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Conserved domains on  [gi|514963311|ref|WP_016651634|]
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MULTISPECIES: methyltransferase [Acinetobacter]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

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; similar to Homo sapiens electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 64-182 3.36e-37

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 129.23  E-value: 3.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  64 PYWIFCWASGLAMAQWLLAEPHhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELEY-LD 142
Cdd:COG3897   47 PFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTrLG 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 514963311 143 DLYQSEP---VDVLLAADVLYDQSN--RF--FLDEFLKFAPEVWVAD 182
Cdd:COG3897  126 DWRDPPAaggFDLILGGDVLYERDLaePLlpFLDRLAAPGGEVLIGD 172
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 64-182 3.36e-37

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 129.23  E-value: 3.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  64 PYWIFCWASGLAMAQWLLAEPHhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELEY-LD 142
Cdd:COG3897   47 PFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTrLG 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 514963311 143 DLYQSEP---VDVLLAADVLYDQSN--RF--FLDEFLKFAPEVWVAD 182
Cdd:COG3897  126 DWRDPPAaggFDLILGGDVLYERDLaePLlpFLDRLAAPGGEVLIGD 172
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
76-159 4.67e-20

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 85.20  E-value: 4.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  76 MAQWLLAEPhhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELE-YLDDlyQSEPVDVLL 154
Cdd:PRK00517 109 CLEALEKLV--LPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNvYLPQ--GDLKADVIV 184


                 ....*...
gi 514963311 155 A---ADVL 159
Cdd:PRK00517 185 AnilANPL 192
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 78-161 7.50e-15

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 71.79  E-value: 7.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVE------LEYLDDLYQsEPVD 151
Cdd:TIGR00406 151 EWL--EDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSdrlqvkLIYLEQPIE-GKAD 227

                          90
                  ....*....|...
gi 514963311  152 VLLA---ADVLYD 161
Cdd:TIGR00406 228 VIVAnilAEVIKE 240
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 78-159 1.69e-14

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: 70.76  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELE---YLDDLYQSEPVDVLL 154
Cdd:pfam06325 153 EAL--ERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARlevYLPGDLPKEKADVVV 230


                  ....*...
gi 514963311  155 A---ADVL 159
Cdd:pfam06325 231 AnilADPL 238
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 92-173 2.64e-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: 44.73  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  92 VLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALL---NDVELEYLD----DLYQSEPVDVLLAADVLYDQSN 164
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAAllaDNVEVLKGDaeelPPEADESFDVIISDPPLHHLVE 81

                         90
                 ....*....|.
gi 514963311 165 RF--FLDEFLK 173
Cdd:cd02440   82 DLarFLEEARR 92
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 64-182 3.36e-37

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 129.23  E-value: 3.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  64 PYWIFCWASGLAMAQWLLAEPHhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELEY-LD 142
Cdd:COG3897   47 PFWAFLWPSGQALARYLLDHPE-VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTrLG 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 514963311 143 DLYQSEP---VDVLLAADVLYDQSN--RF--FLDEFLKFAPEVWVAD 182
Cdd:COG3897  126 DWRDPPAaggFDLILGGDVLYERDLaePLlpFLDRLAAPGGEVLIGD 172
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
76-159 1.24e-23

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 95.24  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  76 MAQWLLAEPHhvKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVE--LE-YLDDLYQSEPVDV 152
Cdd:COG2264  138 CLEALEKLLK--PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEdrIEvVLGDLLEDGPYDL 215

                         90
                 ....*....|
gi 514963311 153 LLA---ADVL 159
Cdd:COG2264  216 VVAnilANPL 225
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
76-159 4.67e-20

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 85.20  E-value: 4.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  76 MAQWLLAEPhhVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELE-YLDDlyQSEPVDVLL 154
Cdd:PRK00517 109 CLEALEKLV--LPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNvYLPQ--GDLKADVIV 184


                 ....*...
gi 514963311 155 A---ADVL 159
Cdd:PRK00517 185 AnilANPL 192
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 78-161 7.50e-15

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 71.79  E-value: 7.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVE------LEYLDDLYQsEPVD 151
Cdd:TIGR00406 151 EWL--EDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSdrlqvkLIYLEQPIE-GKAD 227

