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Conserved domains on  [gi|2110921597|ref|WP_225842473|]
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MULTISPECIES: class I SAM-dependent methyltransferase [Streptomyces]

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]; ...
 35-162 1.33e-32

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: 116.63  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  35 ALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRL----ASLPRLPFADGRFDAVL 110
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVefvvGDAEDLPFPDGSFDLVI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2110921597 111 GNFVLNHVGRPRAALRELRRVTRPGGRVSVTVWTAPPaagHALLGRAVQAAG 162
Cdd:COG2226    93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPD---LAELEELLAEAG 141
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-162 1.33e-32

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: 116.63  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  35 ALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRL----ASLPRLPFADGRFDAVL 110
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVefvvGDAEDLPFPDGSFDLVI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2110921597 111 GNFVLNHVGRPRAALRELRRVTRPGGRVSVTVWTAPPaagHALLGRAVQAAG 162
Cdd:COG2226    93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPD---LAELEELLAEAG 141
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-136 6.93e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 94.94  E-value: 6.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  48 VLDAGTGTGTVAAA-ARELGAEVTAVDAEPDMVARAARTVPEADVRL----ASLPRLPFADGRFDAVLGNFVLNHVGRP- 121
Cdd:pfam13649   1 VLDLGCGTGRLTLAlARRGGARVTGVDLSPEMLERARERAAEAGLNVefvqGDAEDLPFPDGSFDLVVSSGVLHHLPDPd 80

                          90
                  ....*....|....*.
gi 2110921597 122 -RAALRELRRVTRPGG 136
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 39-138 7.38e-19

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 83.06  E-value: 7.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  39 AAGVREGMRVLDAGTGTGTVAAA-ARELGAE--VTAVDAEPDMVA----RAARTVPEADVRLASLPRLPFADGRFDAVLG 111
Cdd:PRK08317   14 LLAVQPGDRVLDVGCGPGNDARElARRVGPEgrVVGIDRSEAMLAlakeRAAGLGPNVEFVRGDADGLPFPDGSFDAVRS 93

                          90       100
                  ....*....|....*....|....*..
gi 2110921597 112 NFVLNHVGRPRAALRELRRVTRPGGRV 138
Cdd:PRK08317   94 DRVLQHLEDPARALAEIARVLRPGGRV 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-145 8.45e-15

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: 68.61  E-value: 8.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  47 RVLDAGTGTGTVA-AAARELGAEVTAVDAEPDMVARA-----ARTVPEADVRLASLPRLPF-ADGRFDAVLGNFVLNH-V 118
Cdd:cd02440     1 RVLDLGCGTGALAlALASGPGARVTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|....*..
gi 2110921597 119 GRPRAALRELRRVTRPGGRVSVTVWTA 145
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLVLA 107
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 40-138 9.89e-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: 71.14  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  40 AGVREGMRVLDAGTGTGTVAAAARELG---AEVTAVDAEPDMVARA-ARTVPEADVRL--ASLPRLPFADGRFDAVLGNF 113
Cdd:TIGR01934  35 IGVFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAkKKSELPLNIEFiqADAEALPFEDNSFDAVTIAF 114

                          90       100
                  ....*....|....*....|....*
gi 2110921597 114 VLNHVGRPRAALRELRRVTRPGGRV 138
Cdd:TIGR01934 115 GLRNVTDIQKALREMYRVLKPGGRL 139
rADc smart00650
Ribosomal RNA adenine dimethylases;
39-112 1.44e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.26  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597   39 AAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEA--------DVRlaslpRLPFADGRFDAVL 110
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAAdnltvihgDAL-----KFDLPKLQPYKVV 82


                   ..
gi 2110921597  111 GN 112
Cdd:smart00650  83 GN 84
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-162 1.33e-32

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: 116.63  E-value: 1.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  35 ALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRL----ASLPRLPFADGRFDAVL 110
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVefvvGDAEDLPFPDGSFDLVI 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2110921597 111 GNFVLNHVGRPRAALRELRRVTRPGGRVSVTVWTAPPaagHALLGRAVQAAG 162
Cdd:COG2226    93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPD---LAELEELLAEAG 141
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 42-142 1.12e-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: 100.48  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  42 VREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRL--ASLPRLPFADGRFDAVLGNFVLNHVG 119
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNVDFvqGDLEDLPLEDGSFDLVICSEVLEHLP 101

                          90       100
                  ....*....|....*....|...
gi 2110921597 120 RPRAALRELRRVTRPGGRVSVTV 142
Cdd:COG2227   102 DPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 48-136 6.93e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 94.94  E-value: 6.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  48 VLDAGTGTGTVAAA-ARELGAEVTAVDAEPDMVARAARTVPEADVRL----ASLPRLPFADGRFDAVLGNFVLNHVGRP- 121
Cdd:pfam13649   1 VLDLGCGTGRLTLAlARRGGARVTGVDLSPEMLERARERAAEAGLNVefvqGDAEDLPFPDGSFDLVVSSGVLHHLPDPd 80

