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Conserved domains on  [gi|1150667147|pdb|5JGK|A]
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Chain A, UbiE/COQ5 family methyltransferase, putative

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]; ...
52-171 3.15e-19

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: 81.96  E-value: 3.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLnhtlqdeAKKTWKLTCGDLSEGMLETTKRRLQDEGwVNAETKIVNALDTGLPDGHYTHVFVAFGF 131
Cdd:COG2226  26 VLDLGCGTGRLALAL-------AERGARVTGVDISPEMLELARERAAEAG-LNVEFVVGDAEDLPFPDGSFDLVISSFVL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
5JGK_A      132 QSFPDANAALKECFRILASGGILASSTW---QNFNWIPIMKAA 171
Cdd:COG2226  98 HHLPDPERALAEIARVLKPGGRLVVVDFsppDLAELEELLAEA 140
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
52-171 3.15e-19

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: 81.96  E-value: 3.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLnhtlqdeAKKTWKLTCGDLSEGMLETTKRRLQDEGwVNAETKIVNALDTGLPDGHYTHVFVAFGF 131
Cdd:COG2226  26 VLDLGCGTGRLALAL-------AERGARVTGVDISPEMLELARERAAEAG-LNVEFVVGDAEDLPFPDGSFDLVISSFVL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
5JGK_A      132 QSFPDANAALKECFRILASGGILASSTW---QNFNWIPIMKAA 171
Cdd:COG2226  98 HHLPDPERALAEIARVLKPGGRLVVVDFsppDLAELEELLAEA 140
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
52-152 3.77e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         52 VLDNACGIGAVSSVLnhtlqdeAKKT-WKLTCGDLSEGMLETTKRRLQDEGwVNAETKIVNALDTGLPDGHYTHVFVAFG 130
Cdd:pfam13649   1 VLDLGCGTGRLTLAL-------ARRGgARVTGVDLSPEMLERARERAAEAG-LNVEFVQGDAEDLPFPDGSFDLVVSSGV 72
                          90       100
                  ....*....|....*....|....
5JGK_A        131 FQSFPDAN--AALKECFRILASGG 152
Cdd:pfam13649  73 LHHLPDPDleAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
46-200 1.11e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 71.72  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A        46 SQKPLIVLDNACGIGaVSSVLnhtLQDEAKKTWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIV-NALDTGLPDGHYTH 124
Cdd:PRK00216  49 VRPGDKVLDLACGTG-DLAIA---LAKAVGKTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQgDAEALPFPDNSFDA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       125 VFVAFGFQSFPDANAALKECFRILASGGILA----SSTWQN----------FNWIPIMKAAI-----------ETIPGnl 179
Cdd:PRK00216 125 VTIAFGLRNVPDIDKALREMYRVLKPGGRLVilefSKPTNPplkkaydfylFKVLPLIGKLIsknaeaysylaESIRA-- 202
                        170       180
                 ....*....|....*....|..
5JGK_A       180 pFPTQKEFIAL-HNAGWDSESY 200
Cdd:PRK00216 203 -FPDQEELAAMlEEAGFERVRY 223
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
52-159 3.58e-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: 47.81  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLNHTLQdeakktWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIVNALD-TGLPDGHYTHVFVAFG 130
Cdd:cd02440   2 VLDLGCGTGALALALASGPG------ARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElPPEADESFDVIISDPP 75
                        90       100       110
                ....*....|....*....|....*....|
5JGK_A      131 FQ-SFPDANAALKECFRILASGGILASSTW 159
Cdd:cd02440  76 LHhLVEDLARFLEEARRLLKPGGVLVLTLV 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
42-158 8.37e-06

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: 46.13  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         42 VANTSQKPLIVLDNACGIGAVSSVLnhtlqdeaKKTW---KLTCGDLSEGMLETTKRRL-----QDEGwvNAETkivnaL 113
Cdd:TIGR02072  28 KEKGIFIPASVLDIGCGTGYLTRAL--------LKRFpqaEFIALDISAGMLAQAKTKLsenvqFICG--DAEK-----L 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
5JGK_A        114 DtgLPDGHYTHVFVAFGFQSFPDANAALKECFRILASGGILASST 158
Cdd:TIGR02072  93 P--LEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
52-171 3.15e-19

