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Conserved domains on  [gi|187034321|emb|CAP26138|]
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Protein CBG06267 [Caenorhabditis briggsae]

Protein Classification

protein N-lysine methyltransferase family protein( domain architecture ID 10563300)

protein N-lysine methyltransferase family protein is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to human METTL21D that specifically trimethylates 'Lys-315' of VCP/p97

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 14-177 8.64e-60

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: 184.84  E-value: 8.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   14 NNDESELTIFQETVTDVGGVIWDSALMTIHYFFK------HPAKFEGKKVLELGSGTGVCGIALAAL--GADVIITDLPE 85
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   86 RIPLLEKNLAANkhLTGNRIKVEVLDWMTDKTPDG-----LDLVLAVDCVYYNSTITPLIDLLKNCDAKE--IIVVSEER 158
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLfdghpVDLILAADCVYNEDSFPLLEKTLKDLLGKEsvILVAYKKR 158

                         170
                  ....*....|....*....
gi 187034321  159 digeaSVAQKTFFKNITEF 177
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 14-177 8.64e-60

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: 184.84  E-value: 8.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   14 NNDESELTIFQETVTDVGGVIWDSALMTIHYFFK------HPAKFEGKKVLELGSGTGVCGIALAAL--GADVIITDLPE 85
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   86 RIPLLEKNLAANkhLTGNRIKVEVLDWMTDKTPDG-----LDLVLAVDCVYYNSTITPLIDLLKNCDAKE--IIVVSEER 158
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLfdghpVDLILAADCVYNEDSFPLLEKTLKDLLGKEsvILVAYKKR 158

                         170
                  ....*....|....*....
gi 187034321  159 digeaSVAQKTFFKNITEF 177
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 35-146 3.23e-08

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: 50.40  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  35 WDSALMTihyfFKHPAKFEGKKVLELGSGTGVCGIALAALGADVIITDLPERipLLEknlAANKHLTGNRIKVEVLDWMT 114
Cdd:COG2227   10 WDRRLAA----LLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPE--ALE---IARERAAELNVDFVQGDLED 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 187034321 115 DKTPDG-LDLVLAVDCVYYnstITPLIDLLKNC 146
Cdd:COG2227   81 LPLEDGsFDLVICSEVLEH---LPDPAALLREL 110
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 29-175 3.45e-06

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 46.16  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  29 DVGGVIWDSALMTIHYFFKHPAKFEGKKVLELGSGT-GVCGIALA-ALGADVIITDL-PERIPLLEKNLAankHLTGNRI 105
Cdd:cd05188  110 EEAALLPEPLATAYHALRRAGVLKPGDTVLVLGAGGvGLLAAQLAkAAGARVIVTDRsDEKLELAKELGA---DHVIDYK 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321 106 KVEVLDWMTDKTPDGLDLVlaVDCVYYNSTITPLIDLLKNCdAKeIIVVSEERDIGEASVAQKTFFKNIT 175
Cdd:cd05188  187 EEDLEEELRLTGGGGADVV--IDAVGGPETLAQALRLLRPG-GR-IVVVGGTSGGPPLDDLRRLLFKELT 252
PRK14968 PRK14968
putative methyltransferase; Provisional
 53-125 1.26e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.12  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187034321  53 EGKKVLELGSGTGVCGIALAALGADVIITDL-PERIPLLEKNLAANkHLTGNRIKVEVLDWMTDKTPDGLDLVL 125
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDInPYAVECAKCNAKLN-NIRNNGVEVIRSDLFEPFRGDKFDVIL 95
 
Name Accession Description Interval E-value
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 14-177 8.64e-60

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: 184.84  E-value: 8.64e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   14 NNDESELTIFQETVTDVGGVIWDSALMTIHYFFK------HPAKFEGKKVLELGSGTGVCGIALAAL--GADVIITDLPE 85
Cdd:pfam10294   1 KLDNPGLRIEEDTGNGIGGHVWDAAVVLSKYLEMkifkelGANNLSGLNVLELGSGTGLVGIAVALLlpGASVTITDLEE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   86 RIPLLEKNLAANkhLTGNRIKVEVLDWMTDKTPDG-----LDLVLAVDCVYYNSTITPLIDLLKNCDAKE--IIVVSEER 158
Cdd:pfam10294  81 ALELLKKNIELN--ALSSKVVVKVLDWGENLPPDLfdghpVDLILAADCVYNEDSFPLLEKTLKDLLGKEsvILVAYKKR 158