                          90
                  ....*....|....*.
gi 2110921597 122 -RAALRELRRVTRPGG 136
Cdd:pfam13649  81 lEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-140 2.60e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 90.80  E-value: 2.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  49 LDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADV--RLASLPRLPFADGRFDAVLGNFVLNHVGRPRAALR 126
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLtfVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 2110921597 127 ELRRVTRPGGRVSV 140
Cdd:pfam08241  81 EIARVLKPGGILII 94
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
11-172 2.03e-22

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 91.21  E-value: 2.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  11 RQAWAGKAEAYAAGFAKLCAYTVPA-----LLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAART 85
Cdd:COG4976     8 EALFDQYADSYDAALVEDLGYEAPAllaeeLLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  86 VPEADVRLASLPRLPFADGRFDAVLGNFVLNHVGRPRAALRELRRVTRPGGRVSVTVWTAPPAAGHALLGRAVQAAGAVR 165
Cdd:COG4976    88 GVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDADGSGRYAHSLDYVRDLLAAA 167


                  ....*..
gi 2110921597 166 PAHLPAL 172
Cdd:COG4976   168 GFEVPGL 174
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
44-142 4.38e-20

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 82.56  E-value: 4.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  44 EGMRVLDAGTGTGTVAA--AARELGAEVTAVDAEPDMVARAARTVPEADVRLASLPRLPFaDGRFDAVLGNFVLNHVGRP 121
Cdd:COG4106     1 PPRRVLDLGCGTGRLTAllAERFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDP-PEPFDLVVSNAALHWLPDH 79

                          90       100
                  ....*....|....*....|.
gi 2110921597 122 RAALRELRRVTRPGGRVSVTV 142
Cdd:COG4106    80 AALLARLAAALAPGGVLAVQV 100
PRK08317 PRK08317
hypothetical protein; Provisional
 39-138 7.38e-19

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 83.06  E-value: 7.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  39 AAGVREGMRVLDAGTGTGTVAAA-ARELGAE--VTAVDAEPDMVA----RAARTVPEADVRLASLPRLPFADGRFDAVLG 111
Cdd:PRK08317   14 LLAVQPGDRVLDVGCGPGNDARElARRVGPEgrVVGIDRSEAMLAlakeRAAGLGPNVEFVRGDADGLPFPDGSFDAVRS 93

                          90       100
                  ....*....|....*....|....*..
gi 2110921597 112 NFVLNHVGRPRAALRELRRVTRPGGRV 138
Cdd:PRK08317   94 DRVLQHLEDPARALAEIARVLRPGGRV 120
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 36-138 2.49e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.59  E-value: 2.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  36 LLHAAGVREGMRVLDAGTGTGTVA-AAARELGAEVTAVDAEPDMVARAARTVPEA------DVRLASLPRLPfADGRFDA 108
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLAlYLARRYGVRVTGVTLSPEQLEYARERAAEAgladrvEVRLADYRDLP-ADGQFDA 121

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2110921597 109 VLGNFVLNHVGRP--RAALRELRRVTRPGGRV 138
Cdd:COG2230   122 IVSIGMFEHVGPEnyPAYFAKVARLLKPGGRL 153
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 16-141 1.13e-17

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 79.80  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  16 GKAEAYAAGFAKLCAYTVPALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRLAS 95
Cdd:PRK10258   14 GRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADHYLAGD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2110921597  96 LPRLPFADGRFDAVLGNFVLNHVGRPRAALRELRRVTRPGGRVSVT 141
Cdd:PRK10258   94 IESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFT 139
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-195 1.85e-17

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 77.47  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  39 AAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRLASlprLPFADGRFDAVLGNFVLNHV 118
Cdd:pfam13489  17 LPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQE---AAVPAGKFDVIVAREVLEHV 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2110921597 119 GRPRAALRELRRVTRPGGRVSVTVWTAPPAAGHALLgravqaagavrpaHLPALAPEDDFPR--TERGLTALLGEAGLR 195
Cdd:pfam13489  94 PDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLL-------------EWPYLRPRNGHISlfSARSLKRLLEEAGFE 159
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 35-141 6.19e-17

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 76.14  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  35 ALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAAR-----TVPEADVRLASLPRLPFADGRFDAV 109
Cdd:COG1041    17 ALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGAREnlehyGYEDADVIRGDARDLPLADESVDAI 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2110921597 110 -----LGNFVLNHVGRP----RAALRELRRVTRPGGRVSVT 141
Cdd:COG1041    97 vtdppYGRSSKISGEELlelyEKALEEAARVLKPGGRVVIV 137
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 39-140 1.63e-16

