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Conserved domains on  [gi|21356361|ref|NP_650017|]
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arginine methyltransferase 1 [Drosophila melanogaster]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 1905023)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
66-231 5.98e-43

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 149.42  E-value: 5.98e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  66 HEEMLKDEVRTVTYRNAMYHnkHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITV 144
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361 145 VKGKIEEIELPngiEGVDIIISEWMGYCLFYESMLDTVLYARDKWLKKDGMMFPDRGTLYITAIEDRQYKDekiNWWDD- 223
Cdd:COG4076  90 INADATDLDLP---EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAE---GFEDWq 163


                ....*...
gi 21356361 224 VYGFDMSC 231
Cdd:COG4076 164 FDGFDFRL 171
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
66-231 5.98e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 149.42  E-value: 5.98e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  66 HEEMLKDEVRTVTYRNAMYHnkHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITV 144
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361 145 VKGKIEEIELPngiEGVDIIISEWMGYCLFYESMLDTVLYARDKWLKKDGMMFPDRGTLYITAIEDRQYKDekiNWWDD- 223
Cdd:COG4076  90 INADATDLDLP---EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAE---GFEDWq 163


                ....*...
gi 21356361 224 VYGFDMSC 231
Cdd:COG4076 164 FDGFDFRL 171
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 95-194 8.38e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    95 VLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQdvITVVKGKIEEIELPNGieGVDIIISeWMGYCL 173
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGLN--VEFVQGDAEDLPFPDG--SFDLVVS-SGVLHH 75

                          90       100
                  ....*....|....*....|...
gi 21356361   174 FYESMLDTVL--YARdkWLKKDG 194
Cdd:pfam13649  76 LPDPDLEAALreIAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-194 1.48e-14

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: 69.00  E-value: 1.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  94 TVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVViDNNLQDVITVVKGKIEEIeLPNGIEGVDIIISeWMGYC 172
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISpVALELARKAA-AALLADNVEVLKGDAEEL-PPEADESFDVIIS-DPPLH 77

                        90       100
                ....*....|....*....|..
gi 21356361 173 LFYESMLDTVLYARDKwLKKDG 194
Cdd:cd02440  78 HLVEDLARFLEEARRL-LKPGG 98
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
87-165 3.39e-12

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 65.56  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   87 KHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDcsnIIEFARQVVIDN-NLQDVitvvkgkIEEIELPNGIEGVDIII 165
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAARENaELNGV-------ELNVYLPQGDLKADVIV 184
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 92-165 2.37e-07

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: 51.76  E-value: 2.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356361    92 GKTVLDVGCGTGILSMFAAKAGAAQVIAVDC-SNIIEFARQVVIDNNLQDVITV-VKGKIEEIELPngiegVDIII 165
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAKVVGIDIdPLAVESARKNAELNQVSDRLQVkLIYLEQPIEGK-----ADVIV 230
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
66-231 5.98e-43

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 149.42  E-value: 5.98e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  66 HEEMLKDEVRTVTYRNAMYHnkHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITV 144
Cdd:COG4076  12 HHPMLNDVERNDAFKAAIER--VVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNpDIAAVARRIIAANGLSDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361 145 VKGKIEEIELPngiEGVDIIISEWMGYCLFYESMLDTVLYARDKWLKKDGMMFPDRGTLYITAIEDRQYKDekiNWWDD- 223
Cdd:COG4076  90 INADATDLDLP---EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNAAQPVESPVDAE---GFEDWq 163


                ....*...
gi 21356361 224 VYGFDMSC 231
Cdd:COG4076 164 FDGFDFRL 171
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
87-165 5.54e-16

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 77.52  E-value: 5.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  87 KHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDcsnIIEFARQVVID----NNLQDVITVVKGKIEEielpngIEGVD 162
Cdd:COG2264 144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVD---IDPVAVEAAREnaelNGVEDRIEVVLGDLLE------DGPYD 214


                ...
gi 21356361 163 III 165
Cdd:COG2264 215 LVV 217
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 95-194 8.38e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 8.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    95 VLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQdvITVVKGKIEEIELPNGieGVDIIISeWMGYCL 173
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSpEMLERARERAAEAGLN--VEFVQGDAEDLPFPDG--SFDLVVS-SGVLHH 75