                         170
                  ....*....|....*....
gi 187034321  159 digeaSVAQKTFFKNITEF 177
Cdd:pfam10294 159 -----REAEKKFFKLLERF 172
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 35-146 3.23e-08

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: 50.40  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  35 WDSALMTihyfFKHPAKFEGKKVLELGSGTGVCGIALAALGADVIITDLPERipLLEknlAANKHLTGNRIKVEVLDWMT 114
Cdd:COG2227   10 WDRRLAA----LLARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPE--ALE---IARERAAELNVDFVQGDLED 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 187034321 115 DKTPDG-LDLVLAVDCVYYnstITPLIDLLKNC 146
Cdd:COG2227   81 LPLEDGsFDLVICSEVLEH---LPDPAALLREL 110
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 53-132 1.71e-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: 45.76  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  53 EGKKVLELGSGTGVCGIALAALGADVIITDL-PERIPLLEKNLAANkhltGNRIKVEVLDWMTDKTPDG-LDLVLAVDCV 130
Cdd:COG2226   22 PGARVLDLGCGTGRLALALAERGARVTGVDIsPEMLELARERAAEA----GLNVEFVVGDAEDLPFPDGsFDLVISSFVL 97


                 ..
gi 187034321 131 YY 132
Cdd:COG2226   98 HH 99
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
35-145 3.20e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.76  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  35 WDSALM-TIHY---------FFKHPAKFEGKKVLELGSGTGVCGIALAALGADVIITDLPERipLLEKnlAANKHLTGNR 104
Cdd:COG4976   18 YDAALVeDLGYeapallaeeLLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEE--MLAK--AREKGVYDRL 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 187034321 105 IKVEVLDWmtDKTPDGLDLVLAVDCVYYNSTITPLIDLLKN 145
Cdd:COG4976   94 LVADLADL--AEPDGRFDLIVAADVLTYLGDLAAVFAGVAR 132
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 29-175 3.45e-06

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 46.16  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  29 DVGGVIWDSALMTIHYFFKHPAKFEGKKVLELGSGT-GVCGIALA-ALGADVIITDL-PERIPLLEKNLAankHLTGNRI 105
Cdd:cd05188  110 EEAALLPEPLATAYHALRRAGVLKPGDTVLVLGAGGvGLLAAQLAkAAGARVIVTDRsDEKLELAKELGA---DHVIDYK 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321 106 KVEVLDWMTDKTPDGLDLVlaVDCVYYNSTITPLIDLLKNCdAKeIIVVSEERDIGEASVAQKTFFKNIT 175
Cdd:cd05188  187 EEDLEEELRLTGGGGADVV--IDAVGGPETLAQALRLLRPG-GR-IVVVGGTSGGPPLDDLRRLLFKELT 252
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-132 6.60e-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: 6.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187034321   57 VLELGSGTGVCGIALA-ALGADVIITDL-PERIPLLEKNLAANkhltGNRIKVEVLDWMTDKTPDG-LDLVLAVDCVYY 132
Cdd:pfam13649   1 VLDLGCGTGRLTLALArRGGARVTGVDLsPEMLERARERAAEA----GLNVEFVQGDAEDLPFPDGsFDLVVSSGVLHH 75
PRK14968 PRK14968
putative methyltransferase; Provisional
 53-125 1.26e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.12  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 187034321  53 EGKKVLELGSGTGVCGIALAALGADVIITDL-PERIPLLEKNLAANkHLTGNRIKVEVLDWMTDKTPDGLDLVL 125
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGKKVVGVDInPYAVECAKCNAKLN-NIRNNGVEVIRSDLFEPFRGDKFDVIL 95
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
52-94 1.95e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.74  E-value: 1.95e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 187034321  52 FEGKKVLELGSGTGVCGIALAALGA-DVIITDL-PERIPLLEKNL 94
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIdPEALEIARENA 88
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 54-126 2.37e-05

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: 43.59  E-value: 2.37e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 187034321  54 GKKVLELGSGTGVCGIALAALGADVIIT--DL-PERIPLLEKNLAANKhlTGNRIKVE---VLDWMTDKTPDGLDLVLA 126
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRSPGARITgvEIqPEAAELARRNVALNG--LEDRITVIhgdLKEFAAELPPGSFDLVVS 114
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 54-125 5.90e-05

