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Conserved domains on  [gi|908435238|ref|XP_013077269|]
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histone-arginine methyltransferase METTL23-like isoform X2 [Biomphalaria glabrata]

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; ...
 26-181 1.11e-21

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 pfam10294:

Pssm-ID: 473071  Cd Length: 172  Bit Score: 88.16  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   26 KKDEHqvTIKILELPGADYGTYIWPCAPILAQYVWQ------NKDLVRTQSILEIGAGTGLPGIVAAK--CGANVILSDs 97
Cdd:pfam10294   1 KLDNP--GLRIEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITD- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   98 ntKPLSLDLCRKSAELNGLKN-VTVCGITWGE-VTPTLTQLPPIDLILASDCFYHSKDFEDVIMTmsfiLHRC--PNANV 173
Cdd:pfam10294  78 --LEEALELLKKNIELNALSSkVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKT----LKDLlgKESVI 151


                  ....*...
gi 908435238  174 WCAYQERS 181
Cdd:pfam10294 152 LVAYKKRR 159
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 26-181 1.11e-21

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 88.16  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   26 KKDEHqvTIKILELPGADYGTYIWPCAPILAQYVWQ------NKDLVRTQSILEIGAGTGLPGIVAAK--CGANVILSDs 97
Cdd:pfam10294   1 KLDNP--GLRIEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITD- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   98 ntKPLSLDLCRKSAELNGLKN-VTVCGITWGE-VTPTLTQLPPIDLILASDCFYHSKDFEDVIMTmsfiLHRC--PNANV 173
Cdd:pfam10294  78 --LEEALELLKKNIELNALSSkVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKT----LKDLlgKESVI 151


                  ....*...
gi 908435238  174 WCAYQERS 181
Cdd:pfam10294 152 LVAYKKRR 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 69-121 4.59e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.36  E-value: 4.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 908435238  69 QSILEIGAGTGLPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGLKNVTV 121
Cdd:PRK14968  25 DRVLEVGTGSGIVAIVAAKNGKKVVGVDIN--PYAVECAKCNAKLNNIRNNGV 75
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 71-143 1.42e-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: 47.11  E-value: 1.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 908435238  71 ILEIGAGTGLPGIVAAKC--GANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCgitWGEVtptLTQLPP--IDLIL 143
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRnpEARVTLVDVN--ARAVELARANAAANGLENVEVL---WSDG---LSGVPDgsFDLIL 121
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-154 2.11e-04

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: 39.34  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  71 ILEIGAGTGLPGIVAAK-CGANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCGITWGEvtPTLTQLPPIDLILASDCFY 149
Cdd:cd02440    2 VLDLGCGTGALALALASgPGARVTGVDIS--PVALELARKAAAALLADNVEVLKGDAEE--LPPEADESFDVIISDPPLH 77


                 ....*
gi 908435238 150 HSKDF 154
Cdd:cd02440   78 HLVED 82
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 62-121 5.05e-04

HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 39.84  E-value: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   62 NKDLVRTQSILEIGAGTGLPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGlKNVTV 121
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDIN--PFAVKELRENAKLNN-VGLDV 70
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 26-181 1.11e-21

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 88.16  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   26 KKDEHqvTIKILELPGADYGTYIWPCAPILAQYVWQ------NKDLVRTQSILEIGAGTGLPGIVAAK--CGANVILSDs 97
Cdd:pfam10294   1 KLDNP--GLRIEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALllPGASVTITD- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   98 ntKPLSLDLCRKSAELNGLKN-VTVCGITWGE-VTPTLTQLPPIDLILASDCFYHSKDFEDVIMTmsfiLHRC--PNANV 173
Cdd:pfam10294  78 --LEEALELLKKNIELNALSSkVVVKVLDWGEnLPPDLFDGHPVDLILAADCVYNEDSFPLLEKT----LKDLlgKESVI 151


                  ....*...
gi 908435238  174 WCAYQERS 181
Cdd:pfam10294 152 LVAYKKRR 159
PRK14968 PRK14968
putative methyltransferase; Provisional
 69-121 4.59e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 48.36  E-value: 4.59e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 908435238  69 QSILEIGAGTGLPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGLKNVTV 121
Cdd:PRK14968  25 DRVLEVGTGSGIVAIVAAKNGKKVVGVDIN--PYAVECAKCNAKLNNIRNNGV 75
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 71-143 1.42e-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: 47.11  E-value: 1.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 908435238  71 ILEIGAGTGLPGIVAAKC--GANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCgitWGEVtptLTQLPP--IDLIL 143
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRnpEARVTLVDVN--ARAVELARANAAANGLENVEVL---WSDG---LSGVPDgsFDLIL 121
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 64-158 5.19e-06

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: 44.98  E-value: 5.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  64 DLVRTQSILEIGAGTGLPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCGitwgevtpTLTQLP----PI 139
Cdd:COG2226   19 GLRPGARVLDLGCGTGRLALALAERGARVTGVDIS--PEMLELARERAAEAGLNVEFVVG--------DAEDLPfpdgSF 88

                         90
                 ....*....|....*....
gi 908435238 140 DLILASDCFYHSKDFEDVI 158
Cdd:COG2226   89 DLVISSFVLHHLPDPERAL 107
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 51-150 7.44e-06

