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Conserved domains on  [gi|145579456|pdb|2GS9|B]
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Chain B, Hypothetical protein TT1324

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-130 9.76e-26

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: 96.99  E-value: 9.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       20 AYVIAEEERALKGL-LPPGESLLEVGAGTGYWLRRLPYPQK--VGVEPSEA*LAVGRRRAPEA----TWVRAWGEALPFP 92
Cdd:COG2226   5 AARYDGREALLAALgLRPGARVLDLGCGTGRLALALAERGArvTGVDISPEMLELARERAAEAglnvEFVVGDAEDLPFP 84

                        90       100       110
                ....*....|....*....|....*....|....*...
2GS9_B       93 GESFDVVLLFTTLEFVEDVERVLLEARRVLRPGGALVV 130
Cdd:COG2226  85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-130 9.76e-26

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: 96.99  E-value: 9.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       20 AYVIAEEERALKGL-LPPGESLLEVGAGTGYWLRRLPYPQK--VGVEPSEA*LAVGRRRAPEA----TWVRAWGEALPFP 92
Cdd:COG2226   5 AARYDGREALLAALgLRPGARVLDLGCGTGRLALALAERGArvTGVDISPEMLELARERAAEAglnvEFVVGDAEDLPFP 84

                        90       100       110
                ....*....|....*....|....*....|....*...
2GS9_B       93 GESFDVVLLFTTLEFVEDVERVLLEARRVLRPGGALVV 130
Cdd:COG2226  85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-130 3.31e-24

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 91.57  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         41 LEVGAGTGYWLRRLP--YPQKVGVEPSEA*LAVGRRRAPEA--TWVRAWGEALPFPGESFDVVLLFTTLEFVEDVERVLL 116
Cdd:pfam08241   1 LDVGCGTGLLTELLArlGARVTGVDISPEMLELAREKAPREglTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
2GS9_B        117 EARRVLRPGGALVV 130
Cdd:pfam08241  81 EIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 34-200 2.01e-21

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 88.29  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        34 LPPGESLLEVGAGTG----YWLRRLPYPQKV-GVEPSEA*LAVGRRRAPEA------TWVRAWGEALPFPGESFDVVllf 102
Cdd:PRK00216  49 VRPGDKVLDLACGTGdlaiALAKAVGKTGEVvGLDFSEGMLAVGREKLRDLglsgnvEFVQGDAEALPFPDNSFDAV--- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       103 tTLEF----VEDVERVLLEARRVLRPGGalVVGVLE----ALSPWAALYrRLGEKGVLPWAqARFLAREdlkallgppea 174
Cdd:PRK00216 126 -TIAFglrnVPDIDKALREMYRVLKPGG--RLVILEfskpTNPPLKKAY-DFYLFKVLPLI-GKLISKN----------- 189

                        170       180
                 ....*....|....*....|....*....
2GS9_B       175 EGEAVFLAP--EAHPPYEE-ADLAgRRAG 200
Cdd:PRK00216 190 AEAYSYLAEsiRAFPDQEElAAML-EEAG 217
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 27-144 1.13e-15

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 72.68  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         27 ERALKGLLP-PGESLLEVGAGTGYWLRRL-----PYPQKVGVEPSEA*LAVGRRRAPE---ATWVRAWGEALPFPGESFD 97
Cdd:TIGR01934  29 RRAVKLIGVfKGQKVLDVACGTGDLAIELaksapDRGKVTGVDFSSEMLEVAKKKSELplnIEFIQADAEALPFEDNSFD 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
2GS9_B         98 VVLLFTTLEFVEDVERVLLEARRVLRPGGALVvgVLE----ALSPWAALYR 144
Cdd:TIGR01934 109 AVTIAFGLRNVTDIQKALREMYRVLKPGGRLV--ILEfskpANALLKKFYK 157
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-135 1.59e-12

