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Conserved domains on  [gi|6323635|ref|NP_013706|]
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sterol 24-C-methyltransferase [Saccharomyces cerevisiae S288C]

Protein Classification

sterol methyltransferase( domain architecture ID 18605639)

sterol methyltransferase such as sterol 24-C-methyltransferase that catalyzes the methyl transfer from S-adenosyl-methionine (SAM or AdoMet) to the C-24 of zymosterol to form fecosterol; acts on a range of sterols with a 24(25)-double bond in the side chain

CATH:  2.20.25.110
EC:  2.1.1.-
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sterol_MT_C pfam08498
Sterol methyltransferase C-terminal; This domain is found to the C-terminus of a ...
305-369 4.78e-32

Sterol methyltransferase C-terminal; This domain is found to the C-terminus of a methyltransferase domain (pfam08241) in fungal and plant sterol methyltransferases.


:

Pssm-ID: 430034  Cd Length: 66  Bit Score: 115.23  E-value: 4.78e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323635    305 TFFRTSYLGRQFTTAMVTVMEKLGLAPEGSKEVTAALENAAVGLVAGGKSKLFTPMMLFVARKPE 369
Cdd:pfam08498   2 TVFRMTKLGRFITHNLVGVLEKLGLAPKGTQKVAESLAKAADALVAGGKKGIFTPMYLFVARKPL 66
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
72-222 7.82e-27

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


:

Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 104.24  E-value: 7.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   72 SYYNVVTDFYEYGWGSSFHFSRFYKGESF----AASIARHEHYLAyKAGIQRGDLVLDVGCGVGGPAREIARFTGCNVIG 147
Cdd:COG2230   1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDdtleEAQEAKLDLILR-KLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTG 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323635  148 LNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEEnTFDKVYAIEATCHAPK--LEGVYSEIYKVLKPGGTFAV 222
Cdd:COG2230  80 VTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADG-QFDAIVSIGMFEHVGPenYPAYFAKVARLLKPGGRLLL 155
 
Name Accession Description Interval E-value
Sterol_MT_C pfam08498
Sterol methyltransferase C-terminal; This domain is found to the C-terminus of a ...
305-369 4.78e-32

Sterol methyltransferase C-terminal; This domain is found to the C-terminus of a methyltransferase domain (pfam08241) in fungal and plant sterol methyltransferases.


Pssm-ID: 430034  Cd Length: 66  Bit Score: 115.23  E-value: 4.78e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323635    305 TFFRTSYLGRQFTTAMVTVMEKLGLAPEGSKEVTAALENAAVGLVAGGKSKLFTPMMLFVARKPE 369
Cdd:pfam08498   2 TVFRMTKLGRFITHNLVGVLEKLGLAPKGTQKVAESLAKAADALVAGGKKGIFTPMYLFVARKPL 66
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
72-222 7.82e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 104.24  E-value: 7.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   72 SYYNVVTDFYEYGWGSSFHFSRFYKGESF----AASIARHEHYLAyKAGIQRGDLVLDVGCGVGGPAREIARFTGCNVIG 147
Cdd:COG2230   1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDdtleEAQEAKLDLILR-KLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTG 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323635  148 LNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEEnTFDKVYAIEATCHAPK--LEGVYSEIYKVLKPGGTFAV 222
Cdd:COG2230  80 VTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADG-QFDAIVSIGMFEHVGPenYPAYFAKVARLLKPGGRLLL 155
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
123-218 2.25e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 87.62  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    123 VLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLsdQMDFVKGDFMKMDFEENTFDKVYAIEATCH--A 200
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpD 78
                          90
                  ....*....|....*...
gi 6323635    201 PKLEGVYSEIYKVLKPGG 218
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
PLN02244 PLN02244
tocopherol O-methyltransferase
60-225 6.32e-19

