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Conserved domains on  [gi|1863098424|gb|QKZ07401|]
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methyltransferase domain-containing protein [Pseudomonas eucalypticola]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-151 1.17e-30

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: 108.95  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  39 IEALLRHIqVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMAR---ADSGCEVWQQNFLALDLPTEHFDGIF 115
Cdd:COG2227    14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAReraAELNVDFVQGDLEDLPLEDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1863098424 116 ANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNPR 151
Cdd:COG2227    93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-151 1.17e-30

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: 108.95  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  39 IEALLRHIqVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMAR---ADSGCEVWQQNFLALDLPTEHFDGIF 115
Cdd:COG2227    14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAReraAELNVDFVQGDLEDLPLEDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1863098424 116 ANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNPR 151
Cdd:COG2227    93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-143 2.06e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 89.55  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  54 ILDFGCGPGRDLRTF-TALGHTATGLDGSERFAEMAR-----ADSGCEVWQQNFLALDLPTEHFDGIFANAVLFHIPTQE 127
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERAReraaeAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 1863098424 128 LPRVLRQLHATLKPGG 143
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 53-146 1.56e-13

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: 63.99  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  53 RILDFGCGPGRDLRTF-TALGHTATGLDGSERFAEMARA------DSGCEVWQQNFLALDL-PTEHFDGIFANAVLFHIP 124
Cdd:cd02440     1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPeADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|..
gi 1863098424 125 tQELPRVLRQLHATLKPGGVLF 146
Cdd:cd02440    81 -EDLARFLEEARRLLKPGGVLV 101
PRK08317 PRK08317
hypothetical protein; Provisional
 40-143 5.24e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 57.25  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  40 EALLRHIQVPAPARILDFGCGPGRDLRTFT-ALGHT--ATGLDGSER---FAEMARADSG--CEVWQQNFLALDLPTEHF 111
Cdd:PRK08317    9 ARTFELLAVQPGDRVLDVGCGPGNDARELArRVGPEgrVVGIDRSEAmlaLAKERAAGLGpnVEFVRGDADGLPFPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1863098424 112 DGIFANAVLFHIPtqELPRVLRQLHATLKPGG 143
Cdd:PRK08317   89 DAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 41-187 3.50e-09

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: 54.60  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  41 ALLRHIQVPAPARILDFGCGPG---RDLR-TFTALGHTATGL-DGSERFAEMARADsgcevwQQNFLA-----LDLPTEH 110
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGyltRALLkRFPQAEFIALDIsAGMLAQAKTKLSE------NVQFICgdaekLPLEDSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424 111 FDGIFANAVL--FHiptqELPRVLRQLHATLKPGGVL-FSSNPRGENQE-----GWNGPRygaYHDLDTWRRVLAEAgFV 182
Cdd:TIGR02072  99 FDLIVSNLALqwCD----DLSQALSELARVLKPGGLLaFSTFGPGTLHElrqsfGQHGLR---YLSLDELKALLKNS-FE 170


                  ....*
gi 1863098424 183 ELEHY 187
Cdd:TIGR02072 171 LLTLE 175
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 99-146 1.05e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 38.81  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1863098424   99 QNFLALDLPTEHFDGIFANAVL--FHIPTQElpRVLRQLHATLKPGGVLF 146
Cdd:smart00138 192 HNLLAESPPLGDFDLIFCRNVLiyFDEPTQR--KLLNRFAEALKPGGYLF 239
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 39-151 1.17e-30

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: 108.95  E-value: 1.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  39 IEALLRHIqVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMAR---ADSGCEVWQQNFLALDLPTEHFDGIF 115
Cdd:COG2227    14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAReraAELNVDFVQGDLEDLPLEDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1863098424 116 ANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNPR 151
Cdd:COG2227    93 CSEVLEHLP--DPAALLRELARLLKPGGLLLLSTPN 126
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
10-208 2.95e-28

