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Conserved domains on  [gi|2468518196|ref|WP_276814371|]
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bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG [Desulfurococcus amylolyticus]

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 ...
 39-143 3.04e-17

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: 74.67  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  39 AARGRVLDLGAGPGFYLWDLKAYGrvDNVVLLDLIYDA-EWFKPELDEETI-IVKGDMLSPPFKASSFDTVLMLASLHHI 116
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEAlEIARERAAELNVdFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                          90       100
                  ....*....|....*....|....*..
gi 2468518196 117 PYREcrlLVLRNVAKLLRSGGILVLTV 143
Cdd:COG2227   101 PDPA---ALLRELARLLKPGGLLLLST 124
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-143 3.04e-17

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: 74.67  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  39 AARGRVLDLGAGPGFYLWDLKAYGrvDNVVLLDLIYDA-EWFKPELDEETI-IVKGDMLSPPFKASSFDTVLMLASLHHI 116
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEAlEIARERAAELNVdFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                          90       100
                  ....*....|....*....|....*..
gi 2468518196 117 PYREcrlLVLRNVAKLLRSGGILVLTV 143
Cdd:COG2227   101 PDPA---ALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-141 1.03e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.61  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  45 LDLGAGPGFYLWDLKAYGRvdNVVLLDLIYDA-EWFKPELDEETI-IVKGDMLSPPFKASSFDTVLMLASLHHIPYREcr 122
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMlELAREKAPREGLtFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE-- 76

                          90
                  ....*....|....*....
gi 2468518196 123 lLVLRNVAKLLRSGGILVL 141
Cdd:pfam08241  77 -RALREIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-144 4.76e-09

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: 52.43  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  43 RVLDLGAGPGFYLWDLKAYGrVDNVVLLDL----IYDAEWFKPELDEETI-IVKGDMLSPPFKA-SSFDTVLMLASLHHI 116
Cdd:cd02440     1 RVLDLGCGTGALALALASGP-GARVTGVDIspvaLELARKAAAALLADNVeVLKGDAEELPPEAdESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|....*...
gi 2468518196 117 PYRecRLLVLRNVAKLLRSGGILVLTVW 144
Cdd:cd02440    80 VED--LARFLEEARRLLKPGGVLVLTLV 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 41-185 4.35e-06

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 46.13  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  41 RGRVLDLGAGPGFYLWDLKAYGRVDNVVLLDLIYDAEWFKPELDEETII-VKGDMLSPPFKASSFDTVLMLASLH--HIP 117
Cdd:TIGR02072  35 PASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDSSFDLIVSNLALQwcDDL 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468518196 118 YRecrllVLRNVAKLLRSGGILVLTVWSPLEFKmplEKRGdgfmLSSRDGKRFYYFYTLDELLKDVGE 185
Cdd:TIGR02072 115 SQ-----ALSELARVLKPGGLLAFSTFGPGTLH---ELRQ----SFGQHGLRYLSLDELKALLKNSFE 170
PRK08317 PRK08317
hypothetical protein; Provisional
 22-141 5.92e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 36.84  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  22 NIGRYRSTGWRnkWILKAARGRVLDLGAGPGFYLWDLKayGRVDN---VVLLD-----LIYDAEWFKPELDEETiIVKGD 93
Cdd:PRK08317    3 DFRRYRARTFE--LLAVQPGDRVLDVGCGPGNDARELA--RRVGPegrVVGIDrseamLALAKERAAGLGPNVE-FVRGD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2468518196  94 MLSPPFKASSFDTVLMLASLHHIPYREcrlLVLRNVAKLLRSGGILVL 141
Cdd:PRK08317   78 ADGLPFPDGSFDAVRSDRVLQHLEDPA---RALAEIARVLRPGGRVVV 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-143 3.04e-17

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: 74.67  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  39 AARGRVLDLGAGPGFYLWDLKAYGrvDNVVLLDLIYDA-EWFKPELDEETI-IVKGDMLSPPFKASSFDTVLMLASLHHI 116
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRG--ADVTGVDISPEAlEIARERAAELNVdFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                          90       100
                  ....*....|....*....|....*..
gi 2468518196 117 PYREcrlLVLRNVAKLLRSGGILVLTV 143
Cdd:COG2227   101 PDPA---ALLRELARLLKPGGLLLLST 124
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 34-146 8.88e-16

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: 71.18  E-value: 8.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  34 KWILKAARGRVLDLGAGPGFYLWDLKAYGRvdNVVLLDLIYDA-EWFKPELDEETI---IVKGDMLSPPFKASSFDTVLM 109
Cdd:COG2226    16 AALGLRPGARVLDLGCGTGRLALALAERGA--RVTGVDISPEMlELARERAAEAGLnveFVVGDAEDLPFPDGSFDLVIS 93

