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Conserved domains on  [gi|1032282675|gb|OAO97002|]
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PRMT1B [Arabidopsis thaliana]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 1905023)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
82-245 2.12e-44

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 153.27  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675  82 HEEMLKDVVRTKTYQNVIYqnKFLIKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECS-QMADMAKEIVKANGFSDVITV 160
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIE--RVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 161 LKGKIEEIELPTpKVDVIISEWMGYFLLFENMLDSVLYARDKWLVEGGVVLPDKASLHLTAIEDSEYkEDKIEFWNsVYG 240
Cdd:COG4076    90 INADATDLDLPE-KADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVD-AEGFEDWQ-FDG 166


                  ....*
gi 1032282675 241 FDMSC 245
Cdd:COG4076   167 FDFRL 171
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
82-245 2.12e-44

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 153.27  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675  82 HEEMLKDVVRTKTYQNVIYqnKFLIKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECS-QMADMAKEIVKANGFSDVITV 160
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIE--RVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 161 LKGKIEEIELPTpKVDVIISEWMGYFLLFENMLDSVLYARDKWLVEGGVVLPDKASLHLTAIEDSEYkEDKIEFWNsVYG 240
Cdd:COG4076    90 INADATDLDLPE-KADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVD-AEGFEDWQ-FDG 166


                  ....*
gi 1032282675 241 FDMSC 245
Cdd:COG4076   167 FDFRL 171
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 111-211 5.04e-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: 64.76  E-value: 5.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQMADMAKEIVKANGFSDVITVLKGKIEEI-ELPTPKVDVIISeWMGYFLLF 189
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIIS-DPPLHHLV 80

                          90       100
                  ....*....|....*....|..
gi 1032282675 190 ENMLDSVLYARDKwLVEGGVVL 211
Cdd:cd02440    81 EDLARFLEEARRL-LKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 111-180 6.38e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 6.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQ-MADMAKEIVKANGFSdvITVLKGKIEEIELPTPKVDVIIS 180
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPeMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVVS 69
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
103-179 1.68e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 1.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032282675 103 KFLIKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECSQMA-DMAKEIVKANGFSDVITVLKGKieeielptPKVDVII 179
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAvEAARENAELNGVELNVYLPQGD--------LKADVIV 184
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 101-180 3.43e-06

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: 47.67  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 101 QNKFLIKDKIVLDVGAGTGILSLFCAKAG-AAHVYAVE-CSQMADMAKEIVKANgfsdvITVLKGKIEEIELPTPKVDVI 178
Cdd:TIGR02072  28 KEKGIFIPASVLDIGCGTGYLTRALLKRFpQAEFIALDiSAGMLAQAKTKLSEN-----VQFICGDAEKLPLEDSSFDLI 102


                  ..
gi 1032282675 179 IS 180
Cdd:TIGR02072 103 VS 104
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
82-245 2.12e-44

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 153.27  E-value: 2.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675  82 HEEMLKDVVRTKTYQNVIYqnKFLIKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECS-QMADMAKEIVKANGFSDVITV 160
Cdd:COG4076    12 HHPMLNDVERNDAFKAAIE--RVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 161 LKGKIEEIELPTpKVDVIISEWMGYFLLFENMLDSVLYARDKWLVEGGVVLPDKASLHLTAIEDSEYkEDKIEFWNsVYG 240
Cdd:COG4076    90 INADATDLDLPE-KADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVD-AEGFEDWQ-FDG 166


                  ....*
gi 1032282675 241 FDMSC 245
Cdd:COG4076   167 FDFRL 171
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 111-180 4.00e-14

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 71.33  E-value: 4.00e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032282675 111 VLDVGAGTGILSLFCA-KAGAAHVYAVEC-SQMADMAKEIVKANGFSDVITVLKGKIEEI--ELPTPKVDVIIS 180
Cdd:COG4123    41 VLDLGTGTGVIALMLAqRSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLKEFaaELPPGSFDLVVS 114
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 111-211 5.04e-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: 64.76  E-value: 5.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQMADMAKEIVKANGFSDVITVLKGKIEEI-ELPTPKVDVIISeWMGYFLLF 189
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIIS-DPPLHHLV 80

