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Conserved domains on  [gi|1083391762|gb|OGF03835|]
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MAG: hypothetical protein A3H14_00565 [Candidatus Doudnabacteria bacterium RIFCSPLOWO2_12_FULL_49_8]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11467871)

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

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-149 3.62e-15

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 68.70  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLkgRNMITIQHDLNEIKnlklPQGQYQFAITSFALHEIPs 125
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL--PNVRFVVADLRDLD----PPEPFDLVVSNAALHWLP- 77

                          90       100
                  ....*....|....*....|....
gi 1083391762 126 iHKQEIFKFIYKNLVSGGMYVLVD 149
Cdd:COG4106    78 -DHAALLARLAAALAPGGVLAVQV 100
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-149 3.62e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 68.70  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLkgRNMITIQHDLNEIKnlklPQGQYQFAITSFALHEIPs 125
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL--PNVRFVVADLRDLD----PPEPFDLVVSNAALHWLP- 77

                          90       100
                  ....*....|....*....|....
gi 1083391762 126 iHKQEIFKFIYKNLVSGGMYVLVD 149
Cdd:COG4106    78 -DHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-143 2.03e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.74  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMiFNKIPAAQIVGVDSSEAMIAKAEDRLK--GRNMITIQHDlneIKNLKLPQGQYQFAITSFALHEI 123
Cdd:pfam13649   1 VLDLGCGTGRLTLA-LARRGGARVTGVDLSPEMLERARERAAeaGLNVEFVQGD---AEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 1083391762 124 PSIHKQEIFKFIYKNLVSGG 143
Cdd:pfam13649  77 PDPDLEAALREIARVLKPGG 96
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 46-92 3.26e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 49.56  E-value: 3.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRNMI 92
Cdd:PRK01683   35 VVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQFV 81
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 46-148 3.70e-07

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: 47.04  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVeEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRNMITIQH---DLNEIknLKLPQGQYQFAITSFALHE 122
Cdd:cd02440     2 VLDLGCGTGAL-ALALASGPGARVTGVDISPVALELARKAAAALLADNVEVlkgDAEEL--PPEADESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*.
gi 1083391762 123 IPSiHKQEIFKFIYKNLVSGGMYVLV 148
Cdd:cd02440    79 LVE-DLARFLEEARRLLKPGGVLVLT 103
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 46-147 1.58e-05

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: 44.58  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRnmitIQHDLNEIKNLKLPQGQYQFAITSFALHEIPS 125
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSEN----VQFICGDAEKLPLEDSSFDLIVSNLALQWCDD 113

                          90       100
                  ....*....|....*....|..
gi 1083391762 126 ihKQEIFKFIYKNLVSGGMYVL 147
Cdd:TIGR02072 114 --LSQALSELARVLKPGGLLAF 133
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-149 3.62e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 68.70  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLkgRNMITIQHDLNEIKnlklPQGQYQFAITSFALHEIPs 125
Cdd:COG4106     5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL--PNVRFVVADLRDLD----PPEPFDLVVSNAALHWLP- 77

                          90       100
                  ....*....|....*....|....
gi 1083391762 126 iHKQEIFKFIYKNLVSGGMYVLVD 149
Cdd:COG4106    78 -DHAALLARLAAALAPGGVLAVQV 100
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-164 1.55e-13

