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Conserved domains on  [gi|530397263|ref|XP_005274289|]
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citrate synthase-lysine N-methyltransferase CSKMT, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_31 super family cl48233
Methyltransferase domain; This family appears to have methyltransferase activity.
 198-330 1.36e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


The actual alignment was detected with superfamily member pfam13847:

Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 58.97  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  198 SPLRVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSPVAVAHMNSLLEggpgqtplcpGHPASSLHFMHADAQNLGAVASS 277
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQ----------KLGFDNVEFEQGDIEELPELLED 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530397263  278 GSFQLLLDKGTWDAVARGGLPrayqlLSECLRVLNPQGTLIqFSDEDPDVRLP 330
Cdd:pfam13847  73 DKFDVVISNCVLNHIPDPDKV-----LQEILRVLKPGGRLI-ISDPDSLAELP 119
 
Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 198-330 1.36e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 58.97  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  198 SPLRVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSPVAVAHMNSLLEggpgqtplcpGHPASSLHFMHADAQNLGAVASS 277
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQ----------KLGFDNVEFEQGDIEELPELLED 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530397263  278 GSFQLLLDKGTWDAVARGGLPrayqlLSECLRVLNPQGTLIqFSDEDPDVRLP 330
Cdd:pfam13847  73 DKFDVVISNCVLNHIPDPDKV-----LQEILRVLKPGGRLI-ISDPDSLAELP 119
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 190-325 6.55e-10

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: 56.93  E-value: 6.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 190 LLQEAQAASPLRVLDVGCGtsslcTGLYTK--SPHPVDVLGVDFSPVAVAHMNSLLEGGPGQtplcpghpassLHFMHAD 267
Cdd:COG2226   14 LLAALGLRPGARVLDLGCG-----TGRLALalAERGARVTGVDISPEMLELARERAAEAGLN-----------VEFVVGD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530397263 268 AQNLGavassgsfqllLDKGTWDAV-ARGGL---PRAYQLLSECLRVLNPQGTLIqFSDEDP 325
Cdd:COG2226   78 AEDLP-----------FPDGSFDLViSSFVLhhlPDPERALAEIARVLKPGGRLV-VVDFSP 127
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 187-322 1.82e-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: 48.44  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  187 LLPLLQEAQAASPLRVLDVGCGTSSLcTGLYTKSPHPVDVLGVDFSpvavahmnslleggPGQTPLCPGHPASSLHFMHA 266
Cdd:TIGR02072  23 LLALLKEKGIFIPASVLDIGCGTGYL-TRALLKRFPQAEFIALDIS--------------AGMLAQAKTKLSENVQFICG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397263  267 DAQNL-------GAVASSGSFQLLLDkgtwdavarggLPRAyqlLSECLRVLNPQGTLIqFSD 322
Cdd:TIGR02072  88 DAEKLpledssfDLIVSNLALQWCDD-----------LSQA---LSELARVLKPGGLLA-FST 135
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 194-317 8.49e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.60  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 194 AQAASPLRVLDVGCGTSSLcTGLYTK-SPHPVDVLGVDFSPvavahmnSLLEggPGQTPLCPGHPASSLHFMHADAQNLG 272
Cdd:PRK00216  47 LGVRPGDKVLDLACGTGDL-AIALAKaVGKTGEVVGLDFSE-------GMLA--VGREKLRDLGLSGNVEFVQGDAEALP 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530397263 273 avassgsfqllLDKGTWDAVARG-GL---PRAYQLLSECLRVLNPQGTL 317
Cdd:PRK00216 117 -----------FPDNSFDAVTIAfGLrnvPDIDKALREMYRVLKPGGRL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 201-318 1.00e-04

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: 41.26  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 201 RVLDVGCGTSSLCTGLYtkSPHPVDVLGVDFSPVAVAHMNSLLEGGpgqtplcpghPASSLHFMHADAQNLgavassgsf 280
Cdd:cd02440    1 RVLDLGCGTGALALALA--SGPGARVTGVDISPVALELARKAAAAL----------LADNVEVLKGDAEEL--------- 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530397263 281 qLLLDKGTWDAV-----ARGGLPRAYQLLSECLRVLNPQGTLI 318
Cdd:cd02440   60 -PPEADESFDVIisdppLHHLVEDLARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 198-330 1.36e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 58.97  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  198 SPLRVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSPVAVAHMNSLLEggpgqtplcpGHPASSLHFMHADAQNLGAVASS 277
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQ----------KLGFDNVEFEQGDIEELPELLED 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530397263  278 GSFQLLLDKGTWDAVARGGLPrayqlLSECLRVLNPQGTLIqFSDEDPDVRLP 330
Cdd:pfam13847  73 DKFDVVISNCVLNHIPDPDKV-----LQEILRVLKPGGRLI-ISDPDSLAELP 119
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 190-325 6.55e-10