                          90
                  ....*....|...
gi 514963311  152 VLLA---ADVLYD 161
Cdd:TIGR00406 228 VIVAnilAEVIKE 240
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 78-159 1.69e-14

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: 70.76  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   78 QWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELE---YLDDLYQSEPVDVLL 154
Cdd:pfam06325 153 EAL--ERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARlevYLPGDLPKEKADVVV 230


                  ....*...
gi 514963311  155 A---ADVL 159
Cdd:pfam06325 231 AnilADPL 238
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
87-131 7.50e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 61.84  E-value: 7.50e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 514963311  87 VKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENA 131
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENA 88
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
85-155 1.05e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 56.58  E-value: 1.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 514963311  85 HHVK-DKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLND----VELEYLD--DLYQSEPVDVLLA 155
Cdd:COG4076   31 RVVKpGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGlsdrITVINADatDLDLPEKADVIIS 108
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 80-137 1.65e-09

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: 55.20  E-value: 1.65e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 514963311  80 LLAE--PHHVKDKVvLDFGAGSGVVAIA-AKMAGAKRVICCDIDPVSLASCRENALLNDVE 137
Cdd:COG2813   40 LLLEhlPEPLGGRV-LDLGCGYGVIGLAlAKRNPEARVTLVDVNARAVELARANAAANGLE 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 75-160 1.87e-09

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: 53.87  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  75 AMAQWLlaEPHHVKDKVVLDFGAGSGVVAIAAKMAGAkRVICCDIDPVSLASCRENALLNDVELEYLD--DL-YQSEPVD 151
Cdd:COG2227   13 RLAALL--ARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQGDleDLpLEDGSFD 89


                 ....*....
gi 514963311 152 VLLAADVLY 160
Cdd:COG2227   90 LVICSEVLE 98
PRK14967 PRK14967
putative methyltransferase; Provisional
 79-155 3.48e-09

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 55.06  E-value: 3.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  79 WLLAEPHHVKDKV----VLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLN----DVELEYLDDLYQSEPV 150
Cdd:PRK14967  23 QLLADALAAEGLGpgrrVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAgvdvDVRRGDWARAVEFRPF 102


                 ....*
gi 514963311 151 DVLLA 155
Cdd:PRK14967 103 DVVVS 107
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 92-159 7.30e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.41  E-value: 7.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514963311   92 VLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVELEYL----DDL-YQSEPVDVLLAADVL 159
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVqgdaEDLpFPDGSFDLVVSSGVL 73
PRK14968 PRK14968
putative methyltransferase; Provisional
 80-136 4.96e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 4.96e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 514963311  80 LLAEPHHVKD-KVVLDFGAGSGVVAIAAKMAGaKRVICCDIDPVSLASCRENALLNDV 136
Cdd:PRK14968  14 LLAENAVDKKgDRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVECAKCNAKLNNI 70
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 88-137 8.44e-08

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: 50.28  E-value: 8.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 514963311   88 KDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDPVSLASCRENALLNDVE 137
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAAlAKESPDAELTMVDINARALESARENLAANGLE 81
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 76-155 1.63e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 50.55  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  76 MAQWLLAEPHHVKDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDPVSLASCRENA---LLNDVELeYLDDLY---QSE 148
Cdd:PRK09328  96 LVEWALEALLLKEPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEALAVARRNAkhgLGARVEF-LQGDWFeplPGG 174


                 ....*..
gi 514963311 149 PVDVLLA 155
Cdd:PRK09328 175 RFDLIVS 181
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 53-163 1.89e-07

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: 49.25  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   53 DEVIRRIWNETPYWIFC--WASGLAMAQWLL------AEPHHVKDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDPVs 123
Cdd:pfam10294   3 DNPGLRIEEDTGNGIGGhvWDAAVVLSKYLEmkifkeLGANNLSGLNVLELGSGTGLVGIAvALLLPGASVTITDLEEA- 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 514963311  124 lascRE--------NALLNDVELEYLD-------DLYQSEPVDVLLAADVLYDQS 163
Cdd:pfam10294  82 ----LEllkknielNALSSKVVVKVLDwgenlppDLFDGHPVDLILAADCVYNED 132
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 88-137 3.24e-07