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 86.72  E-value: 6.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    60 ERRLEDYNEATHSYYNVVTDFYEYGWGSSFHFSRFYKGESFA----ASIARHEHYLAYkAGIQRGDL-----VLDVGCGV 130
Cdd:PLN02244  51 PAATADLKEGIAEFYDESSGVWEDVWGEHMHHGYYDPGASRGdhrqAQIRMIEESLAW-AGVPDDDEkrpkrIVDVGCGI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   131 GGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEENTFDKVYAIEATCHAPKLEGVYSEI 210
Cdd:PLN02244 130 GGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQEL 209
                        170
                 ....*....|....*
gi 6323635   211 YKVLKPGGTFAVYEW 225
Cdd:PLN02244 210 ARVAAPGGRIIIVTW 224
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
123-222 1.09e-13

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 66.68  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  123 VLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIaKAKYYAKKYNLSDQMDFVKGDFMKMDFEE-NTFDKVYAIEATCHAP 201
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPEAdESFDVIISDPPLHHLV 80
                        90       100
                ....*....|....*....|..
gi 6323635  202 KL-EGVYSEIYKVLKPGGTFAV 222
Cdd:cd02440  81 EDlARFLEEARRLLKPGGVLVL 102
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
114-224 6.95e-08

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: 52.65  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    114 KAGIQRGDLVLDVGCGVGGPAREIARFTGC--NVIGLnnnDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEENTFDKV 191
Cdd:TIGR01934  34 LIGVFKGQKVLDVACGTGDLAIELAKSAPDrgKVTGV---DFSSEMLEVAKKKSELPLNIEFIQADAEALPFEDNSFDAV 110
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6323635    192 ---YAIEATCHAPKlegVYSEIYKVLKPGGTFAVYE 224
Cdd:TIGR01934 111 tiaFGLRNVTDIQK---ALREMYRVLKPGGRLVILE 143
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
123-220 5.77e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635     123 VLDVGCGVGGPAREIA-RFTGCNVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKmDFEENTFDKVYAIEATCHAP 201
Cdd:smart00828   3 VLDFGCGYGSDLIDLAeRHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAK-DPFPDTYDLVFGFEVIHHIK 81
                           90
                   ....*....|....*....
gi 6323635     202 KLEGVYSEIYKVLKPGGTF 220
Cdd:smart00828  82 DKMDLFSNISRHLKDGGHL 100
 
Name Accession Description Interval E-value
Sterol_MT_C pfam08498
Sterol methyltransferase C-terminal; This domain is found to the C-terminus of a ...
305-369 4.78e-32

Sterol methyltransferase C-terminal; This domain is found to the C-terminus of a methyltransferase domain (pfam08241) in fungal and plant sterol methyltransferases.


Pssm-ID: 430034  Cd Length: 66  Bit Score: 115.23  E-value: 4.78e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323635    305 TFFRTSYLGRQFTTAMVTVMEKLGLAPEGSKEVTAALENAAVGLVAGGKSKLFTPMMLFVARKPE 369
Cdd:pfam08498   2 TVFRMTKLGRFITHNLVGVLEKLGLAPKGTQKVAESLAKAADALVAGGKKGIFTPMYLFVARKPL 66
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
72-222 7.82e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 104.24  E-value: 7.82e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   72 SYYNVVTDFYEYGWGSSFHFSRFYKGESF----AASIARHEHYLAyKAGIQRGDLVLDVGCGVGGPAREIARFTGCNVIG 147
Cdd:COG2230   1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDdtleEAQEAKLDLILR-KLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTG 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323635  148 LNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEEnTFDKVYAIEATCHAPK--LEGVYSEIYKVLKPGGTFAV 222
Cdd:COG2230  80 VTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADG-QFDAIVSIGMFEHVGPenYPAYFAKVARLLKPGGRLLL 155
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
98-232 5.62e-24

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 96.22  E-value: 5.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   98 ESFAASIARHEHYLAYkAGIQRGDLVLDVGCGVGGPAREIARfTGCNVIGLNNNDYQIAKAKYYAKKYNLsdQMDFVKGD 177
Cdd:COG2226   2 DRVAARYDGREALLAA-LGLRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGL--NVEFVVGD 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6323635  178 FMKMDFEENTFDKVYAIEATCHAPKLEGVYSEIYKVLKPGGTFAVYEWVMTDKYD 232
Cdd:COG2226  78 AEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAE 132
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
123-218 2.25e-21