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: 61.29  E-value: 1.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       40 LLEVGAGTGYWLRRL---PYPQKVGVEPSEA*LAVGRRRAPEATWVRA------WGEALPFPGESFDVVLLFTTLE-FVE 109
Cdd:cd02440   2 VLDLGCGTGALALALasgPGARVTGVDISPVALELARKAAAALLADNVevlkgdAEELPPEADESFDVIISDPPLHhLVE 81

                        90       100
                ....*....|....*....|....*.
2GS9_B      110 DVERVLLEARRVLRPGGALVVGVLEA 135
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-130 9.76e-26

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: 96.99  E-value: 9.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       20 AYVIAEEERALKGL-LPPGESLLEVGAGTGYWLRRLPYPQK--VGVEPSEA*LAVGRRRAPEA----TWVRAWGEALPFP 92
Cdd:COG2226   5 AARYDGREALLAALgLRPGARVLDLGCGTGRLALALAERGArvTGVDISPEMLELARERAAEAglnvEFVVGDAEDLPFP 84

                        90       100       110
                ....*....|....*....|....*....|....*...
2GS9_B       93 GESFDVVLLFTTLEFVEDVERVLLEARRVLRPGGALVV 130
Cdd:COG2226  85 DGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-130 3.31e-24

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 91.57  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         41 LEVGAGTGYWLRRLP--YPQKVGVEPSEA*LAVGRRRAPEA--TWVRAWGEALPFPGESFDVVLLFTTLEFVEDVERVLL 116
Cdd:pfam08241   1 LDVGCGTGLLTELLArlGARVTGVDISPEMLELAREKAPREglTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
2GS9_B        117 EARRVLRPGGALVV 130
Cdd:pfam08241  81 EIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 27-132 2.30e-22

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: 87.77  E-value: 2.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       27 ERALKGLLPPGESLLEVGAGTGY---WLRRLPYpQKVGVEPSEA*LAVGRRRAPE--ATWVRAWGEALPFPGESFDVVLL 101
Cdd:COG2227  15 AALLARLLPAGGRVLDVGCGTGRlalALARRGA-DVTGVDISPEALEIARERAAElnVDFVQGDLEDLPLEDGSFDLVIC 93

                        90       100       110
                ....*....|....*....|....*....|.
2GS9_B      102 FTTLEFVEDVERVLLEARRVLRPGGALVVGV 132
Cdd:COG2227  94 SEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 41-126 1.34e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 84.92  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         41 LEVGAGTGYWLRRLP--YPQKV-GVEPSEA*LAVGRRRA----PEATWVRAWGEALPFPGESFDVVLLFTTLEFV--EDV 111
Cdd:pfam13649   2 LDLGCGTGRLTLALArrGGARVtGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPDL 81

                          90
                  ....*....|....*
2GS9_B        112 ERVLLEARRVLRPGG 126
Cdd:pfam13649  82 EAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 34-200 2.01e-21

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 88.29  E-value: 2.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        34 LPPGESLLEVGAGTG----YWLRRLPYPQKV-GVEPSEA*LAVGRRRAPEA------TWVRAWGEALPFPGESFDVVllf 102
Cdd:PRK00216  49 VRPGDKVLDLACGTGdlaiALAKAVGKTGEVvGLDFSEGMLAVGREKLRDLglsgnvEFVQGDAEALPFPDNSFDAV--- 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       103 tTLEF----VEDVERVLLEARRVLRPGGalVVGVLE----ALSPWAALYrRLGEKGVLPWAqARFLAREdlkallgppea 174
Cdd:PRK00216 126 -TIAFglrnVPDIDKALREMYRVLKPGG--RLVILEfskpTNPPLKKAY-DFYLFKVLPLI-GKLISKN----------- 189

                        170       180
                 ....*....|....*....|....*....
2GS9_B       175 EGEAVFLAP--EAHPPYEE-ADLAgRRAG 200
Cdd:PRK00216 190 AEAYSYLAEsiRAFPDQEElAAML-EEAG 217
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
36-132 3.54e-18

