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Conserved domains on  [gi|2506599999|gb|KAJ8999635|]
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hypothetical protein HRR94_005338 [Exophiala dermatitidis]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-114 1.11e-10

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: 55.77  E-value: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  46 RGDILEA-QLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLgNLAYAVADFT 114
Cdd:COG2226    11 REALLAAlGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-114 1.11e-10

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: 55.77  E-value: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  46 RGDILEA-QLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLgNLAYAVADFT 114
Cdd:COG2226    11 REALLAAlGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-114 2.36e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.71  E-value: 2.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506599999  60 VLDLGTGLGWVAEAAARRCRL-AIGTDISGKNIQLAKQKASRANLgNLAYAVADFT 114
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAE 55
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-110 1.98e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 1.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2506599999  52 AQLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLGNLAYAV 110
Cdd:PRK14968   19 AVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEV 77
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-144 1.85e-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: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  60 VLDLGTGLGWVAEAAARRC-RLAIGTDISGKNIQLAKQKASRANLGNLAYAVADFTlmnevraaiqaasqELNVSPVVRF 138
Cdd:cd02440     2 VLDLGCGTGALALALASGPgARVTGVDISPVALELARKAAAALLADNVEVLKGDAE--------------ELPPEADESF 67


                  ....*.
gi 2506599999 139 HVIFMC 144
Cdd:cd02440    68 DVIISD 73
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 55-105 6.27e-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: 41.18  E-value: 6.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2506599999  55 QPGCHVLDLGTGLGWVAE--AAARRCRLAIGTDISGKNIQLAKQKASRANLGN 105
Cdd:TIGR00536 113 PPILHILDLGTGSGCIALalAYEFPNAEVIAVDISPDALAVAEENAEKNQLEH 165
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-114 1.11e-10

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: 55.77  E-value: 1.11e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  46 RGDILEA-QLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLgNLAYAVADFT 114
Cdd:COG2226    11 REALLAAlGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAE 79
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 48-114 3.32e-10

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


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 54.25  E-value: 3.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506599999  48 DILEAQLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRAnlgNLAYAVADFT 114
Cdd:COG2227    16 ALLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLE 79
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 32-107 1.78e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.01  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  32 FERPGTTL-----RKYVgsrgDILE-AQLQPGCHVLDLGTGLGWVAEAAARRCRL-AIGTDISGKNIQLAKQKASRANLG 104
Cdd:COG2230    25 FEDPDDTLeeaqeAKLD----LILRkLGLKPGMRVLDIGCGWGGLALYLARRYGVrVTGVTLSPEQLEYARERAAEAGLA 100


                  ...
gi 2506599999 105 NLA 107
Cdd:COG2230   101 DRV 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-114 1.87e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 53.38  E-value: 1.87e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506599999  49 ILEAQLQPGCHVLDLGTGLG-WVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLGNLAYAVADFT 114
Cdd:COG0500    19 ALLERLPKGGRVLDLGCGTGrNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLA 85
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 60-114 2.36e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 48.71  E-value: 2.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506599999  60 VLDLGTGLGWVAEAAARRCRL-AIGTDISGKNIQLAKQKASRANLgNLAYAVADFT 114
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAE 55
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 61-114 4.67e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.96  E-value: 4.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2506599999  61 LDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRAnlgNLAYAVADFT 114
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPRE---GLTFVVGDAE 51
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
56-114 6.23e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 44.81  E-value: 6.23e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506599999  56 PGCHVLDLGTGLGWVAEAAARRCRLA--IGTDISGKNIQLAkqkasRANLGNLAYAVADFT 114
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGArvTGVDLSPEMLARA-----RARLPNVRFVVADLR 56
PRK14968 PRK14968
putative methyltransferase; Provisional
 52-110 1.98e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 1.98e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2506599999  52 AQLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLGNLAYAV 110
Cdd:PRK14968   19 AVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEV 77
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-144 1.85e-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: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  60 VLDLGTGLGWVAEAAARRC-RLAIGTDISGKNIQLAKQKASRANLGNLAYAVADFTlmnevraaiqaasqELNVSPVVRF 138
Cdd:cd02440     2 VLDLGCGTGALALALASGPgARVTGVDISPVALELARKAAAALLADNVEVLKGDAE--------------ELPPEADESF 67