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 76.35  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  39 AAGVREGMRVLDAGTGTGTVA-AAARELG--AEVTAVDAEPDM--VAR----AARTVPEADVRLASLPRLPFADGRFDAV 109
Cdd:PRK00216   46 WLGVRPGDKVLDLACGTGDLAiALAKAVGktGEVVGLDFSEGMlaVGReklrDLGLSGNVEFVQGDAEALPFPDNSFDAV 125

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2110921597 110 LGNFVLNHVGRPRAALRELRRVTRPGGRVSV 140
Cdd:PRK00216  126 TIAFGLRNVPDIDKALREMYRVLKPGGRLVI 156
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 20-198 1.72e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 75.72  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  20 AYAAGFAKLCAYTVPALLHA-AGVREGMRVLDAGTGTGTVAAA-ARELGAEVTAVDAEPDMVARAARTVPEA-----DVR 92
Cdd:COG0500     1 PWDSYYSDELLPGLAALLALlERLPKGGRVLDLGCGTGRNLLAlAARFGGRVIGIDLSPEAIALARARAAKAglgnvEFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  93 LASLPRL-PFADGRFDAVLGNFVLNHV--GRPRAALRELRRVTRPGGRVSVTVWTAPPAAGHALLGRAVQAAGAVRPAHL 169
Cdd:COG0500    81 VADLAELdPLPAESFDLVVAFGVLHHLppEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLL 160

                         170       180
                  ....*....|....*....|....*....
gi 2110921597 170 PALAPEDDFPRTERGLTALLGEAGLREPA 198
Cdd:COG0500   161 RLLALELYLRALLAAAATEDLRSDALLES 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 47-145 8.45e-15

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: 68.61  E-value: 8.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  47 RVLDAGTGTGTVA-AAARELGAEVTAVDAEPDMVARA-----ARTVPEADVRLASLPRLPF-ADGRFDAVLGNFVLNH-V 118
Cdd:cd02440     1 RVLDLGCGTGALAlALASGPGARVTGVDISPVALELArkaaaALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHlV 80

                          90       100
                  ....*....|....*....|....*..
gi 2110921597 119 GRPRAALRELRRVTRPGGRVSVTVWTA 145
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLVLA 107
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 40-138 9.89e-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: 71.14  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  40 AGVREGMRVLDAGTGTGTVAAAARELG---AEVTAVDAEPDMVARA-ARTVPEADVRL--ASLPRLPFADGRFDAVLGNF 113
Cdd:TIGR01934  35 IGVFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAkKKSELPLNIEFiqADAEALPFEDNSFDAVTIAF 114

                          90       100
                  ....*....|....*....|....*
gi 2110921597 114 VLNHVGRPRAALRELRRVTRPGGRV 138
Cdd:TIGR01934 115 GLRNVTDIQKALREMYRVLKPGGRL 139
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 49-138 1.15e-14

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 68.16  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  49 LDAGTGTGTVAAAAREL--GAEVTAVDAEPDMVARAARTVPEADVRLASLPRLPFAD------GRFDAVLGNFVLNHVGR 120
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDlgeldpGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 2110921597 121 PRAALRELRRVTRPGGRV 138
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-141 1.33e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 69.37  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  43 REGMRVLDAGTGTGTVA-AAARELG--AEVTAVDAEPDMVARA---ARTVPEADVRLA-----SLPRLpFADGRFDAVLG 111
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSfELAEELGpnAEVVGIDISEEAIEKArenAQKLGFDNVEFEqgdieELPEL-LEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2110921597 112 NFVLNHVGRPRAALRELRRVTRPGGRVSVT 141
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIIS 110
arsM PRK11873
arsenite methyltransferase;
40-140 9.89e-14

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 69.21  E-value: 9.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  40 AGVREGMRVLDAGTGTG-TVAAAARELGAE--VTAVDAEPDMVARAARTVPEADV-----RLASLPRLPFADGRFDAVLG 111
Cdd:PRK11873   73 AELKPGETVLDLGSGGGfDCFLAARRVGPTgkVIGVDMTPEMLAKARANARKAGYtnvefRLGEIEALPVADNSVDVIIS 152

                          90       100
                  ....*....|....*....|....*....
gi 2110921597 112 NFVLNHVGRPRAALRELRRVTRPGGRVSV 140
Cdd:PRK11873  153 NCVINLSPDKERVFKEAFRVLKPGGRFAI 181
PRK14968 PRK14968
putative methyltransferase; Provisional
 36-112 3.69e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 63.38  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  36 LLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRLASLPRL------PFADGRFDAV 109
Cdd:PRK14968   15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIrsdlfePFRGDKFDVI 94


                  ...
gi 2110921597 110 LGN 112
Cdd:PRK14968   95 LFN 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 16-136 1.46e-11

