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Conserved domains on  [gi|665404152|ref|NP_001285572|]
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uncharacterized protein Dmel_CG9643, isoform B [Drosophila melanogaster]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-130 1.42e-17

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: 75.44  E-value: 1.42e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404152  54 EKIDKEASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAQNIAEDnkLSITYKVADLTQPQNELGQFDVV 130
Cdd:COG2227   19 ARLLPAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLEDGSFDLV 91
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-130 1.42e-17

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: 75.44  E-value: 1.42e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404152  54 EKIDKEASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAQNIAEDnkLSITYKVADLTQPQNELGQFDVV 130
Cdd:COG2227   19 ARLLPAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLEDGSFDLV 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-131 3.03e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 73.75  E-value: 3.03e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404152   63 VLDLGCGNGMFLVGLANEgFTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNELGQFDVVH 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVV 68
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-130 3.25e-09

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: 52.82  E-value: 3.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665404152  62 RVLDLGCGNGMFLVGLANEGFtGDLTGVDYSPKAVELA-QNIAEDNKLSITYKVADLTQPQ-NELGQFDVV 130
Cdd:cd02440    1 RVLDLGCGTGALALALASGPG-ARVTGVDISPVALELArKAAAALLADNVEVLKGDAEELPpEADESFDVI 70
PRK08317 PRK08317
hypothetical protein; Provisional
 58-130 8.43e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.79  E-value: 8.43e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404152  58 KEASRVLDLGCGNGMFLVGLANE-GFTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNELGQFDVV 130
Cdd:PRK08317  18 QPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAV 91
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 62-109 9.40e-05

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: 42.34  E-value: 9.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 665404152   62 RVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQNIAEDNKLS 109
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLE 164
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 54-130 1.42e-17

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: 75.44  E-value: 1.42e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404152  54 EKIDKEASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAQNIAEDnkLSITYKVADLTQPQNELGQFDVV 130
Cdd:COG2227   19 ARLLPAGGRVLDVGCGTGRLALALARRGA--DVTGVDISPEALEIARERAAE--LNVDFVQGDLEDLPLEDGSFDLV 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 63-131 3.03e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 73.75  E-value: 3.03e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404152   63 VLDLGCGNGMFLVGLANEgFTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNELGQFDVVH 131
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVV 68
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-195 7.66e-17

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 74.38  E-value: 7.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152   57 DKEASRVLDLGCGNGMFLVGLANE-GFTGDLTGVDYSPKAVELAQNIAEDNKLS-ITYKVADLT--QPQNELGQFDVVHD 132
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEelPELLEDDKFDVVIS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665404152  133 KGTYDAVSLCPDnakekralYLDTVEKLLRTaDSLFVITSCNWtEDELVDSFAEKFVKYYTIP 195
Cdd:pfam13847  81 NCVLNHIPDPDK--------VLQEILRVLKP-GGRLIISDPDS-LAELPAHVKEDSTYYAGCV 133
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 58-170 2.25e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 74.18  E-value: 2.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  58 KEASRVLDLGCGNGMFLVGLANEgFTGDLTGVDYSPKAVELAQNIAEDNKLS-ITYKVADLTQP-QNELGQFDVVHDKGT 135
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELdPLPAESFDLVVAFGV 103

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 665404152 136 YDAVSLcpdnakEKRALYLDTVEKLLRTADSLFVI 170
Cdd:COG0500  104 LHHLPP------EEREALLRELARALKPGGVLLLS 132
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 38-130 2.16e-14

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: 67.71  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  38 FDESAQ-WRTIDWLLNEEKIdKEASRVLDLGCGNGMFLVGLANEGftGDLTGVDYSPKAVELAQNIAEDNKLSITYKVAD 116
Cdd:COG2226    1 FDRVAArYDGREALLAALGL-RPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGLNVEFVVGD 77