                          90       100
                  ....*....|....*....|...
gi 21356361   174 FYESMLDTVL--YARdkWLKKDG 194
Cdd:pfam13649  76 LPDPDLEAALreIAR--VLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 94-194 1.48e-14

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: 69.00  E-value: 1.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  94 TVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVViDNNLQDVITVVKGKIEEIeLPNGIEGVDIIISeWMGYC 172
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISpVALELARKAA-AALLADNVEVLKGDAEEL-PPEADESFDVIIS-DPPLH 77

                        90       100
                ....*....|....*....|..
gi 21356361 173 LFYESMLDTVLYARDKwLKKDG 194
Cdd:cd02440  78 HLVEDLARFLEEARRL-LKPGG 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 92-197 2.46e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 67.26  E-value: 2.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITVVKGKIEEIELPngiEGVDIIIS---- 166
Cdd:COG2230  52 GMRVLDIGCGWGGLALYLARRYGVRVTGVTLSpEQLEYARERAAEAGLADRVEVRLADYRDLPAD---GQFDAIVSigmf 128

                        90       100       110
                ....*....|....*....|....*....|.
gi 21356361 167 EWMGYcLFYESMLDTVlyarDKWLKKDGMMF 197
Cdd:COG2230 129 EHVGP-ENYPAYFAKV----ARLLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 86-197 4.02e-13

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: 65.42  E-value: 4.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  86 NKHLFQGKTVLDVGCGTGILSMFAAKAGaAQVIAVDCS-NIIEFARQVVIDNNlqdvITVVKGKIEEIELPNGieGVDII 164
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISpEALEIARERAAELN----VDFVQGDLEDLPLEDG--SFDLV 91

                        90       100       110
                ....*....|....*....|....*....|...
gi 21356361 165 ISewmGYCLFYESMLDTVLYARDKWLKKDGMMF 197
Cdd:COG2227  92 IC---SEVLEHLPDPAALLRELARLLKPGGLLL 121
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
87-165 3.39e-12

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 65.56  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   87 KHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDcsnIIEFARQVVIDN-NLQDVitvvkgkIEEIELPNGIEGVDIII 165
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVD---IDPQAVEAARENaELNGV-------ELNVYLPQGDLKADVIV 184
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 91-166 6.72e-11

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: 61.70  E-value: 6.72e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356361  91 QGKTVLDVGCGTGILS-MFAAKAGAAQVIAVDC-SNIIEFARQVVIDNNLQDVITVVKGKIEEIELPNGIEGVDIIIS 166
Cdd:COG4123  37 KGGRVLDLGTGTGVIAlMLAQRSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVS 114
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 92-166 1.18e-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: 59.24  E-value: 1.18e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356361  92 GKTVLDVGCGTGILSMFAAKAGaAQVIAVDCS-NIIEFARQVVIDNNLQdvITVVKGKIEEIELPNGieGVDIIIS 166
Cdd:COG2226  23 GARVLDLGCGTGRLALALAERG-ARVTGVDISpEMLELARERAAEAGLN--VEFVVGDAEDLPFPDG--SFDLVIS 93
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 90-192 1.71e-10

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: 60.28  E-value: 1.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  90 FQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDC-SNIIEFARQVVIDNNLQdvITVVKGKIEEielPNGIEGVDIII-SE 167
Cdd:COG3897  69 VAGKRVLELGCGLGLVGIAAAKAGAADVTATDYdPEALAALRLNAALNGVA--ITTRLGDWRD---PPAAGGFDLILgGD 143

