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Conserved domains on  [gi|2630092231|ref|WP_321101359|]
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methyltransferase [Bergeyella zoohelcum]

Protein Classification

tRNA1(Val) (adenine(37)-N6)-methyltransferase( domain architecture ID 11467886)

tRNA(1)(Val) (adenine(37)-N(6))-methyltransferase is a class I SAM-dependent methyltransferase that specifically methylates the adenine in position 37 of tRNA(1)(Val)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
3-229 9.46e-66

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: 203.45  E-value: 9.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231   3 KRKPFYFQKFKIEQTHDVFAVGTDGVLLGALCGCENANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNF 82
Cdd:COG4123     2 RLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  83 KHSPFAERLTATQADINTLTLHEKTT---CIVCNPPFFET-----NESEKHILARQQITLTYAQLIHFAANHLTETGLLS 154
Cdd:COG4123    82 ALNGLEDRITVIHGDLKEFAAELPPGsfdLVVSNPPYFKAgsgrkSPDEARAIARHEDALTLEDLIRAAARLLKPGGRFA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2630092231 155 VIIPHQDTEKFITTCTEQALYLIRNIHIFGIRGGKEIRNIVEFSKKPSAPL--HQDFVIEEMPRQYSAQYLEATKAF 229
Cdd:COG4123   162 LIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRAGLriLPPLVIHDEDGEYTPEVKALLRDF 238
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
3-229 9.46e-66

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: 203.45  E-value: 9.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231   3 KRKPFYFQKFKIEQTHDVFAVGTDGVLLGALCGCENANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNF 82
Cdd:COG4123     2 RLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  83 KHSPFAERLTATQADINTLTLHEKTT---CIVCNPPFFET-----NESEKHILARQQITLTYAQLIHFAANHLTETGLLS 154
Cdd:COG4123    82 ALNGLEDRITVIHGDLKEFAAELPPGsfdLVVSNPPYFKAgsgrkSPDEARAIARHEDALTLEDLIRAAARLLKPGGRFA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2630092231 155 VIIPHQDTEKFITTCTEQALYLIRNIHIFGIRGGKEIRNIVEFSKKPSAPL--HQDFVIEEMPRQYSAQYLEATKAF 229
Cdd:COG4123   162 LIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRAGLriLPPLVIHDEDGEYTPEVKALLRDF 238
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
39-160 4.44e-15

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: 70.31  E-value: 4.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  39 ANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKhSPFAERLTATQADINTLTLHEKTTCIVCNPPFfe 118
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLA-ANGLENGEVVASDVYSGVEDGKFDLIISNPPF-- 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2630092231 119 tnesekhilaRQQITLTYA---QLIHFAANHLTETG-LLSVIIPHQ 160
Cdd:pfam05175 109 ----------HAGLATTYNvaqRFIADAKRHLRPGGeLWIVANRFL 144
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
41-153 2.66e-13

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 67.49  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSpFAERLTATQADINTLTLHEKTTCIVCNPPFfeTN 120
Cdd:PRK09328  111 RVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGDWFEPLPGGRFDLIVSNPPY--IP 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2630092231 121 ESEKHILARQ------QITLT--------YAQLIHFAANHLTETGLL 153
Cdd:PRK09328  188 EADIHLLQPEvrdhepHLALFggedgldfYRRIIEQAPRYLKPGGWL 234
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
42-203 2.32e-12

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: 64.68  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  42 ILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLTLHEKTTCIVCNPPFFETNE 121
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEED 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231 122 sekhiLARQQITltyaqlIHFAAnhltETGLLSVIIPHQDTEKFIttctEQA-LYLIRNIHIFGIRGGKEIRNIVEFSKK 200
Cdd:TIGR00536 198 -----LADLPNV------VRFEP----LLALVGGDDGLNILRQII----ELApDYLKPNGFLVCEIGNWQQKSLKELLRI 258

                  ...
gi 2630092231 201 PSA 203
Cdd:TIGR00536 259 KFT 261
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
41-129 1.96e-06

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: 45.11  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRnPSARIHAVDIHLPAVNLAQHNFKHsPFAERLTATQADINTLTLHEKTTC--IVCNPPFFE 118
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPEADESFdvIISDPPLHH 78
                          90
                  ....*....|.
gi 2630092231 119 TNESEKHILAR 129
Cdd:cd02440    79 LVEDLARFLEE 89
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
3-229 9.46e-66