                         90
                 ....*....|....
gi 665404152 117 LTQPQNELGQFDVV 130
Cdd:COG2226   78 AEDLPFPDGSFDLV 91
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-172 1.08e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.11  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  40 ESAQWRTIDWLLneEKID-KEASRVLDLGCGNGMFLVGLANEgFTGDLTGVDYSPKAVELAQNIAEDNKLS--ITYKVAD 116
Cdd:COG2230   33 EEAQEAKLDLIL--RKLGlKPGMRVLDIGCGWGGLALYLARR-YGVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLAD 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665404152 117 LTQPQNElGQFDVVHDKGTYDAVSlcpdnaKEKRALYLDTVEKLLRtADSLFVITS 172
Cdd:COG2230  110 YRDLPAD-GQFDAIVSIGMFEHVG------PENYPAYFAKVARLLK-PGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
59-130 7.15e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 64.25  E-value: 7.15e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665404152  59 EASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVElaqnIAEDNKLSITYKVADLTQPQNELGQFDVV 130
Cdd:COG4976   46 PFGRVLDLGCGTGLLGEALRPRGY--RLTGVDLSEEMLA----KAREKGVYDRLLVADLADLAEPDGRFDLI 111
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
59-131 8.83e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 59.45  E-value: 8.83e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665404152  59 EASRVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQNIAEDnklsITYKVADLTQPQNElGQFDVVH 131
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLDPP-EPFDLVV 68
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
57-130 1.32e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 61.07  E-value: 1.32e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404152  57 DKEASRVLDLGCGNGMFLVGLANEGfTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPqNELGQFDVV 130
Cdd:COG2263   43 DIEGKTVLDLGCGTGMLAIGAALLG-AKKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRI-PLGGSVDTV 114
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 34-130 1.06e-10

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: 59.13  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  34 GEIWfdESAQwRTIDWLLNEEKIDKEasRVLDLGCGNGmfLVGL-ANEGFTGDLTGVDYSPKAVE-LAQNiAEDNKLSIT 111
Cdd:COG3897   50 AFLW--PSGQ-ALARYLLDHPEVAGK--RVLELGCGLG--LVGIaAAKAGAADVTATDYDPEALAaLRLN-AALNGVAIT 121

                         90
                 ....*....|....*....
gi 665404152 112 YKVADLTQPQnELGQFDVV 130
Cdd:COG3897  122 TRLGDWRDPP-AAGGFDLI 139
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 47-130 2.09e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 55.93  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  47 IDWLLNEEKiDKEASRVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQ-NiAEDNKLS--ITYKVADLTQPQNE 123
Cdd:COG2890  101 VELALALLP-AGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARrN-AERLGLEdrVRFLQGDLFEPLPG 178


                 ....*..
gi 665404152 124 LGQFDVV 130
Cdd:COG2890  179 DGRFDLI 185
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-130 3.25e-09

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: 52.82  E-value: 3.25e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665404152  62 RVLDLGCGNGMFLVGLANEGFtGDLTGVDYSPKAVELA-QNIAEDNKLSITYKVADLTQPQ-NELGQFDVV 130
Cdd:cd02440    1 RVLDLGCGTGALALALASGPG-ARVTGVDISPVALELArKAAAALLADNVEVLKGDAEELPpEADESFDVI 70
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 58-167 3.67e-09

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: 54.77  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  58 KEASRVLDLGCGNGmfLVGL--ANEGFTGDLTGVDYSPKAVELAQ-NIAEdNKLS--ITYKVADLTQPQNEL--GQFDVV 130
Cdd:COG4123   36 KKGGRVLDLGTGTG--VIALmlAQRSPGARITGVEIQPEAAELARrNVAL-NGLEdrITVIHGDLKEFAAELppGSFDLV 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 665404152 131 ------HDKGTydavSLCPDNAKEKRALYLD--TVEKLLRTADSL 167
Cdd:COG4123  113 vsnppyFKAGS----GRKSPDEARAIARHEDalTLEDLIRAAARL 153
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-130 4.95e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 51.90  E-value: 4.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665404152   64 LDLGCGNGMFLVGLANEGFTgdLTGVDYSPKAVELAQNIAEDNKLsiTYKVADLTQPQNELGQFDVV 130
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELAREKAPREGL--TFVVGDAEDLPFPDNSFDLV 63
PRK08317 PRK08317
hypothetical protein; Provisional
 58-130 8.43e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.79  E-value: 8.43e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665404152  58 KEASRVLDLGCGNGMFLVGLANE-GFTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNELGQFDVV 130
Cdd:PRK08317  18 QPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAV 91
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 64-131 1.25e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.83  E-value: 1.25e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665404152   64 LDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQNIAEDNKLS----ITYKVADLTQPqnELGQFDVVH 131
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLnavrVELFQLDLGEL--DPGSFDVVV 70
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 47-130 1.43e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 53.63  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  47 IDWLLNEEKiDKEASRVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQ-NIAEDNKLSITYKVADLTQPqNELG 125
Cdd:PRK09328  97 VEWALEALL-LKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARrNAKHGLGARVEFLQGDWFEP-LPGG 174


