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Conserved domains on  [gi|1021491120|ref|XP_016188577|]
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tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit trmt61a [Arachis ipaensis]

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
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
69-306 3.43e-126

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.).


The actual alignment was detected with superfamily member pfam08704:

Pssm-ID: 473071  Cd Length: 242  Bit Score: 360.27  E-value: 3.43e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  69 GFVYLLAPTPELWTLVLSHRTQILYIADISFVIMYLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGS 148
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 149 ARDDFERTGLSSIISVRVRDIQGEGFPNEFAGLADAVFLDLPQPWLAIPSAAKMLKQDGT-LCSFSPCVEQVQRSCETLQ 227
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFLTEVSGKADAVFLDLPSPWEAVPHAWKALKVEGGrFCSFSPCIEQVQRTCQALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 228 NC-FTDIRTFEVLLRTYEVREGKME--NLNGDNNGSNGSSLPCKRRQrSGGSYAPDSTVSS-VMARPCGEARGHTGFLTF 303
Cdd:pfam08704 161 ELgFTEISTLEVLLRVYDVRTVSLPviDLGIDREKENERTRTEGLSN-DDKSEDNSGNSMLgTALKPMSEAVGHTGYLTF 239

                  ...
gi 1021491120 304 ARL 306
Cdd:pfam08704 240 ATK 242
 
Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
69-306 3.43e-126

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 360.27  E-value: 3.43e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  69 GFVYLLAPTPELWTLVLSHRTQILYIADISFVIMYLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGS 148
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 149 ARDDFERTGLSSIISVRVRDIQGEGFPNEFAGLADAVFLDLPQPWLAIPSAAKMLKQDGT-LCSFSPCVEQVQRSCETLQ 227
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFLTEVSGKADAVFLDLPSPWEAVPHAWKALKVEGGrFCSFSPCIEQVQRTCQALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 228 NC-FTDIRTFEVLLRTYEVREGKME--NLNGDNNGSNGSSLPCKRRQrSGGSYAPDSTVSS-VMARPCGEARGHTGFLTF 303
Cdd:pfam08704 161 ELgFTEISTLEVLLRVYDVRTVSLPviDLGIDREKENERTRTEGLSN-DDKSEDNSGNSMLgTALKPMSEAVGHTGYLTF 239

                  ...
gi 1021491120 304 ARL 306
Cdd:pfam08704 240 ATK 242
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
19-305 1.68e-78

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 239.29  E-value: 1.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  19 GDLVIVYERHDNMKAVTVAENSVLQNRFGVFKHSEWIGKPFGSKVFSNKGGFVYLLAPTPELWTLVLSHRTQILYIADIS 98
Cdd:COG2519     2 GDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  99 FVIMYLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIISVRVRDIQgEGFPNEF 178
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIR-EGIDEGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 179 aglADAVFLDLPQPWLAIPSAAKMLKQDGTLCSFSPCVEQVQRSCETLQNC-FTDIRTFEVLLRTYEVREGKMenlngdn 257
Cdd:COG2519   161 ---VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESgFTDIEAVETLLREWKVEGLAV------- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1021491120 258 ngsngsslpckrrqrsggsyapdstvssvmaRPCGEARGHTGFLTFAR 305
Cdd:COG2519   231 -------------------------------RPEHRMVGHTGFLVFAR 247
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
100-209 1.86e-06

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 47.89  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 100 VIMYLEVVPGCLVLESGTGSGSLTTSLARAVaptGHVHTFDFHEQRAGSARDDFERTGLSSIIsVRVRDIQgEGFPNE-- 177
Cdd:PRK00312   70 MTELLELKPGDRVLEIGTGSGYQAAVLAHLV---RRVFSVERIKTLQWEAKRRLKQLGLHNVS-VRHGDGW-KGWPAYap 144
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1021491120 178 F-AGLADAVFLDLPQPWLaipsaaKMLKQDGTL 209
Cdd:PRK00312  145 FdRILVTAAAPEIPRALL------EQLKEGGIL 171
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
93-168 9.24e-04

protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]


Pssm-ID: 272896 [Multi-domain]  Cd Length: 215  Bit Score: 39.81  E-value: 9.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021491120  93 YIADISFVIM---YLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIIsVRVRD 168
Cdd:TIGR00080  59 TISAPHMVAMmteLLELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRKLGLDNVI-VIVGD 136
 
Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
69-306 3.43e-126

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 360.27  E-value: 3.43e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  69 GFVYLLAPTPELWTLVLSHRTQILYIADISFVIMYLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGS 148
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 149 ARDDFERTGLSSIISVRVRDIQGEGFPNEFAGLADAVFLDLPQPWLAIPSAAKMLKQDGT-LCSFSPCVEQVQRSCETLQ 227
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFLTEVSGKADAVFLDLPSPWEAVPHAWKALKVEGGrFCSFSPCIEQVQRTCQALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 228 NC-FTDIRTFEVLLRTYEVREGKME--NLNGDNNGSNGSSLPCKRRQrSGGSYAPDSTVSS-VMARPCGEARGHTGFLTF 303
Cdd:pfam08704 161 ELgFTEISTLEVLLRVYDVRTVSLPviDLGIDREKENERTRTEGLSN-DDKSEDNSGNSMLgTALKPMSEAVGHTGYLTF 239

                  ...
gi 1021491120 304 ARL 306
Cdd:pfam08704 240 ATK 242
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
19-305 1.68e-78

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 239.29  E-value: 1.68e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  19 GDLVIVYERHDNMKAVTVAENSVLQNRFGVFKHSEWIGKPFGSKVFSNKGGFVYLLAPTPELWTLVLSHRTQILYIADIS 98
Cdd:COG2519     2 GDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120  99 FVIMYLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIISVRVRDIQgEGFPNEF 178
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIR-EGIDEGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 179 aglADAVFLDLPQPWLAIPSAAKMLKQDGTLCSFSPCVEQVQRSCETLQNC-FTDIRTFEVLLRTYEVREGKMenlngdn 257
Cdd:COG2519   161 ---VDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALRESgFTDIEAVETLLREWKVEGLAV------- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1021491120 258 ngsngsslpckrrqrsggsyapdstvssvmaRPCGEARGHTGFLTFAR 305
Cdd:COG2519   231 -------------------------------RPEHRMVGHTGFLVFAR 247
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
112-188 3.71e-10

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 57.89  E-value: 3.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1021491120 112 VLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIISVRVRDIQgEGFPNEFAGLADAVFLD 188
Cdd:COG4122    20 ILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDAL-EVLPRLADGPFDLVFID 95
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
104-209 1.29e-08

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 53.94  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 104 LEVVPGCLVLESGTGSGSLTTSLARAVaptGHVHTFDFHEQRAGSARDDFERTGLSSiISVRVRDiqG-EGFPNE--Fag 180
Cdd:COG2518    62 LDLKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARERLAALGYDN-VTVRVGD--GaLGWPEHapF-- 133
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1021491120 181 laDAVFL-----DLPQPWLAipsaakMLKQDGTL 209
Cdd:COG2518   134 --DRIIVtaaapEVPEALLE------QLAPGGRL 159
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
103-194 1.32e-06

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 48.13  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 103 YLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIIsVRVRDiqG-EGFPnEFAGL 181
Cdd:pfam01135  68 LLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVI-VVVGD--GrQGWP-EFAPY 143
                          90
                  ....*....|....*...
gi 1021491120 182 aDAVFL-----DLPQPWL 194
Cdd:pfam01135 144 -DAIHVgaaapEIPEALI 160
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
100-209 1.86e-06

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 47.89  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 100 VIMYLEVVPGCLVLESGTGSGSLTTSLARAVaptGHVHTFDFHEQRAGSARDDFERTGLSSIIsVRVRDIQgEGFPNE-- 177
Cdd:PRK00312   70 MTELLELKPGDRVLEIGTGSGYQAAVLAHLV---RRVFSVERIKTLQWEAKRRLKQLGLHNVS-VRHGDGW-KGWPAYap 144
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1021491120 178 F-AGLADAVFLDLPQPWLaipsaaKMLKQDGTL 209
Cdd:PRK00312  145 FdRILVTAAAPEIPRALL------EQLKEGGIL 171
PRK08317 PRK08317
hypothetical protein; Provisional
104-209 6.43e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 46.47  E-value: 6.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 104 LEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARddfERT-GLSSIISVRVRDIQGEGFPNEF--AG 180
Cdd:PRK08317   15 LAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAK---ERAaGLGPNVEFVRGDADGLPFPDGSfdAV 91
                          90       100
                  ....*....|....*....|....*....
gi 1021491120 181 LADAVFLDLPQPWLAIPSAAKMLKQDGTL 209
Cdd:PRK08317   92 RSDRVLQHLEDPARALAEIARVLRPGGRV 120
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
108-230 1.20e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.33  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 108 PGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSiISVRVRDIqgEGFPNEFAG------L 181
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDI--EELPELLEDdkfdvvI 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1021491120 182 ADAVFLDLPQPWLAIPSAAKMLKQDGTLCSFSPCV-----EQVQRSCETLQNCF 230
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSlaelpAHVKEDSTYYAGCV 133
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
104-186 2.24e-05