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: 81.96  E-value: 3.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLnhtlqdeAKKTWKLTCGDLSEGMLETTKRRLQDEGwVNAETKIVNALDTGLPDGHYTHVFVAFGF 131
Cdd:COG2226  26 VLDLGCGTGRLALAL-------AERGARVTGVDISPEMLELARERAAEAG-LNVEFVVGDAEDLPFPDGSFDLVISSFVL 97
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
5JGK_A      132 QSFPDANAALKECFRILASGGILASSTW---QNFNWIPIMKAA 171
Cdd:COG2226  98 HHLPDPERALAEIARVLKPGGRLVVVDFsppDLAELEELLAEA 140
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
52-152 3.77e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 3.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         52 VLDNACGIGAVSSVLnhtlqdeAKKT-WKLTCGDLSEGMLETTKRRLQDEGwVNAETKIVNALDTGLPDGHYTHVFVAFG 130
Cdd:pfam13649   1 VLDLGCGTGRLTLAL-------ARRGgARVTGVDLSPEMLERARERAAEAG-LNVEFVQGDAEDLPFPDGSFDLVVSSGV 72
                          90       100
                  ....*....|....*....|....
5JGK_A        131 FQSFPDAN--AALKECFRILASGG 152
Cdd:pfam13649  73 LHHLPDPDleAALREIARVLKPGG 96
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
46-200 1.11e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 71.72  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A        46 SQKPLIVLDNACGIGaVSSVLnhtLQDEAKKTWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIV-NALDTGLPDGHYTH 124
Cdd:PRK00216  49 VRPGDKVLDLACGTG-DLAIA---LAKAVGKTGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQgDAEALPFPDNSFDA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       125 VFVAFGFQSFPDANAALKECFRILASGGILA----SSTWQN----------FNWIPIMKAAI-----------ETIPGnl 179
Cdd:PRK00216 125 VTIAFGLRNVPDIDKALREMYRVLKPGGRLVilefSKPTNPplkkaydfylFKVLPLIGKLIsknaeaysylaESIRA-- 202
                        170       180
                 ....*....|....*....|..
5JGK_A       180 pFPTQKEFIAL-HNAGWDSESY 200
Cdd:PRK00216 203 -FPDQEELAAMlEEAGFERVRY 223
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
53-155 1.49e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 64.99  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         53 LDNACGIGAVSSVLnhtlqdeAKKTWKLTCGDLSEGMLETTKRRLQDEGWVNAETkivNALDTGLPDGHYTHVFVAFGFQ 132
Cdd:pfam08241   1 LDVGCGTGLLTELL-------ARLGARVTGVDISPEMLELAREKAPREGLTFVVG---DAEDLPFPDNSFDLVLSSEVLH 70
                          90       100
                  ....*....|....*....|...
5JGK_A        133 SFPDANAALKECFRILASGGILA 155
Cdd:pfam08241  71 HVEDPERALREIARVLKPGGILI 93
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
48-154 3.71e-13

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 67.46  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         48 KPLIVLDNACGIGAVSSvlnhTLQDEAKKTWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIVNALDTGLPDGHYTHVFV 127
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTF----GLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTI 117
                          90       100
                  ....*....|....*....|....*..
5JGK_A        128 AFGFQSFPDANAALKECFRILASGGIL 154
Cdd:pfam01209 118 SFGLRNFPDYLKVLKEAFRVLKPGGRV 144
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
52-158 1.12e-10

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: 58.11  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLnhtlqdeAKKTWKLTCGDLSEGMLETTKRRLQDegwVNAETKIVNALDTGLPDGHYTHVFVAFGF 131
Cdd:COG2227  28 VLDVGCGTGRLALAL-------ARRGADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDLPLEDGSFDLVICSEVL 97
                        90       100
                ....*....|....*....|....*..
5JGK_A      132 QSFPDANAALKECFRILASGGILASST 158
Cdd:COG2227  98 EHLPDPAALLRELARLLKPGGLLLLST 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
3-159 9.55e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.85  E-value: 9.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A        3 MSKSDYIQNMFQT------KSFVDRYKYtEKLTGLYAQTLVDYSGVANTSqkpliVLDNACGIGAVSSVLnhtlqdeAKK 76
Cdd:COG4976   1 MALDAYVEALFDQyadsydAALVEDLGY-EAPALLAEELLARLPPGPFGR-----VLDLGCGTGLLGEAL-------RPR 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       77 TWKLTCGDLSEGMLETTKRRLQDEGWVNAEtkivnALDTGLPDGHYTHVFVAFGFQSFPDANAALKECFRILASGGILAS 156
Cdd:COG4976  68 GYRLTGVDLSEEMLAKAREKGVYDRLLVAD-----LADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIF 142