                          90       100
                  ....*....|....*....|..
gi 1032282675 190 ENMLDSVLYARDKwLVEGGVVL 211
Cdd:cd02440    81 EDLARFLEEARRL-LKPGGVLV 101
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 111-180 6.38e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.12  E-value: 6.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQ-MADMAKEIVKANGFSdvITVLKGKIEEIELPTPKVDVIIS 180
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPeMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVVS 69
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
107-179 1.04e-10

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 61.73  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 107 KDKIVLDVGAGTGILSLFCAKAGAAHVYAVecsqmaDM-------AKEIVKANGFSDVITVLKGKIeeieLPTPKVDVII 179
Cdd:COG2264   148 PGKTVLDVGCGSGILAIAAAKLGAKRVLAV------DIdpvaveaARENAELNGVEDRIEVVLGDL----LEDGPYDLVV 217
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 102-211 1.20e-10

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: 58.49  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 102 NKFLIKDKIVLDVGAGTGILSLFCAKAGaAHVYAVECS-QMADMAKEIVKANGfsdvITVLKGKIEEIELPTPKVDVIIS 180
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISpEALEIARERAAELN----VDFVQGDLEDLPLEDGSFDLVIC 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032282675 181 ewmgyFLLFENMLDSVLYARD--KWLVEGGVVL 211
Cdd:COG2227    94 -----SEVLEHLPDPAALLRElaRLLKPGGLLL 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 111-211 1.61e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 59.17  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQ-MADMAKEIVKANGFSDVITVLKGKIEEIELPTPkVDVIIS----EWMG- 184
Cdd:COG2230    55 VLDIGCGWGGLALYLARRYGVRVTGVTLSPeQLEYARERAAEAGLADRVEVRLADYRDLPADGQ-FDAIVSigmfEHVGp 133

                          90       100
                  ....*....|....*....|....*....
gi 1032282675 185 --YFLLFENMLDsvlyardkWLVEGGVVL 211
Cdd:COG2230   134 enYPAYFAKVAR--------LLKPGGRLL 154
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
103-179 1.68e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 57.85  E-value: 1.68e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1032282675 103 KFLIKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECSQMA-DMAKEIVKANGFSDVITVLKGKieeielptPKVDVII 179
Cdd:PRK00517  115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAvEAARENAELNGVELNVYLPQGD--------LKADVIV 184
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 106-179 4.32e-09

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 56.05  E-value: 4.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032282675 106 IKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECSQMA-DMAKEIVKANGFSdvITVLKGKIEEIElPTPKVDVII 179
Cdd:COG3897    69 VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEAlAALRLNAALNGVA--ITTRLGDWRDPP-AAGGFDLIL 140
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 111-180 1.57e-08

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: 53.07  E-value: 1.57e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032282675 111 VLDVGAGTGILSLFCAKAGaAHVYAVECSQ-MADMAKEIVKANGFSdvITVLKGKIEEIELPTPKVDVIIS 180
Cdd:COG2226    26 VLDLGCGTGRLALALAERG-ARVTGVDISPeMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVIS 93
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 107-179 3.57e-08

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 54.19  E-value: 3.57e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032282675 107 KDKIVLDVGAGTGILSLFCAKAGAAHVYAVECSQMA-DMAKEIVKANGFSDVITV-LKGkieeiELPTPKVDVII 179
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAvRAAKENAELNGVEARLEVyLPG-----DLPKEKADVVV 230
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
106-180 1.03e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.83  E-value: 1.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032282675 106 IKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECSQ-MADMAKEivKANGFSDVITVLKGKIEEIELPtPKVDVIIS 180
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPeALEIARE--NAERLGVRVDFIRADVTRIPLG-GSVDTVVM 116
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 111-180 2.53e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 50.69  E-value: 2.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQ-MADMAKEIVKANGFSDViTVLKGKIEEI-ELPTPKVDVIIS 180
Cdd:COG0500    30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPeAIALARARAAKAGLGNV-EFLVADLAELdPLPAESFDLVVA 100
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 105-179 3.20e-07