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 104.70  E-value: 2.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  10 QITDVTLGNYNQTAERFregtrDHDVSQN---------IEALLRHIQVPAPARILDFGCGPGRDLRTFTALGHTATGLDG 80
Cdd:COG4976     2 ALDAYVEALFDQYADSY-----DAALVEDlgyeapallAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  81 SERFAEMARA-DSGCEVWQQNFLALDLPTEHFDGIFANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNPRGENqEGwn 159
Cdd:COG4976    77 SEEMLAKAREkGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLG--DLAAVFAGVARALKPGGLFIFSVEDADG-SG-- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1863098424 160 gpRYgaYHDLDTWRRVLAEAGFvelehyyrpaglpreQQPWLASVWRKA 208
Cdd:COG4976   152 --RY--AHSLDYVRDLLAAAGF---------------EVPGLLVVARKP 181
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-181 2.01e-24

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: 93.52  E-value: 2.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  40 EALLRHIQVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMAR-----ADSGCEVWQQNFLALDLPTEHFDGI 114
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELAReraaeAGLNVEFVVGDAEDLPFPDGSFDLV 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863098424 115 FANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNprgenqegWNGPrygayhDLDTWRRVLAEAGF 181
Cdd:COG2226    92 ISSFVLHHLP--DPERALAEIARVLKPGGRLVVVD--------FSPP------DLAELEELLAEAGF 142
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
50-146 2.19e-24

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 92.19  E-value: 2.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  50 APARILDFGCGPGRDLRTFTAL--GHTATGLDGSERFAEMARA-DSGCEVWQQNFLALDLPtEHFDGIFANAVLFHIPtq 126
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARArLPNVRFVVADLRDLDPP-EPFDLVVSNAALHWLP-- 77

                          90       100
                  ....*....|....*....|
gi 1863098424 127 ELPRVLRQLHATLKPGGVLF 146
Cdd:COG4106    78 DHAALLARLAAALAPGGVLA 97
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-143 2.06e-23

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 89.55  E-value: 2.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  54 ILDFGCGPGRDLRTF-TALGHTATGLDGSERFAEMAR-----ADSGCEVWQQNFLALDLPTEHFDGIFANAVLFHIPTQE 127
Cdd:pfam13649   1 VLDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERAReraaeAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*.
gi 1863098424 128 LPRVLRQLHATLKPGG 143
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-182 6.91e-20

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 83.43  E-value: 6.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  49 PAPARILDFGCGPGRDLRTFTAL-GHTATGLDGSERFAEMARAD------SGCEVWQQNFLAL-DLPTEHFDGIFANAVL 120
Cdd:COG0500    25 PKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARaakaglGNVEFLVADLAELdPLPAESFDLVVAFGVL 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863098424 121 FHIPTQELPRVLRQLHATLKPGGVLF----SSNPRGENQEGWNGPRYGAYHDLDTWRRVLAEAGFV 182
Cdd:COG0500   105 HHLPPEEREALLRELARALKPGGVLLlsasDAAAALSLARLLLLATASLLELLLLLRLLALELYLR 170
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 26-146 2.22e-19

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 80.74  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  26 FREGTRDHDVSQN--IEALLRHIQVPAPARILDFGCGPGRDLRTF-TALGHTATGLDGSERFAEMARA-------DSGCE 95
Cdd:COG2230    25 FEDPDDTLEEAQEakLDLILRKLGLKPGMRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYAREraaeaglADRVE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1863098424  96 VWQQNFLALDlPTEHFDGIFANAVLFHIPTQELPRVLRQLHATLKPGGVLF 146
Cdd:COG2230   105 VRLADYRDLP-ADGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLL 154
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 55-146 2.66e-18

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 76.16  E-value: 2.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  55 LDFGCGPGRDLRTFTALGHTATGLDGSERFAEMARA---DSGCEVWQQNFLALDLPTEHFDGIFANAVLFHIPtqELPRV 131
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkapREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVE--DPERA 78

                          90
                  ....*....|....*
gi 1863098424 132 LRQLHATLKPGGVLF 146
Cdd:pfam08241  79 LREIARVLKPGGILI 93
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 31-181 7.13e-16