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 76.02  E-value: 3.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       36 PGESLLEVGAGTGYW----LRRLPYPQKVGVEPSEA*LAVGRRRAPEATWVRAWGEALPfPGESFDVVLLFTTLEFVEDV 111
Cdd:COG4106   1 PPRRVLDLGCGTGRLtallAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLPDH 79

                        90       100
                ....*....|....*....|.
2GS9_B      112 ERVLLEARRVLRPGGALVVGV 132
Cdd:COG4106  80 AALLARLAAALAPGGVLAVQV 100
PRK08317 PRK08317
hypothetical protein; Provisional
 36-130 8.98e-18

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 78.44  E-value: 8.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        36 PGESLLEVGAGTGYWLRRL-----PYPQKVGVEPSEA*LAVGRRRA----PEATWVRAWGEALPFPGESFDVVLLFTTLE 106
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELarrvgPEGRVVGIDRSEAMLALAKERAaglgPNVEFVRGDADGLPFPDGSFDAVRSDRVLQ 98

                         90       100
                 ....*....|....*....|....
2GS9_B       107 FVEDVERVLLEARRVLRPGGALVV 130
Cdd:PRK08317  99 HLEDPARALAEIARVLRPGGRVVV 122
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-129 2.80e-16

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 73.49  E-value: 2.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        3 FASLAEAYEAWYGTPLGAYVIAEE-ERALKGLLP-PGESLLEVGAGTGYWLRRL-PYPQKV-GVEPSEA*LAVGRRRAPE 78
Cdd:COG4976  11 FDQYADSYDAALVEDLGYEAPALLaEELLARLPPgPFGRVLDLGCGTGLLGEALrPRGYRLtGVDLSEEMLAKAREKGVY 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
2GS9_B       79 ATWVRAWGEALPFPGESFDVVLLFTTLEFVEDVERVLLEARRVLRPGGALV 129
Cdd:COG4976  91 DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 27-144 1.13e-15

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 72.68  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         27 ERALKGLLP-PGESLLEVGAGTGYWLRRL-----PYPQKVGVEPSEA*LAVGRRRAPE---ATWVRAWGEALPFPGESFD 97
Cdd:TIGR01934  29 RRAVKLIGVfKGQKVLDVACGTGDLAIELaksapDRGKVTGVDFSSEMLEVAKKKSELplnIEFIQADAEALPFEDNSFD 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
2GS9_B         98 VVLLFTTLEFVEDVERVLLEARRVLRPGGALVvgVLE----ALSPWAALYR 144
Cdd:TIGR01934 109 AVTIAFGLRNVTDIQKALREMYRVLKPGGRLV--ILEfskpANALLKKFYK 157
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
36-163 2.15e-15

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 72.09  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         36 PGESLLEVGAGTGYWLRRL-----PYPQKVGVEPSEA*LAVGRRRAPEA-----TWVRAWGEALPFPGESFDVVLLFTTL 105
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLsdsagSSGKVVGLDINENMLKEGEKKAKEEgkyniEFLQGNAEELPFEDDSFDIVTISFGL 121

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
2GS9_B        106 EFVEDVERVLLEARRVLRPGGALVvgVLEALSPWAALYRRLGE---KGVLPWAqARFLARE 163
Cdd:pfam01209 122 RNFPDYLKVLKEAFRVLKPGGRVV--CLEFSKPENPLLSQAYElyfKYVMPFM-GKMFAKS 179
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-128 8.46e-14