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: 62.69  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  16 GKAEAYAAGFAKL---CAYTVPALLHAAGVREGMRVLDAGTGTGTVAAAARELG--AEVTAVDAEPDMVARAARTVPEA- 89
Cdd:TIGR02072   3 NKAAKTYDRHAKIqreMAKRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLSENv 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2110921597  90 DVRLASLPRLPFADGRFDAVLGNFVLNHVGRPRAALRELRRVTRPGG 136
Cdd:TIGR02072  83 QFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG 129
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 36-140 2.29e-10

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: 59.00  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  36 LLHAAGVREGMRVLDAGTGTGTVA--AAARELGAEVTAVDAEPDMVARAARTV------PEADVRLASLPRLP--FADGR 105
Cdd:COG4123    29 LAAFAPVKKGGRVLDLGTGTGVIAlmLAQRSPGARITGVEIQPEAAELARRNValngleDRITVIHGDLKEFAaeLPPGS 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2110921597 106 FDAVLGN--FVLNHVGRP-----RAA------------LRELRRVTRPGGRVSV 140
Cdd:COG4123   109 FDLVVSNppYFKAGSGRKspdeaRAIarhedaltledlIRAAARLLKPGGRFAL 162
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
41-140 7.15e-10

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 57.83  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  41 GVREGMRVLDAGTGTGTVAAA-ARELGA--EVTAVDAEPDMVARAARTVPE---ADVRL--ASLPRLPFADGRFDAVLGN 112
Cdd:pfam01209  39 GVKRGNKFLDVAGGTGDWTFGlSDSAGSsgKVVGLDINENMLKEGEKKAKEegkYNIEFlqGNAEELPFEDDSFDIVTIS 118

                          90       100
                  ....*....|....*....|....*...
gi 2110921597 113 FVLNHVGRPRAALRELRRVTRPGGRVSV 140
Cdd:pfam01209 119 FGLRNFPDYLKVLKEAFRVLKPGGRVVC 146
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
35-112 8.69e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.14  E-value: 8.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  35 ALLHAA---GVREGMRVLDAGTGTGTVAAAARELGAE-VTAVDAEPDMVARAARTVPE----ADVRLASLPRLPFaDGRF 106
Cdd:COG2263    33 ELLHLAylrGDIEGKTVLDLGCGTGMLAIGAALLGAKkVVGVDIDPEALEIARENAERlgvrVDFIRADVTRIPL-GGSV 111


                  ....*.
gi 2110921597 107 DAVLGN 112
Cdd:COG2263   112 DTVVMN 117
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 31-137 4.09e-08

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 52.01  E-value: 4.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  31 YTVPALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARtvpeadvRLASL----PRLPFADGR- 105
Cdd:COG2518    53 YIVARMLEALDLKPGDRVLEIGTGSGYQAAVLARLAGRVYSVERDPELAERARE-------RLAALgydnVTVRVGDGAl 125

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2110921597 106 -------FDAVLGNFVLNHVgrPRAALRELrrvtRPGGR 137
Cdd:COG2518   126 gwpehapFDRIIVTAAAPEV--PEALLEQL----APGGR 158
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 1-118 5.37e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 52.15  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597   1 MTQTVFDRSERQAWA---GKAEAYA------AGFAKLCAyTVPALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTA 71
Cdd:PRK07580   12 EVRTYFNRTGFDRWAriySDAPVSKvratvrAGHQRMRD-TVLSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVA 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2110921597  72 VDAEPDMVARAARTVPEADVRlaslPRLPFADGRFDAVLGNFvlNHV 118
Cdd:PRK07580   91 SDISPQMVEEARERAPEAGLA----GNITFEVGDLESLLGRF--DTV 131
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 37-140 5.42e-08

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 52.47  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  37 LHAAGVREGMRVLDAGTGTGTVAAA-ARELGAE--VTAVDAEPDMVARAARTV------PEADVRLASLpRLPFADGRFD 107
Cdd:COG2519    84 IARLDIFPGARVLEAGTGSGALTLAlARAVGPEgkVYSYERREDFAEIARKNLerfglpDNVELKLGDI-REGIDEGDVD 162

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2110921597 108 AVlgnfVLNhVGRPRAALRELRRVTRPGGRVSV 140
Cdd:COG2519   163 AV----FLD-MPDPWEALEAVAKALKPGGVLVA 190
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
46-140 2.93e-07

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 50.35  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  46 MRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVrlasLPRLPFA-----------DGRFDAVLGNFV 114
Cdd:PRK11036   46 LRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGV----SDNMQFIhcaaqdiaqhlETPVDLILFHAV 121

                          90       100
                  ....*....|....*....|....*.
gi 2110921597 115 LNHVGRPRAALRELRRVTRPGGRVSV 140
Cdd:PRK11036  122 LEWVADPKSVLQTLWSVLRPGGALSL 147
PRK05785 PRK05785
hypothetical protein; Provisional
 47-133 3.36e-07