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: 56.93  E-value: 6.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 190 LLQEAQAASPLRVLDVGCGtsslcTGLYTK--SPHPVDVLGVDFSPVAVAHMNSLLEGGPGQtplcpghpassLHFMHAD 267
Cdd:COG2226   14 LLAALGLRPGARVLDLGCG-----TGRLALalAERGARVTGVDISPEMLELARERAAEAGLN-----------VEFVVGD 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530397263 268 AQNLGavassgsfqllLDKGTWDAV-ARGGL---PRAYQLLSECLRVLNPQGTLIqFSDEDP 325
Cdd:COG2226   78 AEDLP-----------FPDGSFDLViSSFVLhhlPDPERALAEIARVLKPGGRLV-VVDFSP 127
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 193-318 3.13e-09

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: 54.64  E-value: 3.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 193 EAQAASPLRVLDVGCGtsslcTGLYTKS--PHPVDVLGVDFSPVAVAHMNSLLeggpgqtplcpghPASSLHFMHADAQN 270
Cdd:COG2227   19 ARLLPAGGRVLDVGCG-----TGRLALAlaRRGADVTGVDISPEALEIARERA-------------AELNVDFVQGDLED 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530397263 271 LGavassgsfqllLDKGTWDAV-ARGGL---PRAYQLLSECLRVLNPQGTLI 318
Cdd:COG2227   81 LP-----------LEDGSFDLViCSEVLehlPDPAALLRELARLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 202-315 7.78e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.57  E-value: 7.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  202 VLDVGCGTSSLCTGLYTKspHPVDVLGVDFSPVAVAHMNSLLEGGPGQtplcpghpassLHFMHADAQNLGavassgsfq 281
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR--GGARVTGVDLSPEMLERARERAAEAGLN-----------VEFVQGDAEDLP--------- 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530397263  282 llLDKGTWDAV-ARGGL-----PRAYQLLSECLRVLNPQG 315
Cdd:pfam13649  59 --FPDGSFDLVvSSGVLhhlpdPDLEAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
172-326 1.37e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.15  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 172 PTFDWFF----GYDEVQGLLLPLLQEAQAASPLRVLDVGCGtsslcTGLYTK--SPHPVDVLGVDFSP--VAVAHMNSLl 243
Cdd:COG4976   16 DSYDAALvedlGYEAPALLAEELLARLPPGPFGRVLDLGCG-----TGLLGEalRPRGYRLTGVDLSEemLAKAREKGV- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 244 eggpgqtplcpghpasSLHFMHADAQNLgaVASSGSFQLLLdkgTWDAVARGGLPRAyqLLSECLRVLNPQGTLIqFSDE 323
Cdd:COG4976   90 ----------------YDRLLVADLADL--AEPDGRFDLIV---AADVLTYLGDLAA--VFAGVARALKPGGLFI-FSVE 145


                 ...
gi 530397263 324 DPD 326
Cdd:COG4976  146 DAD 148
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
199-318 3.27e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.90  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 199 PLRVLDVGCGTSSLCTGLYTKSPHpVDVLGVDFSPVAVAHMNSLLEGgpgqtplcpghpassLHFMHADAQNL------G 272
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARLPN---------------VRFVVADLRDLdppepfD 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530397263 273 AVASSGSFQllldkgtWdavarggLPRAYQLLSECLRVLNPQGTLI 318
Cdd:COG4106   66 LVVSNAALH-------W-------LPDHAALLARLAAALAPGGVLA 97
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 187-322 1.82e-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: 48.44  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  187 LLPLLQEAQAASPLRVLDVGCGTSSLcTGLYTKSPHPVDVLGVDFSpvavahmnslleggPGQTPLCPGHPASSLHFMHA 266
Cdd:TIGR02072  23 LLALLKEKGIFIPASVLDIGCGTGYL-TRALLKRFPQAEFIALDIS--------------AGMLAQAKTKLSENVQFICG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530397263  267 DAQNL-------GAVASSGSFQLLLDkgtwdavarggLPRAyqlLSECLRVLNPQGTLIqFSD 322
Cdd:TIGR02072  88 DAEKLpledssfDLIVSNLALQWCDD-----------LSQA---LSELARVLKPGGLLA-FST 135
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 203-318 2.69e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 45.35  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  203 LDVGCGTSSLCTGLYTKSPHpvdVLGVDFSPVAVAHMNSLLEGGPgqtplcpghpassLHFMHADAQNLG-------AVA 275
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKAPREG-------------LTFVVGDAEDLPfpdnsfdLVL 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 530397263  276 SSGSFQLLLDkgtwdavargglprAYQLLSECLRVLNPQGTLI 318
Cdd:pfam08241  65 SSEVLHHVED--------------PERALREIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 176-318 5.94e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 46.45  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 176 WFFGYDEVQ--GLLLPLLQEAQAASPLRVLDVGCGTSSLCTGLytKSPHPVDVLGVDFSPVAVAHMNSlleggpgqtpLC 253
Cdd:COG0500    2 WDSYYSDELlpGLAALLALLERLPKGGRVLDLGCGTGRNLLAL--AARFGGRVIGIDLSPEAIALARA----------RA 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530397263 254 PGHPASSLHFMHADAQNLGAVaSSGSFQLLLDKGTWDAVARGGLPRayqLLSECLRVLNPQGTLI 318
Cdd:COG0500   70 AKAGLGNVEFLVADLAELDPL-PAESFDLVVAFGVLHHLPPEEREA---LLRELARALKPGGVLL 130
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 192-333 2.07e-05