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: 203.45  E-value: 9.46e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231   3 KRKPFYFQKFKIEQTHDVFAVGTDGVLLGALCGCENANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNF 82
Cdd:COG4123     2 RLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  83 KHSPFAERLTATQADINTLTLHEKTT---CIVCNPPFFET-----NESEKHILARQQITLTYAQLIHFAANHLTETGLLS 154
Cdd:COG4123    82 ALNGLEDRITVIHGDLKEFAAELPPGsfdLVVSNPPYFKAgsgrkSPDEARAIARHEDALTLEDLIRAAARLLKPGGRFA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2630092231 155 VIIPHQDTEKFITTCTEQALYLIRNIHIFGIRGGKEIRNIVEFSKKPSAPL--HQDFVIEEMPRQYSAQYLEATKAF 229
Cdd:COG4123   162 LIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRAGLriLPPLVIHDEDGEYTPEVKALLRDF 238
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
41-164 1.15e-18

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: 80.62  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHsPFAERLTATQADINTLTLHEKTTCIVCNPPFfetn 120
Cdd:COG2813    52 RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAA-NGLENVEVLWSDGLSGVPDGSFDLILSNPPF---- 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2630092231 121 esekhilaRQQITLTYA---QLIHFAANHLTETG-LLSVIIPHQDTEK 164
Cdd:COG2813   127 --------HAGRAVDKEvahALIADAARHLRPGGeLWLVANRHLPYER 166
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
41-153 1.38e-15

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 73.65  E-value: 1.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADI-NTLTLHEKTTCIVCNPPFFet 119
Cdd:COG2890   115 RVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLfEPLPGDGRFDLIVSNPPYI-- 192
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2630092231 120 NESEKHILARQ------QITLT--------YAQLIHFAANHLTETGLL 153
Cdd:COG2890   193 PEDEIALLPPEvrdhepRLALDggedgldfYRRIIAQAPRLLKPGGWL 240
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
39-160 4.44e-15

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: 70.31  E-value: 4.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  39 ANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKhSPFAERLTATQADINTLTLHEKTTCIVCNPPFfe 118
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLA-ANGLENGEVVASDVYSGVEDGKFDLIISNPPF-- 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2630092231 119 tnesekhilaRQQITLTYA---QLIHFAANHLTETG-LLSVIIPHQ 160
Cdd:pfam05175 109 ----------HAGLATTYNvaqRFIADAKRHLRPGGeLWIVANRFL 144
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
41-153 2.66e-13

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 67.49  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSpFAERLTATQADINTLTLHEKTTCIVCNPPFfeTN 120
Cdd:PRK09328  111 RVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGDWFEPLPGGRFDLIVSNPPY--IP 187
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2630092231 121 ESEKHILARQ------QITLT--------YAQLIHFAANHLTETGLL 153
Cdd:PRK09328  188 EADIHLLQPEvrdhepHLALFggedgldfYRRIIEQAPRYLKPGGWL 234
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
42-203 2.32e-12

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: 64.68  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  42 ILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLTLHEKTTCIVCNPPFFETNE 121
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEED 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231 122 sekhiLARQQITltyaqlIHFAAnhltETGLLSVIIPHQDTEKFIttctEQA-LYLIRNIHIFGIRGGKEIRNIVEFSKK 200
Cdd:TIGR00536 198 -----LADLPNV------VRFEP----LLALVGGDDGLNILRQII----ELApDYLKPNGFLVCEIGNWQQKSLKELLRI 258

                  ...
gi 2630092231 201 PSA 203
Cdd:TIGR00536 259 KFT 261
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
41-113 2.03e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 2.03e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFkhspfaERLTATQADINTLTLHEKTTCIVCN 113
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEPFDLVVSN 70
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
42-130 1.62e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 53.34  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  42 ILEIGTGTGLISLMMAQRnPSARIHAVDIHLPAVNLAQHNFKHSPFaeRLTATQADINTLTLHEKT-TCIVCNPPFFETN 120
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSfDLVVSSGVLHHLP 77
                          90
                  ....*....|
gi 2630092231 121 ESEKHILARQ 130
Cdd:pfam13649  78 DPDLEAALRE 87
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
27-92 1.13e-08

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 52.88  E-value: 1.13e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2630092231  27 GVLLGALCGCENANTILEIGTGTGLISLMMAQR-NPSARIHAVDIHLPAVNLAQHNFKHSPFAERLT 92
Cdd:COG4122     5 GRLLYLLARLLGAKRILEIGTGTGYSTLWLARAlPDDGRLTTIEIDPERAAIARENFARAGLADRIR 71
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
41-116 4.59e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 51.44  E-value: 4.59e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSaRIHAVDIHLPAVNLAQHNFKhsPFAERLTATQADINTLTLHEKTTCIVCNPPF 116
Cdd:COG2263    48 TVLDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRIPLGGSVDTVVMNPPF 120
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
41-101 2.59e-07

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: 48.45  E-value: 2.59e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2630092231  41 TILEIGTGTGLISLMMAQRNpsARIHAVDIHLPAVNLAQHNFKHSPFaeRLTATQADINTL 101
Cdd:COG2226    25 RVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL 81
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
41-113 4.16e-07

