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Conserved domains on  [gi|313768071|ref|YP_004061502|]
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hypothetical protein BpV1_072 [Bathycoccus sp. RCC1105 virus BpV1]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 1-128 3.35e-21

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: 85.07  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   1 MEEIRKYHNESKRL--LIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRAKnmKIRVNFYEGDI 78
Cdd:COG2227    1 MSDPDARDFWDRRLaaLLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA--ELNVDFVQGDL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313768071  79 --FACPQRKYDVICYNFALHYIFETNKLFEtsllAIKNRIKPGGQFIGIIPN 128
Cdd:COG2227   79 edLPLEDGSFDLVICSEVLEHLPDPAALLR----ELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 1-128 3.35e-21

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: 85.07  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   1 MEEIRKYHNESKRL--LIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRAKnmKIRVNFYEGDI 78
Cdd:COG2227    1 MSDPDARDFWDRRLaaLLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA--ELNVDFVQGDL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313768071  79 --FACPQRKYDVICYNFALHYIFETNKLFEtsllAIKNRIKPGGQFIGIIPN 128
Cdd:COG2227   79 edLPLEDGSFDLVICSEVLEHLPDPAALLR----ELARLLKPGGLLLLSTPN 126
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 4-196 5.20e-21

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 89.03  E-value: 5.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071    4 IRKYHNESKRLLIQSATREGD------SILDVGCGFGGDLQKWRHAGANISMC-EPNPESLKEAKSR---------AKNM 67
Cdd:pfam03291  39 LRNFNNWIKSLLISLYASKTFqnsnkrKVLDLGCGKGGDLEKWFKGGISQLIGtDIAEVSIEQCRERynklrsgnkSKYY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   68 KIRVNFYEGD--------IFACPQRKYDVICYNFALHYIFETNKLFETSLLAIKNRIKPGGQFIGIIPNSDNIIMNT--- 136
Cdd:pfam03291 119 KFDAEFITGDcfvsslreVFEDPFGKFDIVSCQFAIHYSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFISALTikr 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  137 -----PVKDELGNY-----FLMKHTSSGNFGEKLYVHLADtpyyADGPKVEPIAHKDMLFTRMEDLGFTL 196
Cdd:pfam03291 199 lfaieKDLPSFGNSiysvkFEEEPPQVPLFGIKYDYNLED----AVDDVPEYIVPFETLVSLAEEYGLEL 264
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 26-123 1.26e-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: 59.37  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  26 ILDVGCGFGGDLQKW-RHAGANISMCEPNPESLKEAKSRAKNMKI-RVNFYEGDIFA---CPQRKYDVICYNFALHYIFE 100
Cdd:cd02440    2 VLDLGCGTGALALALaSGPGARVTGVDISPVALELARKAAAALLAdNVEVLKGDAEElppEADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|...
gi 313768071 101 TNKLFetsLLAIKNRIKPGGQFI 123
Cdd:cd02440   82 DLARF---LEEARRLLKPGGVLV 101
PRK14968 PRK14968
putative methyltransferase; Provisional
 14-92 2.76e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.05  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  14 LLIQSAT-REGDSILDVGCGFG---GDLQKwrhAGANISMCEPNPESLKEAKSRAKNMKIR---VNFYEGDIFAC-PQRK 85
Cdd:PRK14968  14 LLAENAVdKKGDRVLEVGTGSGivaIVAAK---NGKKVVGVDINPYAVECAKCNAKLNNIRnngVEVIRSDLFEPfRGDK 90


                 ....*..
gi 313768071  86 YDVICYN 92
Cdd:PRK14968  91 FDVILFN 97
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
25-147 2.86e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071    25 SILDVGCGFGGDLQKW--RHAGANISMCEPNPESLKEAKSR--AKNMKIRVNFYEGDIFACPQ-RKYDVICYNFALHYIF 99
Cdd:smart00828   2 RVLDFGCGYGSDLIDLaeRHPHLQLHGYTISPEQAEVGRERirALGLQGRIRIFYRDSAKDPFpDTYDLVFGFEVIHHIK 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 313768071   100 ETNKLFetslLAIKNRIKPGGQFI--GIIPNSDniimnTPVKDELGNYFL 147
Cdd:smart00828  82 DKMDLF----SNISRHLKDGGHLVlaDFIANLL-----SAIEHEETTSYL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 1-128 3.35e-21