                ...
5JGK_A      157 STW 159
Cdd:COG4976 143 SVE 145
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
53-154 2.10e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.83  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         53 LDNACGIGAVSSVLNhtlqdEAKKTWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIVNALDTG-LPDGHYTHVFVAFGF 131
Cdd:pfam08242   1 LEIGCGTGTLLRALL-----EALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGeLDPGSFDVVVASNVL 75
                          90       100
                  ....*....|....*....|...
5JGK_A        132 QSFPDANAALKECFRILASGGIL 154
Cdd:pfam08242  76 HHLADPRAVLRNIRRLLKPGGVL 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
47-154 1.03e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       47 QKPLIVLDNACGIGAVSSVLnhtlqdEAKKTWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIVNALDTG-LPDGHYTHV 125
Cdd:COG0500  25 PKGGRVLDLGCGTGRNLLAL------AARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDpLPAESFDLV 98
                        90       100       110
                ....*....|....*....|....*....|.
5JGK_A      126 FV--AFGFQSFPDANAALKECFRILASGGIL 154
Cdd:COG0500  99 VAfgVLHHLPPEEREALLRELARALKPGGVL 129
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
52-159 3.58e-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: 47.81  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLNHTLQdeakktWKLTCGDLSEGMLETTKRRLQDEGWVNAETKIVNALD-TGLPDGHYTHVFVAFG 130
Cdd:cd02440   2 VLDLGCGTGALALALASGPG------ARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElPPEADESFDVIISDPP 75
                        90       100       110
                ....*....|....*....|....*....|
5JGK_A      131 FQ-SFPDANAALKECFRILASGGILASSTW 159
Cdd:cd02440  76 LHhLVEDLARFLEEARRLLKPGGVLVLTLV 105
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
52-155 5.94e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.74  E-value: 5.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       52 VLDNACGIGAVSSVLNHTLQDeakktWKLTCGDLSEGMLETTKRRLQDEGWVNAEtkiVNALDtglPDGHYTHVFVAFGF 131
Cdd:COG4106   5 VLDLGCGTGRLTALLAERFPG-----ARVTGVDLSPEMLARARARLPNVRFVVAD---LRDLD---PPEPFDLVVSNAAL 73
                        90       100
                ....*....|....*....|....
5JGK_A      132 QSFPDANAALKECFRILASGGILA 155
Cdd:COG4106  74 HWLPDHAALLARLAAALAPGGVLA 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
42-158 8.37e-06

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: 46.13  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         42 VANTSQKPLIVLDNACGIGAVSSVLnhtlqdeaKKTW---KLTCGDLSEGMLETTKRRL-----QDEGwvNAETkivnaL 113
Cdd:TIGR02072  28 KEKGIFIPASVLDIGCGTGYLTRAL--------LKRFpqaEFIALDISAGMLAQAKTKLsenvqFICG--DAEK-----L 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
5JGK_A        114 DtgLPDGHYTHVFVAFGFQSFPDANAALKECFRILASGGILASST 158
Cdd:TIGR02072  93 P--LEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
PRK08317 PRK08317
hypothetical protein; Provisional
52-219 3.90e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.16  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A        52 VLDNACGIGAvssvLNHTLQDEAKKTWKLTCGDLSEGMLETTKRRLQDEGwVNAETKIVNALDTGLPDGHYTHVFVAFGF 131
Cdd:PRK08317  23 VLDVGCGPGN----DARELARRVGPEGRVVGIDRSEAMLALAKERAAGLG-PNVEFVRGDADGLPFPDGSFDAVRSDRVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A       132 QSFPDANAALKECFRILASGG--ILASSTWQNFNWIPIMKAAIETIpgnlpfptqKEFIALHNAGWDSESYIQSELEKLG 209
Cdd:PRK08317  98 QHLEDPARALAEIARVLRPGGrvVVLDTDWDTLVWHSGDRALMRKI---------LNFWSDHFADPWLGRRLPGLFREAG 168
                        170
                 ....*....|
5JGK_A       210 FRDVKVIPVP 219
Cdd:PRK08317 169 LTDIEVEPYT 178
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
48-166 2.05e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5JGK_A         48 KPLIVLDNACGIGAVSSVLNHTLQDEAKKTwkltcG-DLSEGMLETTKRRLQDEGWVNAETKI--VNALDTGLPDGHYTH 124
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVV-----GiDISEEAIEKARENAQKLGFDNVEFEQgdIEELPELLEDDKFDV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
5JGK_A        125 VFVAFGFQSFPDANAALKECFRILASGGILASSTWQNFNWIP 166
Cdd:pfam13847  78 VISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELP 119
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
133-154 8.94e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 36.00  E-value: 8.94e-03
                        10        20
                ....*....|....*....|..
5JGK_A      133 SFPDANAALKECFRILASGGIL 154
Cdd:COG4627  60 DYEEAPLALKECYRVLKPGGIL 81
 
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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