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 64.70  E-value: 8.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         41 LEVGAGTGYWLRRL----PYPQKVGVEPSEA*LAVGRRRAPEATWVRAW------GEALPFPGESFDVVLLFTTLEFVED 110
Cdd:pfam08242   1 LEIGCGTGTLLRALlealPGLEYTGLDISPAALEAARERLAALGLLNAVrvelfqLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
2GS9_B        111 VERVLLEARRVLRPGGAL 128
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 9-198 4.68e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.94  E-value: 4.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        9 AYEAWYGTPLGAYVIAEeeRALKGLLPPGESLLEVGAGTGYWLRRL---PYPQKVGVEPSEA*LAVGRRRAPEATW---- 81
Cdd:COG0500   1 PWDSYYSDELLPGLAAL--LALLERLPKGGRVLDLGCGTGRNLLALaarFGGRVIGIDLSPEAIALARARAAKAGLgnve 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       82 --VRAWGEALPFPGESFDVVLLFTTLEFVEDVER--VLLEARRVLRPGGALVvgvleaLSPWAALYRRLGEKGVLPWAQA 157
Cdd:COG0500  79 flVADLAELDPLPAESFDLVVAFGVLHHLPPEEReaLLRELARALKPGGVLL------LSASDAAAALSLARLLLLATAS 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
2GS9_B      158 RF--LAREDLKALLGPPEAEGEAVFLAPEAHPPYEEADLAGRR 198
Cdd:COG0500 153 LLelLLLLRLLALELYLRALLAAAATEDLRSDALLESANALEY 195
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-135 1.59e-12

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: 61.29  E-value: 1.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       40 LLEVGAGTGYWLRRL---PYPQKVGVEPSEA*LAVGRRRAPEATWVRA------WGEALPFPGESFDVVLLFTTLE-FVE 109
Cdd:cd02440   2 VLDLGCGTGALALALasgPGARVTGVDISPVALELARKAAAALLADNVevlkgdAEELPPEADESFDVIISDPPLHhLVE 81

                        90       100
                ....*....|....*....|....*.
2GS9_B      110 DVERVLLEARRVLRPGGALVVGVLEA 135
Cdd:cd02440  82 DLARFLEEARRLLKPGGVLVLTLVLA 107
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 31-130 5.83e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 55.71  E-value: 5.83e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       31 KGLLPPGESLLEVGAGTGYWLRRLP--YPQKV-GVEPSEA*LAVGRRRAPEA------TWVRAWGEALPFPGeSFDVVLL 101
Cdd:COG2230  46 KLGLKPGMRVLDIGCGWGGLALYLArrYGVRVtGVTLSPEQLEYARERAAEAgladrvEVRLADYRDLPADG-QFDAIVS 124

                        90       100       110
                ....*....|....*....|....*....|.
2GS9_B      102 FTTLEFV--EDVERVLLEARRVLRPGGALVV 130
Cdd:COG2230 125 IGMFEHVgpENYPAYFAKVARLLKPGGRLLL 155
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 39-169 6.15e-10

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: 56.91  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         39 SLLEVGAGTGY----WLRRLPYPQKVGVEPSEA*LAVGRRRAPEA-TWVRAWGEALPFPGESFDVVLLFTTLEFVEDVER 113
Cdd:TIGR02072  37 SVLDIGCGTGYltraLLKRFPQAEFIALDISAGMLAQAKTKLSENvQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQ 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
2GS9_B        114 VLLEARRVLRPGGALVVGVL--EALSPWAALYRRLGEkgvlpwaqaRFLAREDLKALL 169
Cdd:TIGR02072 117 ALSELARVLKPGGLLAFSTFgpGTLHELRQSFGQHGL---------RYLSLDELKALL 165
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 36-130 7.22e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 52.80  E-value: 7.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         36 PGESLLEVGAGTGYWLRRL-----PYPQKVGVEPSEA*LAVGRRRAPE-----ATWVRAWGEALP--FPGESFDVVLLFT 103
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELaeelgPNAEVVGIDISEEAIEKARENAQKlgfdnVEFEQGDIEELPelLEDDKFDVVISNC 82

                          90       100
                  ....*....|....*....|....*..
2GS9_B        104 TLEFVEDVERVLLEARRVLRPGGALVV 130
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLII 109
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 34-145 1.47e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.05  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B         34 LPPGESLLEVGAGTGYWLR--RLPYPQKVGVEPSEA*LAVGRRRAPEATwvrAWGEALPFPGESFDVVLLFTTLEFVEDV 111
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRllRAQGFSVTGVDPSPIAIERALLNVRFDQ---FDEQEAAVPAGKFDVIVAREVLEHVPDP 96