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: 85.07  E-value: 3.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   1 MEEIRKYHNESKRL--LIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRAKnmKIRVNFYEGDI 78
Cdd:COG2227    1 MSDPDARDFWDRRLaaLLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA--ELNVDFVQGDL 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 313768071  79 --FACPQRKYDVICYNFALHYIFETNKLFEtsllAIKNRIKPGGQFIGIIPN 128
Cdd:COG2227   79 edLPLEDGSFDLVICSEVLEHLPDPAALLR----ELARLLKPGGLLLLSTPN 126
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 4-196 5.20e-21

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 89.03  E-value: 5.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071    4 IRKYHNESKRLLIQSATREGD------SILDVGCGFGGDLQKWRHAGANISMC-EPNPESLKEAKSR---------AKNM 67
Cdd:pfam03291  39 LRNFNNWIKSLLISLYASKTFqnsnkrKVLDLGCGKGGDLEKWFKGGISQLIGtDIAEVSIEQCRERynklrsgnkSKYY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   68 KIRVNFYEGD--------IFACPQRKYDVICYNFALHYIFETNKLFETSLLAIKNRIKPGGQFIGIIPNSDNIIMNT--- 136
Cdd:pfam03291 119 KFDAEFITGDcfvsslreVFEDPFGKFDIVSCQFAIHYSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFISALTikr 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  137 -----PVKDELGNY-----FLMKHTSSGNFGEKLYVHLADtpyyADGPKVEPIAHKDMLFTRMEDLGFTL 196
Cdd:pfam03291 199 lfaieKDLPSFGNSiysvkFEEEPPQVPLFGIKYDYNLED----AVDDVPEYIVPFETLVSLAEEYGLEL 264
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 2-123 4.54e-18

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: 77.34  E-value: 4.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   2 EEIRKYHNESKRLLIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRAKNMKIRVNFYEGDIFAC 81
Cdd:COG2226    2 DRVAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 313768071  82 P--QRKYDVICYNFALHYIFETNKLFEtsllAIKNRIKPGGQFI 123
Cdd:COG2226   82 PfpDGSFDLVISSFVLHHLPDPERALA----EIARVLKPGGRLV 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 26-120 3.36e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.06  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   26 ILDVGCGFGGDLQKW-RHAGANISMCEPNPESLKEAKSRAKNMKIRVNFYEGDIFACPQ--RKYDVICYNFALHYIfeTN 102
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFpdGSFDLVVSSGVLHHL--PD 78

                          90
                  ....*....|....*...
gi 313768071  103 KLFETSLLAIKNRIKPGG 120
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 21-123 9.36e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.55  E-value: 9.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  21 REGDSILDVGCGFGGDLqkWRHAGANISM---CEPNPESLKEAKSRAKNMKI-RVNFYEGDIFAC---PQRKYDVICYNF 93
Cdd:COG0500   25 PKGGRVLDLGCGTGRNL--LALAARFGGRvigIDLSPEAIALARARAAKAGLgNVEFLVADLAELdplPAESFDLVVAFG 102

                         90       100       110
                 ....*....|....*....|....*....|.
gi 313768071  94 ALHYIfetNKLFETSLLA-IKNRIKPGGQFI 123
Cdd:COG0500  103 VLHHL---PPEEREALLReLARALKPGGVLL 130
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
22-123 1.21e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 61.76  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  22 EGDSILDVGCGFGGDLQK--WRHAGANISMCEPNPESLKEAKSRAKNmkirVNFYEGDIFA-CPQRKYDVICYNFALHYI 98
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALlaERFPGARVTGVDLSPEMLARARARLPN----VRFVVADLRDlDPPEPFDLVVSNAALHWL 76

                         90       100
                 ....*....|....*....|....*
gi 313768071  99 FETNKLFEtsllAIKNRIKPGGQFI 123
Cdd:COG4106   77 PDHAALLA----RLAAALAPGGVLA 97
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 26-123 1.26e-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: 59.37  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  26 ILDVGCGFGGDLQKW-RHAGANISMCEPNPESLKEAKSRAKNMKI-RVNFYEGDIFA---CPQRKYDVICYNFALHYIFE 100
Cdd:cd02440    2 VLDLGCGTGALALALaSGPGARVTGVDISPVALELARKAAAALLAdNVEVLKGDAEElppEADESFDVIISDPPLHHLVE 81