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.29  E-value: 7.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  51 CAPILAQYVWQNKDLVRTQSILEIGAGTG-LPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGLKNVT--VCGIT-W 126
Cdd:COG0500   10 LLPGLAALLALLERLPKGGRVLDLGCGTGrNLLALAARFGGRVIGIDLS--PEAIALARARAAKAGLGNVEflVADLAeL 87

                         90       100
                 ....*....|....*....|....
gi 908435238 127 GEVTptltqLPPIDLILASDCFYH 150
Cdd:COG0500   88 DPLP-----AESFDLVVAFGVLHH 106
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 71-150 7.94e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 43.32  E-value: 7.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   71 ILEIGAGTGLPGIVAAK-CGANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCGitwgevtpTLTQLP----PIDLILAS 145
Cdd:pfam13649   1 VLDLGCGTGRLTLALARrGGARVTGVDLS--PEMLERARERAAEAGLNVEFVQG--------DAEDLPfpdgSFDLVVSS 70


                  ....*
gi 908435238  146 DCFYH 150
Cdd:pfam13649  71 GVLHH 75
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
55-144 1.49e-04

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 41.70  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  55 LAQYVWQNKdlvrtqSILEIGAGTGLPGIVAAKCGA-NVILSDsnTKPLSLDLCRKSAELNGLKN-VTVcgitwgeVTPT 132
Cdd:COG2264  142 LEKLLKPGK------TVLDVGCGSGILAIAAAKLGAkRVLAVD--IDPVAVEAARENAELNGVEDrIEV-------VLGD 206

                         90
                 ....*....|..
gi 908435238 133 LTQLPPIDLILA 144
Cdd:COG2264  207 LLEDGPYDLVVA 218
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 55-158 1.57e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 40.39  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  55 LAQYVwqNKDLVRTQSILEIGAGTGLPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGLKnvTVCGitwgevtpTLT 134
Cdd:COG2227   14 LAALL--ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDIS--PEALEIARERAAELNVD--FVQG--------DLE 79

                         90       100
                 ....*....|....*....|....*...
gi 908435238 135 QLP----PIDLILASDCFYHSKDFEDVI 158
Cdd:COG2227   80 DLPledgSFDLVICSEVLEHLPDPAALL 107
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 71-154 2.11e-04

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: 39.34  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  71 ILEIGAGTGLPGIVAAK-CGANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCGITWGEvtPTLTQLPPIDLILASDCFY 149
Cdd:cd02440    2 VLDLGCGTGALALALASgPGARVTGVDIS--PVALELARKAAAALLADNVEVLKGDAEE--LPPEADESFDVIISDPPLH 77


                 ....*
gi 908435238 150 HSKDF 154
Cdd:cd02440   78 HLVED 82
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-165 3.51e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.50  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   72 LEIGAGTG--LPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGLKNVTVCgiTWGEVTPTLTQLPPIDLILASDCFY 149
Cdd:pfam08242   1 LEIGCGTGtlLRALLEALPGLEYTGLDIS--PAALEAARERLAALGLLNAVRV--ELFQLDLGELDPGSFDVVVASNVLH 76

                          90
                  ....*....|....*.
gi 908435238  150 HSKDFEDVIMTMSFIL 165
Cdd:pfam08242  77 HLADPRAVLRNIRRLL 92
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 62-121 5.05e-04

HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 39.84  E-value: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   62 NKDLVRTQSILEIGAGTGLPGIVAAKCGANVILSDSNtkPLSLDLCRKSAELNGlKNVTV 121
Cdd:TIGR00537  14 NLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDIN--PFAVKELRENAKLNN-VGLDV 70
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 72-158 7.36e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.64  E-value: 7.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238   72 LEIGAGTGLPGIVAAKCGANVILSDSNTKplSLDLCRKSAELNGLKnvTVCGitwgevtpTLTQLP----PIDLILASDC 147
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPE--MLELAREKAPREGLT--FVVG--------DAEDLPfpdnSFDLVLSSEV 68

                          90
                  ....*....|.
gi 908435238  148 FYHSKDFEDVI 158
Cdd:pfam08241  69 LHHVEDPERAL 79
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 69-121 1.62e-03

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 38.21  E-value: 1.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 908435238  69 QSILEIGAGTGLPGIVAAKC--GANVILSDSNTKplsldlcrKSAELN------GLKNVTV 121
Cdd:COG0357   69 ARVLDVGSGAGFPGIPLAIArpDLQVTLVDSLGK--------KIAFLRevvrelGLKNVTV 121
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 54-121 6.88e-03

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: 36.66  E-value: 6.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 908435238  54 ILAQYVwqnkDLVRTQSILEIGAGTGLPGI-VAAKC-GANVILSDSNtkPLSLDLCRKSAELNGLKN-VTV 121
Cdd:COG4123   28 LLAAFA----PVKKGGRVLDLGTGTGVIALmLAQRSpGARITGVEIQ--PEAAELARRNVALNGLEDrITV 92
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
55-144 9.55e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 36.28  E-value: 9.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 908435238  55 LAQYVWQNKdlvrtqSILEIGAGTGLPGIVAAKCGANVILS-DsnTKPLSLDLCRKSAELNGLK-NVTVcgitwgevtpt 132
Cdd:PRK00517 113 LEKLVLPGK------TVLDVGCGSGILAIAAAKLGAKKVLAvD--IDPQAVEAARENAELNGVElNVYL----------- 173

                         90
                 ....*....|..
gi 908435238 133 LTQLPPIDLILA 144
Cdd:PRK00517 174 PQGDLKADVIVA 185
 
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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