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 71.69  E-value: 7.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  31 RDHDVSQNIEALLRHIqvPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMARADSGCEvwQQNFLALDLPTEH 110
Cdd:pfam13489   5 RERLLADLLLRLLPKL--PSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFD--QFDEQEAAVPAGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424 111 FDGIFANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNP--------RGENQEGWNgPRYG--AYHDLDTWRRVLAEAG 180
Cdd:pfam13489  81 FDVIVAREVLEHVP--DPPALLRQIAALLKPGGLLLLSTPlasdeadrLLLEWPYLR-PRNGhiSLFSARSLKRLLEEAG 157


                  .
gi 1863098424 181 F 181
Cdd:pfam13489 158 F 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 53-146 1.56e-13

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: 63.99  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  53 RILDFGCGPGRDLRTF-TALGHTATGLDGSERFAEMARA------DSGCEVWQQNFLALDL-PTEHFDGIFANAVLFHIP 124
Cdd:cd02440     1 RVLDLGCGTGALALALaSGPGARVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPeADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|..
gi 1863098424 125 tQELPRVLRQLHATLKPGGVLF 146
Cdd:cd02440    81 -EDLARFLEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 55-145 2.83e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.46  E-value: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  55 LDFGCGPGRDLRTFTALGHTA--TGLDGSERFAEMAR----ADSGCEVWQQNFLALDLPTE---HFDGIFANAVLFHIPt 125
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeyTGLDISPAALEAARerlaALGLLNAVRVELFQLDLGELdpgSFDVVVASNVLHHLA- 79

                          90       100
                  ....*....|....*....|
gi 1863098424 126 qELPRVLRQLHATLKPGGVL 145
Cdd:pfam08242  80 -DPRAVLRNIRRLLKPGGVL 98
PRK08317 PRK08317
hypothetical protein; Provisional
 40-143 5.24e-10

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 57.25  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  40 EALLRHIQVPAPARILDFGCGPGRDLRTFT-ALGHT--ATGLDGSER---FAEMARADSG--CEVWQQNFLALDLPTEHF 111
Cdd:PRK08317    9 ARTFELLAVQPGDRVLDVGCGPGNDARELArRVGPEgrVVGIDRSEAmlaLAKERAAGLGpnVEFVRGDADGLPFPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1863098424 112 DGIFANAVLFHIPtqELPRVLRQLHATLKPGG 143
Cdd:PRK08317   89 DAVRSDRVLQHLE--DPARALAEIARVLRPGG 118
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 53-180 1.44e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 54.35  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  53 RILDFGCGPGRDL-RTFTALGHTA--TGLDGSERFAEMARAD------SGCEVWQQNFLALD--LPTEHFDGIFANAVLF 121
Cdd:pfam13847   6 RVLDLGCGTGHLSfELAEELGPNAevVGIDISEEAIEKARENaqklgfDNVEFEQGDIEELPelLEDDKFDVVISNCVLN 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1863098424 122 HIPtqELPRVLRQLHATLKPGGVLFSSNPRG---------ENQEGWNGPRYGAYhDLDTWRRVLAEAG 180
Cdd:pfam13847  86 HIP--DPDKVLQEILRVLKPGGRLIISDPDSlaelpahvkEDSTYYAGCVGGAI-LKKKLYELLEEAG 150
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 42-145 2.34e-09

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 55.33  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  42 LLRHIQVPAPARILDFGCGPGRDlrtfTALGH------TATGLDGSERFAEMARAdsgcEVWQQNFLALDL----PTEHF 111
Cdd:PRK01683   23 LLARVPLENPRYVVDLGCGPGNS----TELLVerwpaaRITGIDSSPAMLAEARS----RLPDCQFVEADIaswqPPQAL 94

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1863098424 112 DGIFANAVLFHIPTQE--LPRVLRQlhatLKPGGVL 145
Cdd:PRK01683   95 DLIFANASLQWLPDHLelFPRLVSL----LAPGGVL 126
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 41-187 3.50e-09

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: 54.60  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  41 ALLRHIQVPAPARILDFGCGPG---RDLR-TFTALGHTATGL-DGSERFAEMARADsgcevwQQNFLA-----LDLPTEH 110
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGyltRALLkRFPQAEFIALDIsAGMLAQAKTKLSE------NVQFICgdaekLPLEDSS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424 111 FDGIFANAVL--FHiptqELPRVLRQLHATLKPGGVL-FSSNPRGENQE-----GWNGPRygaYHDLDTWRRVLAEAgFV 182
Cdd:TIGR02072  99 FDLIVSNLALqwCD----DLSQALSELARVLKPGGLLaFSTFGPGTLHElrqsfGQHGLR---YLSLDELKALLKNS-FE 170


