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Conserved domains on  [gi|2585747368|ref|WP_313572833|]
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methyltransferase domain-containing protein [Empedobacter sp.]

Protein Classification

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

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 25-146 2.53e-21

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 85.84  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  25 TEAEDFIQKITNYLQ--LPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQFENEY-LKFEKHDMREV-YH 100
Cdd:COG2227     5 DARDFWDRRLAALLArlLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnVDFVQGDLEDLpLE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2585747368 101 PNEFDAVFnlftSFGYFENYEDNFKVFEAVKQQIKSHGIFVLDYLN 146
Cdd:COG2227    85 DGSFDLVI----CSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 25-146 2.53e-21

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 85.84  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  25 TEAEDFIQKITNYLQ--LPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQFENEY-LKFEKHDMREV-YH 100
Cdd:COG2227     5 DARDFWDRRLAALLArlLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnVDFVQGDLEDLpLE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2585747368 101 PNEFDAVFnlftSFGYFENYEDNFKVFEAVKQQIKSHGIFVLDYLN 146
Cdd:COG2227    85 DGSFDLVI----CSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-138 4.66e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 65.66  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  46 VLDLACGKGRHAITL-NKLGFDVLGIDLSEESIKYAKQ---FENEYLKFEKHDMREV-YHPNEFDAVFNLFtSFGYFENy 120
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERAREraaEAGLNVEFVQGDAEDLpFPDGSFDLVVSSG-VLHHLPD- 78

                          90
                  ....*....|....*...
gi 2585747368 121 EDNFKVFEAVKQQIKSHG 138
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-145 3.49e-10

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: 55.51  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  45 KVLDLACGKGRHAITLNKLGFD-VLGIDLSEESIKYAKQFENEYL----KFEKHDMREV--YHPNEFDAVFNLFTSFGYF 117
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadnvEVLKGDAEELppEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*...
gi 2585747368 118 ENYEDnfkVFEAVKQQIKSHGIFVLDYL 145
Cdd:cd02440    81 EDLAR---FLEEARRLLKPGGVLVLTLV 105
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 2-77 1.04e-07

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 51.48  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2585747368   2 DLQWFVKWFNSP--YYHILYkNRSLTEAEdfiqkITNYLQLPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESI 77
Cdd:PRK12335   84 DLECQLSFYCKPedYFHKKY-NLTATHSE-----VLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSL 155
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 25-146 2.53e-21

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 85.84  E-value: 2.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  25 TEAEDFIQKITNYLQ--LPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQFENEY-LKFEKHDMREV-YH 100
Cdd:COG2227     5 DARDFWDRRLAALLArlLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELnVDFVQGDLEDLpLE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2585747368 101 PNEFDAVFnlftSFGYFENYEDNFKVFEAVKQQIKSHGIFVLDYLN 146
Cdd:COG2227    85 DGSFDLVI----CSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 15-142 3.37e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 81.13  E-value: 3.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  15 YHILY---KNRSLTEA-EDFIQKITNYLQLPQHAKVLDLACGKGRHAITLNK-LGFDVLGIDLSEESIKYAKQFENEY-- 87
Cdd:COG2230    20 YSCAYfedPDDTLEEAqEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARrYGVRVTGVTLSPEQLEYARERAAEAgl 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2585747368  88 ---LKFEKHDMREVYHPNEFDAVFnlftSFGYFE-----NYEDnfkVFEAVKQQIKSHGIFVL 142
Cdd:COG2230   100 adrVEVRLADYRDLPADGQFDAIV----SIGMFEhvgpeNYPA---YFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
28-148 6.38e-17

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 75.81  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  28 EDFIQKITNYLQLPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQfENEYLKFEKHDMREVYHPNE-FDA 106
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKARE-KGVYDRLLVADLADLAEPDGrFDL 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2585747368 107 VFnLFTSFGYFENYEDnfkVFEAVKQQIKSHGIFVLDYLNAE 148
Cdd:COG4976   111 IV-AADVLTYLGDLAA---VFAGVARALKPGGLFIFSVEDAD 148
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 30-152 2.90e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 71.87  E-value: 2.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  30 FIQKITNYLQLPQHAKVLDLACGKGRHAITL-NKLGFDVLGIDLSEESIKYAKQFENEY----LKFEKHDMREV--YHPN 102
Cdd:COG0500    14 LAALLALLERLPKGGRVLDLGCGTGRNLLALaARFGGRVIGIDLSPEAIALARARAAKAglgnVEFLVADLAELdpLPAE 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2585747368 103 EFDAVFnLFTSFgYFENYEDNFKVFEAVKQQIKSHGIFVLDYLNAEKVVS 152
Cdd:COG0500    94 SFDLVV-AFGVL-HHLPPEEREALLRELARALKPGGVLLLSASDAAAALS 141
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 29-142 2.96e-15