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 49.87  E-value: 3.24e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 514963311  88 KDKVVLDFGAGSGVVAI-AAKMAGAKrVICCDIDPVSLASCRENALLNDVE 137
Cdd:COG1867   57 REISYLDALAASGIRGLrYALEVGIK-VTLNDIDPEAVELIRENLELNGLE 106
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 77-163 8.06e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.99  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  77 AQWLLAEPHHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENA---LLNDVELeYLDDLYQSEP---- 149
Cdd:COG0500   15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAakaGLGNVEF-LVADLAELDPlpae 93

                         90
                 ....*....|....*
gi 514963311 150 -VDVLLAADVLYDQS 163
Cdd:COG0500   94 sFDLVVAFGVLHHLP 108
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 76-155 1.40e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 47.84  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  76 MAQWLLAEPHHVKDKVVLDFGAGSGVVAIA-AKMAGAKRVICCDIDPVSLASCRENALLNDVELE-------YLDDLYQS 147
Cdd:COG2890  100 LVELALALLPAGAPPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDALAVARRNAERLGLEDRvrflqgdLFEPLPGD 179


                 ....*...
gi 514963311 148 EPVDVLLA 155
Cdd:COG2890  180 GRFDLIVS 187
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 70-160 1.64e-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: 46.14  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  70 WASGLAMAQWLLAEPHHVKDKVVLDFGAGSGVVAIAAKMAGAkRVICCDIDPVSLASCRENALLNDVELEYL----DDL- 144
Cdd:COG2226    4 VAARYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGLNVEFVvgdaEDLp 82

                         90
                 ....*....|....*.
gi 514963311 145 YQSEPVDVLLAADVLY 160
Cdd:COG2226   83 FPDGSFDLVISSFVLH 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 92-173 2.64e-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: 44.73  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  92 VLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALL---NDVELEYLD----DLYQSEPVDVLLAADVLYDQSN 164
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAAllaDNVEVLKGDaeelPPEADESFDVIISDPPLHHLVE 81

                         90
                 ....*....|.
gi 514963311 165 RF--FLDEFLK 173
Cdd:cd02440   82 DLarFLEEARR 92
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 87-175 3.43e-06

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 46.78  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  87 VKD-KVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDVEleylddlyqsEPVDVLL--AADVLYDQS 163
Cdd:COG2520  178 VKPgERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIRLNKVE----------DRVTPILgdAREVAPELE 247

                         90       100
                 ....*....|....*....|.
gi 514963311 164 NRF---------FLDEFLKFA 175
Cdd:COG2520  248 GKAdriimnlphSADEFLDAA 268
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 88-199 4.95e-06

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 45.32  E-value: 4.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  88 KDKVVLDFGAGSGVVAIAAKMAGAkRVICCDIDPVSLASCREN---ALLNDVELEYLD--DL-YQSEPVDVlLAADVLYD 161
Cdd:COG1041   26 EGDTVLDPFCGTGTILIEAGLLGR-RVIGSDIDPKMVEGARENlehYGYEDADVIRGDarDLpLADESVDA-IVTDPPYG 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 514963311 162 QS----NRFFLDEFLKFAPE-----------VWVADSRVKNFSHPQYLKIDER 199
Cdd:COG1041  104 RSskisGEELLELYEKALEEaarvlkpggrvVIVTPRDIDELLEEAGFKVLER 156
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 91-161 5.71e-06

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 46.06  E-value: 5.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514963311  91 VVLDFGAGSGVVAI-AAKMAGAKRVICCDIDPVSLASCRENALLNDVEleylDDLYQSEPVDVLLAADVLYD 161
Cdd:PRK04338  60 SVLDALSASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGLE----NEKVFNKDANALLHEERKFD 127
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
92-160 2.26e-05