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: 41.81  E-value: 5.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187034321   54 GKKVLELGSGTGVCGIALAALGADVIIT--DLPER-IPLLEKNLAANKHLTGNRIKVEVLDwmtDKTPDGLDLVL 125
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDAELTmvDINARaLESARENLAANGLENGEVVASDVYS---GVEDGKFDLII 103
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 56-132 6.79e-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: 40.49  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  56 KVLELGSGTGVCGIALA-ALGADVIITDLPERipLLEKNLAANKHLTGNRIKVEVLDWMT--DKTPDGLDLVLAVDCVYY 132
Cdd:cd02440    1 RVLDLGCGTGALALALAsGPGARVTGVDISPV--ALELARKAAAALLADNVEVLKGDAEElpPEADESFDVIISDPPLHH 78
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 55-125 2.98e-04

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


Pssm-ID: 443298  Cd Length: 173  Bit Score: 39.78  E-value: 2.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187034321  55 KKVLELGSGTGVCGIALA-ALGADVIIT--DL-PERIPLLEKNLAANKHltGNRIKVEV---LDWMTDKTPDGLDLVL 125
Cdd:COG4122   18 KRILEIGTGTGYSTLWLArALPDDGRLTtiEIdPERAAIARENFARAGL--ADRIRLILgdaLEVLPRLADGPFDLVF 93
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 58-146 6.17e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.73  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321   58 LELGSGTGVCGIALAAL--GADVIITDL-PERIPLLEKNLAANKHLTGNRIKVEVLDwMTDKTPDGLDLVLAVDCVYYns 134
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDIsPAALEAARERLAALGLLNAVRVELFQLD-LGELDPGSFDVVVASNVLHH-- 77

                          90
                  ....*....|..
gi 187034321  135 tITPLIDLLKNC 146
Cdd:pfam08242  78 -LADPRAVLRNI 88
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 53-126 8.41e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 39.37  E-value: 8.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187034321  53 EGKKVLELGSGTGVCGIALAAL--GADVIITDL-PERIPLLEKNLaanKHLTGNRIKVEVLDWMTDKTPDGLDLVLA 126
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALALAKErpDAEVTAVDIsPEALAVARRNA---KHGLGARVEFLQGDWFEPLPGGRFDLIVS 181
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 46-126 1.14e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 38.98  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  46 FKHPAKFEGKKVLELGSGTGVCGIALAAL--GADVIITDL-PERIPLLEKNLAANKhlTGNRIKVEVLDWMTDKTPDG-L 121
Cdd:COG2890  105 LALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDIsPDALAVARRNAERLG--LEDRVRFLQGDLFEPLPGDGrF 182


                 ....*
gi 187034321 122 DLVLA 126
Cdd:COG2890  183 DLIVS 187
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 53-146 1.26e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.36  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  53 EGKKVLELGSGTGVCGIALAAL-GADVIITDL-PERIPLLEKNLAANKHltgNRIKVEVLDW-MTDKTPDG-LDLVLAVD 128
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAARfGGRVIGIDLsPEAIALARARAAKAGL---GNVEFLVADLaELDPLPAEsFDLVVAFG 102

                         90
                 ....*....|....*...
gi 187034321 129 CVYYNSTItPLIDLLKNC 146
Cdd:COG0500  103 VLHHLPPE-EREALLREL 119
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
52-126 2.51e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 37.85  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  52 FEGKKVLELGSGTGVCGIALAALGA-DVIITDL-PERIPLLEKNLAANKhlTGNRIKVEvldwmtdkTPDGL-----DLV 124
Cdd:COG2264  147 KPGKTVLDVGCGSGILAIAAAKLGAkRVLAVDIdPVAVEAARENAELNG--VEDRIEVV--------LGDLLedgpyDLV 216


                 ..
gi 187034321 125 LA 126
Cdd:COG2264  217 VA 218
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 54-132 2.88e-03

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 36.83  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187034321  54 GKKVLELGSGTGVCGIALAA-LGADVIITDL-PERIPLLEKNLAAnkHLTGNRIKVEVLDWMTDKTPDGLDLVLAVDCVY 131
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLARrYGVRVTGVTLsPEQLEYARERAAE--AGLADRVEVRLADYRDLPADGQFDAIVSIGMFE 129


                 .
gi 187034321 132 Y 132
Cdd:COG2230  130 H 130
 
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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