                  ....*
gi 1863098424 183 ELEHY 187
Cdd:TIGR02072 171 LLTLE 175
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 23-146 2.34e-07

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: 49.03  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  23 AERFREGTRdhdvsqnieALLRHIQVPAPARILDFGCGPGrdlrtftALGHTA---------TGLDGSERFAEMARA--- 90
Cdd:COG2813    31 RDRLDIGTR---------LLLEHLPEPLGGRVLDLGCGYG-------VIGLALakrnpearvTLVDVNARAVELARAnaa 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1863098424  91 ---DSGCEVWQQNFLAlDLPTEHFDGIFANAVlFHIPTQELPRVLRQL----HATLKPGGVLF 146
Cdd:COG2813    95 angLENVEVLWSDGLS-GVPDGSFDLILSNPP-FHAGRAVDKEVAHALiadaARHLRPGGELW 155
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 24-143 4.35e-06

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 45.88  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  24 ERFREGTRDHDVSQNIEALLRH---IQVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSE------------------ 82
Cdd:pfam05724   8 KRWVEGQTPFHQEGVNPLLVRHwdaLKLPPGLRVLVPLCGKALDMVWLAEQGHFVVGVEISElavekffaeaglsppite 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1863098424  83 -RFAEMARADsGCEVWQQNFLALDlPTE--HFDGIFANAVLFHIPTQELPRVLRQLHATLKPGG 143
Cdd:pfam05724  88 lSGFKEYSSG-NISLYCGDFFTLP-REElgKFDLIYDRAALCALPPEMRPRYAKQMYELLPPGG 149
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 35-145 7.98e-06

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: 45.33  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  35 VSQNIEALLRHIQVPAPARILDFGCGPG----------RDLRTFTALGHTATGLDGSERFAEMARADSGCEV-WQQNFLA 103
Cdd:COG5459    65 VRAALAELAEAGPDFAPLTVLDVGAGPGtaawaaadawPSLLDATLLERSAAALALGRRLARAAANPALETAeWRLADLA 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1863098424 104 LDLPTEHFDGIFANAVLFHIPTQELPRVLRQLhaTLKPGGVL 145
Cdd:COG5459   145 AALPAPPADLVVASYVLNELADAARAALVDRL--WLAPDGAL 184
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 37-145 8.07e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 45.13  E-value: 8.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  37 QNIEALLRHIQVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMARADSGCEVWQQ-NFLALDLPTEHFDGIF 115
Cdd:PRK10258   29 QSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAADHYLAgDIESLPLATATFDLAW 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1863098424 116 AN-AVLFhipTQELPRVLRQLHATLKPGGVL 145
Cdd:PRK10258  109 SNlAVQW---CGNLSTALRELYRVVRPGGVV 136
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 32-159 2.52e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 43.81  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  32 DHDVSQNIEA---LLRHIQVPAPARILDFGCGPGRDLRTFT-ALGHTATGLDGSERFAEMAR----ADSGCEVWQQNFLA 103
Cdd:PTZ00098   31 DYISSGGIEAttkILSDIELNENSKVLDIGSGLGGGCKYINeKYGAHVHGVDICEKMVNIAKlrnsDKNKIEFEANDILK 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1863098424 104 LDLPTEHFDGIFANAVLFHIPTQELPRVLRQLHATLKPGGVLFSSNPRGENQEGWN 159
Cdd:PTZ00098  111 KDFPENTFDMIYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADKIENWD 166
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
104-197 2.68e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 42.93  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424 104 LDLPTEHFDGIFANAVLFHIPTQELPRVLRQLHATLKPGGVLFSSNPRGENQEGWNGPRYGAYHDLDTWRRVLAEAGFVe 183
Cdd:COG4627    40 LPFPDNSVDAIYSSHVLEHLDYEEAPLALKECYRVLKPGGILRIVVPDLEHVARLYLAEYDAALDVAELRLAGPIDPLG- 118