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 42.12  E-value: 2.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 514963311  92 VLDFGAGSGVV--AIAAKMAGAkRVICCDIDPVSLASCRENalLNDVELEYLD--DLYQSEPVDVLLAADVLY 160
Cdd:COG4106    5 VLDLGCGTGRLtaLLAERFPGA-RVTGVDLSPEMLARARAR--LPNVRFVVADlrDLDPPEPFDLVVSNAALH 74
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
49-159 2.33e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 43.45  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  49 DRLDDEVIRRIWNETPYWIfcwasglamAQWLLAEPHHVKDKVVLDFGAGSGVVAIAAKMAGaKRVICCDIDPVSLASCR 128
Cdd:COG4976   16 DSYDAALVEDLGYEAPALL---------AEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEEMLAKAR 85

                         90       100       110
                 ....*....|....*....|....*....|..
gi 514963311 129 ENALLNDVELEYLDDLYQ-SEPVDVLLAADVL 159
Cdd:COG4976   86 EKGVYDRLLVADLADLAEpDGRFDLIVAADVL 117
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 92-137 4.40e-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: 43.21  E-value: 4.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 514963311  92 VLDFGAGSGVVAI--AAKMAGAkRVICCDIDPVSLASCRENALLNDVE 137
Cdd:COG4123   41 VLDLGTGTGVIALmlAQRSPGA-RITGVEIQPEAAELARRNVALNGLE 87
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 85-169 7.69e-05

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 42.86  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  85 HHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCRENALLNDveleyLDDLYQSEPVDVLLAADVLYDQSN 164
Cdd:COG1092  213 ELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNG-----LDDRHEFVQADAFDWLRELAREGE 287


                 ....*...
gi 514963311 165 RF---FLD 169
Cdd:COG1092  288 RFdliILD 295
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 86-164 1.17e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.86  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   86 HVKDKVVLDFGAGSGVVA--IAAKMAGAKRVICCDIDPVSLASCRENA---LLNDVEL-----EYLDDLYQSEPVDVLLA 155
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSfeLAEELGPNAEVVGIDISEEAIEKARENAqklGFDNVEFeqgdiEELPELLEDDKFDVVIS 80


                  ....*....
gi 514963311  156 ADVLYDQSN 164
Cdd:pfam13847  81 NCVLNHIPD 89
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
85-201 1.22e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 41.46  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   85 HHVKDKVVLDFGAGSGVVAIAAKMAGAKRVICCDIDPVSLASCREN---------ALLNDVELEYLDDLYQSEPVDVLLA 155
Cdd:pfam03602  38 PYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQILKENlqllglpgaVLVMDALLALLRLAGKGPVFDIVFL 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 514963311  156 ----ADVLYDQSnrffLDEFLK---FAPEVWVA---DSRVKNFSHPQYL-KIDERSA 201
Cdd:pfam03602 118 dppyAKGLIEEV----LDLLAEkgwLKPNALIYvetEKRGELPEQPGNLeLVREKKY 170
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 88-154 1.43e-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: 42.09  E-value: 1.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 514963311  88 KDKVVLDFGAGSGV--VAIAAKmagAKRVICCDIDPVSLASCRENALLN----------DVElEYLDDLYQSEPVDVLL 154
Cdd:COG2265  233 GGERVLDLYCGVGTfaLPLARR---AKKVIGVEIVPEAVEDARENARLNglknvefvagDLE-EVLPELLWGGRPDVVV 307
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
 91-137 2.46e-04

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


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 40.80  E-value: 2.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 514963311   91 VVLDFGAGSGVVAI-AAKMAGAKRVICCDIDPVSLASCRENALLNDVE 137
Cdd:pfam02475 102 VVVDMFAGIGPFSIpIAKHSKARRVYAIELNPESYKYLKENIKLNKVE 149
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 51-159 5.00e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.14  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311  51 LDDEVIRRIWNET-PYWIFCWASG---LAMAQW----LLAEPHHVKD-KVVLDFGAGSGVVAI-AAKMAGAkRVICCDID 120
Cdd:COG2230    5 LGNDFYRLFLDPTmTYSCAYFEDPddtLEEAQEakldLILRKLGLKPgMRVLDIGCGWGGLALyLARRYGV-RVTGVTLS 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 514963311 121 PVSLASCRENA----LLNDVELEYLD--DLYQSEPVDVLLAADVL 159
Cdd:COG2230   84 PEQLEYARERAaeagLADRVEVRLADyrDLPADGQFDAIVSIGMF 128
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 85-131 5.25e-04