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: 65.40  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKipAAQIVGVDSSEAMIAKAEDRL--KGRNMITIQHDlneIKNLKLPQGQYQFAITSFALHEI 123
Cdd:COG2226    26 VLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAaeAGLNVEFVVGD---AEDLPFPDGSFDLVISSFVLHHL 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1083391762 124 PsiHKQEIFKFIYKNLVSGGMYVLVDRFKIESDSLASAYES 164
Cdd:COG2226   101 P--DPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAE 139
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-143 2.03e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.74  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMiFNKIPAAQIVGVDSSEAMIAKAEDRLK--GRNMITIQHDlneIKNLKLPQGQYQFAITSFALHEI 123
Cdd:pfam13649   1 VLDLGCGTGRLTLA-LARRGGARVTGVDLSPEMLERARERAAeaGLNVEFVQGD---AEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 1083391762 124 PSIHKQEIFKFIYKNLVSGG 143
Cdd:pfam13649  77 PDPDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 46-205 3.70e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.01  E-value: 3.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIpAAQIVGVDSSEAMIAKAEDRLKGRNM--IT-IQHDLNEIKnlKLPQGQYQFAITSFALHE 122
Cdd:COG0500    30 VLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLgnVEfLVADLAELD--PLPAESFDLVVAFGVLHH 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762 123 IPSIHKQEIFKFIYKNLVSGGMYVLVDRFKIESDSLASAYESQWRSQTKSATWTDWKEPFAEYKKRMSIKEDFPDLVEDQ 202
Cdd:COG0500   107 LPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRLLALELYLRALLAAAATEDLRSDAL 186


                  ...
gi 1083391762 203 LAW 205
Cdd:COG0500   187 LES 189
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-144 7.09e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.99  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  47 LDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRNMITI-QHDLNEIKNLKLPQGQYQFAITSFALHEIPs 125
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAvRVELFQLDLGELDPGSFDVVVASNVLHHLA- 79

                          90
                  ....*....|....*....
gi 1083391762 126 iHKQEIFKFIYKNLVSGGM 144
Cdd:pfam08242  80 -DPRAVLRNIRRLLKPGGV 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-149 9.56e-11

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: 57.33  E-value: 9.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKipAAQIVGVDSSEAMIAKAEDRLKGRNMITIQHDLNEiknLKLPQGQYQFAITSFALHEIPS 125
Cdd:COG2227    28 VLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAELNVDFVQGDLED---LPLEDGSFDLVICSEVLEHLPD 102

                          90       100
                  ....*....|....*....|....
gi 1083391762 126 IhkQEIFKFIYKNLVSGGMYVLVD 149
Cdd:COG2227   103 P--AALLRELARLLKPGGLLLLST 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
9-143 1.15e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.47  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762   9 KFAMGWDADAAVNNPSRARLLDLLLTIITDSYSNDGMILDLGFGTGLVEEMIFNKipAAQIVGVDSSEAMIAKAEDRLKG 88
Cdd:COG4976    13 QYADSYDAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKGVY 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1083391762  89 RNMitIQHDLNEiknLKLPQGQYQFAITSFALHEIPSIhkQEIFKFIYKNLVSGG 143
Cdd:COG4976    91 DRL--LVADLAD---LAEPDGRFDLIVAADVLTYLGDL--AAVFAGVARALKPGG 138
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-147 2.43e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.97  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  47 LDLGFGTGLVEEMIFNKipAAQIVGVDSSEAMIAKAEDRLKGRNMITIQHDlneIKNLKLPQGQYQFAITSFALHEIPSI 126
Cdd:pfam08241   1 LDVGCGTGLLTELLARL--GARVTGVDISPEMLELAREKAPREGLTFVVGD---AEDLPFPDNSFDLVLSSEVLHHVEDP 75

                          90       100
                  ....*....|....*....|.
gi 1083391762 127 HKqeIFKFIYKNLVSGGMYVL 147
Cdd:pfam08241  76 ER--ALREIARVLKPGGILII 94
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 46-92 3.26e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 49.56  E-value: 3.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRNMI 92
Cdd:PRK01683   35 VVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRLPDCQFV 81
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 46-148 3.70e-07

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: 47.04  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVeEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRNMITIQH---DLNEIknLKLPQGQYQFAITSFALHE 122
Cdd:cd02440     2 VLDLGCGTGAL-ALALASGPGARVTGVDISPVALELARKAAAALLADNVEVlkgDAEEL--PPEADESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*.
gi 1083391762 123 IPSiHKQEIFKFIYKNLVSGGMYVLV 148
Cdd:cd02440    79 LVE-DLARFLEEARRLLKPGGVLVLT 103
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 46-147 1.58e-05

