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Conserved domains on  [gi|1267610976|ref|WP_098383386|]
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cyclopropane-fatty-acyl-phospholipid synthase family protein [Priestia megaterium]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11454891)

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.-.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 24-140 1.13e-17

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


:

Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 77.28  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  24 KINRIIDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRIPEEKITYIVKDAKQVVSEyv 103
Cdd:COG2230    39 KLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAD-- 116

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1267610976 104 NHFDVGICVGSTHALGSLELT--LQSLKRNVKKGGFILV 140
Cdd:COG2230   117 GQFDAIVSIGMFEHVGPENYPayFAKVARLLKPGGRLLL 155
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 24-140 1.13e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 77.28  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  24 KINRIIDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRIPEEKITYIVKDAKQVVSEyv 103
Cdd:COG2230    39 KLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAD-- 116

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1267610976 104 NHFDVGICVGSTHALGSLELT--LQSLKRNVKKGGFILV 140
Cdd:COG2230   117 GQFDAIVSIGMFEHVGPENYPayFAKVARLLKPGGRLLL 155
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-136 1.46e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.42  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  40 VLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRIPeeKITYIVKDAKQVVSEYvNHFDVGICVGSTHALG 119
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPD-GSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 1267610976 120 --SLELTLQSLKRNVKKGG 136
Cdd:pfam13649  78 dpDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-140 3.72e-09

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: 52.82  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  39 KVLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRiPEEKITYIVKDAKQVVSEYVNHFDVGICVGSTHAL 118
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 1267610976 119 -GSLELTLQSLKRNVKKGGFILV 140
Cdd:cd02440    80 vEDLARFLEEARRLLKPGGVLVL 102
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 37-139 4.17e-04

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: 40.35  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  37 PAKVLDIGAGKCElLIRLVKKYGIEA--TAVELYEGSIleakQQAQKRIPeEKITYIVKDAKQVVSEyVNHFDVGICVGS 114
Cdd:TIGR02072  35 PASVLDIGCGTGY-LTRALLKRFPQAefIALDISAGML----AQAKTKLS-ENVQFICGDAEKLPLE-DSSFDLIVSNLA 107

                          90       100
                  ....*....|....*....|....*
gi 1267610976 115 THALGSLELTLQSLKRNVKKGGFIL 139
Cdd:TIGR02072 108 LQWCDDLSQALSELARVLKPGGLLA 132
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 29-97 7.91e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 36.67  E-value: 7.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267610976  29 IDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVEL-YEGSILE-AKQQAQKRIPEEKITYIVKDAKQ 97
Cdd:PRK00216   44 IKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLdFSEGMLAvGREKLRDLGLSGNVEFVQGDAEA 114
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 24-140 1.13e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 77.28  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  24 KINRIIDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRIPEEKITYIVKDAKQVVSEyv 103
Cdd:COG2230    39 KLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAD-- 116

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1267610976 104 NHFDVGICVGSTHALGSLELT--LQSLKRNVKKGGFILV 140
Cdd:COG2230   117 GQFDAIVSIGMFEHVGPENYPayFAKVARLLKPGGRLLL 155
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 27-140 1.22e-14

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: 68.51  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  27 RIIDFLQ--LEPPAKVLDIGAGKCELLIRLVKKyGIEATAVELYEGSIleakQQAQKRIPEEKITYIVKDAKQVVSEYvN 104
Cdd:COG2227    13 RLAALLArlLPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEAL----EIARERAAELNVDFVQGDLEDLPLED-G 86