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 87.62  E-value: 2.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    123 VLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLsdQMDFVKGDFMKMDFEENTFDKVYAIEATCH--A 200
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlpD 78
                          90
                  ....*....|....*...
gi 6323635    201 PKLEGVYSEIYKVLKPGG 218
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
124-222 1.11e-20

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 85.79  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    124 LDVGCGVGGPAREIARFtGCNVIGLNNNDYQIAKAKYYAKKYNLsdqmDFVKGDFMKMDFEENTFDKVYAIEATCHAPKL 203
Cdd:pfam08241   1 LDVGCGTGLLTELLARL-GARVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDP 75
                          90
                  ....*....|....*....
gi 6323635    204 EGVYSEIYKVLKPGGTFAV 222
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
PLN02244 PLN02244
tocopherol O-methyltransferase
60-225 6.32e-19

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 86.72  E-value: 6.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    60 ERRLEDYNEATHSYYNVVTDFYEYGWGSSFHFSRFYKGESFA----ASIARHEHYLAYkAGIQRGDL-----VLDVGCGV 130
Cdd:PLN02244  51 PAATADLKEGIAEFYDESSGVWEDVWGEHMHHGYYDPGASRGdhrqAQIRMIEESLAW-AGVPDDDEkrpkrIVDVGCGI 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   131 GGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEENTFDKVYAIEATCHAPKLEGVYSEI 210
Cdd:PLN02244 130 GGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQEL 209
                        170
                 ....*....|....*
gi 6323635   211 YKVLKPGGTFAVYEW 225
Cdd:PLN02244 210 ARVAAPGGRIIIVTW 224
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
117-222 4.05e-15

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: 71.20  E-value: 4.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  117 IQRGDLVLDVGCGVGGPAREIARFtGCNVIGLNNNDYQIAKAKYYAKKYNLsdqmDFVKGDFMKMDFEENTFDKVYAIEA 196
Cdd:COG2227  22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAELNV----DFVQGDLEDLPLEDGSFDLVICSEV 96
                        90       100
                ....*....|....*....|....*.
gi 6323635  197 TCHAPKLEGVYSEIYKVLKPGGTFAV 222
Cdd:COG2227  97 LEHLPDPAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
123-222 1.09e-13

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 66.68  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  123 VLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIaKAKYYAKKYNLSDQMDFVKGDFMKMDFEE-NTFDKVYAIEATCHAP 201
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPEAdESFDVIISDPPLHHLV 80
                        90       100
                ....*....|....*....|..
gi 6323635  202 KL-EGVYSEIYKVLKPGGTFAV 222
Cdd:cd02440  81 EDlARFLEEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
91-224 2.61e-12

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 66.11  E-value: 2.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    91 FSRFYKGESFAAsiarhehylaykAGIQRGDLVLDVGCGVGGPAREIARFTGCN--VIGLNNNDYQIAKAKYYAKKYNLs 168
Cdd:PRK08317   3 DFRRYRARTFEL------------LAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERAAGLGP- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323635   169 dQMDFVKGDFMKMDFEENTFDKVYAIEATCHAPKLEGVYSEIYKVLKPGGTFAVYE 224
Cdd:PRK08317  70 -NVEFVRGDADGLPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
119-222 4.03e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 59.07  E-value: 4.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  119 RGDLVLDVGCGVGGPAREIA-RFTGCNVIGLnnnDyqiakakyyakkynLSDQM-----------DFVKGDFMKMDFEEn 186
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAeRFPGARVTGV---D--------------LSPEMlarararlpnvRFVVADLRDLDPPE- 62
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6323635  187 TFDKVYAIEATCHAPKLEGVYSEIYKVLKPGGTFAV 222
Cdd:COG4106  63 PFDLVVSNAALHWLPDHAALLARLAAALAPGGVLAV 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
123-222 6.97e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.04  E-value: 6.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    123 VLDVGCGVGGPAREIAR--FTGCNVIGLNNNDYQIAKAKYYAKKYNLSDqMDFVKGDF--MKMDFEENTFDKVYAIEATC 198
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIeeLPELLEDDKFDVVISNCVLN 85
                          90       100
                  ....*....|....*....|....
gi 6323635    199 HAPKLEGVYSEIYKVLKPGGTFAV 222
Cdd:pfam13847  86 HIPDPDKVLQEILRVLKPGGRLII 109
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
123-279 7.22e-10