                          90       100       110
                  ....*....|....*....|....*....|....
2GS9_B        112 ERVLLEARRVLRPGGALVVGVLEALSPWAALYRR 145
Cdd:pfam13489  97 PALLRQIAALLKPGGLLLLSTPLASDEADRLLLE 130
arsM PRK11873
arsenite methyltransferase;
34-130 3.81e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 46.09  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        34 LPPGESLLEVGAGTGY--WL--RRLPYPQKV-GVEPSEA*LAVGRRRAPEAtwvrawG-----------EALPFPGESFD 97
Cdd:PRK11873  75 LKPGETVLDLGSGGGFdcFLaaRRVGPTGKViGVDMTPEMLAKARANARKA------GytnvefrlgeiEALPVADNSVD 148

                         90       100       110
                 ....*....|....*....|....*....|...
2GS9_B        98 VVLLFTTLEFVEDVERVLLEARRVLRPGGALVV 130
Cdd:PRK11873 149 VIISNCVINLSPDKERVFKEAFRVLKPGGRFAI 181
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
89-132 2.15e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 43.32  E-value: 2.15e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
2GS9_B       89 LPFPGESFDVVLLFTTLE--FVEDVERVLLEARRVLRPGGALVVGV 132
Cdd:COG4627  40 LPFPDNSVDAIYSSHVLEhlDYEEAPLALKECYRVLKPGGILRIVV 85
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 92-130 6.31e-04

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: 39.59  E-value: 6.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
2GS9_B         92 PGESFDVVLLFTTLEFVEDVERVLLEARRVLRPGGALVV 130
Cdd:TIGR01983 109 KAGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFF 147
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 40-131 2.25e-03

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 38.33  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        40 LLEVGAGTGYW---LRRLPYPQKVGV-EPSEA*LAVGRRRAP--EATWVRAWGEALPFPGESFDVVLLFTTLEFVEDVER 113
Cdd:PLN02490 117 VVDVGGGTGFTtlgIVKHVDAKNVTIlDQSPHQLAKAKQKEPlkECKIIEGDAEDLPFPTDYADRYVSAGSIEYWPDPQR 196

                         90
                 ....*....|....*....
2GS9_B       114 VLLEARRVLRPGG-ALVVG 131
Cdd:PLN02490 197 GIKEAYRVLKIGGkACLIG 215
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 35-130 3.98e-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: 36.71  E-value: 3.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B       35 PPGESLLEVGAGTGY---WL-RRLPYPQKVGVEPSEA*LAVGRR--RAPEATWVRA-WGEAL-PFPGESFDVVLL---FT 103
Cdd:COG2813  48 PLGGRVLDLGCGYGViglALaKRNPEARVTLVDVNARAVELARAnaAANGLENVEVlWSDGLsGVPDGSFDLILSnppFH 127

                        90       100
                ....*....|....*....|....*....
2GS9_B      104 TLEFVED--VERVLLEARRVLRPGGALVV 130
Cdd:COG2813 128 AGRAVDKevAHALIADAARHLRPGGELWL 156
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 38-169 5.73e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 36.66  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GS9_B        38 ESLLEVGAGTG----YWLRRlpYPQKVGVEPSEA*LAVGRRRAPEATWVRAWGEALPFPGESFDVVLLFTTLEFVEDVER 113
Cdd:PRK10258  44 THVLDAGCGPGwmsrYWRER--GSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLST 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
2GS9_B       114 VLLEARRVLRPGG-----ALVVGVLEAL-SPWAALYRRlgekgvlPWAQaRFLAREDLKALL 169
Cdd:PRK10258 122 ALRELYRVVRPGGvvaftTLVQGSLPELhQAWQAVDER-------PHAN-RFLPPDAIEQAL 175
 
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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