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 51.72  E-value: 3.20e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032282675 105 LIKDKIVLDVGAGTGILSLFCAKAgAAHVYAVECS-QMADMAKEIVKANGFSDViTVLKGKIEEI---ELPTPKVDVII 179
Cdd:COG2265   231 LTGGERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGLKNV-EFVAGDLEEVlpeLLWGGRPDVVV 307
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 111-180 7.29e-07

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.15  E-value: 7.29e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032282675 111 VLDVGAGTGILSLFCAKA-GAAHVYAVECSQMA-DMAKEIVKANGFSDVITVLKGKIEEIELPTPKVDVIIS 180
Cdd:COG2890   116 VLDLGTGSGAIALALAKErPDARVTAVDISPDAlAVARRNAERLGLEDRVRFLQGDLFEPLPGDGRFDLIVS 187
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 111-180 2.15e-06

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 47.88  E-value: 2.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032282675 111 VLDVGAGTGILSLFCAKAGA-AHVYAVECSQMA-DMAKEIVKANGFSDViTVLKGKIEEiELPTPKVDVIIS 180
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPeARVTLVDVNARAvELARANAAANGLENV-EVLWSDGLS-GVPDGSFDLILS 122
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 112-183 3.32e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.96  E-value: 3.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032282675 112 LDVGAGTGILSLFCAKAGaAHVYAVE-CSQMADMAKEivkaNGFSDVITVLKGKIEEIELPTPKVDVIISEWM 183
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDiSPEMLELARE----KAPREGLTFVVGDAEDLPFPDNSFDLVLSSEV 68
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 101-180 3.43e-06

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: 47.67  E-value: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 101 QNKFLIKDKIVLDVGAGTGILSLFCAKAG-AAHVYAVE-CSQMADMAKEIVKANgfsdvITVLKGKIEEIELPTPKVDVI 178
Cdd:TIGR02072  28 KEKGIFIPASVLDIGCGTGYLTRALLKRFpQAEFIALDiSAGMLAQAKTKLSEN-----VQFICGDAEKLPLEDSSFDLI 102


                  ..
gi 1032282675 179 IS 180
Cdd:TIGR02072 103 VS 104
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 111-180 1.40e-05

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 44.89  E-value: 1.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032282675 111 VLDVGAGTGILSLFCAKAGA-AHVYAVECSQMA-DMAKEIVKANGFsDVITVLKGKIEEiELPTPKVDVIIS 180
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPdAELTMVDINARAlESARENLAANGL-ENGEVVASDVYS-GVEDGKFDLIIS 104
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 112-210 2.20e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.74  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 112 LDVGAGTGILSLFCAKAGA-AHVYAVECS-QMADMAKEIVKANGFSDVITVLKGKIEEIELPTPKVDVIIsewMGYFLLF 189
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPgLEYTGLDISpAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVV---ASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 1032282675 190 ENMLDSVLYARDKWLVEGGVV 210
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
arsM PRK11873
arsenite methyltransferase;
110-180 2.54e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 45.32  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 110 IVLDVGAGTGILSLFCAKA-GA-AHVYAVecsqmaDMAKEIV---KAN----GFSDViTVLKGKIEEIELPTPKVDVIIS 180
Cdd:PRK11873   80 TVLDLGSGGGFDCFLAARRvGPtGKVIGV------DMTPEMLakaRANarkaGYTNV-EFRLGEIEALPVADNSVDVIIS 152
PRK14968 PRK14968
putative methyltransferase; Provisional
 107-211 3.47e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.12  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 107 KDKIVLDVGAGTGILSLFCAKAGAAHV------YAVECsqmadmAKEIVKANGF---------SDVITVLKGKIEEI--- 168
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKNGKKVVgvdinpYAVEC------AKCNAKLNNIrnngvevirSDLFEPFRGDKFDVilf 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1032282675 169 ---ELPTPKvDVIISEWMGYFL--------LFENMLDSVlyarDKWLVEGGVVL 211
Cdd:PRK14968   97 nppYLPTEE-EEEWDDWLNYALsggkdgreVIDRFLDEV----GRYLKPGGRIL 145
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 108-233 3.78e-05

