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Conserved domains on  [gi|502943538|ref|WP_013178514|]
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tRNA (guanosine(46)-N(7))-methyltransferase TrmB [Truepera radiovictrix]

Protein Classification

tRNA (guanine(46)-N(7))-methyltransferase TrmB( domain architecture ID 11415463)

tRNA (guanine(46)-N(7))-methyltransferase TrmB catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA

CATH:  3.40.50.150
EC:  2.1.1.33
Gene Symbol:  trmB
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
20-211 9.25e-49

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 439990  Cd Length: 204  Bit Score: 162.61  E-value: 9.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  20 PLLPWRR-FQFPLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLL 98
Cdd:COG0220   11 ELLPLGLdLKGPLDWAELFGNDAP---LVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  99 KVGAEFAVRhLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAF 178
Cdd:COG0220   88 RGDAVELLE-LFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGF 166
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 502943538 179 ALEE-----AEAPPAVFETKYALKWKGQGKRLFYQVFR 211
Cdd:COG0220  167 ENLAetgdyAPRPEDRPLTKYERKGLRLGRPIYYLIFR 204
 
Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
20-211 9.25e-49

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 162.61  E-value: 9.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  20 PLLPWRR-FQFPLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLL 98
Cdd:COG0220   11 ELLPLGLdLKGPLDWAELFGNDAP---LVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  99 KVGAEFAVRhLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAF 178
Cdd:COG0220   88 RGDAVELLE-LFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGF 166
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 502943538 179 ALEE-----AEAPPAVFETKYALKWKGQGKRLFYQVFR 211
Cdd:COG0220  167 ENLAetgdyAPRPEDRPLTKYERKGLRLGRPIYYLIFR 204
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
23-198 8.46e-38

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 134.13  E-value: 8.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  23 PWRRFQF-PLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVG 101
Cdd:PRK00121  22 LWPRLSPaPLDWAELFGNDAP---IHLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGLTNLRLLCGD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538 102 AEFAVRHLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAFALE 181
Cdd:PRK00121  99 AVEVLLDMFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALYARKLKPGGEIHFATDWEGYAEYMLEVLSAEGGFLVS 178
                        170       180
                 ....*....|....*....|.
gi 502943538 182 EAEAPPAVFE----TKYALKW 198
Cdd:PRK00121 179 EAGDYVPRPEgrpmTEYERKG 199
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
44-206 7.16e-36

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 128.18  E-value: 7.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538   44 ALLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEFAVRHLFPPGSLASITVNFP 123
Cdd:pfam02390   2 APVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNALDVLPNYFPPGSLQKIFINFP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  124 DPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAF---ALEEAEAPPAVFE----TKYAL 196
Cdd:pfam02390  82 DPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFerlDLENDLAPGPLSPlrpaTEYEQ 161
                         170
                  ....*....|
gi 502943538  197 KWKGQGKRLF 206
Cdd:pfam02390 162 KVQRLGGPIY 171
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
27-160 2.68e-26

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 103.21  E-value: 2.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538   27 FQFPLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEFAV 106
Cdd:TIGR00091   3 SLDKPDFATVFGNKAP---LHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHVLCGDANELL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502943538  107 RHLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATD 160
Cdd:TIGR00091  80 DKFFPDGSLSKVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTD 133
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
48-157 2.10e-05

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: 42.80  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  48 VEVGFGDGRYTvRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEfaVRHLFPPGSLASITVNFPDPWP 127
Cdd:cd02440    3 LDLGCGTGALA-LALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAE--ELPPEADESFDVIISDPPLHHL 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 502943538 128 KERHegrrllrASFFRLAAARLAPRGVILL 157
Cdd:cd02440   80 VEDL-------ARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
20-211 9.25e-49

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 162.61  E-value: 9.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  20 PLLPWRR-FQFPLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLL 98
Cdd:COG0220   11 ELLPLGLdLKGPLDWAELFGNDAP---LVLEIGFGKGEFLVELAAANPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  99 KVGAEFAVRhLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAF 178
Cdd:COG0220   88 RGDAVELLE-LFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALLARVLKPGGELHLATDWEDYAEEMLEVLSAHPGF 166
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 502943538 179 ALEE-----AEAPPAVFETKYALKWKGQGKRLFYQVFR 211
Cdd:COG0220  167 ENLAetgdyAPRPEDRPLTKYERKGLRLGRPIYYLIFR 204
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
23-198 8.46e-38

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 134.13  E-value: 8.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  23 PWRRFQF-PLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVG 101
Cdd:PRK00121  22 LWPRLSPaPLDWAELFGNDAP---IHLEIGFGKGEFLVEMAKANPDINFIGIEVHEPGVGKALKKIEEEGLTNLRLLCGD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538 102 AEFAVRHLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAFALE 181
Cdd:PRK00121  99 AVEVLLDMFPDGSLDRIYLNFPDPWPKKRHHKRRLVQPEFLALYARKLKPGGEIHFATDWEGYAEYMLEVLSAEGGFLVS 178
                        170       180
                 ....*....|....*....|.
gi 502943538 182 EAEAPPAVFE----TKYALKW 198
Cdd:PRK00121 179 EAGDYVPRPEgrpmTEYERKG 199
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
44-206 7.16e-36