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 49.69  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  47 RVLDAGTGTGTVAAAAREL-GAEVTAVDAEPDMVARAArtvpEADVR-LASLPRLPFADGRFDAVLGNFVLNHVGRPRAA 124
Cdd:PRK05785   54 KVLDVAAGKGELSYHFKKVfKYYVVALDYAENMLKMNL----VADDKvVGSFEALPFRDKSFDVVMSSFALHASDNIEKV 129


                  ....*....
gi 2110921597 125 LRELRRVTR 133
Cdd:PRK05785  130 IAEFTRVSR 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 35-137 1.14e-06

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: 47.88  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  35 ALLHAAGVREGMRVLDAGTGTGTVA--AAARELGAEVTAVDAEPDMVARAART-----VPEADVRLASLpRLPFADGRFD 107
Cdd:COG2813    40 LLLEHLPEPLGGRVLDLGCGYGVIGlaLAKRNPEARVTLVDVNARAVELARANaaangLENVEVLWSDG-LSGVPDGSFD 118

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2110921597 108 AVLGN--FvlnHVGRPR--AALREL----RRVTRPGGR 137
Cdd:COG2813   119 LILSNppF---HAGRAVdkEVAHALiadaARHLRPGGE 153
PRK14967 PRK14967
putative methyltransferase; Provisional
 37-112 2.96e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 46.97  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  37 LHAAGVREGMRVLDAGTGTGTVAAAARELGAE-VTAVDAEPDMVARA-----ARTVPeADVRLASLPRLpFADGRFDAVL 110
Cdd:PRK14967   29 LAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGsVTAVDISRRAVRSArlnalLAGVD-VDVRRGDWARA-VEFRPFDVVV 106


                  ..
gi 2110921597 111 GN 112
Cdd:PRK14967  107 SN 108
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 45-117 3.89e-06

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 46.72  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  45 GMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRlaslPRLPF-------ADGRFDAVLGNFVLNH 117
Cdd:TIGR02021  56 GKRVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMARNRAQGRDVA----GNVEFevndllsLCGEFDIVVCMDVLIH 131
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
39-138 4.45e-06

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 46.82  E-value: 4.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  39 AAGVREGMRVLDAGTGTGTVAAAARELGA-EVTAVDAEPDMVARAAR-------TVPEADVRLAS----LPRLPfaDGRF 106
Cdd:COG2521   127 LVGVRRGDRVLDTCTGLGYTAIEALKRGArEVITVEKDPNVLELAELnpwsrelANERIKIILGDasevIKTFP--DESF 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2110921597 107 DAVLgnfvlnHvGRPRAAL----------RELRRVTRPGGRV 138
Cdd:COG2521   205 DAII------H-DPPRFSLagelyslefyRELYRVLKPGGRL 239
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 44-136 4.51e-06

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 47.04  E-value: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  44 EGMRVLDAGTGTGTVAAAARELGAEVTAVDAePDMVARAARTVPEADVRLASL-------PRLPFADGRFDAVLGNFVLN 116
Cdd:PLN02396  131 EGLKFIDIGCGGGLLSEPLARMGATVTGVDA-VDKNVKIARLHADMDPVTSTIeylcttaEKLADEGRKFDAVLSLEVIE 209

                          90       100
                  ....*....|....*....|
gi 2110921597 117 HVGRPRAALRELRRVTRPGG 136
Cdd:PLN02396  210 HVANPAEFCKSLSALTIPNG 229
PLN02244 PLN02244
tocopherol O-methyltransferase
 47-143 1.17e-05

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 45.89  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  47 RVLDAGTGTG-TVAAAARELGAEVTAVDAEPDMVARAARTVPEADV------RLASLPRLPFADGRFDAVLGNFVLNHVG 119
Cdd:PLN02244  121 RIVDVGCGIGgSSRYLARKYGANVKGITLSPVQAARANALAAAQGLsdkvsfQVADALNQPFEDGQFDLVWSMESGEHMP 200

                          90       100
                  ....*....|....*....|....
gi 2110921597 120 RPRAALRELRRVTRPGGRVSVTVW 143
Cdd:PLN02244  201 DKRKFVQELARVAAPGGRIIIVTW 224
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 40-140 1.54e-05

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 45.27  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  40 AGVREGMRVLDAGTGTGTVAAAARE---LGAEVTAVDAEPDMVARAARTVPEADVRLAS--------LPRLPFADGRFDA 108
Cdd:PLN02233   69 SGAKMGDRVLDLCCGSGDLAFLLSEkvgSDGKVMGLDFSSEQLAVAASRQELKAKSCYKniewiegdATDLPFDDCYFDA 148

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2110921597 109 VLGNFVLNHVGRPRAALRELRRVTRPGGRVSV 140
Cdd:PLN02233  149 ITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSI 180
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
42-138 2.39e-05

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 44.78  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  42 VREGMRVLDAGTGTGTVAAAARELGA-EVTAVDAEPDMVaRAART------VPEA-DVRLASLprlpFADGRFDAVLGNF 113
Cdd:COG2264   146 LKPGKTVLDVGCGSGILAIAAAKLGAkRVLAVDIDPVAV-EAAREnaelngVEDRiEVVLGDL----LEDGPYDLVVANI 220