                        90       100
                ....*....|....*....|....*.
gi 21356361 168 wmgycLFYE-SMLDTVLyardKWLKK 192
Cdd:COG3897 144 -----VLYErDLAEPLL----PFLDR 160
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
90-166 3.60e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 58.76  E-value: 3.60e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356361  90 FQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVidNNLQDVITVVKGKIEEIELpngIEGVDIIIS 166
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDpEALEIARENA--ERLGVRVDFIRADVTRIPL---GGSVDTVVM 116
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 87-166 2.37e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 53.77  E-value: 2.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  87 KHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCSNI-IEFARQVVIDNNLQDViTVVKGKIEEIElPNGIEGVDIII 165
Cdd:COG0500  22 ERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEaIALARARAAKAGLGNV-EFLVADLAELD-PLPAESFDLVV 99


                .
gi 21356361 166 S 166
Cdd:COG0500 100 A 100
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
91-166 2.70e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 50.98  E-value: 2.70e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356361  91 QGKTVLDVGCGTGILS-MFAAKAGAAQVIAVD-CSNIIEFARQvvidnNLQDViTVVKGKIEEIELPngiEGVDIIIS 166
Cdd:COG4106   1 PPRRVLDLGCGTGRLTaLLAERFPGARVTGVDlSPEMLARARA-----RLPNV-RFVVADLRDLDPP---EPFDLVVS 69
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 92-166 4.49e-08

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: 52.50  E-value: 4.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCGTGILSMFAAKAGA-AQVIAVDCSNI-IEFARQVVIDNNLQDVitvvkgkieEIELPNGIEGV-----DII 164
Cdd:COG2813  50 GGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNARaVELARANAAANGLENV---------EVLWSDGLSGVpdgsfDLI 120


                ..
gi 21356361 165 IS 166
Cdd:COG2813 121 LS 122
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 89-173 9.73e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 52.46  E-value: 9.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   89 LFQGKTVLDVGCGTGILSMFAAKAG--AAQVIAVD-CSNIIEFARQVVIDNNLQDVITVVKGKIEEIELPNgiEGVDIII 165
Cdd:PRK00216  49 VRPGDKVLDLACGTGDLAIALAKAVgkTGEVVGLDfSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPD--NSFDAVT 126


                 ....*...
gi 21356361  166 sewMGYCL 173
Cdd:PRK00216 127 ---IAFGL 131
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 91-165 9.78e-08

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: 53.04  E-value: 9.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356361    91 QGKTVLDVGCGTGILSMFAAKAGAAQVIAVDcsnIIEFARQVVIDNNLQDVITvvkgKIEEIELPNGI--EGVDIII 165
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVD---IDPVAVRAAKENAELNGVE----ARLEVYLPGDLpkEKADVVV 230
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 92-165 2.37e-07

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: 51.76  E-value: 2.37e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21356361    92 GKTVLDVGCGTGILSMFAAKAGAAQVIAVDC-SNIIEFARQVVIDNNLQDVITV-VKGKIEEIELPngiegVDIII 165
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAKVVGIDIdPLAVESARKNAELNQVSDRLQVkLIYLEQPIEGK-----ADVIV 230
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 96-197 2.57e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.04  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    96 LDVGCGTGILSMFAAKAGaAQVIAVD-CSNIIEFARQVVIDNNLqdviTVVKGKIEEIELPNGIegVDIIISEWMgycLF 174
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDiSPEMLELAREKAPREGL----TFVVGDAEDLPFPDNS--FDLVLSSEV---LH 70

                          90       100
                  ....*....|....*....|...
gi 21356361   175 YESMLDTVLYARDKWLKKDGMMF 197
Cdd:pfam08241  71 HVEDPERALREIARVLKPGGILI 93
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 92-166 6.63e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.57  E-value: 6.63e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356361    92 GKTVLDVGCGTGILSMFAAK--AGAAQVIAVDCS-NIIEFARQVVIDNNLQDViTVVKGKIEEIELPNGIEGVDIIIS 166
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISeEAIEKARENAQKLGFDNV-EFEQGDIEELPELLEDDKFDVVIS 80
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 88-147 3.78e-06

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: 48.25  E-value: 3.78e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21356361  88 HLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCSN-IIEFARQVVIDNNLQDVITVVKG 147
Cdd:COG1092 213 ELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSAtALEWAKENAALNGLDDRHEFVQA 273
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 92-165 4.30e-06