                 ....*
gi 665404152 126 QFDVV 130
Cdd:PRK09328 175 RFDLI 179
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 45-130 2.83e-08

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 52.15  E-value: 2.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  45 RTID----WLlnEEKIDKEASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAQNIAEDNKLS--ITYKVADLT 118
Cdd:PRK07580  47 RMRDtvlsWL--PADGDLTGLRILDAGCGVGSLSIPLARRGA--KVVASDISPQMVEEARERAPEAGLAgnITFEVGDLE 122

                         90
                 ....*....|..
gi 665404152 119 QpqnELGQFDVV 130
Cdd:PRK07580 123 S---LLGRFDTV 131
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 57-130 5.44e-08

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: 50.96  E-value: 5.44e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404152  57 DKEASRVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQNIAEDNKLS-ITYKVADLTQPQNElGQFDVV 130
Cdd:COG2813   47 EPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEnVEVLWSDGLSGVPD-GSFDLI 120
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-131 5.85e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 50.50  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152   47 IDWLLNEEKIDKEASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAqniaednKLSITYKVADLTQPQNELGQ 126
Cdd:pfam13489  10 ADLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGF--SVTGVDPSPIAIERA-------LLNVRFDQFDEQEAAVPAGK 80


                  ....*
gi 665404152  127 FDVVH 131
Cdd:pfam13489  81 FDVIV 85
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 59-128 1.15e-07

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 51.10  E-value: 1.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  59 EASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNElGQFD 128
Cdd:PRK12335 120 KPGKALDLGCGQGRNSLYLALLGF--DVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQ-EEYD 186
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 62-130 3.67e-07

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: 48.36  E-value: 3.67e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152   62 RVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQNIAEDNKL-SITYKVADLTQPQnELGQFDVV 130
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLeNGEVVASDVYSGV-EDGKFDLI 102
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 62-171 6.26e-07

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 48.19  E-value: 6.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152   62 RVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAqniAEDNKLS----------------ITYKVADL-TQPQNEL 124
Cdd:pfam05724  40 RVLVPLCGKALDMVWLAEQGH--FVVGVEISELAVEKF---FAEAGLSppitelsgfkeyssgnISLYCGDFfTLPREEL 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 665404152  125 GQFDVVhdkgtYDAVSLCPDNAkEKRALYLDTVEKLLRTADSLFVIT 171
Cdd:pfam05724 115 GKFDLI-----YDRAALCALPP-EMRPRYAKQMYELLPPGGRGLLIT 155
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 57-130 7.72e-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: 48.63  E-value: 7.72e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665404152  57 DKEASRVLDLGCGNGMFLVGLANEGftGDLTGVDYSPKAVELAQNIAEDNKLS-ITYKVADLTQPQNEL---GQFDVV 130
Cdd:COG2265  231 LTGGERVLDLYCGVGTFALPLARRA--KKVIGVEIVPEAVEDARENARLNGLKnVEFVAGDLEEVLPELlwgGRPDVV 306
PLN02244 PLN02244
tocopherol O-methyltransferase
 42-130 7.54e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 45.89  E-value: 7.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  42 AQWRTIDWLLN----EEKIDKEASRVLDLGCGNGMFLVGLANEgFTGDLTGVDYSPKAVELAQNIAEDNKLS--ITYKVA 115
Cdd:PLN02244  97 AQIRMIEESLAwagvPDDDEKRPKRIVDVGCGIGGSSRYLARK-YGANVKGITLSPVQAARANALAAAQGLSdkVSFQVA 175