                          90       100
                  ....*....|....*....|....*...
gi 2110921597 114 ---VLnhvgrpRAALRELRRVTRPGGRV 138
Cdd:COG2264   221 lanPL------IELAPDLAALLKPGGYL 242
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 37-110 3.10e-05

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 44.78  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  37 LHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRLAS---------LPRLpFADGRFD 107
Cdd:COG2265   226 LEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEfvagdleevLPEL-LWGGRPD 304


                  ...
gi 2110921597 108 AVL 110
Cdd:COG2265   305 VVV 307
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 37-112 3.13e-05

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 44.38  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  37 LHAAGVREGMRVLDAGTGTGTVAAA-AREL-GAEVTAVDAEPD--MVAR---AARTVPEADVRLASLprL-PFADGRFDA 108
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALAlAKERpDAEVTAVDISPEalAVARrnaKHGLGARVEFLQGDW--FePLPGGRFDL 178


                  ....
gi 2110921597 109 VLGN 112
Cdd:PRK09328  179 IVSN 182
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
32-136 4.75e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 43.18  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  32 TVPALLHAAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVR-----LASLPRLPFaDGRF 106
Cdd:PRK11207   18 THSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDnlhtaVVDLNNLTF-DGEY 96

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2110921597 107 DAVLGNFVLNHVGRPR--AALRELRRVTRPGG 136
Cdd:PRK11207   97 DFILSTVVLMFLEAKTipGLIANMQRCTKPGG 128
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
42-138 5.38e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.60  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  42 VREGMRVLDAGTGTGTVAAAARELGA-EVTAVDAEPdmVA-RAARtvpeADVRL---ASLPRLPFADGRFDAVLGNfVLN 116
Cdd:PRK00517  117 VLPGKTVLDVGCGSGILAIAAAKLGAkKVLAVDIDP--QAvEAAR----ENAELngvELNVYLPQGDLKADVIVAN-ILA 189

                          90       100
                  ....*....|....*....|....*.
gi 2110921597 117 HVgrpraaLREL----RRVTRPGGRV 138
Cdd:PRK00517  190 NP------LLELapdlARLLKPGGRL 209
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 18-142 8.09e-05

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 43.36  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  18 AEAYAAGFAKLCAYTvpALLHAAGVREGMRVL--DAGTGTGTVA-AAARELGAEVTAVDAEP--DMVAR--AARTVpeaD 90
Cdd:cd08267   119 EEAAALPVAGLTALQ--ALRDAGKVKPGQRVLinGASGGVGTFAvQIAKALGAHVTGVCSTRnaELVRSlgADEVI---D 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2110921597  91 VRLASLPRLPFADGRFDavlgnFVLNHVGRPRAALRELRRVTRPGGRVsVTV 142
Cdd:cd08267   194 YTTEDFVALTAGGEKYD-----VIFDAVGNSPFSLYRASLALKPGGRY-VSV 239
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 37-112 8.67e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.83  E-value: 8.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  37 LHAAGVREGMRVLDAGTGTGTVAAA-AREL-GAEVTAVDAEPD--MVAR--AARTVPEADVR------LASLPrlpfADG 104
Cdd:COG2890   105 LALLPAGAPPRVLDLGTGSGAIALAlAKERpDARVTAVDISPDalAVARrnAERLGLEDRVRflqgdlFEPLP----GDG 180


                  ....*...
gi 2110921597 105 RFDAVLGN 112
Cdd:COG2890   181 RFDLIVSN 188
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
39-86 1.51e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.95  E-value: 1.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2110921597  39 AAGVREGMRVLDAGTGTGTVAAAARELGAE-VTAVDAEPDMVARAARTV 86
Cdd:COG4076    30 ERVVKPGDVVLDIGTGSGLLSMLAARAGAKkVYAVEVNPDIAAVARRII 78
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
31-142 1.67e-04

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 41.58  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  31 YTVPALLHAAGVREGMRVLDAGTGTGTVAAA-ARELGAEVTAVDAE--PDMVARAARTVPEADvrLASLpRLPFADGR-- 105
Cdd:pfam01135  60 HMHAMMLELLELKPGMRVLEIGSGSGYLTACfARMVGEVGRVVSIEhiPELVEIARRNLEKLG--LENV-IVVVGDGRqg 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2110921597 106 ------FDAVlgnfvlnHVGR-----PRAALRELrrvtRPGGRVSVTV 142
Cdd:pfam01135 137 wpefapYDAI-------HVGAaapeiPEALIDQL----KEGGRLVIPV 173
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 39-143 2.51e-04