                  ....*.
gi 2506599999 139 HVIFMC 144
Cdd:cd02440    68 DVIISD 73
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
49-114 5.10e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 5.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506599999  49 ILEAQLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLgnlayAVADFT 114
Cdd:COG4976    39 LARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRL-----LVADLA 99
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 55-105 6.27e-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: 41.18  E-value: 6.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2506599999  55 QPGCHVLDLGTGLGWVAE--AAARRCRLAIGTDISGKNIQLAKQKASRANLGN 105
Cdd:TIGR00536 113 PPILHILDLGTGSGCIALalAYEFPNAEVIAVDISPDALAVAEENAEKNQLEH 165
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 56-116 1.07e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.71  E-value: 1.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506599999  56 PGCHVLDLGTGLGWVAEAAARRCRL---AIGTDISGKNIQLAKQKASRANLGNLAYAVADFTLM 116
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPnaeVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEEL 66
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 60-104 1.51e-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: 1.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2506599999  60 VLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLG 104
Cdd:TIGR00537  23 VLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNVG 67
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 49-113 1.96e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.76  E-value: 1.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506599999  49 ILEAQLQPGCHVLDLGTGLGWVAEAAARRCRLA--IGTDISGKNIQLAKQKASRANLGNLAYAVADF 113
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALALAKERPDAevTAVDISPEALAVARRNAKHGLGARVEFLQGDW 167
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
46-143 4.09e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 38.73  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  46 RGDIleaqlqPGCHVLDLGTGLGWVAEAAARR-CRLAIGTDISGKNIQLAKQKASRANlGNLAYAVADFTlmnevraaiq 124
Cdd:COG2263    41 RGDI------EGKTVLDLGCGTGMLAIGAALLgAKKVVGVDIDPEALEIARENAERLG-VRVDFIRADVT---------- 103

                          90
                  ....*....|....*....
gi 2506599999 125 aasqelNVSPVVRFHVIFM 143
Cdd:COG2263   104 ------RIPLGGSVDTVVM 116
PRK08317 PRK08317
hypothetical protein; Provisional
 42-112 4.58e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 38.76  E-value: 4.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506599999  42 YVGSRGDILEA-QLQPGCHVLDLGTGLGWVAEAAARRCR---LAIGTDISGKNIQLAKQKASrANLGNLAYAVAD 112
Cdd:PRK08317    4 FRRYRARTFELlAVQPGDRVLDVGCGPGNDARELARRVGpegRVVGIDRSEAMLALAKERAA-GLGPNVEFVRGD 77
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 52-112 7.56e-04

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: 38.23  E-value: 7.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506599999  52 AQLQPGCHVLDLGTGLGWVAEAAARRCRLAIGTDISGKNIQLAKQKASRANLGNLAYAVAD 112
Cdd:COG2265   229 LDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGD 289
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 31-77 1.12e-03

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 37.69  E-value: 1.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2506599999  31 HFERPGTTLRKYVGSRGDIL--EAQLQPGCHVLDLGTGLGWVAEAAARR 77
Cdd:pfam02353  34 YFERPDMTLEEAQQAKLDLIldKLGLKPGMTLLDIGCGWGGLMRRAAER 82
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 52-112 1.31e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.44  E-value: 1.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506599999  52 AQLQPGCHVLDLGTGLGWVAEAAARRCRL---AIGTDISGKNIQLAKQKASRANL-GNLAYAVAD 112
Cdd:PRK00216   47 LGVRPGDKVLDLACGTGDLAIALAKAVGKtgeVVGLDFSEGMLAVGREKLRDLGLsGNVEFVQGD 111
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 50-135 1.38e-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: 37.25  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506599999  50 LEAQLQPGCHVLDLGTGLGWVAEAAAR-RCRLAIGTDISGKNIQLAKQKASRanlgnlayavadftlmNEVRAAIQA-AS 127
Cdd:pfam06325 155 LERLVKPGESVLDVGCGSGILAIAALKlGAKKVVGVDIDPVAVRAAKENAEL----------------NGVEARLEVyLP 218


                  ....*...
gi 2506599999 128 QELNVSPV 135
Cdd:pfam06325 219 GDLPKEKA 226
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
53-97 5.37e-03

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 35.59  E-value: 5.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2506599999  53 QLQPGCHVLDLGTGLGWVAEAAARRCRLAI-GTDISGKNIQLAKQK 97
Cdd:PRK11705  164 QLKPGMRVLDIGCGWGGLARYAAEHYGVSVvGVTISAEQQKLAQER 209
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
50-93 7.54e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 35.13  E-value: 7.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2506599999  50 LEAQLQPGCHVLDLGTGLGWVAEAAARR-CRLAIGTDI-------SGKNIQL 93
Cdd:PRK00517  113 LEKLVLPGKTVLDVGCGSGILAIAAAKLgAKKVLAVDIdpqaveaARENAEL 164
arsM PRK11873
arsenite methyltransferase;
52-105 7.71e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 35.31  E-value: 7.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506599999  52 AQLQPGCHVLDLGTGLGWVAEAAARRC---RLAIGTDISGKNIQLAKQKASRANLGN 105
Cdd:PRK11873   73 AELKPGETVLDLGSGGGFDCFLAARRVgptGKVIGVDMTPEMLAKARANARKAGYTN 129
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 51-105 9.57e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 34.74  E-value: 9.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506599999  51 EAQLQPGCHVLDLGTGLGWVAEAAARRCRLA--IGTDISGKNIQLAKQKASRANLGN 105
Cdd:COG2890   107 LLPAGAPPRVLDLGTGSGAIALALAKERPDArvTAVDISPDALAVARRNAERLGLED 163
 
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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