                         90
                 ....*....|....*.
gi 665404152 116 D-LTQPqNELGQFDVV 130
Cdd:PLN02244 176 DaLNQP-FEDGQFDLV 190
PRK06202 PRK06202
hypothetical protein; Provisional
 62-154 8.94e-06

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 44.99  E-value: 8.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  62 RVLDLGCGNGMFLVGLA----NEGFTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNElgQFDVV------H 131
Cdd:PRK06202  63 TLLDIGCGGGDLAIDLArwarRDGLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAEGE--RFDVVtsnhflH 140

                         90       100
                 ....*....|....*....|...
gi 665404152 132 DKGTYDAVSLCPDNAKEKRALYL 154
Cdd:PRK06202 141 HLDDAEVVRLLADSAALARRLVL 163
PRK14968 PRK14968
putative methyltransferase; Provisional
 50-130 1.30e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.12  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  50 LLNEEKIDKEASRVLDLGCGNGMFLVGLANEGftGDLTGVDYSPKAVELAQNIAEDNKLS---ITYKVADLTQPQNElGQ 126
Cdd:PRK14968  14 LLAENAVDKKGDRVLEVGTGSGIVAIVAAKNG--KKVVGVDINPYAVECAKCNAKLNNIRnngVEVIRSDLFEPFRG-DK 90


                 ....
gi 665404152 127 FDVV 130
Cdd:PRK14968  91 FDVI 94
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
54-130 9.06e-05

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 42.63  E-value: 9.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665404152  54 EKIDKEAS-RVLDLGCGNGMFLVGLANEGFTG-DLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNeLGQFDVV 130
Cdd:COG0827  109 EKFTKKEGlRILDPAVGTGNLLTTVLNQLKKKvNAYGVEVDDLLIRLAAVLANLQGHPVELFHQDALQPLL-IDPVDVV 186
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 62-109 9.40e-05

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: 42.34  E-value: 9.40e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 665404152   62 RVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQNIAEDNKLS 109
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLE 164
PRK14967 PRK14967
putative methyltransferase; Provisional
 61-130 1.02e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 41.96  E-value: 1.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  61 SRVLDLGCGNGMFLVGLANEGfTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNElGQFDVV 130
Cdd:PRK14967  38 RRVLDLCTGSGALAVAAAAAG-AGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEF-RPFDVV 105
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 58-130 1.05e-04

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


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 41.47  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404152  58 KEASRVLDLGCGNGMFLV--GLANegftGDLTGVDYSPKAVELAQ-NIAEDNKLSITYKVADLTQPQNELGQFDVV 130
Cdd:COG1041   25 KEGDTVLDPFCGTGTILIeaGLLG----RRVIGSDIDPKMVEGAReNLEHYGYEDADVIRGDARDLPLADESVDAI 96
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
59-130 1.81e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 40.87  E-value: 1.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404152  59 EASRVLDLGCGNGMFLVGLANEGFtgDLTGVDYSPKAVELAQNIAEDNKLS-ITYKVADLtqpqNEL---GQFDVV 130
Cdd:PRK11207  30 KPGKTLDLGCGNGRNSLYLAANGF--DVTAWDKNPMSIANLERIKAAENLDnLHTAVVDL----NNLtfdGEYDFI 99
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 60-162 4.08e-04

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: 39.78  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  60 ASRVLDLGCGNG----MFLVGLANEGftgDLTGVDYSPKAVELAQNIAEDNKLS--ITYKVADLTQ--PQNELGQFDVV- 130
Cdd:COG4122   17 AKRILEIGTGTGystlWLARALPDDG---RLTTIEIDPERAAIARENFARAGLAdrIRLILGDALEvlPRLADGPFDLVf 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 665404152 131 --HDKGTYDAvslcpdnakekralYLDTVEKLLR 162
Cdd:COG4122   94 idADKSNYPD--------------YLELALPLLR 113
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 53-130 1.11e-03

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: 38.81  E-value: 1.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665404152   53 EEKIDKEASRVLDLGCGNGMFLVGLANEGFTGDLTGVDYSPKAVELAQniaEDNKLSITYKVADLTQPQNELGQFDVV 130
Cdd:TIGR02072  28 KEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAK---TKLSENVQFICGDAEKLPLEDSSFDLI 102
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
49-130 1.39e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 38.62  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  49 WLlneEKIDKEASRVLDLGCGngmflvglanegfTG------------DLTGVDYSPKAVELAQNIAEDNKLS--ITYKV 114
Cdd:COG2264  141 AL---EKLLKPGKTVLDVGCG-------------SGilaiaaaklgakRVLAVDIDPVAVEAARENAELNGVEdrIEVVL 204

