NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2532229353|ref|XP_057983893|]
View 

uncharacterized protein LOC131168466 [Malania oleifera]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.41e-123

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: 353.33  E-value: 1.41e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  69 GFVYVLAPTPELWTLVLSHRTQILYIADISFVILYLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAIS 148
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 149 AREDFEKTGLSSLVTVGVRDIQGQGFPDEHSGLADSVFLDLPQPWLAIPSASKMLK-QDGILCSFSPCIEQVQRSSETLR 227
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFLTEVSGKADAVFLDLPSPWEAVPHAWKALKvEGGRFCSFSPCIEQVQRTCQALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 228 S-DFTDIRTYEVLLRPYEVREVK---TNCGQDNVSGSFGLLPCKRRQR-SIEENNADeiPSSTVWARPSAETRGHTGYLT 302
Cdd:pfam08704 161 ElGFTEISTLEVLLRVYDVRTVSlpvIDLGIDREKENERTRTEGLSNDdKSEDNSGN--SMLGTALKPMSEAVGHTGYLT 238

                  ....
gi 2532229353 303 FARL 306
Cdd:pfam08704 239 FATK 242
 
Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
69-306 1.41e-123

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: 353.33  E-value: 1.41e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  69 GFVYVLAPTPELWTLVLSHRTQILYIADISFVILYLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAIS 148
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 149 AREDFEKTGLSSLVTVGVRDIQGQGFPDEHSGLADSVFLDLPQPWLAIPSASKMLK-QDGILCSFSPCIEQVQRSSETLR 227
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFLTEVSGKADAVFLDLPSPWEAVPHAWKALKvEGGRFCSFSPCIEQVQRTCQALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 228 S-DFTDIRTYEVLLRPYEVREVK---TNCGQDNVSGSFGLLPCKRRQR-SIEENNADeiPSSTVWARPSAETRGHTGYLT 302
Cdd:pfam08704 161 ElGFTEISTLEVLLRVYDVRTVSlpvIDLGIDREKENERTRTEGLSNDdKSEDNSGN--SMLGTALKPMSEAVGHTGYLT 238

                  ....
gi 2532229353 303 FARL 306
Cdd:pfam08704 239 FATK 242
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
19-305 1.37e-80

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: 244.30  E-value: 1.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  19 GDLVIVYERHDNMKAVKVCEGSVLQNRFGLFKHSDWIGKPFGSKVLSNKGGFVYVLAPTPELWTLVLSHRTQILYIADIS 98
Cdd:COG2519     2 GDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  99 FVILYLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTF----DFHEQraisAREDFEKTGLSSLVTVGVRDIQgQGF 174
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYerreDFAEI----ARKNLERFGLPDNVELKLGDIR-EGI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 175 PDehsGLADSVFLDLPQPWLAIPSASKMLKQDGILCSFSPCIEQVQRSSETLR-SDFTDIRTYEVLLRPYEVREVKTncg 253
Cdd:COG2519   157 DE---GDVDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALReSGFTDIEAVETLLREWKVEGLAV--- 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2532229353 254 qdnvsgsfgllpckrrqrsieennadeipsstvwaRPSAETRGHTGYLTFAR 305
Cdd:COG2519   231 -----------------------------------RPEHRMVGHTGFLVFAR 247
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
100-209 3.67e-06

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 47.12  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 100 VILYLEIVPGCVVLESGTGSGSLTTSLAKAVaptGHVYTFDFHEQRAISAREDFEKTGLSSlvtVGVRDIQGQ-GFPDEh 178
Cdd:PRK00312   70 MTELLELKPGDRVLEIGTGSGYQAAVLAHLV---RRVFSVERIKTLQWEAKRRLKQLGLHN---VSVRHGDGWkGWPAY- 142
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2532229353 179 sGLADSV-----FLDLPQPWLaipsasKMLKQDGIL 209
Cdd:PRK00312  143 -APFDRIlvtaaAPEIPRALL------EQLKEGGIL 171
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
103-164 1.67e-05

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: 45.20  E-value: 1.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532229353 103 YLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAISAREDFEKTGLSSLVTV 164
Cdd:TIGR00080  72 LLELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRKLGLDNVIVI 133
 
Name Accession Description Interval E-value
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
69-306 1.41e-123