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1267610976 105 HFDVGICVGSTHALGSLELTLQSLKRNVKKGGFILV 140
Cdd:COG2227    87 SFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 27-157 2.68e-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: 65.02  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  27 RIIDFLQLEPPAKVLDIGAGKCELLIRLVKKyGIEATAVELYEGSILEAKQQAQKRipEEKITYIVKDAKQV-VSEyvNH 105
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEA--GLNVEFVVGDAEDLpFPD--GS 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1267610976 106 FDVGICVGSTHALGSLELTLQSLKRNVKKGGFILVGEGYWkkkPSQAYLEAL 157
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP---PDLAELEEL 136
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 25-169 3.25e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.40  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  25 INRIIDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRiPEEKITYIVKDAKQVVSEYVN 104
Cdd:COG0500    15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKA-GLGNVEFLVADLAELDPLPAE 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267610976 105 HFDVGICVGSTHALGSLELT--LQSLKRNVKKGGFILVgeGYWKKKPSQAYLEALGGADESELKEHH 169
Cdd:COG0500    94 SFDLVVAFGVLHHLPPEEREalLRELARALKPGGVLLL--SASDAAAALSLARLLLLATASLLELLL 158
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-136 1.46e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.42  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  40 VLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRIPeeKITYIVKDAKQVVSEYvNHFDVGICVGSTHALG 119
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPD-GSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 1267610976 120 --SLELTLQSLKRNVKKGG 136
Cdd:pfam13649  78 dpDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-140 3.72e-09

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: 52.82  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  39 KVLDIGAGKCELLIRLVKKYGIEATAVELYEGSILEAKQQAQKRiPEEKITYIVKDAKQVVSEYVNHFDVGICVGSTHAL 118
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAAL-LADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|...
gi 1267610976 119 -GSLELTLQSLKRNVKKGGFILV 140
Cdd:cd02440    80 vEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-140 2.67e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 47.27  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  41 LDIGAGKCeLLIRLVKKYGIEATAVELYEGSIleakQQAQKRIPEEKITYIVKDAKQV-VSEyvNHFDVGICVGSTHALG 119
Cdd:pfam08241   1 LDVGCGTG-LLTELLARLGARVTGVDISPEML----ELAREKAPREGLTFVVGDAEDLpFPD--NSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 1267610976 120 SLELTLQSLKRNVKKGGFILV 140
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 26-140 3.28e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.88  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  26 NRIIDFLQ-----LEPPAKVLDIGAGKCELLiRLVKKYGIEATAVELYEGSILEAKQQAQKripeekityiVKDAKQVVS 100
Cdd:pfam13489   7 RLLADLLLrllpkLPSPGRVLDFGCGTGIFL-RLLRAQGFSVTGVDPSPIAIERALLNVRF----------DQFDEQEAA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1267610976 101 EYVNHFDVGICVGSTHALGSLELTLQSLKRNVKKGGFILV 140
Cdd:pfam13489  76 VPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLL 115
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 34-148 6.61e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  34 LEPPAKVLDIGAGKCELLIRLVKKYG--IEATAVELYEGSILEAKQQAQKRIPE---------EKITYIVKDAKqvvsey 102
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGFDnvefeqgdiEELPELLEDDK------ 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1267610976 103 vnhFDVGICVGSTHALGSLELTLQSLKRNVKKGGFILVGEGYWKKK 148
Cdd:pfam13847  75 ---FDVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAE 117
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 24-140 1.14e-05

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 45.40  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  24 KINRIIDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVELYEgsilEAKQQAQKRIPEEKITYIVKDAKQVVSEYV 103
Cdd:pfam02353  49 KLDLILDKLGLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSK----NQYKLARKRVAAEGLARKVEVLLQDYRDFD 124