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2468518196 110 LASLHHIPYREcrlLVLRNVAKLLRSGGILVLTVWSP 146
Cdd:COG2226    94 SFVLHHLPDPE---RALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-141 1.03e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.61  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  45 LDLGAGPGFYLWDLKAYGRvdNVVLLDLIYDA-EWFKPELDEETI-IVKGDMLSPPFKASSFDTVLMLASLHHIPYREcr 122
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMlELAREKAPREGLtFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE-- 76

                          90
                  ....*....|....*....
gi 2468518196 123 lLVLRNVAKLLRSGGILVL 141
Cdd:pfam08241  77 -RALREIARVLKPGGILII 94
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 44-137 1.17e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.81  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  44 VLDLGAGPGFYLWDLKAYGRVDnVVLLDLIYDA-EWFKPELDEETI---IVKGDMLSPPFKASSFDTVLMLASLHHIPYR 119
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR-VTGVDLSPEMlERARERAAEAGLnveFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*...
gi 2468518196 120 EcRLLVLRNVAKLLRSGG 137
Cdd:pfam13649  80 D-LEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 42-192 8.38e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.46  E-value: 8.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  42 GRVLDLGAGPGFYLWDLKAYGRVDnVVLLDL----IYDAEWFKPELDEETI-IVKGDML-SPPFKASSFDTVLMLASLHH 115
Cdd:COG0500    28 GRVLDLGCGTGRNLLALAARFGGR-VIGIDLspeaIALARARAAKAGLGNVeFLVADLAeLDPLPAESFDLVVAFGVLHH 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468518196 116 IPyRECRLLVLRNVAKLLRSGGILVLTVWSPLEFKMpLEKRGDGFMLSSRDGKRFYYFYTLDELLKDVGEAGFTILE 192
Cdd:COG0500   107 LP-PEEREALLRELARALKPGGVLLLSASDAAAALS-LARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDL 181
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-144 4.76e-09

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: 52.43  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  43 RVLDLGAGPGFYLWDLKAYGrVDNVVLLDL----IYDAEWFKPELDEETI-IVKGDMLSPPFKA-SSFDTVLMLASLHHI 116
Cdd:cd02440     1 RVLDLGCGTGALALALASGP-GARVTGVDIspvaLELARKAAAALLADNVeVLKGDAEELPPEAdESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|....*...
gi 2468518196 117 PYRecRLLVLRNVAKLLRSGGILVLTVW 144
Cdd:cd02440    80 VED--LARFLEEARRLLKPGGVLVLTLV 105
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-139 5.13e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.98  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  45 LDLGAGPGFYLWDLKAYGRVDNVVLLDL----IYDAEWFKPELDEETI----IVKGDMLSPPFKasSFDTVLMLASLHHI 116
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDIspaaLEAARERLAALGLLNAvrveLFQLDLGELDPG--SFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|...
gi 2468518196 117 PYREcrlLVLRNVAKLLRSGGIL 139
Cdd:pfam08242  79 ADPR---AVLRNIRRLLKPGGVL 98
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
42-143 7.37e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 51.36  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  42 GRVLDLGAGPGFYLWDLKAYGRVDNVVLLDLiyDA---EWFKPELDEETIIVkGDMLSPPFkASSFDTVLMLASLHHIPY 118
Cdd:COG4106     3 RRVLDLGCGTGRLTALLAERFPGARVTGVDL--SPemlARARARLPNVRFVV-ADLRDLDP-PEPFDLVVSNAALHWLPD 78

                          90       100
                  ....*....|....*....|....*
gi 2468518196 119 REcrlLVLRNVAKLLRSGGILVLTV 143
Cdd:COG4106    79 HA---ALLARLAAALAPGGVLAVQV 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-192 1.21e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 49.73  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  40 ARGRVLDLGAGPGfyLWDLKAYGRVDNVVLLDLIYDAewfkPELDEETIIVKG-DMLSPPFKASSFDTVLMLASLHHIPY 118
Cdd:pfam13489  22 SPGRVLDFGCGTG--IFLRLLRAQGFSVTGVDPSPIA----IERALLNVRFDQfDEQEAAVPAGKFDVIVAREVLEHVPD 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468518196 119 recRLLVLRNVAKLLRSGGILVLTVWSPlEFKMPlEKRGDGFMLSSRDGKRfyYFYTLDELLKDVGEAGFTILE 192
Cdd:pfam13489  96 ---PPALLRQIAALLKPGGLLLLSTPLA-SDEAD-RLLLEWPYLRPRNGHI--SLFSARSLKRLLEEAGFEVVS 162
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
42-197 2.11e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 49.23  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  42 GRVLDLGAGPGFYLWDLKAYGrvDNVVLLDL------------IYDAewfkpeldeetiIVKGDMLSPPFKASSFDTVLM 109
Cdd:COG4976    48 GRVLDLGCGTGLLGEALRPRG--YRLTGVDLseemlakarekgVYDR------------LLVADLADLAEPDGRFDLIVA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196 110 LASLHHIPYREcrlLVLRNVAKLLRSGGILVLTVWSPlefkmplekrgdgfmlssrDGKRFYYfYTLDELLKDVGEAGFT 189
Cdd:COG4976   114 ADVLTYLGDLA---AVFAGVARALKPGGLFIFSVEDA-------------------DGSGRYA-HSLDYVRDLLAAAGFE 170