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 45.33  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263  192 QEAQAASPLRVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSPvavahmnSLLEGGPGQTPLcpghpASSLHFMHADAQnl 271
Cdd:TIGR01934  33 KLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSS-------EMLEVAKKKSEL-----PLNIEFIQADAE-- 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530397263  272 gavassgsfQLLLDKGTWDAVARG-GL---PRAYQLLSECLRVLNPQGtliqfsdedpdvRLPCLE 333
Cdd:TIGR01934  99 ---------ALPFEDNSFDAVTIAfGLrnvTDIQKALREMYRVLKPGG------------RLVILE 143
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 201-318 2.40e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.15  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 201 RVLDVGCGTSSLctGLYTKSPHPVDVLGVDFSPVAVAHMNSLLE--GGPGQtplcpghpassLHFMHADAQNLG------ 272
Cdd:COG2230   54 RVLDIGCGWGGL--ALYLARRYGVRVTGVTLSPEQLEYARERAAeaGLADR-----------VEVRLADYRDLPadgqfd 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530397263 273 AVASSGSFQllldkgtwdAVARGGLPRayqLLSECLRVLNPQGTLI 318
Cdd:COG2230  121 AIVSIGMFE---------HVGPENYPA---YFAKVARLLKPGGRLL 154
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 194-317 8.49e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.60  E-value: 8.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 194 AQAASPLRVLDVGCGTSSLcTGLYTK-SPHPVDVLGVDFSPvavahmnSLLEggPGQTPLCPGHPASSLHFMHADAQNLG 272
Cdd:PRK00216  47 LGVRPGDKVLDLACGTGDL-AIALAKaVGKTGEVVGLDFSE-------GMLA--VGREKLRDLGLSGNVEFVQGDAEALP 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530397263 273 avassgsfqllLDKGTWDAVARG-GL---PRAYQLLSECLRVLNPQGTL 317
Cdd:PRK00216 117 -----------FPDNSFDAVTIAfGLrnvPDIDKALREMYRVLKPGGRL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 201-318 1.00e-04

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: 41.26  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 201 RVLDVGCGTSSLCTGLYtkSPHPVDVLGVDFSPVAVAHMNSLLEGGpgqtplcpghPASSLHFMHADAQNLgavassgsf 280
Cdd:cd02440    1 RVLDLGCGTGALALALA--SGPGARVTGVDISPVALELARKAAAAL----------LADNVEVLKGDAEEL--------- 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530397263 281 qLLLDKGTWDAV-----ARGGLPRAYQLLSECLRVLNPQGTLI 318
Cdd:cd02440   60 -PPEADESFDVIisdppLHHLVEDLARFLEEARRLLKPGGVLV 101
PRK08317 PRK08317
hypothetical protein; Provisional
 201-326 7.32e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530397263 201 RVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSP--VAVAHMNSLLEGGPgqtplcpghpassLHFMHADAQNLG------ 272
Cdd:PRK08317  22 RVLDVGCGPGNDARELARRVGPEGRVVGIDRSEamLALAKERAAGLGPN-------------VEFVRGDADGLPfpdgsf 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 530397263 273 -AVASSGSFQLLLDKGtwdavargglprayQLLSECLRVLNPQGTLIQFsdeDPD 326
Cdd:PRK08317  89 dAVRSDRVLQHLEDPA--------------RALAEIARVLRPGGRVVVL---DTD 126
 
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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