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 41.65  E-value: 2.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  39 AAGVREGMRVLDAGTGTG--TVAAAARelGAEVTAVDAEPDMVARAARTVP--------EADVRLASLPRLpfADGRFDA 108
Cdd:COG0030    32 AAGITPGDTVLEIGPGLGalTRALLER--AARVTAVEIDRRLAAILRETFAaypnltviEGDALKVDLPAL--AAGEPLK 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2110921597 109 VLGNF-----------VLNHVGRPRAAL----RE--LRRVTRPG----GRVSVTVW 143
Cdd:COG0030   108 VVGNLpynistpilfkLLEARPPIEDAVlmvqKEvaERLVAKPGskdyGRLSVLVQ 163
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 36-138 2.97e-04

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: 41.16  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  36 LLHAAGVREGMRVLDAGTGTGTVAA-AARELGAEVTAVDAEPDMVARAARTVPEAD------VRLASLPRLpfaDGRFDA 108
Cdd:pfam02353  53 ILDKLGLKPGMTLLDIGCGWGGLMRrAAERYDVNVVGLTLSKNQYKLARKRVAAEGlarkveVLLQDYRDF---DEPFDR 129

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2110921597 109 VLGNFVLNHVGRPRAAL--RELRRVTRPGGRV 138
Cdd:pfam02353 130 IVSVGMFEHVGHENYDTffKKLYNLLPPGGLM 161
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 37-165 4.51e-04

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 41.07  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  37 LHA---AGVREGMRVLDAGTGT--GTVAAAARELGA-EVTAVDAEPDMVARAARTVPEADVRLASLPRLPFAD--GRFDA 108
Cdd:cd08232   155 LHAvnrAGDLAGKRVLVTGAGPigALVVAAARRAGAaEIVATDLADAPLAVARAMGADETVNLARDPLAAYAAdkGDFDV 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2110921597 109 VL---GNfvlnhvgrpRAALRELRRVTRPGGRVsVTVWTAP---PAAGHALLGRAVQAAGAVR 165
Cdd:cd08232   235 VFeasGA---------PAALASALRVVRPGGTV-VQVGMLGgpvPLPLNALVAKELDLRGSFR 287
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 47-146 7.19e-04

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 40.28  E-value: 7.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  47 RVLDAGTGTGTVAAA-ARELGAEVTA----VDAEPDMVARAARTVPEADVRLASLPRLPFADGRFDAVLgnfvlnhvgRP 121
Cdd:PRK11088   88 ALLDIGCGEGYYTHAlADALPEITTMqlfgLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAII---------RI 158

                          90       100
                  ....*....|....*....|....*..
gi 2110921597 122 RAALR--ELRRVTRPGGRVsVTVWTAP 146
Cdd:PRK11088  159 YAPCKaeELARVVKPGGIV-ITVTPGP 184
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 44-124 8.31e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 40.23  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  44 EGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEADVRLAS--LPR-----LPFADGRFDAVLGNFVLN 116
Cdd:PLN02585  144 AGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAERRAKEALAALPPevLPKfeandLESLSGKYDTVTCLDVLI 223


                  ....*...
gi 2110921597 117 HVGRPRAA 124
Cdd:PLN02585  224 HYPQDKAD 231
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 99-140 1.19e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 38.52  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2110921597  99 LPFADGRFDAVLGNFVLNHVGRPRAALRELRRVTRPGGRVSV 140
Cdd:PLN02232   38 LPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSI 79
rADc smart00650
Ribosomal RNA adenine dimethylases;
39-112 1.44e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.26  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597   39 AAGVREGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARTVPEA--------DVRlaslpRLPFADGRFDAVL 110
Cdd:smart00650   8 AANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAAdnltvihgDAL-----KFDLPKLQPYKVV 82


                   ..
gi 2110921597  111 GN 112
Cdd:smart00650  83 GN 84
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
43-103 1.53e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 39.14  E-value: 1.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2110921597  43 REGMRVLDAGTGTGTVAAAARELGAEVTAVDAEPDMVARAARtvpeadvRLASLPRLPFAD 103
Cdd:COG0863   181 NPGDIVLDPFAGSGTTLVAAERLGRRFIGIEIDPEYVEVARR-------RLEEATGLEFEE 234
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 36-142 1.85e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 37.31  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  36 LLHAAGVREGMRVLDAGTGTGTVA--AAARELGAEVTAVDAEPDMVA-----RAARTVPEADVRLASLPRLPFADGR-FD 107
Cdd:TIGR02469  11 TLAKLRLRPGDVLWDIGAGTGSVTieAARLVPNGRVYAIERNPEALDliernLRRFGVSNIVIVEGDAPEAPEALLPdPD 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2110921597 108 AVlgnFVLNHVGRPRAALRELRRVTRPGGRVSVTV 142
Cdd:TIGR02469  91 AV---FVGGSGGLLQEILEAVERRLRPGGRIVLNA 122
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 44-116 1.87e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 39.17  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  44 EGMRVLDAGTGTGTV---AAAARELGAEVTAVDAEPDMV--------ARAARTVPEADVRLASLPRlPFADGRFDAVLGN 112
Cdd:COG5459    80 APLTVLDVGAGPGTAawaAADAWPSLLDATLLERSAAALalgrrlarAAANPALETAEWRLADLAA-ALPAPPADLVVAS 158