                         90       100
                 ....*....|....*....|...
gi 313768071 101 TNKLFetsLLAIKNRIKPGGQFI 123
Cdd:cd02440   82 DLARF---LEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 27-122 3.04e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 58.15  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   27 LDVGCGFGGDLQKWRHA--GANISMCEPNPESLKEAKSRAKNMKI----RVNFYEGDIFACPQRKYDVICYNFALHYIFE 100
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLlnavRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90       100
                  ....*....|....*....|..
gi 313768071  101 TNKLFETsllaIKNRIKPGGQF 122
Cdd:pfam08242  81 PRAVLRN----IRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 21-123 6.74e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 58.20  E-value: 6.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   21 REGDSILDVGCGFGGDLQKWRH---AGANISMCEPNPESLKEAKSRAKNMK-IRVNFYEGDIFACPQ----RKYDVICYN 92
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGfDNVEFEQGDIEELPElledDKFDVVISN 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 313768071   93 FALHYIFETNKLFETsllaIKNRIKPGGQFI 123
Cdd:pfam13847  82 CVLNHIPDPDKVLQE----ILRVLKPGGRLI 108
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 27-123 3.47e-10

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.98  E-value: 3.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   27 LDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRAKNMKirVNFYEGDIFACPQR--KYDVICYNFALHYIFETNKL 104
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFPdnSFDLVLSSEVLHHVEDPERA 78

                          90
                  ....*....|....*....
gi 313768071  105 FEtsllAIKNRIKPGGQFI 123
Cdd:pfam08241  79 LR----EIARVLKPGGILI 93
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
12-123 9.70e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.08  E-value: 9.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  12 KRLLIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRaknmKIRVNFYEGDI--FACPQRKYDVI 89
Cdd:COG4976   36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK----GVYDRLLVADLadLAEPDGRFDLI 111

                         90       100       110
                 ....*....|....*....|....*....|....
gi 313768071  90 CYNFALHYIFETNKLFEtsllAIKNRIKPGGQFI 123
Cdd:COG4976  112 VAADVLTYLGDLAAVFA----GVARALKPGGLFI 141
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 1-130 6.18e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 50.50  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071    1 MEEIRKYHNESKRLLIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPeslkEAKSRAKNMKIRVNFYEGDIfA 80
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSP----IAIERALLNVRFDQFDEQEA-A 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 313768071   81 CPQRKYDVICYNFALHYIFETNKLFETsllaIKNRIKPGGQFIGIIPNSD 130
Cdd:pfam13489  76 VPAGKFDVIVAREVLEHVPDPPALLRQ----IAALLKPGGLLLLSTPLAS 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 21-123 9.21e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 49.93  E-value: 9.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  21 REGDSILDVGCGFGGDLQKW-RHAGANISMCEPNPESLKEAKSRAKNMKI--RVNFYEGDIFA-CPQRKYDVICYNFALH 96
Cdd:COG2230   50 KPGMRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYARERAAEAGLadRVEVRLADYRDlPADGQFDAIVSIGMFE 129

                         90       100
                 ....*....|....*....|....*..
gi 313768071  97 YIfeTNKLFETSLLAIKNRIKPGGQFI 123
Cdd:COG2230  130 HV--GPENYPAYFAKVARLLKPGGRLL 154
PRK14968 PRK14968
putative methyltransferase; Provisional
 14-92 2.76e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.05  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  14 LLIQSAT-REGDSILDVGCGFG---GDLQKwrhAGANISMCEPNPESLKEAKSRAKNMKIR---VNFYEGDIFAC-PQRK 85
Cdd:PRK14968  14 LLAENAVdKKGDRVLEVGTGSGivaIVAAK---NGKKVVGVDINPYAVECAKCNAKLNNIRnngVEVIRSDLFEPfRGDK 90


                 ....*..
gi 313768071  86 YDVICYN 92
Cdd:PRK14968  91 FDVILFN 97
PRK08317 PRK08317
hypothetical protein; Provisional
 4-137 3.09e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 43.39  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   4 IRKYHNESKRLLiqsATREGDSILDVGCGFGGDLQ--KWR-HAGANISMCEPNPESLKEAKSRAKNMKIRVNFYEGDIFA 80
Cdd:PRK08317   4 FRRYRARTFELL---AVQPGDRVLDVGCGPGNDARelARRvGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  81 CPQRK--YDVICYNFALHYIFETNKlfetsLLAIKNRI-KPGGQFIGIIPNSDNIIMNTP 137
Cdd:PRK08317  81 LPFPDgsFDAVRSDRVLQHLEDPAR-----ALAEIARVlRPGGRVVVLDTDWDTLVWHSG 135
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 21-127 7.22e-05