                          90
                  ....*....|....
gi 1863098424 184 LEHYYRPAGLPREQ 197
Cdd:COG4627   119 IILGERLAGLAARH 132
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 40-146 3.15e-05

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


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 42.58  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  40 EALLRHIQVPAPARILDFGCGPGrdlrtftALG---------HTATGLDGSERFAEMARAD------SGCEVWQQNFLAl 104
Cdd:pfam05175  21 RLLLEHLPKDLSGKVLDLGCGAG-------VLGaalakespdAELTMVDINARALESARENlaanglENGEVVASDVYS- 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1863098424 105 DLPTEHFDGIFANAVlFHIPTQELPRVLRQLHAT----LKPGGVLF 146
Cdd:pfam05175  93 GVEDGKFDLIISNPP-FHAGLATTYNVAQRFIADakrhLRPGGELW 137
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 42-181 1.50e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 41.60  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  42 LLRHIQVPAPARILDFGCGPGRDLRTFTALGHTA--TGLDGSERFAEMARADSgcevwqQNFLALDL----PTEHFDGIF 115
Cdd:PRK14103   21 LLARVGAERARRVVDLGCGPGNLTRYLARRWPGAviEALDSSPEMVAAARERG------VDARTGDVrdwkPKPDTDVVV 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1863098424 116 ANAVLFHIPtqELPRVLRQLHATLKPGGVLFSSNPrgenqEGWNGPRYGAYHDL---DTWRRVLAEAGF 181
Cdd:PRK14103   95 SNAALQWVP--EHADLLVRWVDELAPGSWIAVQVP-----GNFDAPSHAAVRALarrEPWAKLLRDIPF 156
TehB pfam03848
Tellurite resistance protein TehB;
30-143 4.41e-04

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 39.83  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  30 TRDHdvSQNIEAllrhIQVPAPARILDFGCGPGRDLRTFTALGHTATGLDGSE-------RFAEMARADS-GCEVWQQNF 101
Cdd:pfam03848  16 TPTH--SEVLEA----VKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNEnsianlqRIKEKENLDNiHTALYDINN 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1863098424 102 LALDlptEHFDGIFANAVLFHIPTQELPRVLRQLHATLKPGG 143
Cdd:pfam03848  90 ATID---ENYDFILSTVVLMFLEPERIPGIIANMQECTNPGG 128
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
18-145 5.89e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 39.56  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  18 NYNQTAERFRE---GT-----RDHDVSQNIEALLRHIQvPAPARILDFGCGPGRDLRTFTALGHTATGLDGSERFAEMAR 89
Cdd:PRK11036    5 NFDDIAEKFSRniyGTtkgqiRQAILWQDLDRLLAELP-PRPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAK 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863098424  90 ADSGCEVWQQNFLALDLPT----EHFDGIfANAVLFHI-------PTQelprVLRQLHATLKPGGVL 145
Cdd:PRK11036   84 QAAEAKGVSDNMQFIHCAAqdiaQHLETP-VDLILFHAvlewvadPKS----VLQTLWSVLRPGGAL 145
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 107-184 7.15e-04

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.73  E-value: 7.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424 107 PTEHFDGIFANAVLFHIptQELPRVLRQLHATLKPGG-VLFSSNPRgenQEGWNGPRYGAY--------HDLDTWRRVLA 177
Cdd:PLN02336  329 PDNSFDVIYSRDTILHI--QDKPALFRSFFKWLKPGGkVLISDYCR---SPGTPSPEFAEYikqrgydlHDVQAYGQMLK 403


                  ....*..
gi 1863098424 178 EAGFVEL 184
Cdd:PLN02336  404 DAGFDDV 410
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
98-146 9.36e-04

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 38.99  E-value: 9.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1863098424  98 QQNFLALDLPTEHFDGIF-ANaVL--FHIPTQElpRVLRQLHATLKPGGVLF 146
Cdd:COG1352   194 QHNLLDDPPPFGRFDLIFcRN-VLiyFDPELQR--RVLRRFHDSLAPGGYLF 242
PRK06202 PRK06202
hypothetical protein; Provisional
 42-133 9.36e-04