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 45.54  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 104 LEVVPGCLVLESGTGSGSLTTSLARAvAPTGHVHTFDFHEQRAGSARDDFERTGLSsiisvRVRDIQGEGfPNEFAGL-- 181
Cdd:COG2242   243 LALRPGDVLWDIGAGSGSVSIEAARL-APGGRVYAIERDPERAALIRANARRFGVP-----NVEVVEGEA-PEALADLpd 315

                  ....*
gi 1021491120 182 ADAVF 186
Cdd:COG2242   316 PDAVF 320
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
100-210 9.67e-05

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: 41.90  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 100 VIMYLEVVPGCLVLESGTGSGSLTTSLARAvapTGHVHTFDFHEQRAGSARDDFERTGLSsiISVRVRDIQGEGFPNEFa 179
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGS- 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1021491120 180 glADAVFL-----DLPQPWLAIPSAAKMLKQDGTLC 210
Cdd:COG2226    88 --FDLVISsfvlhHLPDPERALAEIARVLKPGGRLV 121
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
106-209 1.03e-04

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: 41.16  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 106 VVPGCLVLESGTGSGSLTTSLARAVAptgHVHTFDFHEQRAGSARDDFERTGlssiISVRVRDIQGEGFPNEFaglADAV 185
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGA---DVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLEDGS---FDLV 91
                          90       100
                  ....*....|....*....|....*....
gi 1021491120 186 FL-----DLPQPWLAIPSAAKMLKQDGTL 209
Cdd:COG2227    92 ICsevleHLPDPAALLRELARLLKPGGLL 120
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
112-207 3.20e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 112 VLESGTGSGSLTTSLARAVAptGHVHTFDFHEQRAGSARDDFERTGLSsiISVRVRDIQGEGFPNE-FaglaDAVF---- 186
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGsF----DLVVssgv 72
                          90       100
                  ....*....|....*....|....
gi 1021491120 187 ---LDLPQPWLAIPSAAKMLKQDG 207
Cdd:pfam13649  73 lhhLPDPDLEAALREIARVLKPGG 96
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
104-186 6.35e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.53  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 104 LEVVPGCLVLESGTGSGSLTTSLARAvapTG-HVHTFDFHEQRAGSARDDFERTGLSSIISVRVRDIQGEGFPNEFagla 182
Cdd:COG2230    47 LGLKPGMRVLDIGCGWGGLALYLARR---YGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQF---- 119

                  ....
gi 1021491120 183 DAVF 186
Cdd:COG2230   120 DAIV 123
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
93-168 9.24e-04

protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]


Pssm-ID: 272896 [Multi-domain]  Cd Length: 215  Bit Score: 39.81  E-value: 9.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021491120  93 YIADISFVIM---YLEVVPGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIIsVRVRD 168
Cdd:TIGR00080  59 TISAPHMVAMmteLLELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRKLGLDNVI-VIVGD 136
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
106-164 7.40e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 37.32  E-value: 7.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1021491120 106 VVPGCLVLESGTGSGSLTTSLARAVAptGHVHTFDFHEQRAGSARDDFERTGLSSIISV 164
Cdd:COG4076    33 VKPGDVVLDIGTGSGLLSMLAARAGA--KKVYAVEVNPDIAAVARRIIAANGLSDRITV 89
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
100-164 8.57e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 36.71  E-value: 8.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021491120 100 VIMYLEVV---PGCLVLESGTGSGSLTTSLARAVAPTGHVHTFDFHEQRAGSARDDFERTGLSSIISV 164
Cdd:PRK13944   61 VAMMCELIeprPGMKILEVGTGSGYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIERLGYWGVVEV 128
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
108-209 9.58e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 35.18  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021491120 108 PGCLVLESGTGSGSLTTSLARAVaPTGHVHTFDFHEQRAGSARDDFERtglssiISVRVRDIQGEGFPNEFAG-LADAVF 186
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARARLPN------VRFVVADLRDLDPPEPFDLvVSNAAL 73
                          90       100
                  ....*....|....*....|...
gi 1021491120 187 LDLPQPWLAIPSAAKMLKQDGTL 209
Cdd:COG4106    74 HWLPDHAALLARLAAALAPGGVL 96
 
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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