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 59.21  E-value: 7.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   123 VLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNlsdQMDFVKGDFMKMDFEENTFDKVYAIEATCHAP- 201
Cdd:PTZ00098  56 VLDIGSGLGGGCKYINEKYGAHVHGVDICEKMVNIAKLRNSDKN---KIEFEANDILKKDFPENTFDMIYSRDAILHLSy 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   202 -KLEGVYSEIYKVLKPGGTFAVYEWVMTDK--YDENNPEH-RKIAYEIelgdgIPKMFHVDVarkaLKNCGFEVLVSEDL 277
Cdd:PTZ00098 133 aDKKKLFEKCYKWLKPNGILLITDYCADKIenWDEEFKAYiKKRKYTL-----IPIQEYGDL----IKSCNFQNVVAKDI 203

                 ..
gi 6323635   278 AD 279
Cdd:PTZ00098 204 SD 205
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
68-222 3.43e-09

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: 57.34  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635     68 EATHSYYNVVTDFYEYGWGSSFHFS-RFYKGESF---AASIARHEHYLAyKAGIQRGDLVLDVGCGVGGPAREIARFTGC 143
Cdd:pfam02353   7 ENIQAHYDLSNDFFALFLDPTMTYScAYFERPDMtleEAQQAKLDLILD-KLGLKPGMTLLDIGCGWGGLMRRAAERYDV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    144 NVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFmkMDFEENtFDKVYAIEATCHAPK--LEGVYSEIYKVLKPGGTFA 221
Cdd:pfam02353  86 NVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDY--RDFDEP-FDRIVSVGMFEHVGHenYDTFFKKLYNLLPPGGLML 162

                  .
gi 6323635    222 V 222
Cdd:pfam02353 163 L 163
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
107-222 3.58e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.08  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  107 HEHYLAYKAGIQRGDLVLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLSdQMDFVKGDFMK-MDFEE 185
Cdd:COG0500  14 LAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLG-NVEFLVADLAElDPLPA 92
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6323635  186 NTFDKVYAIEATCHAP--KLEGVYSEIYKVLKPGGTFAV 222
Cdd:COG0500  93 ESFDLVVAFGVLHHLPpeEREALLRELARALKPGGVLLL 131
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
114-224 5.48e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 56.31  E-value: 5.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   114 KAGIQRGDLVLDVGCGVGGPAREIARFTG--CNVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEENTFDkV 191
Cdd:PRK00216  46 WLGVRPGDKVLDLACGTGDLAIALAKAVGktGEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFD-A 124
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6323635   192 YAIeatchA------PKLEGVYSEIYKVLKPGGTFAVYE 224
Cdd:PRK00216 125 VTI-----AfglrnvPDIDKALREMYRVLKPGGRLVILE 158
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
124-220 6.79e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.76  E-value: 6.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    124 LDVGCGVGGPAREIAR-FTGCNVIGLNNNDYQIAKAKYYAKKYNLSD--QMDFVKGDFMKMDFEenTFDKVYAIEATCHA 200
Cdd:pfam08242   1 LEIGCGTGTLLRALLEaLPGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPG--SFDVVVASNVLHHL 78
                          90       100
                  ....*....|....*....|
gi 6323635    201 PKLEGVYSEIYKVLKPGGTF 220
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
114-224 6.95e-08

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: 52.65  E-value: 6.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    114 KAGIQRGDLVLDVGCGVGGPAREIARFTGC--NVIGLnnnDYQIAKAKYYAKKYNLSDQMDFVKGDFMKMDFEENTFDKV 191
Cdd:TIGR01934  34 LIGVFKGQKVLDVACGTGDLAIELAKSAPDrgKVTGV---DFSSEMLEVAKKKSELPLNIEFIQADAEALPFEDNSFDAV 110
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 6323635    192 ---YAIEATCHAPKlegVYSEIYKVLKPGGTFAVYE 224
Cdd:TIGR01934 111 tiaFGLRNVTDIQK---ALREMYRVLKPGGRLVILE 143
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
94-223 3.24e-07