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: 353.33  E-value: 1.41e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  69 GFVYVLAPTPELWTLVLSHRTQILYIADISFVILYLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAIS 148
Cdd:pfam08704   1 GFVYVLQPTPELWTLNLPHRTQILYTPDISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 149 AREDFEKTGLSSLVTVGVRDIQGQGFPDEHSGLADSVFLDLPQPWLAIPSASKMLK-QDGILCSFSPCIEQVQRSSETLR 227
Cdd:pfam08704  81 AREEFREHGIDQLVTVTHRDVCKEGFLTEVSGKADAVFLDLPSPWEAVPHAWKALKvEGGRFCSFSPCIEQVQRTCQALA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 228 S-DFTDIRTYEVLLRPYEVREVK---TNCGQDNVSGSFGLLPCKRRQR-SIEENNADeiPSSTVWARPSAETRGHTGYLT 302
Cdd:pfam08704 161 ElGFTEISTLEVLLRVYDVRTVSlpvIDLGIDREKENERTRTEGLSNDdKSEDNSGN--SMLGTALKPMSEAVGHTGYLT 238

                  ....
gi 2532229353 303 FARL 306
Cdd:pfam08704 239 FATK 242
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
19-305 1.37e-80

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: 244.30  E-value: 1.37e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  19 GDLVIVYERHDNMKAVKVCEGSVLQNRFGLFKHSDWIGKPFGSKVLSNKGGFVYVLAPTPELWTLVLSHRTQILYIADIS 98
Cdd:COG2519     2 GDRVLLTDPKGRKYLVRLEEGKKFHTHKGIIDHDDLIGKPEGSVVTTSKGKEFLVLRPTLYDYVLSMKRGTQIIYPKDAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  99 FVILYLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTF----DFHEQraisAREDFEKTGLSSLVTVGVRDIQgQGF 174
Cdd:COG2519    82 YIIARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYerreDFAEI----ARKNLERFGLPDNVELKLGDIR-EGI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 175 PDehsGLADSVFLDLPQPWLAIPSASKMLKQDGILCSFSPCIEQVQRSSETLR-SDFTDIRTYEVLLRPYEVREVKTncg 253
Cdd:COG2519   157 DE---GDVDAVFLDMPDPWEALEAVAKALKPGGVLVAYVPTVNQVSKLVEALReSGFTDIEAVETLLREWKVEGLAV--- 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2532229353 254 qdnvsgsfgllpckrrqrsieennadeipsstvwaRPSAETRGHTGYLTFAR 305
Cdd:COG2519   231 -----------------------------------RPEHRMVGHTGFLVFAR 247
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
104-209 7.67e-08

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 51.63  E-value: 7.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 104 LEIVPGCVVLESGTGSGSLTTSLAKAVaptGHVYTFDFHEQRAISAREDFEKTGLSSlVTVGVRDiqG-QGFPDEhsGLA 182
Cdd:COG2518    62 LDLKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARERLAALGYDN-VTVRVGD--GaLGWPEH--APF 133
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2532229353 183 DSVFL-----DLPQPWLAipsaskMLKQDGIL 209
Cdd:COG2518   134 DRIIVtaaapEVPEALLE------QLAPGGRL 159
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
112-188 8.62e-08

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: 50.95  E-value: 8.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 112 VLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAISAREDFEKTGLSSLVTVgvrdIQGQGF---PDEHSGLADSVFLD 188
Cdd:COG4122    20 ILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRIRL----ILGDALevlPRLADGPFDLVFID 95
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
106-218 1.45e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.11  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 106 IVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFhEQRAIS-AREDFEKTGLSSlVTVGVRDIQ--GQGFPDEH--SG 180
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDI-SEEAIEkARENAQKLGFDN-VEFEQGDIEelPELLEDDKfdVV 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2532229353 181 LADSVFLDLPQPWLAIPSASKMLKQDGILCSFSPCIEQ 218
Cdd:pfam13847  79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLA 116
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
70-209 1.54e-07

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.83  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353  70 FVYVLAPTPelwtlvlshrtqILYIADIS------FVILYLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHE 143
Cdd:pfam01135  41 YAYEDIPLS------------IGYGQTISaphmhaMMLELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIP 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2532229353 144 QRAISAREDFEKTGLSSLVTVgVRDiqG-QGFPDE------HSGLADSvflDLPQPWLaipsasKMLKQDGIL 209
Cdd:pfam01135 109 ELVEIARRNLEKLGLENVIVV-VGD--GrQGWPEFapydaiHVGAAAP---EIPEALI------DQLKEGGRL 169
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
100-209 3.67e-06

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 47.12  E-value: 3.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 100 VILYLEIVPGCVVLESGTGSGSLTTSLAKAVaptGHVYTFDFHEQRAISAREDFEKTGLSSlvtVGVRDIQGQ-GFPDEh 178
Cdd:PRK00312   70 MTELLELKPGDRVLEIGTGSGYQAAVLAHLV---RRVFSVERIKTLQWEAKRRLKQLGLHN---VSVRHGDGWkGWPAY- 142
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2532229353 179 sGLADSV-----FLDLPQPWLaipsasKMLKQDGIL 209
Cdd:PRK00312  143 -APFDRIlvtaaAPEIPRALL------EQLKEGGIL 171
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
103-164 1.67e-05