                         90
                 ....*....|....*.
gi 665404152 115 ADLTQPqnelGQFDVV 130
Cdd:COG2264  205 GDLLED----GPYDLV 216
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 44-130 1.86e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.21  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  44 WR--TIDWLLNeekidKEASRVLDLGCGNGMFLVGLANE-GFTGDLTGVDYSPKAVELAQNIAEDNKLS--ITYKVADLT 118
Cdd:PRK00216  39 WRrkTIKWLGV-----RPGDKVLDLACGTGDLAIALAKAvGKTGEVVGLDFSEGMLAVGREKLRDLGLSgnVEFVQGDAE 113

                         90
                 ....*....|....*
gi 665404152 119 Q---PQNelgQFDVV 130
Cdd:PRK00216 114 AlpfPDN---SFDAV 125
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 47-130 2.10e-03

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: 38.40  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152   47 IDWLlneEKIDKEASRVLDLGCGNGMFLVGLANEGfTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVadlTQPQNEL-G 125
Cdd:pfam06325 152 LEAL---ERLVKPGESVLDVGCGSGILAIAALKLG-AKKVVGVDIDPVAVRAAKENAELNGVEARLEV---YLPGDLPkE 224


                  ....*
gi 665404152  126 QFDVV 130
Cdd:pfam06325 225 KADVV 229
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
58-131 4.68e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 36.96  E-value: 4.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665404152   58 KEASRVLDLGCGNGMFLVGLANE-GFTGDLTGVDYSPKAVELAQ-NIAEDNKLSITYKVADLTQPQNELGQFDVVH 131
Cdd:pfam01135  72 KPGMRVLEIGSGSGYLTACFARMvGEVGRVVSIEHIPELVEIARrNLEKLGLENVIVVVGDGRQGWPEFAPYDAIH 147
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 54-135 5.47e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 37.42  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  54 EKID-KEASRVLDLGCGNGMFLVGLAnEGFTGDLTGVDYSPKAVELAQNIAEDNKLSITYKVADLTQPQNELGQFDVVHD 132
Cdd:PLN02336 260 DKLDlKPGQKVLDVGCGIGGGDFYMA-ENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYS 338


                 ...
gi 665404152 133 KGT 135
Cdd:PLN02336 339 RDT 341
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
47-130 5.97e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 36.67  E-value: 5.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  47 IDWLlneEKIDKEASRVLDLGCGNGMFLVGLANEGfTGDLTGVDYSPKAVELAQNIAEDNKLSItykvaDLTQPQNELgQ 126
Cdd:PRK00517 110 LEAL---EKLVLPGKTVLDVGCGSGILAIAAAKLG-AKKVLAVDIDPQAVEAARENAELNGVEL-----NVYLPQGDL-K 179


                 ....
gi 665404152 127 FDVV 130
Cdd:PRK00517 180 ADVI 183
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 51-170 6.16e-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: 36.86  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404152  51 LNEEKIDKEASRVLDLGCGNG-------MFLVGLAnegftgDLTGVDYSPKAVELAQNIAEDnklsitYKVADLTQPQNE 123
Cdd:COG5459   72 LAEAGPDFAPLTVLDVGAGPGtaawaaaDAWPSLL------DATLLERSAAALALGRRLARA------AANPALETAEWR 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 665404152 124 LGQFDVVHDKGTYDAVSLC------PDNAKEkralylDTVEKLLRTADSLFVI 170
Cdd:COG5459  140 LADLAAALPAPPADLVVASyvlnelADAARA------ALVDRLWLAPDGALLI 186
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 59-80 8.95e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 35.81  E-value: 8.95e-03
                          10        20
                  ....*....|....*....|..
gi 665404152   59 EASRVLDLGCGNGMFLVGLANE 80
Cdd:TIGR02081  13 PGSRVLDLGCGDGELLALLRDE 34
 
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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