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 49.95  E-value: 3.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   94 FYKGeSFAASIARHehyLAYKAGIQRGDLVLDVGCGVGGPAREiARFTGCNVIGlnnNDyqIAKAKYYAKKYNLS----D 169
Cdd:COG1041   5 FYPG-SLDPRLARA---LVNLAGAKEGDTVLDPFCGTGTILIE-AGLLGRRVIG---SD--IDPKMVEGARENLEhygyE 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323635  170 QMDFVKGDFMKMDFEENTFDKV-----YAIEATCHAPKLEGVYS----EIYKVLKPGGTFAVY 223
Cdd:COG1041  75 DADVIRGDARDLPLADESVDAIvtdppYGRSSKISGEELLELYEkaleEAARVLKPGGRVVIV 137
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
123-272 3.39e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 49.73  E-value: 3.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    123 VLDVGCGVGGPAREIARFtGCNVIGLNNNDYQIAKAKyyakkynlsDQMDFVKGDFMKMDFEENTFDKVYAIEATCHAPK 202
Cdd:pfam13489  26 VLDFGCGTGIFLRLLRAQ-GFSVTGVDPSPIAIERAL---------LNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPD 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    203 LEGVYSEIYKVLKPGGTFAVYEWVMTDKYDENNPEHRKIAYEielgDGIPKMFHVDVARKALKNCGFEVL 272
Cdd:pfam13489  96 PPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPR----NGHISLFSARSLKRLLEEAGFEVV 161
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
114-221 3.55e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.00  E-value: 3.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  114 KAGIQRGDLVLDVGCGVGGPAREIARFtGCNVIGLnnnDyqiakakyyakkynLSDQM-----------DFVKGDFMKMD 182
Cdd:COG4976  41 RLPPGPFGRVLDLGCGTGLLGEALRPR-GYRLTGV---D--------------LSEEMlakarekgvydRLLVADLADLA 102
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6323635  183 FEENTFDKVYAIEATCHAPKLEGVYSEIYKVLKPGGTFA 221
Cdd:COG4976 103 EPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
123-221 7.38e-07