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 39.29  E-value: 5.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 514963311  85 HHVKDKVVLDFGAGSGVVAIAAkmA--GAKRVICCDIDPVSLASCRENA 131
Cdd:COG0742   38 PDIEGARVLDLFAGSGALGLEA--LsrGAASVVFVEKDRKAAAVIRKNL 84
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 71-129 7.19e-04

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. 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.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 39.91  E-value: 7.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514963311  71 ASGLAMAQWLLAEP-----HHVK------DKVVLDFGAGS-GVVAI-AAKMAGAKRVICCDIDPVSLASCRE 129
Cdd:cd08232  137 PDGLSLRRAALAEPlavalHAVNragdlaGKRVLVTGAGPiGALVVaAARRAGAAEIVATDLADAPLAVARA 208
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-179 8.40e-04

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 37.26  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 514963311   93 LDFGAGSGVVAIAAKMAGAkRVICCDIDPVSLASCRENALLNDVEL--EYLDDL-YQSEPVDVLLAADVLydqsnrFFLD 169
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREGLTFvvGDAEDLpFPDNSFDLVLSSEVL------HHVE 73

                          90
                  ....*....|
gi 514963311  170 EFLKFAPEVW 179
Cdd:pfam08241  74 DPERALREIA 83
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 90-121 1.19e-03

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 39.01  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 514963311  90 KVVLDFGAGS-G-VVAIAAKMAGAKRVICCDIDP 121
Cdd:cd05285  164 DTVLVFGAGPiGlLTAAVAKAFGATKVVVTDIDP 197
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 91-137 1.36e-03

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 37.68  E-value: 1.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 514963311   91 VVLDFGAGSGVVAI-AAKMAGAKRVICCDIDPVSLASCRENALLNDVE 137
Cdd:TIGR01444   1 VVIDVGANIGDTSLyFARKGAEGRVIAFEPLPDAYEILEENVKLNNLP 48
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 88-144 1.55e-03

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: 38.99  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514963311  88 KDKVVLDFGAGSGVVAI-AAKMAGAKRVICCDIDPVSLASCRENAL---LNDVEL------EYLDDL 144
Cdd:COG2242  247 PGDVLWDIGAGSGSVSIeAARLAPGGRVYAIERDPERAALIRANARrfgVPNVEVvegeapEALADL 313
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 89-154 1.85e-03

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, 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. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 38.78  E-value: 1.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 514963311  89 DKVVLDFGAGS-GVVAIA-AKMAGAKRVICCDIDPVSLASCRE---NALLNDVELEY------LDDLYQSEPVDVLL 154
Cdd:cd08231  178 GDTVVVQGAGPlGLYAVAaAKLAGARRVIVIDGSPERLELAREfgaDATIDIDELPDpqrraiVRDITGGRGADVVI 254
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 93-159 4.27e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 35.42  E-value: 4.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 514963311   93 LDFGAGSGVVAIA-AKMAGAKRVICCDIDPVSLASCRENALLND------VELEYLDDLYQ-SEPVDVLLAADVL 159
Cdd:pfam08242   1 LEIGCGTGTLLRAlLEALPGLEYTGLDISPAALEAARERLAALGllnavrVELFQLDLGELdPGSFDVVVASNVL 75
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 89-129 4.75e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 37.43  E-value: 4.75e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 514963311  89 DKVVLDFGAGS-GV-VAIAAKMAGAKRVICCDIDPVSLASCRE 129
Cdd:COG1063  162 GDTVLVIGAGPiGLlAALAARLAGAARVIVVDRNPERLELARE 204
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 90-154 6.06e-03

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 36.83  E-value: 6.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 514963311  90 KVVLDFGAGS-GVVAIA-AKMAGAKRVICCDIDPVSLASCRENA---LLNDVELEYLD--DLYQSEPVDVLL 154
Cdd:cd05281  165 KSVLITGCGPiGLMAIAvAKAAGASLVIASDPNPYRLELAKKMGadvVINPREEDVVEvkSVTDGTGVDVVL 236
 
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.
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