ....*...
gi 1232315491 222 LETTGFVL 229
Cdd:TIGR01983 191 LESAGLRV 198
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 93-194 5.95e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.18  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  93 DGRGKRLLDVGCGDGGFL-RAAQRLGWQ--VSGTELEP-------QQARSLGLD-VRAEIDDF------RASEKFDCVTF 155
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSfELAEELGPNaeVVGIDISEeaiekarENAQKLGFDnVEFEQGDIeelpelLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232315491 156 WHSLEHLPRPHEALRQARERLQPGGVLLVSVPDAGGWQA 194
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELP 119
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
95-184 1.01e-05

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 46.76  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  95 RGKRLLDVGCGDGGFLR-AAQRLGWQVSGTELEPQQA-----RSLGLDVRAEIDDFRA-SEKFDCVTFWHSLEHL-PRPH 166
Cdd:PRK11705  167 PGMRVLDIGCGWGGLARyAAEHYGVSVVGVTISAEQQklaqeRCAGLPVEIRLQDYRDlNGQFDRIVSVGMFEHVgPKNY 246

                          90
                  ....*....|....*....
gi 1232315491 167 EA-LRQARERLQPGGVLLV 184
Cdd:PRK11705  247 RTyFEVVRRCLKPDGLFLL 265
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 79-232 1.78e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.14  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  79 RIWRR--IRLLkriaGDGRGKRLLDVGCGDG----GFLRAAQRLGWqVSGTE-----LEPQQARSLGLDVRAEIDdFR-- 145
Cdd:PRK00216   37 RVWRRktIKWL----GVRPGDKVLDLACGTGdlaiALAKAVGKTGE-VVGLDfsegmLAVGREKLRDLGLSGNVE-FVqg 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491 146 -------ASEKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLV---SVPDAGGWQ--------------ARLFGR-- 199
Cdd:PRK00216  111 daealpfPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVIlefSKPTNPPLKkaydfylfkvlpliGKLISKna 190

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1232315491 200 ---HWLhldvPRHLFHF-NRPSLARLLETTGFVLVGH 232
Cdd:PRK00216  191 eaySYL----AESIRAFpDQEELAAMLEEAGFERVRY 223
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 81-183 4.37e-05

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 44.70  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  81 WRRIRLLKRIAgDGRGKRLLDVGCGDGGFLraaqrlgWQVSGTE------LEPQQ---------ARSLGLDVRAE----- 140
Cdd:pfam08003 102 WKWDRVLPHLS-PLKGRTILDVGCGNGYHM-------WRMLGEGaamvvgIDPSElflcqfeavRKLLGNDQRAHllplg 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1232315491 141 IDDFRASEKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLL 183
Cdd:pfam08003 174 IEQLPALAAFDTVFSMGVLYHRRSPLDHLLQLKDQLVKGGELV 216
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 82-184 9.35e-05

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 43.47  E-value: 9.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  82 RRIRLLKRIAGDGRGKRLLDVGCGDGGFL-RAAQRLGWQVSGTELEPQQAR-------SLGLDVRAEID-----DFRasE 148
Cdd:pfam02353  48 AKLDLILDKLGLKPGMTLLDIGCGWGGLMrRAAERYDVNVVGLTLSKNQYKlarkrvaAEGLARKVEVLlqdyrDFD--E 125

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315491 149 KFDCVTFWHSLEHL-PRPHEALRQARER-LQPGGVLLV 184
Cdd:pfam02353 126 PFDRIVSVGMFEHVgHENYDTFFKKLYNlLPPGGLMLL 163
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
78-184 1.41e-04

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 42.43  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  78 YRIWRRirLLKRIAGDGRGKRLLDVGCGDG----GFLRAAQRLGwQVSGTELEP-------QQARSLG-LDVR------- 138
Cdd:pfam01209  27 HRLWKD--FTMKCMGVKRGNKFLDVAGGTGdwtfGLSDSAGSSG-KVVGLDINEnmlkegeKKAKEEGkYNIEflqgnae 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1232315491 139 --AEIDDfraseKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLV 184
Cdd:pfam01209 104 elPFEDD-----SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVC 146
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
97-189 3.31e-04