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 45.24  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 108 DKIVLDVGAGTGILSLFCAKAGAAHVYAVECSQMA-DMAKEIVKANGFSDVITVLKGKI-EEIELPTPKVDVIIsewMGY 185
Cdd:COG2520   181 GERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAvEYLKENIRLNKVEDRVTPILGDArEVAPELEGKADRII---MNL 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1032282675 186 FLLFENMLDSVLYArdkwLVEGGVVlpdkaslHL-TAIEDSEYKEDKIE 233
Cdd:COG2520   258 PHSADEFLDAALRA----LKPGGVI-------HYyEIVPEEDPFERAEE 295
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 106-210 4.45e-05

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 43.92  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 106 IKDKIVLDVGAGTGILSLFCAKAGAAHVYAVECS-QMADMAKEIVKANGFSDVITVLKGKIEEI--ELPTPKVDVIisew 182
Cdd:COG0742    40 IEGARVLDLFAGSGALGLEALSRGAASVVFVEKDrKAAAVIRKNLEKLGLEDRARVIRGDALRFlkRLAGEPFDLV---- 115

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1032282675 183 mgyFL-------LFENMLDSVlyARDKWLVEGGVV 210
Cdd:COG0742   116 ---FLdppyakgLLEKALELL--AENGLLAPGGLI 145
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 105-168 5.36e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.06  E-value: 5.36e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032282675 105 LIKDKIVLDVGAGTGILSLFCAKAGaAHVYAVECS-QMADMAKEIVKANGFSDVITVLKGKIEEI 168
Cdd:PRK07580   61 DLTGLRILDAGCGVGSLSIPLARRG-AKVVASDISpQMVEEARERAPEAGLAGNITFEVGDLESL 124
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
111-211 1.07e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.96  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 111 VLDVGAGTGILS-LFCAKAGAAHVYAVE-CSQMADMAKEivKANGfsdvITVLKGKIEEIELPtPKVDVIISEWMGYFL- 187
Cdd:COG4106     5 VLDLGCGTGRLTaLLAERFPGARVTGVDlSPEMLARARA--RLPN----VRFVVADLRDLDPP-EPFDLVVSNAALHWLp 77

                          90       100
                  ....*....|....*....|....*...
gi 1032282675 188 ----LFENMLDsvlyardkWLVEGGVVL 211
Cdd:COG4106    78 dhaaLLARLAA--------ALAPGGVLA 97
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
105-180 1.59e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 42.97  E-value: 1.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032282675 105 LIKDKIVLDVGAGTGILSLFCAKAgAAHVYAVEC-SQMADMAKEIVKANGFsdvITVLKGkiEEIELPTPKVDVIIS 180
Cdd:PRK14896   27 DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDEIAAGN---VEIIEG--DALKVDLPEFNKVVS 97
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 107-180 2.72e-04

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.46  E-value: 2.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032282675 107 KDKIVLDVGAGTGILSLFCAKA-GAAHVYAVECSQMA-DMAKEIVKANGFSDViTVLKGKIEEiELPTPKVDVIIS 180
Cdd:PRK09328  108 EPLRVLDLGTGSGAIALALAKErPDAEVTAVDISPEAlAVARRNAKHGLGARV-EFLQGDWFE-PLPGGRFDLIVS 181
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 110-160 3.31e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 40.37  E-value: 3.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032282675 110 IVLDVGAGTGILSLFCAKAGA-AHVYAVECS-QMADMAKEIVKANGFSDVITV 160
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpDAYEILEENVKLNNLPNVVLL 53
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
70-180 8.85e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.98  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675  70 DYYFDSYshfgihEEMLKDVVRTKTYQNV---IYQNKFLIKDKIVLDVGAGTGILSLFCAKAGaAHVYAVECSQ-MADMA 145
Cdd:COG4976    12 DQYADSY------DAALVEDLGYEAPALLaeeLLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEeMLAKA 84