                  ....
gi 2110921597 113 FVLN 116
Cdd:COG5459   159 YVLN 162
PRK06202 PRK06202
hypothetical protein; Provisional
 46-133 2.61e-03

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 38.44  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  46 MRVLDAGTGTGTVA------AAARELGAEVTAVDAEPDMVARAARTVPEADVRL--ASLPRLPFADGRFDAVLGNFVLNH 117
Cdd:PRK06202   62 LTLLDIGCGGGDLAidlarwARRDGLRLEVTAIDPDPRAVAFARANPRRPGVTFrqAVSDELVAEGERFDVVTSNHFLHH 141

                          90
                  ....*....|....*...
gi 2110921597 118 VGRP--RAALRELRRVTR 133
Cdd:PRK06202  142 LDDAevVRLLADSAALAR 159
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 18-140 3.99e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.07  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  18 AEAYAAGFAKLCAYTvpALLHAAGVREGMRVLDAGTGT-GT-VAAAARELGAEVTAVDAEPDMVARA----ARTVPEADV 91
Cdd:cd05188   110 EEAALLPEPLATAYH--ALRRAGVLKPGDTVLVLGAGGvGLlAAQLAKAAGARVIVTDRSDEKLELAkelgADHVIDYKE 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2110921597  92 RLASLPRLPFADGRFDAvlgnfVLNHVGRPrAALRELRRVTRPGGRVSV 140
Cdd:cd05188   188 EDLEEELRLTGGGGADV-----VIDAVGGP-ETLAQALRLLRPGGRIVV 230
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 46-137 4.25e-03

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 37.95  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  46 MRVLDAGTGTG-TVAAAARELGAE-VTAVDAEPDMVARAARTVPEADVRL--ASLPRLPFADGRFDAVLGNFVLNHVGRP 121
Cdd:PLN02490  115 LKVVDVGGGTGfTTLGIVKHVDAKnVTILDQSPHQLAKAKQKEPLKECKIieGDAEDLPFPTDYADRYVSAGSIEYWPDP 194

                          90
                  ....*....|....*.
gi 2110921597 122 RAALRELRRVTRPGGR 137
Cdd:PLN02490  195 QRGIKEAYRVLKIGGK 210
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 28-140 4.37e-03

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 37.78  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  28 LCAYTVP--ALLHAaGVREGMRVLDAGTGT-GTVAAA-ARELGAEVTAVDAEPDMVARAAR-----TVPEADVRLASLPR 98
Cdd:COG1064   145 LCAGITAyrALRRA-GVGPGDRVAVIGAGGlGHLAVQiAKALGAEVIAVDRSPEKLELARElgadhVVNSSDEDPVEAVR 223

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2110921597  99 lpfADGRFDAvlgnfVLNHVGRPrAALRELRRVTRPGGRVSV 140
Cdd:COG1064   224 ---ELTGADV-----VIDTVGAP-ATVNAALALLRRGGRLVL 256
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 42-84 7.23e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 37.25  E-value: 7.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2110921597  42 VREGMRVLDAGTGTGTVAAAARELGA-EVTAVDAEPDMVaRAAR 84
Cdd:pfam06325 159 VKPGESVLDVGCGSGILAIAALKLGAkKVVGVDIDPVAV-RAAK 201
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
41-120 7.73e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 37.13  E-value: 7.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  41 GVREGMRVLDAGTGTGTVAA-AARELGAEVTAV--DAEPDMVARAartvpeadvRLASLP---RLpfAD-----GRFDAV 109
Cdd:PRK11705  164 QLKPGMRVLDIGCGWGGLARyAAEHYGVSVVGVtiSAEQQKLAQE---------RCAGLPveiRL--QDyrdlnGQFDRI 232

                          90
                  ....*....|...
gi 2110921597 110 --LGNFvlNHVGR 120
Cdd:PRK11705  233 vsVGMF--EHVGP 243
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 38-138 8.27e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 37.17  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2110921597  38 HA---AGVREGMRVLDAGTG-TG-TVAAAARELGAEVTAVDAEPDMVARAARTvpEADVRLASLPRLPFAD--GRFDAVL 110
Cdd:cd08261   150 HAvrrAGVTAGDTVLVVGAGpIGlGVIQVAKARGARVIVVDIDDERLEFAREL--GADDTINVGDEDVAARlrELTDGEG 227

                          90       100
                  ....*....|....*....|....*...
gi 2110921597 111 GNFVLNHVGRPrAALRELRRVTRPGGRV 138
Cdd:cd08261   228 ADVVIDATGNP-ASMEEAVELVAHGGRV 254
 
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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