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 40.62  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  97 KRLLDVGCGDggflraaQRL-GWQvsGTELEPqqarSLGLDVRAEIDD---FrASEKFDCVTFWHSLEHLPrPHEALRQA 172
Cdd:COG4627     4 PLKLNIGCGP-------KRLpGWL--NVDIVP----APGVDIVGDLTDplpF-PDNSVDAIYSSHVLEHLD-YEEAPLAL 68

                          90       100
                  ....*....|....*....|
gi 1232315491 173 RE--R-LQPGGVLLVSVPDA 189
Cdd:COG4627    69 KEcyRvLKPGGILRIVVPDL 88
PRK08317 PRK08317
hypothetical protein; Provisional
 76-188 6.21e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 40.69  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  76 AGYRIWRRIRLLKRiagdgRGKRLLDVGCGDGGFLRAaqrLGWQVSGT-------------ELEPQQARSLGLDVRAEID 142
Cdd:PRK08317    5 RRYRARTFELLAVQ-----PGDRVLDVGCGPGNDARE---LARRVGPEgrvvgidrseamlALAKERAAGLGPNVEFVRG 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1232315491 143 D-----FrASEKFDCVTFWHSLEHLPRPHEALRQARERLQPGGVLLVSVPD 188
Cdd:PRK08317   77 DadglpF-PDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTD 126
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
85-182 8.60e-04

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 40.61  E-value: 8.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  85 RLLKRIAgDGRGKRLLDVGCGDGGFL------RAAQRLGwqvsgteLEPQQ---------ARSLGLDVRAE-----IDDF 144
Cdd:PRK15068  113 RVLPHLS-PLKGRTVLDVGCGNGYHMwrmlgaGAKLVVG-------IDPSQlflcqfeavRKLLGNDQRAHllplgIEQL 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315491 145 RASEKFDCVtFwhS---LEHLPRPHEALRQARERLQPGGVL 182
Cdd:PRK15068  185 PALKAFDTV-F--SmgvLYHRRSPLDHLKQLKDQLVPGGEL 222
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 86-187 9.41e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 40.06  E-value: 9.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  86 LLKRIaGDGRGKRLLDVGCGDGGFLRA-AQRL-GWQVSGTELEPQ---QARSLGLDVR-AEIDDFRASEKFDCVTFWHSL 159
Cdd:PRK14103   21 LLARV-GAERARRVVDLGCGPGNLTRYlARRWpGAVIEALDSSPEmvaAARERGVDARtGDVRDWKPKPDTDVVVSNAAL 99

                          90       100
                  ....*....|....*....|....*...
gi 1232315491 160 EHLPRPHEALRQARERLQPGGVLLVSVP 187
Cdd:PRK14103  100 QWVPEHADLLVRWVDELAPGSWIAVQVP 127
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 96-196 2.33e-03

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 38.59  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  96 GKRLLDVGCGDGGFLRAAQRLGwQVSGTELEPQQARSL-----GLDV-RAEID---DFRASEKFDCVTFWHSLEHLPRPH 166
Cdd:pfam07021  14 GSRVLDLGCGDGTLLYLLKEEK-GVDGYGIELDAAGVAecvakGLYViQGDLDeglEHFPDKSFDYVILSQTLQATRNPR 92

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315491 167 EALrqaRERLQPGGVLLVSVPDAGGWQARL 196
Cdd:pfam07021  93 EVL---DEMLRIGRRCIVSFPNFGHWRVRW 119
PLN02244 PLN02244
tocopherol O-methyltransferase
 95-185 7.82e-03

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 37.80  E-value: 7.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315491  95 RGKRLLDVGCGDGGFLR-AAQRLGWQVSGTELEPQQA---------RSLGLDVRAEIDD-----FRASEkFDCVTFWHSL 159
Cdd:PLN02244  118 RPKRIVDVGCGIGGSSRyLARKYGANVKGITLSPVQAaranalaaaQGLSDKVSFQVADalnqpFEDGQ-FDLVWSMESG 196

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315491 160 EHLPRP----HEALRQARerlqPGG-VLLVS 185
Cdd:PLN02244  197 EHMPDKrkfvQELARVAA----PGGrIIIVT 223
 
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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