                  ....*...
gi 2468518196 190 IlEHRYFI 197
Cdd:COG4976   171 V-PGLLVV 177
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 41-185 4.35e-06

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 46.13  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  41 RGRVLDLGAGPGFYLWDLKAYGRVDNVVLLDLIYDAEWFKPELDEETII-VKGDMLSPPFKASSFDTVLMLASLH--HIP 117
Cdd:TIGR02072  35 PASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENVQfICGDAEKLPLEDSSFDLIVSNLALQwcDDL 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468518196 118 YRecrllVLRNVAKLLRSGGILVLTVWSPLEFKmplEKRGdgfmLSSRDGKRFYYFYTLDELLKDVGE 185
Cdd:TIGR02072 115 SQ-----ALSELARVLKPGGLLAFSTFGPGTLH---ELRQ----SFGQHGLRYLSLDELKALLKNSFE 170
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 43-143 1.98e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 43.38  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  43 RVLDLGAGPG-FYLWDLKAYGRvdNVVLLDL-IYDAEWFKPELDEETI-----IVKGDMLSPPFKASsFDTVLMLASLHH 115
Cdd:COG2230    54 RVLDIGCGWGgLALYLARRYGV--RVTGVTLsPEQLEYARERAAEAGLadrveVRLADYRDLPADGQ-FDAIVSIGMFEH 130

                          90       100
                  ....*....|....*....|....*...
gi 2468518196 116 IPYRECRLLvLRNVAKLLRSGGILVLTV 143
Cdd:COG2230   131 VGPENYPAY-FAKVARLLKPGGRLLLHT 157
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
41-143 6.48e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 41.78  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  41 RGRVLDLGAGPgFYLWDLKAYgRVDNVVLLDLIYDAEWfkpeldeetiivkgdMLspPFKASSFDTVLMLASLHHIPYRE 120
Cdd:COG4627     3 SPLKLNIGCGP-KRLPGWLNV-DIVPAPGVDIVGDLTD---------------PL--PFPDNSVDAIYSSHVLEHLDYEE 63

                          90       100
                  ....*....|....*....|...
gi 2468518196 121 CRLLvLRNVAKLLRSGGILVLTV 143
Cdd:COG4627    64 APLA-LKECYRVLKPGGILRIVV 85
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-142 1.26e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.17  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  43 RVLDLGAGPGFYLWDLKAYGRVD-NVVLLDLIYDA------EWFKPELDEETIIVkGDMLSPP--FKASSFDTVLMLASL 113
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGPNaEVVGIDISEEAiekareNAQKLGFDNVEFEQ-GDIEELPelLEDDKFDVVISNCVL 84

                          90       100
                  ....*....|....*....|....*....
gi 2468518196 114 HHIPYRECrllVLRNVAKLLRSGGILVLT 142
Cdd:pfam13847  85 NHIPDPDK---VLQEILRVLKPGGRLIIS 110
PRK08317 PRK08317
hypothetical protein; Provisional
 22-141 5.92e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 36.84  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  22 NIGRYRSTGWRnkWILKAARGRVLDLGAGPGFYLWDLKayGRVDN---VVLLD-----LIYDAEWFKPELDEETiIVKGD 93
Cdd:PRK08317    3 DFRRYRARTFE--LLAVQPGDRVLDVGCGPGNDARELA--RRVGPegrVVGIDrseamLALAKERAAGLGPNVE-FVRGD 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2468518196  94 MLSPPFKASSFDTVLMLASLHHIPYREcrlLVLRNVAKLLRSGGILVL 141
Cdd:PRK08317   78 ADGLPFPDGSFDAVRSDRVLQHLEDPA---RALAEIARVLRPGGRVVV 122
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 42-150 7.04e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 36.03  E-value: 7.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468518196  42 GRVLDLGAGPG-F--YLWDLKAyGRvdnVVLLDLIYDAEWfKPELDEETIIVKGDMLSP-------PFKASSFDTVLM-L 110
Cdd:pfam01728  23 KTVLDLGAAPGgWsqVALQRGA-GK---VVGVDLGPMQLW-KPRNDPGVTFIQGDIRDPetldlleELLGRKVDLVLSdG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2468518196 111 A---SLHHI--PYRECRLL--VLRNVAKLLRSGGILVLTVWSPLEFK 150
Cdd:pfam01728  98 SpfiSGNKVldHLRSLDLVkaALEVALELLRKGGNFVCKVFQGEDFS 144
 
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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