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1032282675 146 KEivKANGfsdvITVLKGKIEEIELPTPKVDVIIS 180
Cdd:COG4976    85 RE--KGVY----DRLLVADLADLAEPDGRFDLIVA 113
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 111-160 1.02e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 40.07  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1032282675 111 VLDVGAGTG----ILSLFcakagAAHVYAVECSQ-MADMAKEIVKANGFSDVITV 160
Cdd:COG2518    70 VLEIGTGSGyqaaVLARL-----AGRVYSVERDPeLAERARERLAALGYDNVTVR 119
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 107-211 1.22e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 40.32  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 107 KDKIVLDVGAGTGILSLFCAKA--GAAHVYAVECS-QMADMAKEIVKANGFSDVITV--LKGKIEEiELPTPKVDVIIse 181
Cdd:COG5459    80 APLTVLDVGAGPGTAAWAAADAwpSLLDATLLERSaAALALGRRLARAAANPALETAewRLADLAA-ALPAPPADLVV-- 156

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1032282675 182 wMGYFL--LFENMLDSVlyARDKWLVEGGVVL 211
Cdd:COG5459   157 -ASYVLneLADAARAAL--VDRLWLAPDGALL 185
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 106-136 1.39e-03

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 40.04  E-value: 1.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1032282675 106 IKDKIVLDVGAGTGilsLF--CA-KAGAAHVYAV 136
Cdd:COG1189    76 VAGKVCLDIGASTG---GFtdCLlQRGAAKVYAV 106
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 105-179 1.58e-03

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: 40.15  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 105 LIKDKIVLDVGAGTGILSLFCAKAG-AAHVYAVECSqmaDMAKEIVKAN----GFSDViTVLKGKIEEI--ELPTPkvDV 177
Cdd:COG2242   245 LRPGDVLWDIGAGSGSVSIEAARLApGGRVYAIERD---PERAALIRANarrfGVPNV-EVVEGEAPEAlaDLPDP--DA 318


                  ..
gi 1032282675 178 II 179
Cdd:COG2242   319 VF 320
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 103-136 1.89e-03

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 38.72  E-value: 1.89e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1032282675 103 KFLIKDKIVLDVGAGTGILSLFCAKAGAAHVYAV 136
Cdd:pfam01728  17 GLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGV 50
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 107-180 2.14e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.17  E-value: 2.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032282675 107 KDKIVLDVGAGTGILSLFCAK--AGAAHVYAVECSQ-MADMAKEIVKANGFSDViTVLKGKIEEIE--LPTPKVDVIIS 180
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEeAIEKARENAQKLGFDNV-EFEQGDIEELPelLEDDKFDVVIS 80
PRK14967 PRK14967
putative methyltransferase; Provisional
 111-142 5.24e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.11  E-value: 5.24e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVECSQMA 142
Cdd:PRK14967   40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRA 71
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 111-171 5.80e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.83  E-value: 5.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1032282675 111 VLDVGAGTGILSLFCAKAG--AAHVYAVECSQ-MADMAKEIVKANGFSDVITVLKGKIEEIELP 171
Cdd:PRK00216   55 VLDLACGTGDLAIALAKAVgkTGEVVGLDFSEgMLAVGREKLRDLGLSGNVEFVQGDAEALPFP 118
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 111-260 5.85e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.03  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032282675 111 VLDVGAGTGILSLFCAKAGAAHVYAVE-CSQMADMAKEIVKANgfsDVITVLKGKIEEIELPTPKVDVIISEWMGYFLLF 189
Cdd:PTZ00098   56 VLDIGSGLGGGCKYINEKYGAHVHGVDiCEKMVNIAKLRNSDK---NKIEFEANDILKKDFPENTFDMIYSRDAILHLSY 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032282675 190 EN--MLDSVLYardKWLVEGGVVLpdkaslhltaIEDseYKEDKIEFWNSvyGFDMSCIKKKAMMEPLVDTVD 260
Cdd:PTZ00098  133 ADkkKLFEKCY---KWLKPNGILL----------ITD--YCADKIENWDE--EFKAYIKKRKYTLIPIQEYGD 188
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 111-180 7.91e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 37.72  E-value: 7.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032282675 111 VLDVGAGTGILSLFCAKAGA-AHVYAVECSQMA-DMAKEIVKANGFSDVITVLKGKIEEiELPTPKVDVIIS 180
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEFPnAEVIAVDISPDAlAVAEENAEKNQLEHRVEFIQSNLFE-PLAGQKIDIIVS 188
 
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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