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: 45.20  E-value: 1.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2532229353 103 YLEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAISAREDFEKTGLSSLVTV 164
Cdd:TIGR00080  72 LLELKPGMKVLEIGTGSGYQAAVLAEIVGRDGLVVSIERIPELAEKAERRLRKLGLDNVIVI 133
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
106-164 6.99e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.49  E-value: 6.99e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2532229353 106 IVPGCVVLESGTGSGSLTTSLAKAVAptGHVYTFDFHEQRAISAREDFEKTGLSSLVTV 164
Cdd:COG4076    33 VKPGDVVLDIGTGSGLLSMLAARAGA--KKVYAVEVNPDIAAVARRIIAANGLSDRITV 89
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
100-210 1.69e-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: 41.13  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 100 VILYLEIVPGCVVLESGTGSGSLTTSLAKAvapTGHVYTFDFHEQRAISAREDFEKTGLSSLVTVGvrDIQGQGFPDEHs 179
Cdd:COG2226    14 LLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLNVEFVVG--DAEDLPFPDGS- 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2532229353 180 glADSVFL-----DLPQPWLAIPSASKMLKQDGILC 210
Cdd:COG2226    88 --FDLVISsfvlhHLPDPERALAEIARVLKPGGRLV 121
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
104-192 1.88e-04

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: 42.85  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 104 LEIVPGCVVLESGTGSGSLTTSLAKAvAPTGHVYTFDFHEQRAISAREDFEKTGLSSLVTVgvrdiqgqgfpdehSGLAD 183
Cdd:COG2242   243 LALRPGDVLWDIGAGSGSVSIEAARL-APGGRVYAIERDPERAALIRANARRFGVPNVEVV--------------EGEAP 307

                  ....*....
gi 2532229353 184 SVFLDLPQP 192
Cdd:COG2242   308 EALADLPDP 316
PRK08317 PRK08317
hypothetical protein; Provisional
104-207 2.86e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.46  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 104 LEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAISAREdfEKTGLSSLVTVGVRDIQGQGFPDEH--SGL 181
Cdd:PRK08317   15 LAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPDGSfdAVR 92
                          90       100
                  ....*....|....*....|....*.
gi 2532229353 182 ADSVFLDLPQPWLAIPSASKMLKQDG 207
Cdd:PRK08317   93 SDRVLQHLEDPARALAEIARVLRPGG 118
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
108-164 7.01e-04

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 40.18  E-value: 7.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2532229353 108 PGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAISAREDFEKTGLSSLVTV 164
Cdd:PRK13944   72 PGMKILEVGTGSGYQAAVCAEAIERRGKVYTVEIVKELAIYAAQNIERLGYWGVVEV 128
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
106-209 1.01e-03

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: 38.46  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 106 IVPGCVVLESGTGSGSLTTSLAKAVAptgHVYTFDFHEQRAISAREDFEKTGlsslVTVGVRDIQGQGFPDEHsglADSV 185
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGA---DVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLEDGS---FDLV 91
                          90       100
                  ....*....|....*....|....*....
gi 2532229353 186 FL-----DLPQPWLAIPSASKMLKQDGIL 209
Cdd:COG2227    92 ICsevleHLPDPAALLRELARLLKPGGLL 120
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
104-168 2.22e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 38.46  E-value: 2.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2532229353 104 LEIVPGCVVLESGTGSGSLTTSLAKAVAPTGHVYTFDFHEQRAISAREDFEKTGLSSlVTVGVRD 168
Cdd:PRK13942   72 LDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGYDN-VEVIVGD 135
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
112-210 5.53e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.20  E-value: 5.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 112 VLESGTGSGSLTTSLAKAVAptGHVYTFDFHEqRAIS-AREDFEKTGLSSlVTVGVRDIQG-QGFPDEHSGL--ADSVFL 187
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFG--GRVIGIDLSP-EAIAlARARAAKAGLGN-VEFLVADLAElDPLPAESFDLvvAFGVLH 105
                          90       100
                  ....*....|....*....|....*
gi 2532229353 188 DLPQPWL--AIPSASKMLKQDGILC 210
Cdd:COG0500   106 HLPPEEReaLLRELARALKPGGVLL 130
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
112-207 7.02e-03

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.23  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2532229353 112 VLESGTGSGSLTTSLAKAVAptGHVYTFDFHEQRAISAREDFEKTGLSslVTVGVRDIQGQGFPDEHsglADSVF----- 186
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGS---FDLVVssgvl 73
                          90       100
                  ....*....|....*....|...
gi 2532229353 187 --LDLPQPWLAIPSASKMLKQDG 207
Cdd:pfam13649  74 hhLPDPDLEAALREIARVLKPGG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH