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Conserved domains on  [gi|499897918|ref|WP_011578652|]
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MULTISPECIES: FkbM family methyltransferase [Chelativorans]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 49-182 1.26e-12

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 TIGR01444:

Pssm-ID: 473071  Cd Length: 143  Bit Score: 63.10  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   49 VLELGAGLGVITSIIA-AIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLSNgiLAAGP-PRKISFYQRADFWMSSGFV 126
Cdd:TIGR01444   2 VIDVGANIGDTSLYFArKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLN--AAVGDrDGELEFNVSDDDTGNSSLL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499897918  127 EQGPYERVIEIT--SRNVDAFIGKHGI---NVLVMDVEGAELELLQNAE---LPGIERVFLELH 182
Cdd:TIGR01444  80 PTPDADRESEIEveVVTLDDLVEEFGLdkvDLLKIDVEGAELEVLRGAAetlLEKRPVIVLEVH 143
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 49-182 1.26e-12

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: 63.10  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   49 VLELGAGLGVITSIIA-AIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLSNgiLAAGP-PRKISFYQRADFWMSSGFV 126
Cdd:TIGR01444   2 VIDVGANIGDTSLYFArKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLN--AAVGDrDGELEFNVSDDDTGNSSLL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499897918  127 EQGPYERVIEIT--SRNVDAFIGKHGI---NVLVMDVEGAELELLQNAE---LPGIERVFLELH 182
Cdd:TIGR01444  80 PTPDADRESEIEveVVTLDDLVEEFGLdkvDLLKIDVEGAELEVLRGAAetlLEKRPVIVLEVH 143
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 53-202 9.83e-10

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 55.65  E-value: 9.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   53 GAGLGVITSIIAAIDDV-----RVWSFEADPQTVQ-LAKRVIDLNCNGNVDLSNGILAAGPPRKISFYQRADF-WMSSGF 125
Cdd:pfam05050   3 GANDGVWDSVALLFEKKcggggEVLAIEPNPNKLEkLDCTLLNLALGNDVGLYEFYLGGKGGGGYLLFAVGDPqGASTSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918  126 VEQGPYERVIEITSRNVDAFIGKHG---INVLVMDVEGAELELLQNAELpGIER-----VFLELHDHLY-GLAGVQAITT 196
Cdd:pfam05050  83 VLGGEEAKYIEVETVTLDSFLEEIKksdIDLLKIDVEGAELEVLEGAEK-TLKRcqpniIVIEVHFFHYfGGPLFDEIRQ 161


                  ....*.
gi 499897918  197 AMARRG 202
Cdd:pfam05050 162 FLRECG 167
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
31-101 4.66e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 51.96  E-value: 4.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499897918  31 YEANEA--RRIPRAIRPGDRVLELGAGLGVITSIIAAIDDVRVWSFEADPQTVQLAKRVIDLN-CNGNVDLSNG 101
Cdd:COG4076   19 VERNDAfkAAIERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANgLSDRITVINA 92
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-101 4.42e-05

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 41.26  E-value: 4.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499897918  48 RVLELGAGLGVITSIIAAIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLSNG 101
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKG 54
rADc smart00650
Ribosomal RNA adenine dimethylases;
36-113 6.59e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 6.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918    36 ARRIPRA--IRPGDRVLELGAGLGVITSIIAAIDDvRVWSFEADPQTVQ-LAKRVIDlncNGNVDLSNG-ILAAGPPRKI 111
Cdd:smart00650   2 IDKIVRAanLRPGDTVLEIGPGKGALTEELLERAK-RVTAIEIDPRLAPrLREKFAA---ADNLTVIHGdALKFDLPKLQ 77


                   ..
gi 499897918   112 SF 113
Cdd:smart00650  78 PY 79
PRK14968 PRK14968
putative methyltransferase; Provisional
 43-99 1.28e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 1.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499897918  43 IRPGDRVLELGAGLGvITSIIAAIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLS 99
Cdd:PRK14968  21 DKKGDRVLEVGTGSG-IVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVE 76
 
Name Accession Description Interval E-value
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 49-182 1.26e-12

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: 63.10  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   49 VLELGAGLGVITSIIA-AIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLSNgiLAAGP-PRKISFYQRADFWMSSGFV 126
Cdd:TIGR01444   2 VIDVGANIGDTSLYFArKGAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLLN--AAVGDrDGELEFNVSDDDTGNSSLL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499897918  127 EQGPYERVIEIT--SRNVDAFIGKHGI---NVLVMDVEGAELELLQNAE---LPGIERVFLELH 182
Cdd:TIGR01444  80 PTPDADRESEIEveVVTLDDLVEEFGLdkvDLLKIDVEGAELEVLRGAAetlLEKRPVIVLEVH 143
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 53-202 9.83e-10

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 55.65  E-value: 9.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   53 GAGLGVITSIIAAIDDV-----RVWSFEADPQTVQ-LAKRVIDLNCNGNVDLSNGILAAGPPRKISFYQRADF-WMSSGF 125
Cdd:pfam05050   3 GANDGVWDSVALLFEKKcggggEVLAIEPNPNKLEkLDCTLLNLALGNDVGLYEFYLGGKGGGGYLLFAVGDPqGASTSS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918  126 VEQGPYERVIEITSRNVDAFIGKHG---INVLVMDVEGAELELLQNAELpGIER-----VFLELHDHLY-GLAGVQAITT 196
Cdd:pfam05050  83 VLGGEEAKYIEVETVTLDSFLEEIKksdIDLLKIDVEGAELEVLEGAEK-TLKRcqpniIVIEVHFFHYfGGPLFDEIRQ 161


                  ....*.
gi 499897918  197 AMARRG 202
Cdd:pfam05050 162 FLRECG 167
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
31-101 4.66e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 51.96  E-value: 4.66e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499897918  31 YEANEA--RRIPRAIRPGDRVLELGAGLGVITSIIAAIDDVRVWSFEADPQTVQLAKRVIDLN-CNGNVDLSNG 101
Cdd:COG4076   19 VERNDAfkAAIERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANgLSDRITVINA 92
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 36-111 5.66e-06

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 45.89  E-value: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918  36 ARRIPRA--IRPGDRVLELGAGLGVITSIIAAIDDvRVWSFEADPQTVQ-LAKRVIDLncnGNVDLSNG--------ILA 104
Cdd:COG0030   26 IRRIVDAagITPGDTVLEIGPGLGALTRALLERAA-RVTAVEIDRRLAAiLRETFAAY---PNLTVIEGdalkvdlpALA 101


                 ....*..
gi 499897918 105 AGPPRKI 111
Cdd:COG0030  102 AGEPLKV 108
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 42-135 6.55e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 45.46  E-value: 6.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918  42 AIRPGDRVLELGAGLGVITSIIAAIDDvRVWSFEADPQTVQLAKRVID-LNCNgNVDLSNGILAAGPPrkisfyqradfw 120
Cdd:COG2518   63 DLKPGDRVLEIGTGSGYQAAVLARLAG-RVYSVERDPELAERARERLAaLGYD-NVTVRVGDGALGWP------------ 128

                         90
                 ....*....|....*
gi 499897918 121 mssgfvEQGPYERVI 135
Cdd:COG2518  129 ------EHAPFDRII 137
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-101 4.42e-05

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 41.26  E-value: 4.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499897918  48 RVLELGAGLGVITSIIAAIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLSNG 101
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKG 54
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 33-91 8.98e-05

Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of unknown function, Swiss:O27901. However, homologous proteins have been found in yeast suggesting this protein may be involved in methionine biosynthesis, transport and/or utilization.


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 41.95  E-value: 8.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   33 ANEARRIPRAIRPGDRVLELGAGLGVITSIIAAI-DDVRVWSFEADPQTVQLAKRVIDLN 91
Cdd:pfam02475  87 IAERERIAKLVEPGEVVVDMFAGIGPFSIPIAKHsKARRVYAIELNPESYKYLKENIKLN 146
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 43-91 2.91e-04

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: 40.90  E-value: 2.91e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 499897918  43 IRPGDRVLELGAGLGVITSIIAA-IDDVRVWSFEADPQTVQLAKRVIDLN 91
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQrSPGARITGVEIQPEAAELARRNVALN 84
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 36-101 3.93e-04

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 40.68  E-value: 3.93e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499897918   36 ARRIPRA--IRPGDRVLELGAGLGVITSIIAAIDDvRVWSFEADPQTVQ-LAKRVIDLNcngNVDLSNG 101
Cdd:TIGR00755  18 IRKIVEAanIQEGDRVLEIGPGLGALTEPLLKRAK-KVTAIEIDPRLAErLRKLLSLYN---NLEIIEG 82
rADc smart00650
Ribosomal RNA adenine dimethylases;
36-113 6.59e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 6.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918    36 ARRIPRA--IRPGDRVLELGAGLGVITSIIAAIDDvRVWSFEADPQTVQ-LAKRVIDlncNGNVDLSNG-ILAAGPPRKI 111
Cdd:smart00650   2 IDKIVRAanLRPGDTVLEIGPGKGALTEELLERAK-RVTAIEIDPRLAPrLREKFAA---ADNLTVIHGdALKFDLPKLQ 77


                   ..
gi 499897918   112 SF 113
Cdd:smart00650  78 PY 79
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 43-86 9.63e-04

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: 39.37  E-value: 9.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 499897918  43 IRPGDRVLELGAGLGVITSIIAAI--DDVRVWSFEADPQTVQLAKR 86
Cdd:COG2519   89 IFPGARVLEAGTGSGALTLALARAvgPEGKVYSYERREDFAEIARK 134
PRK14968 PRK14968
putative methyltransferase; Provisional
 43-99 1.28e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 38.34  E-value: 1.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499897918  43 IRPGDRVLELGAGLGvITSIIAAIDDVRVWSFEADPQTVQLAKRVIDLNCNGNVDLS 99
Cdd:PRK14968  21 DKKGDRVLEVGTGSG-IVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVE 76
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
36-78 3.47e-03

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 37.11  E-value: 3.47e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 499897918  36 ARRIPRAIRPGD--RVLELGAGLGVITSIIAA--IDDVRVWSFEADP 78
Cdd:COG3963   34 ARAMASEVDWSGagPVVELGPGTGVFTRAILArgVPDARLLAVEINP 80
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
43-135 6.19e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 36.58  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499897918   43 IRPGDRVLELGAGLGVITSIIAAI--DDVRVWSFEADPQTVQLAKRVIDlncngNVDLSNGILAAGPPRKisfyqradfw 120
Cdd:pfam01135  71 LKPGMRVLEIGSGSGYLTACFARMvgEVGRVVSIEHIPELVEIARRNLE-----KLGLENVIVVVGDGRQ---------- 135

                          90
                  ....*....|....*
gi 499897918  121 mssGFVEQGPYERVI 135
Cdd:pfam01135 136 ---GWPEFAPYDAIH 147
 
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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