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: 44.58  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRnmitIQHDLNEIKNLKLPQGQYQFAITSFALHEIPS 125
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSEN----VQFICGDAEKLPLEDSSFDLIVSNLALQWCDD 113

                          90       100
                  ....*....|....*....|..
gi 1083391762 126 ihKQEIFKFIYKNLVSGGMYVL 147
Cdd:TIGR02072 114 --LSQALSELARVLKPGGLLAF 133
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-148 8.78e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 8.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEmIFNKIPaAQIVGVDSSEAMIAKAedrlkGRNMITIQHDLNEIKNlklPQGQYQFAITSFALHEIPS 125
Cdd:pfam13489  26 VLDFGCGTGIFLR-LLRAQG-FSVTGVDPSPIAIERA-----LLNVRFDQFDEQEAAV---PAGKFDVIVAREVLEHVPD 95

                          90       100
                  ....*....|....*....|...
gi 1083391762 126 IHkqEIFKFIYKNLVSGGmYVLV 148
Cdd:pfam13489  96 PP--ALLRQIAALLKPGG-LLLL 115
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 46-125 8.52e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.29  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLkgrnmitIQHDLNEIKNLKlPQGQYQFAITSFALHEIPS 125
Cdd:PRK14103   33 VVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARERG-------VDARTGDVRDWK-PKPDTDVVVSNAALQWVPE 104
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 46-199 1.79e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.41  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  46 ILDLGFGTGlVEEMIFNKIPAAQIVGVDSSEAMIAKAEDRLKGRNmiTIQHDLNEIKNLKLPQGQYQFAITSFALHEIPS 125
Cdd:PTZ00098   56 VLDIGSGLG-GGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKN--KIEFEANDILKKDFPENTFDMIYSRDAILHLSY 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1083391762 126 IHKQEIFKFIYKNLVSGGMYVLVDRFKIESDslasayesqwrsqtksatwtDWKEPFAEY-KKR----MSIkEDFPDLV 199
Cdd:PTZ00098  133 ADKKKLFEKCYKWLKPNGILLITDYCADKIE--------------------NWDEEFKAYiKKRkytlIPI-QEYGDLI 190
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 46-111 2.07e-03

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: 38.20  E-value: 2.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1083391762  46 ILDLGFGTGLVEEMIFNKIPAAQIVGVDSSEAMIAKAED-----RLKGRnmITIQH-DLNEIKNlKLPQGQY 111
Cdd:COG4123    41 VLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRnvalnGLEDR--ITVIHgDLKEFAA-ELPPGSF 109
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
68-230 3.47e-03

carboxy-S-adenosyl-L-methionine synthase CmoA;


Pssm-ID: 185348  Cd Length: 247  Bit Score: 37.70  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762  68 QIVGVDSSEAMIAKAEDRLKGRNMIT-IQHDLNEIKNLKLPQGQyqFAITSFALHEIPSIHKQEIFKFIYKNLVSGGMYV 146
Cdd:PRK15451   84 KIIAIDNSPAMIERCRRHIDAYKAPTpVDVIEGDIRDIAIENAS--MVVLNFTLQFLEPSERQALLDKIYQGLNPGGALV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1083391762 147 LVDRFKIESDSLASAYESQWRSQTKSATWTDwkepfAEYKKRMSIKED--FPDLVEDQLAWLRESGFKAACLQLE-FDRG 223
Cdd:PRK15451  162 LSEKFSFEDAKVGELLFNMHHDFKRANGYSE-----LEISQKRSMLENvmLTDSVETHKARLHKAGFEHSELWFQcFNFG 236


                  ....*..
gi 1083391762 224 LIVGLKS 230
Cdd:PRK15451  237 SLVALKA 243
 
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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