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: 70.41  E-value: 2.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  29 DFIQKITNYLQLPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQFENEY---LKFEKHDMREV-YHPNEF 104
Cdd:COG2226     9 DGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglnVEFVVGDAEDLpFPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2585747368 105 DAVFNLFTsfgyFENYEDNFKVFEAVKQQIKSHGIFVL 142
Cdd:COG2226    89 DLVISSFV----LHHLPDPERALAEIARVLKPGGRLVV 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-138 4.66e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 65.66  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  46 VLDLACGKGRHAITL-NKLGFDVLGIDLSEESIKYAKQ---FENEYLKFEKHDMREV-YHPNEFDAVFNLFtSFGYFENy 120
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERAREraaEAGLNVEFVQGDAEDLpFPDGSFDLVVSSG-VLHHLPD- 78

                          90
                  ....*....|....*...
gi 2585747368 121 EDNFKVFEAVKQQIKSHG 138
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-142 7.97e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 62.30  E-value: 7.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  47 LDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQ-FENEYLKFEKHDMREV-YHPNEFDAVFnlftSFGYFENYEDNF 124
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkAPREGLTFVVGDAEDLpFPDNSFDLVL----SSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 2585747368 125 KVFEAVKQQIKSHGIFVL 142
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
42-143 3.33e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.60  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  42 QHAKVLDLACGKGRHAITLNKL--GFDVLGIDLSEESIKYAKQfENEYLKFEKHDMREVYHPNEFDAVFnLFTSFGYFen 119
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARA-RLPNVRFVVADLRDLDPPEPFDLVV-SNAALHWL-- 76

                          90       100
                  ....*....|....*....|....
gi 2585747368 120 yEDNFKVFEAVKQQIKSHGIFVLD 143
Cdd:COG4106    77 -PDHAALLARLAAALAPGGVLAVQ 99
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-145 3.49e-10

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: 55.51  E-value: 3.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  45 KVLDLACGKGRHAITLNKLGFD-VLGIDLSEESIKYAKQFENEYL----KFEKHDMREV--YHPNEFDAVFNLFTSFGYF 117
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKAAAALLadnvEVLKGDAEELppEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....*...
gi 2585747368 118 ENYEDnfkVFEAVKQQIKSHGIFVLDYL 145
Cdd:cd02440    81 EDLAR---FLEEARRLLKPGGVLVLTLV 105
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 45-170 3.67e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 56.66  E-value: 3.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  45 KVLDLACGKGRHAITLNKLGF---DVLGIDLSEESIKYAKQ------FENeyLKFEK---HDMREVYHPNEFDAVFnlft 112
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKAREnaqklgFDN--VEFEQgdiEELPELLEDDKFDVVI---- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2585747368 113 SFGYFENYEDNFKVFEAVKQQIKSHGIFVLDYLNAEKVVSKMIPYEEKLIDGILFKIT 170
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAI 137
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 2-77 1.04e-07

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 51.48  E-value: 1.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2585747368   2 DLQWFVKWFNSP--YYHILYkNRSLTEAEdfiqkITNYLQLPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESI 77
Cdd:PRK12335   84 DLECQLSFYCKPedYFHKKY-NLTATHSE-----VLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSL 155
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-148 2.09e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 46.27  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  40 LPQHAKVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQFeneyLKFEKHDMREVYHPNEFdavFNLFTSFGYFEN 119
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLN----VRFDQFDEQEAAVPAGK---FDVIVAREVLEH 92

                          90       100
                  ....*....|....*....|....*....
gi 2585747368 120 YEDNFKVFEAVKQQIKSHGIFVLDYLNAE 148
Cdd:pfam13489  93 VPDPPALLRQIAALLKPGGLLLLSTPLAS 121
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
44-107 2.86e-05

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 43.57  E-value: 2.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  44 AKVLDLACGKGRHAITLNKLGFDVLGIDLSE------ESIKYAKQFENeyLKFEKHDMREVYHPNEFDAV 107
Cdd:PRK11207   32 GKTLDLGCGNGRNSLYLAANGFDVTAWDKNPmsianlERIKAAENLDN--LHTAVVDLNNLTFDGEYDFI 99
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 38-142 1.13e-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: 42.31  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  38 LQLPQHAKVLDLACGKG---RHAITlnKLGFDVLGIDLSEESIKYAKQ-FENEYLKfekhDMREVYH------PNEFDAV 107
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGglmRRAAE--RYDVNVVGLTLSKNQYKLARKrVAAEGLA----RKVEVLLqdyrdfDEPFDRI 130

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2585747368 108 --FNLFTSFGYfENYEDNFKvfeAVKQQIKSHGIFVL 142
Cdd:pfam02353 131 vsVGMFEHVGH-ENYDTFFK---KLYNLLPPGGLMLL 163
TehB pfam03848
Tellurite resistance protein TehB;
45-82 1.76e-04

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 41.37  E-value: 1.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2585747368  45 KVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQ 82
Cdd:pfam03848  33 KVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQR 70
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
45-108 1.79e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 41.04  E-value: 1.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2585747368  45 KVLDLACGKGRHAITLNKLGF-DVLGIDLSEESIKYAKQFENEY---LKFEKHDMREVYHPNEFDAVF 108
Cdd:COG2263    48 TVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLgvrVDFIRADVTRIPLGGSVDTVV 115
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
23-142 5.26e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 40.60  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  23 SLTEA-EDFIQKITNYLQLPQHAKVLDLACGKG---RHAITlnKLGFDVLGIDLSEESIKYAKQF-ENEYLKFEKHDMRE 97
Cdd:PRK11705  147 TLEEAqEAKLDLICRKLQLKPGMRVLDIGCGWGglaRYAAE--HYGVSVVGVTISAEQQKLAQERcAGLPVEIRLQDYRD 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2585747368  98 VYHPneFDAVFnlftSFGYFE-----NYEDNFKVfeaVKQQIKSHGIFVL 142
Cdd:PRK11705  225 LNGQ--FDRIV----SVGMFEhvgpkNYRTYFEV---VRRCLKPDGLFLL 265
PRK14968 PRK14968
putative methyltransferase; Provisional
 45-109 2.30e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 37.96  E-value: 2.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2585747368  45 KVLDLACGKGRHAITLNKLGFDVLGIDLSEESIKYAKQ------FENEYLKFEKHDMREVYHPNEFDAV-FN 109
Cdd:PRK14968   26 RVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCnaklnnIRNNGVEVIRSDLFEPFRGDKFDVIlFN 97
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 33-149 5.20e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 37.26  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  33 KITNYLQLPQHAKVLDLACGKGRHAITLN-KLGFDVLGIDLSEESIKYAKQF--ENEYLKFEKHDMREVYHP-NEFDAVF 108
Cdd:PTZ00098   43 KILSDIELNENSKVLDIGSGLGGGCKYINeKYGAHVHGVDICEKMVNIAKLRnsDKNKIEFEANDILKKDFPeNTFDMIY 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2585747368 109 NLFTSFGYfeNYEDNFKVFEAVKQQIKSHGIFVL-DYLNAEK 149
Cdd:PTZ00098  123 SRDAILHL--SYADKKKLFEKCYKWLKPNGILLItDYCADKI 162
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 45-216 8.66e-03

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 36.64  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368  45 KVLDLACGKGRHAITLNKLGFDVL-GIDLSEESIK-----YAKQFENEYLKFEKHD------------MREVYHPNE--F 104
Cdd:pfam03291  66 KVLDLGCGKGGDLEKWFKGGISQLiGTDIAEVSIEqcrerYNKLRSGNKSKYYKFDaefitgdcfvssLREVFEDPFgkF 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2585747368 105 DAVFNLFTSFGYFENYEDNFKVFEAVKQQIKSHGIFVLDYLNAEKVV------SKMIPYEEKLIDGILFKIT---KSVQN 175
Cdd:pfam03291 146 DIVSCQFAIHYSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFISaltikrLFAIEKDLPSFGNSIYSVKfeeEPPQV 225

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2585747368 176 GFIKKEIDFRDKGEIFHFEEFVrlIYFNDFKKIYETEGFIL 216
Cdd:pfam03291 226 PLFGIKYDYNLEDAVDDVPEYI--VPFETLVSLAEEYGLEL 264
 
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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