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 128.18  E-value: 7.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538   44 ALLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEFAVRHLFPPGSLASITVNFP 123
Cdd:pfam02390   2 APVFLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNALDVLPNYFPPGSLQKIFINFP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  124 DPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAF---ALEEAEAPPAVFE----TKYAL 196
Cdd:pfam02390  82 DPWPKKRHHKRRLLQPEFLKEYARVLKPGGVLHLATDVEEYAEEMLKHLAEHPLFerlDLENDLAPGPLSPlrpaTEYEQ 161
                         170
                  ....*....|
gi 502943538  197 KWKGQGKRLF 206
Cdd:pfam02390 162 KVQRLGGPIY 171
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
27-160 2.68e-26

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 103.21  E-value: 2.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538   27 FQFPLEWAAQFPHHDPaalLHVEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEFAV 106
Cdd:TIGR00091   3 SLDKPDFATVFGNKAP---LHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHVLCGDANELL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502943538  107 RHLFPPGSLASITVNFPDPWPKERHEGRRLLRASFFRLAAARLAPRGVILLATD 160
Cdd:TIGR00091  80 DKFFPDGSLSKVFLNFPDPWPKKRHNKRRITQPHFLKEYANVLKKGGVIHFKTD 133
PRK14121 PRK14121
tRNA (guanine-N(7)-)-methyltransferase; Provisional
48-203 3.81e-16

tRNA (guanine-N(7)-)-methyltransferase; Provisional


Pssm-ID: 237615  Cd Length: 390  Bit Score: 78.46  E-value: 3.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  48 VEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEFaVRHLFPPGSLASITVNFPDPWP 127
Cdd:PRK14121 127 IEIGFGSGRHLLYQAKNNPNKLFIGIEIHTPSIEQVLKQIELLNLKNLLIINYDARL-LLELLPSNSVEKIFVHFPVPWD 205
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502943538 128 KERHegRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEA--SGAFALEEAEAPPAVfeTKYALKWKGQGK 203
Cdd:PRK14121 206 KKPH--RRVISEDFLNEALRVLKPGGTLELRTDSELYFEFSLELFLKlpKAKIEIKKNAQLEVS--SKYEDRWKKQNK 279
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
48-178 2.18e-08

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 55.26  E-value: 2.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  48 VEVGFGDGRYTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEFAVRHLfPPGSLASITVNFPDPWP 127
Cdd:PRK01544 352 LEIGFGMGEHFINQAKMNPDALFIGVEVYLNGVANVLKLAGEQNITNFLLFPNNLDLILNDL-PNNSLDGIYILFPDPWI 430
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502943538 128 KERHEGRRLLRASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASGAF 178
Cdd:PRK01544 431 KNKQKKKRIFNKERLKILQDKLKDNGNLVFASDIENYFYEAIELIQQNGNF 481
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
48-157 2.10e-05

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: 42.80  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  48 VEVGFGDGRYTvRRALEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKVGAEfaVRHLFPPGSLASITVNFPDPWP 127
Cdd:cd02440    3 LDLGCGTGALA-LALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAE--ELPPEADESFDVIISDPPLHHL 79
                         90       100       110
                 ....*....|....*....|....*....|
gi 502943538 128 KERHegrrllrASFFRLAAARLAPRGVILL 157
Cdd:cd02440   80 VEDL-------ARFLEEARRLLKPGGVLVL 102
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
31-186 3.32e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.06  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  31 LEWAAQFPHHDPAALLhVEVGFGDGRYTVRRAlEAPQERFVGLEISSASLQRGLKRVRREGVANVKLLKvgAEFAVRHLF 110
Cdd:COG0500   15 AALLALLERLPKGGRV-LDLGCGTGRNLLALA-ARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLV--ADLAELDPL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538 111 PPGS----LASITVNFPDPwpkerhegrrLLRASFFRLAAARLAPRGVILLAtdhPEYLAFAQREAEASGAFALEEAEAP 186
Cdd:COG0500   91 PAESfdlvVAFGVLHHLPP----------EEREALLRELARALKPGGVLLLS---ASDAAAALSLARLLLLATASLLELL 157
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
25-176 6.26e-04

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: 39.59  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  25 RRFQFPLEWAAQFPHHDPAALLhvEVGFGDGRYTvrRALEAPQERFVGLEISSASLQRGLKRVRREGVaNVKLLKVGAEf 104
Cdd:COG2226    6 ARYDGREALLAALGLRPGARVL--DLGCGTGRLA--LALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502943538 105 avrHL-FPPGSLASITVNF-----PDPwpkerhegrrllrASFFRLAAARLAPRGVILLATDHPEYLAFAQREAEASG 176
Cdd:COG2226   80 ---DLpFPDGSFDLVISSFvlhhlPDP-------------ERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAG 141
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
49-160 3.10e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 37.60  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502943538  49 EVGFGDGRyTVRRALEAPQERFVGLEISSASLQRGLKRVRREGVAN-VKLLKVGAefavRHLFPPGS---LASITVNFpd 124
Cdd:COG2230   57 DIGCGWGG-LALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADY----RDLPADGQfdaIVSIGMFE-- 129
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502943538 125 pwpkerHEGRRLLRAsFFRLAAARLAPRGVILLATD 160
Cdd:COG2230  130 ------HVGPENYPA-YFAKVARLLKPGGRLLLHTP 158
 
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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