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1267610976 104 NHFDVGICVGSTHALG--SLELTLQSLKRNVKKGGFILV 140
Cdd:pfam02353 125 EPFDRIVSVGMFEHVGheNYDTFFKKLYNLLPPGGLMLL 163
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-138 1.27e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.74  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  41 LDIGAGKCELLIRLVKKY-GIEATAVELYEGSILEAKQQ--AQKRIPEEKITYIVKDAkqvVSEYVNHFDVGICVGSTHA 117
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERlaALGLLNAVRVELFQLDL---GELDPGSFDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 1267610976 118 LGSLELTLQSLKRNVKKGGFI 138
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
22-140 5.49e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 42.68  E-value: 5.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  22 ETKINRIIDFLQLEPPAKVLDIGAGkCELLIRLVKKYGIEATAVELYEGSIleakQQAQKRipEEKITYIVKDAKQVVSE 101
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCG-TGLLGEALRPRGYRLTGVDLSEEML----AKAREK--GVYDRLLVADLADLAEP 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1267610976 102 YvNHFDVGICVGSTHALGSLELTLQSLKRNVKKGG-FILV 140
Cdd:COG4976   105 D-GRFDLIVAADVLTYLGDLAAVFAGVARALKPGGlFIFS 143
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
36-140 7.96e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.58  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  36 PPAKVLDIGAGKCELLIRLVKKY-GIEATAVELYEGSIleakQQAQKRIPEekITYIVKDAKQVvsEYVNHFDVGICVGS 114
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEML----ARARARLPN--VRFVVADLRDL--DPPEPFDLVVSNAA 72

                          90       100
                  ....*....|....*....|....*.
gi 1267610976 115 THALGSLELTLQSLKRNVKKGGFILV 140
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLAV 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 37-139 4.17e-04

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: 40.35  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  37 PAKVLDIGAGKCElLIRLVKKYGIEA--TAVELYEGSIleakQQAQKRIPeEKITYIVKDAKQVVSEyVNHFDVGICVGS 114
Cdd:TIGR02072  35 PASVLDIGCGTGY-LTRALLKRFPQAefIALDISAGML----AQAKTKLS-ENVQFICGDAEKLPLE-DSSFDLIVSNLA 107

                          90       100
                  ....*....|....*....|....*
gi 1267610976 115 THALGSLELTLQSLKRNVKKGGFIL 139
Cdd:TIGR02072 108 LQWCDDLSQALSELARVLKPGGLLA 132
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
34-140 8.30e-04

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 39.43  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  34 LEPPAKVLDIGAGKCELLIRLVKKYGIE-ATAVELyEGSILEAkqqAQKRIPE-------EKITYIVKDAKQVVSEYVNH 105
Cdd:COG0421    35 HPNPKRVLIIGGGDGGLARELLKHPPVErVDVVEI-DPEVVEL---AREYFPLlapafddPRLRVVIGDGRAFLREAEES 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1267610976 106 FDVgICVGSTHALG-SLELT----LQSLKRNVKKGGfILV 140
Cdd:COG0421   111 YDV-IIVDLTDPVGpAEGLFtrefYEDCRRALKPGG-VLV 148
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
20-97 7.26e-03

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 36.96  E-value: 7.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267610976  20 ISETKINRIIDFLQLEPPAKVLDIGAGKCELLIRLVkKYGIEATAVELYEGSileAKQQAQKRIPEEKITYIVKDAKQ 97
Cdd:pfam00398  14 KDPKVINEIVDKANLRESDTVLEIGPGKGALTVILA-KRAKQVVAIEIDPRL---AKLLQKKLSLDENLTVIHQDFLK 87
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 29-97 7.91e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 36.67  E-value: 7.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1267610976  29 IDFLQLEPPAKVLDIGAGKCELLIRLVKKYGIEATAVEL-YEGSILE-AKQQAQKRIPEEKITYIVKDAKQ 97
Cdd:PRK00216   44 IKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLdFSEGMLAvGREKLRDLGLSGNVEFVQGDAEA 114
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 30-111 8.53e-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: 36.66  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267610976  30 DFLQLEPPAKVLDIGAGKCELLIRLVKKY-GIEATAVELYEgsilEAKQQAQKRI----PEEKITYIVKDAKQVVSEY-V 103
Cdd:COG4123    31 AFAPVKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQP----EAAELARRNValngLEDRITVIHGDLKEFAAELpP 106


                  ....*...
gi 1267610976 104 NHFDVGIC 111
Cdd:COG4123   107 GSFDLVVS 114
 
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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