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: 47.70  E-value: 4.16e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2630092231  41 TILEIGTGTGLISLMMAQRNpsARIHAVDIHLPAVNLAQHNFKHspfaERLTATQADINTLTLHEKT-TCIVCN 113
Cdd:COG2227    27 RVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAE----LNVDFVQGDLEDLPLEDGSfDLVICS 94
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
42-166 5.42e-07

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 49.86  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  42 ILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLTLHEKTTCIVCNPPFFETNE 121
Cdd:PRK01544  142 ILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFENIEKQKFDFIVSNPPYISHSE 221
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2630092231 122 SEKHILArqqiTLTYAQLIHFAANhltETGLLSVIIPHQDTEKFI 166
Cdd:PRK01544  222 KSEMAIE----TINYEPSIALFAE---EDGLQAYFIIAENAKQFL 259
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
41-112 6.81e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.49  E-value: 6.81e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2630092231  41 TILEIGTGTGLISlMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLTLHEKTTCIVC 112
Cdd:COG4076    38 VVLDIGTGSGLLS-MLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVIIS 108
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
41-129 1.96e-06

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: 45.11  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRnPSARIHAVDIHLPAVNLAQHNFKHsPFAERLTATQADINTLTLHEKTTC--IVCNPPFFE 118
Cdd:cd02440     1 RVLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPEADESFdvIISDPPLHH 78
                          90
                  ....*....|.
gi 2630092231 119 TNESEKHILAR 129
Cdd:cd02440    79 LVEDLARFLEE 89
PRK14968 PRK14968
putative methyltransferase; Provisional
41-124 2.68e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.43  E-value: 2.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRNpsARIHAVDIHLPAVNLAQHNFKHSPFAER-LTATQADINTLTLHEKTTCIVCNPPFFET 119
Cdd:PRK14968   26 RVLEVGTGSGIVAIVAAKNG--KKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPFRGDKFDVILFNPPYLPT 103

                  ....*
gi 2630092231 120 NESEK 124
Cdd:PRK14968  104 EEEEE 108
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
20-124 5.90e-06

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: 45.23  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  20 VFAVGTDGVLLGALCGCENANTILEIGTGTGLISLMMAQRnpSARIHAVDIHLPAVNLAQHNFKHSpfAERLTATQADIN 99
Cdd:TIGR00537   1 VYEPAEDSLLLEANLRELKPDDVLEIGAGTGLVAIRLKGK--GKCILTTDINPFAVKELRENAKLN--NVGLDVVMTDLF 76
                          90       100
                  ....*....|....*....|....*
gi 2630092231 100 TlTLHEKTTCIVCNPPFFETNESEK 124
Cdd:TIGR00537  77 K-GVRGKFDVILFNPPYLPLEDDLR 100
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
42-153 8.90e-06

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 45.70  E-value: 8.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  42 ILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQ--ADINtltlhEKTTCIVCNPPFFET 119
Cdd:PRK09489  200 VLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEGEVFASNvfSDIK-----GRFDMIISNPPFHDG 274
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2630092231 120 nesekhilarQQITLTYAQ-LIHFAANHLTETGLL 153
Cdd:PRK09489  275 ----------IQTSLDAAQtLIRGAVRHLNSGGEL 299
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
56-115 9.12e-06

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 45.86  E-value: 9.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  56 MAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLTLHEKTTCIVCNPP 115
Cdd:COG0116   244 RIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPP 303
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
39-113 9.71e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.33  E-value: 9.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2630092231  39 ANTILEIGTGTGLISLMMAQR-NPSARIHAVDIHLPAVNLAQHNFKHSPFaERLTATQADINTLTLHEKTTC---IVCN 113
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELLEDDKfdvVISN 81
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
43-98 2.50e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.97  E-value: 2.50e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2630092231  43 LEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPF--AERLTATQADI 98
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLlnAVRVELFQLDL 58
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
43-113 3.45e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 41.50  E-value: 3.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2630092231  43 LEIGTGTGLISLMMAQRNPsaRIHAVDIHLPAVNLAQHNFKHSPFAERltatQADINTLTLHEKT-TCIVCN 113
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFV----VGDAEDLPFPDNSfDLVLSS 66
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
41-112 1.00e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.45  E-value: 1.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2630092231  41 TILEIGTGTGLISLMMAQRNpSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLTLHEKTTCIVC 112
Cdd:COG2230    54 RVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVS 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
19-166 1.40e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 41.44  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  19 DVFAVGTDGVLLGALCGCENAN---TILEIGTGTGLISLMMAQRNpSARIHAVDIHLPAVNLAQHN----------FKHS 85
Cdd:COG0500     4 SYYSDELLPGLAALLALLERLPkggRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARaakaglgnveFLVA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  86 PFAERLTATQADINTLTLHektTCIVCNPPFFETnesekhilarqqitltyaQLIHFAANHLTETGLLSVIIPHQDTEKF 165
Cdd:COG0500    83 DLAELDPLPAESFDLVVAF---GVLHHLPPEERE------------------ALLRELARALKPGGVLLLSASDAAAALS 141