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: 49.98  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    123 VLDVGCGVGGPAREIA-RFTGCNVIGLNNNDYQIakakyYAKKYNLSDQMDFVKGDFMKMDFEENTFDKVYAIEAT--CH 199
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLkRFPQAEFIALDISAGML-----AQAKTKLSENVQFICGDAEKLPLEDSSFDLIVSNLALqwCD 112
                          90       100
                  ....*....|....*....|..
gi 6323635    200 apKLEGVYSEIYKVLKPGGTFA 221
Cdd:TIGR02072 113 --DLSQALSELARVLKPGGLLA 132
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
116-224 2.46e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 48.20  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635    116 GIQRGDLVLDVGCGVGGPAREIARFTGCN--VIGLNNNDYQIAKAKYYAKKYNLSdQMDFVKGDFMKMDFEENTFDKV-- 191
Cdd:pfam01209  39 GVKRGNKFLDVAGGTGDWTFGLSDSAGSSgkVVGLDINENMLKEGEKKAKEEGKY-NIEFLQGNAEELPFEDDSFDIVti 117
                          90       100       110
                  ....*....|....*....|....*....|....
gi 6323635    192 -YAIEATCHAPKlegVYSEIYKVLKPGGTFAVYE 224
Cdd:pfam01209 118 sFGLRNFPDYLK---VLKEAFRVLKPGGRVVCLE 148
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
120-279 3.14e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.90  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   120 GDLVLDVGCGVGGPAREIARFTGCNVIGLNNNDYQIAKAKYYAKKYNLSdqMDFVKGDFMKMDFEENTFDKVYAIEATCH 199
Cdd:PLN02336 267 GQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCS--VEFEVADCTKKTYPDNSFDVIYSRDTILH 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   200 APKLEGVYSEIYKVLKPGGTFAVYEWVMTDKydenNPEHRKIAYEIELGdgiPKMFHVDVARKALKNCGFEVLVSEDLAD 279
Cdd:PLN02336 345 IQDKPALFRSFFKWLKPGGKVLISDYCRSPG----TPSPEFAEYIKQRG---YDLHDVQAYGQMLKDAGFDDVIAEDRTD 417
arsM PRK11873
arsenite methyltransferase;
115-222 3.81e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 44.94  E-value: 3.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   115 AGIQRGDLVLDVGCGVGGPAREIARFTGCN--VIGLNNNDYQIAKAKYYAKKYNLSDqMDFVKGDFMKMDFEENTFDkvy 192
Cdd:PRK11873  73 AELKPGETVLDLGSGGGFDCFLAARRVGPTgkVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVD--- 148
                         90       100       110
                 ....*....|....*....|....*....|...
gi 6323635   193 AIEATC---HAPKLEGVYSEIYKVLKPGGTFAV 222
Cdd:PRK11873 149 VIISNCvinLSPDKERVFKEAFRVLKPGGRFAI 181
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
123-221 9.51e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 43.59  E-value: 9.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   123 VLDVGCGVGGPAREiARFTGCNVIGLNnndyqiakakyyakkynLSDQM-----------DFVKGDFMKMDFEENTFDKV 191
Cdd:PRK10258  46 VLDAGCGPGWMSRY-WRERGSQVTALD-----------------LSPPMlaqarqkdaadHYLAGDIESLPLATATFDLA 107
                         90       100       110
                 ....*....|....*....|....*....|
gi 6323635   192 YAIEATCHAPKLEGVYSEIYKVLKPGGTFA 221
Cdd:PRK10258 108 WSNLAVQWCGNLSTALRELYRVVRPGGVVA 137
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
183-220 1.42e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 39.08  E-value: 1.42e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6323635  183 FEENTFDKVYA---IEatcHAPKLEGVY--SEIYKVLKPGGTF 220
Cdd:COG4627  42 FPDNSVDAIYSshvLE---HLDYEEAPLalKECYRVLKPGGIL 81
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
115-218 2.60e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.12  E-value: 2.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635  115 AGIQRGDLVLDVGCGVGGPAREIARFTGCNVI-------------------GLNNNDYQIakakyyakkyNLSDQMDFVK 175
Cdd:COG2521 128 VGVRRGDRVLDTCTGLGYTAIEALKRGAREVItvekdpnvlelaelnpwsrELANERIKI----------ILGDASEVIK 197
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6323635  176 gdfmkmDFEENTFDKVYaieatcHAP---KLEG------VYSEIYKVLKPGG 218
Cdd:COG2521 198 ------TFPDESFDAII------HDPprfSLAGelysleFYRELYRVLKPGG 237
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
115-217 4.14e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 38.72  E-value: 4.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635   115 AGIQRGDLVLDVGCGVGGPAREIARFTGCN--VIGLNNNDYQIAKAKYYAKKYNLS--DQMDFVKGDFMKMDFEENTFDK 190
Cdd:PLN02233  69 SGAKMGDRVLDLCCGSGDLAFLLSEKVGSDgkVMGLDFSSEQLAVAASRQELKAKScyKNIEWIEGDATDLPFDDCYFDA 148
                         90       100       110
                 ....*....|....*....|....*....|
gi 6323635   191 V---YAIEATCHAPKlegVYSEIYKVLKPG 217
Cdd:PLN02233 149 ItmgYGLRNVVDRLK---AMQEMYRVLKPG 175
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
123-220 5.77e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323635     123 VLDVGCGVGGPAREIA-RFTGCNVIGLNNNDYQIAKAKYYAKKYNLSDQMDFVKGDFMKmDFEENTFDKVYAIEATCHAP 201
Cdd:smart00828   3 VLDFGCGYGSDLIDLAeRHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAK-DPFPDTYDLVFGFEVIHHIK 81
                           90
                   ....*....|....*....
gi 6323635     202 KLEGVYSEIYKVLKPGGTF 220
Cdd:smart00828  82 DKMDLFSNISRHLKDGGHL 100
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
114-149 9.33e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 37.91  E-value: 9.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 6323635   114 KAGIQRGDLVLDVGCGVGGPAREIARFTGCNVIGLN 149
Cdd:PRK11705 162 KLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVT 197
 
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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