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 42.44  E-value: 7.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  21 REGDSILDVGCGFG--GDLQKWRHAGANISMCEPNPESLKEAKsraKNMKI-----RVNFYEGDI----FACPQRKYD-V 88
Cdd:COG4123   36 KKGGRVLDLGTGTGviALMLAQRSPGARITGVEIQPEAAELAR---RNVALngledRITVIHGDLkefaAELPPGSFDlV 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 313768071  89 IC----YNFALHYI----------FETNKLFETSLLAIKNRIKPGGQFIGIIP 127
Cdd:COG4123  113 VSnppyFKAGSGRKspdearaiarHEDALTLEDLIRAAARLLKPGGRFALIHP 165
PRK06202 PRK06202
hypothetical protein; Provisional
 13-97 1.17e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 41.91  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  13 RLLIQSATREgdSILDVGCGfGGD----LQKW-RHAG--ANISMCEPNPESLKEAKSRAKNMKIRVNFYEGDIFACPQRK 85
Cdd:PRK06202  53 RPALSADRPL--TLLDIGCG-GGDlaidLARWaRRDGlrLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGER 129

                         90
                 ....*....|..
gi 313768071  86 YDVICYNFALHY 97
Cdd:PRK06202 130 FDVVTSNHFLHH 141
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 13-129 3.95e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 39.50  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071   13 RLLIQS-ATREGDSILDVGCGFG--GDLQKWRHAGANISMCEPNPESLKEAKSRAKNMKI-RVNFYEGDIFA-CPQRKYD 87
Cdd:pfam05175  21 RLLLEHlPKDLSGKVLDLGCGAGvlGAALAKESPDAELTMVDINARALESARENLAANGLeNGEVVASDVYSgVEDGKFD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 313768071   88 VICYNFALHYIFETN-----KLFETSllaiKNRIKPGGQFIgIIPNS 129
Cdd:pfam05175 101 LIISNPPFHAGLATTynvaqRFIADA----KRHLRPGGELW-IVANR 142
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
16-123 1.12e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.86  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  16 IQSATREGDSILDVGCGfGGDLQKW--RHAGANISMCEPNPESLKEAKSRAKNMKI--RVNFYEGDIFAC-PQRKYDVIc 90
Cdd:COG4076   29 IERVVKPGDVVLDIGTG-SGLLSMLaaRAGAKKVYAVEVNPDIAAVARRIIAANGLsdRITVINADATDLdLPEKADVI- 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 313768071  91 ynfalhyIFET--NKLFETSLLAI-----KNRIKPGGQFI 123
Cdd:COG4076  107 -------ISEMldTALLDEGQVPIlnharKRLLKPGGRII 139
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 13-122 1.31e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 38.25  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071  13 RLLIQSA-TREGDSILDVGCGFG--GDLQKWRHAGANISMCEPNPESLKEAKsraKNMKI----RVNFYEGDIFAC-PQR 84
Cdd:COG2813   39 RLLLEHLpEPLGGRVLDLGCGYGviGLALAKRNPEARVTLVDVNARAVELAR---ANAAAngleNVEVLWSDGLSGvPDG 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 313768071  85 KYDVICYN------FALHYiFETNKLFETSllaiKNRIKPGGQF 122
Cdd:COG2813  116 SFDLILSNppfhagRAVDK-EVAHALIADA----ARHLRPGGEL 154
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 13-82 1.96e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 38.20  E-value: 1.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 313768071  13 RLLIQSATREGDSILDVGCGFGGDLQKWRHAGANISMCEPNPESLKEAKSRAknmkiRVNFY-EGDIFACP 82
Cdd:PRK10258  33 ALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKD-----AADHYlAGDIESLP 98
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
25-147 2.86e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 2.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 313768071    25 SILDVGCGFGGDLQKW--RHAGANISMCEPNPESLKEAKSR--AKNMKIRVNFYEGDIFACPQ-RKYDVICYNFALHYIF 99
Cdd:smart00828   2 RVLDFGCGYGSDLIDLaeRHPHLQLHGYTISPEQAEVGRERirALGLQGRIRIFYRDSAKDPFpDTYDLVFGFEVIHHIK 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 313768071   100 ETNKLFetslLAIKNRIKPGGQFI--GIIPNSDniimnTPVKDELGNYFL 147
Cdd:smart00828  82 DKMDLF----SNISRHLKDGGHLVlaDFIANLL-----SAIEHEETTSYL 122
 
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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