                  .
gi 2630092231 166 I 166
Cdd:COG0500   142 L 142
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
41-160 3.01e-04

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: 41.10  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPsARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQ-ADIntltLHEKTTCIVCNppffet 119
Cdd:pfam06325 164 SVLDVGCGSGILAIAALKLGA-KKVVGVDIDPVAVRAAKENAELNGVEARLEVYLpGDL----PKEKADVVVAN------ 232
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2630092231 120 nesekhILARQQItltyaQLIHFAANHLTETGL--LSVIIPHQ 160
Cdd:pfam06325 233 ------ILADPLI-----ELAPDIYALVKPGGYliLSGILKEQ 264
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
41-158 5.21e-04

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 40.32  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  41 TILEIGTGTG-LISLMMAQRNPSARIHAVDIHLPAVNLAQH--NFKHSPFaerlTATQADINTLTLHEKTTCIVCNPPF- 116
Cdd:COG0827   118 RILDPAVGTGnLLTTVLNQLKKKVNAYGVEVDDLLIRLAAVlaNLQGHPV----ELFHQDALQPLLIDPVDVVISDLPVg 193
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2630092231 117 ----------FETNESEKHilarqqitlTYAQ--LIHFAANHLTETGLLSVIIP 158
Cdd:COG0827   194 yypnderakrFKLKADEGH---------SYAHhlFIEQSLNYLKPGGYLFFLVP 238
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
41-84 9.80e-04

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 39.76  E-value: 9.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2630092231  41 TILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKH 84
Cdd:COG2242   250 VLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARR 293
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
26-91 1.30e-03

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 38.63  E-value: 1.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2630092231  26 DGVLLGALCGCENANTILEIGTGTGLISLMMAQRNP-SARIHAVDIHLPAVNLAQHNFKHSPFAERL 91
Cdd:pfam01596  31 EGQFLGMLVKLTGAKNVLEIGVFTGYSALAMALALPeDGKITAIDIDPEAYEIAKKFIQKAGVAHKI 97
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
5-153 1.37e-03

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 39.29  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231   5 KPFYFQKFKIEQTHDVFAVGTDGVLLGALCGCENANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHN--- 81
Cdd:PRK14966  218 REFYGRRFAVNPNVLIPRPETEHLVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNaad 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  82 ------FKHSPFAERLTATQAdintltlheKTTCIVCNPPFFETNE---SEKHILARQQITLT--------YAQLIHFAA 144
Cdd:PRK14966  298 lgarveFAHGSWFDTDMPSEG---------KWDIIVSNPPYIENGDkhlLQGDLRFEPQIALTdfsdglscIRTLAQGAP 368

                  ....*....
gi 2630092231 145 NHLTETGLL 153
Cdd:PRK14966  369 DRLAEGGFL 377
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
42-113 2.96e-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: 37.65  E-value: 2.96e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2630092231  42 ILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKhspfaERLTATQADINTLTLHEKT-TCIVCN 113
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS-----ENVQFICGDAEKLPLEDSSfDLIVSN 105
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
41-102 3.67e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 37.51  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2630092231  41 TILEIGTGTGLISLMMAQRnpSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQADINTLT 102
Cdd:PRK07580   66 RILDAGCGVGSLSIPLARR--GAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESLL 125
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
32-113 4.54e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.90  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630092231  32 ALCGCENANTILEIGTGTGLISLMMAQRnpSARIHAVDIHLPAVNLAQHNFKHSPFaerltaTQADINTLTLHEKT-TCI 110
Cdd:COG4976    40 ARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKGVYDRL------LVADLADLAEPDGRfDLI 111

                  ...
gi 2630092231 111 VCN 113
Cdd:COG4976   112 VAA 114
TrmK COG2384
tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase ...
40-112 4.61e-03

tRNA A22 N1-methylase [Translation, ribosomal structure and biogenesis]; tRNA A22 N1-methylase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441950  Cd Length: 228  Bit Score: 37.07  E-value: 4.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2630092231  40 NTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKHSPFAERLTATQAD-INTLTLHEKTTCIVC 112
Cdd:COG2384    17 ARVADIGTDHAYLPIYLVKNGIIKKAIAGDVNEGPLEKAKKNVKKYGLEDKIEVRLGDgLEVLEPGEVDTIVIA 90
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
38-84 6.33e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 36.52  E-value: 6.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2630092231  38 NANTILEIGTGTGLISLMMAQRNPSARIHAVDIHLPAVNLAQHNFKH 84
Cdd:PRK08287   31 RAKHLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQR 77
 
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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