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 38.83  E-value: 9.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  42 LLRHIQVPA-----PARILDFGCGPG---RDLRTFTA---LGHTATGLDGSERFAEMARA---DSGCEVWQQNFLALDLP 107
Cdd:PRK06202   47 LYRRLLRPAlsadrPLTLLDIGCGGGdlaIDLARWARrdgLRLEVTAIDPDPRAVAFARAnprRPGVTFRQAVSDELVAE 126

                          90       100
                  ....*....|....*....|....*.
gi 1863098424 108 TEHFDGIFANAVLFHIPTQELPRVLR 133
Cdd:PRK06202  127 GERFDVVTSNHFLHHLDDAEVVRLLA 152
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 99-146 1.05e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 38.81  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1863098424   99 QNFLALDLPTEHFDGIFANAVL--FHIPTQElpRVLRQLHATLKPGGVLF 146
Cdd:smart00138 192 HNLLAESPPLGDFDLIFCRNVLiyFDEPTQR--KLLNRFAEALKPGGYLF 239
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 51-143 1.10e-03

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 38.77  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  51 PARILDFGCGPGRDLRTFTALGHTATGLDGSE----RFAEMARA---DSGCEVWQQNFLALdlpTEHFDGIFANAVLFHI 123
Cdd:PRK12335  121 PGKALDLGCGQGRNSLYLALLGFDVTAVDINQqsleNLQEIAEKenlNIRTGLYDINSASI---QEEYDFILSTVVLMFL 197

                          90       100
                  ....*....|....*....|
gi 1863098424 124 PTQELPRVLRQLHATLKPGG 143
Cdd:PRK12335  198 NRERIPAIIKNMQEHTNPGG 217
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
42-146 1.89e-03

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 38.30  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  42 LLRHIQVPAPARILDFGCGPGRDLrtFTALGH---TATGLDGSERFaemaradsgceVWQ----QNFLALDLPTEH---- 110
Cdd:PRK15068  114 VLPHLSPLKGRTVLDVGCGNGYHM--WRMLGAgakLVVGIDPSQLF-----------LCQfeavRKLLGNDQRAHLlplg 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1863098424 111 ---------FDGIFANAVLFH----IPTqelprvLRQLHATLKPGGVLF 146
Cdd:PRK15068  181 ieqlpalkaFDTVFSMGVLYHrrspLDH------LKQLKDQLVPGGELV 223
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 100-146 5.69e-03

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 36.49  E-value: 5.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1863098424 100 NFLALDLPTEHFDGIFANAVL--FHIPTQElpRVLRQLHATLKPGGVLF 146
Cdd:pfam01739 125 NLLDEYPPLGDFDVIFCRNVLiyFDEETQR--KILNRFAEKLKPGGYLF 171
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
30-143 5.72e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 36.25  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  30 TRDHdvSQNIEALlrhiQVPAPARILDFGCGPGRDLRTFTALGHTATGLD---GSERFAEMARADSGCEVWQQNflALDL 106
Cdd:PRK11207   16 TRTH--SEVLEAV----KVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDknpMSIANLERIKAAENLDNLHTA--VVDL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1863098424 107 PTEHFDG----IFANAVLFHIPTQELPRVLRQLHATLKPGG 143
Cdd:PRK11207   88 NNLTFDGeydfILSTVVLMFLEAKTIPGLIANMQRCTKPGG 128
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 42-145 7.56e-03

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 36.61  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863098424  42 LLRHIQVPAPARILDFGCGPGRDL-RTFTALGHTATGLDGSERFA---EMARADSGcevwqQNFLALDLP--------TE 109
Cdd:pfam08003 107 VLPHLSPLKGRTILDVGCGNGYHMwRMLGEGAAMVVGIDPSELFLcqfEAVRKLLG-----NDQRAHLLPlgieqlpaLA 181

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1863098424 110 HFDGIFANAVLFH--IPTQElprvLRQLHATLKPGGVL 145
Cdd:pfam08003 182 AFDTVFSMGVLYHrrSPLDH----LLQLKDQLVKGGEL 215
 
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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