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: 48.21  E-value: 4.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCGT-GILSMFAAKA-GAAQVIAVDCS-NIIEFARQ----VVIDNNLQDVITVVKgkieeiELPNGiEGVDII 164
Cdd:COG1063 162 GDTVLVIGAGPiGLLAALAARLaGAARVIVVDRNpERLELARElgadAVVNPREEDLVEAVR------ELTGG-RGADVV 234


                .
gi 21356361 165 I 165
Cdd:COG1063 235 I 235
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 76-165 4.62e-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: 47.70  E-value: 4.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  76 TVTYRnAMYHNKHLFQGKTVLDVGCGT-GILSMFAAKAGAAQVIAVDCSNI-IEFARQVVIDnnlqDVITVVKGKIEEIE 153
Cdd:cd05188 120 ATAYH-ALRRAGVLKPGDTVLVLGAGGvGLLAAQLAKAAGARVIVTDRSDEkLELAKELGAD----HVIDYKEEDLEEEL 194

                        90
                ....*....|..
gi 21356361 154 LPNGIEGVDIII 165
Cdd:cd05188 195 RLTGGGGADVVI 206
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 92-152 8.77e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 46.37  E-value: 8.77e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21356361   92 GKTVLDVGCGTGILSMFAAKAGaAQVIAVDCS-NIIEFARQVVIDNNLQDVITVVKGKIEEI 152
Cdd:PRK07580  64 GLRILDAGCGVGSLSIPLARRG-AKVVASDISpQMVEEARERAPEAGLAGNITFEVGDLESL 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
50-166 1.08e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 45.37  E-value: 1.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  50 MTSRDY---YFDSYAHfgIHEEMLkdeVRTVTYRNAMYHNKHLFQ------GKTVLDVGCGTGILSMFAAKAGaAQVIAV 120
Cdd:COG4976   1 MALDAYveaLFDQYAD--SYDAAL---VEDLGYEAPALLAEELLArlppgpFGRVLDLGCGTGLLGEALRPRG-YRLTGV 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21356361 121 DCS-NIIEFARQvvidNNLQDviTVVKGKIEEIELPNGieGVDIIIS 166
Cdd:COG4976  75 DLSeEMLAKARE----KGVYD--RLLVADLADLAEPDG--RFDLIVA 113
PRK14967 PRK14967
putative methyltransferase; Provisional
 88-123 1.31e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.81  E-value: 1.31e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 21356361   88 HLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS 123
Cdd:PRK14967  33 GLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDIS 68
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 87-194 1.43e-05

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 46.24  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    87 KHL--FQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCSNI----IEFARQVVIDNNLqdvitvvkgkieEIELPNGIE- 159
Cdd:pfam08003 109 PHLspLKGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELflcqFEAVRKLLGNDQR------------AHLLPLGIEq 176

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 21356361   160 -----GVDIIISewMGYCLFYESMLDTVLYARDKwLKKDG 194
Cdd:pfam08003 177 lpalaAFDTVFS--MGVLYHRRSPLDHLLQLKDQ-LVKGG 213
PRK14968 PRK14968
putative methyltransferase; Provisional
 92-121 2.08e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.89  E-value: 2.08e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 21356361   92 GKTVLDVGCGTGILSMFAAKAGaAQVIAVD 121
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNG-KKVVGVD 52
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 91-166 3.45e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.14  E-value: 3.45e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356361  91 QGKTVLDVGCGTGILSMFAAKA-GAAQVIAVDCSNI-IEFARQVVIDNNLQDVITVVKGKIEEiELPnGIEGVDIIIS 166
Cdd:COG2890 112 APPRVLDLGTGSGAIALALAKErPDARVTAVDISPDaLAVARRNAERLGLEDRVRFLQGDLFE-PLP-GDGRFDLIVS 187
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 92-164 6.25e-05

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: 44.53  E-value: 6.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCG-TGILSMFAAKA-GAAQVIAVDCSNI-IEFARQ----VVIDNNLQDVITVVKGKieeielpnGIEGVDII 164
Cdd:cd05281 164 GKSVLITGCGpIGLMAIAVAKAaGASLVIASDPNPYrLELAKKmgadVVINPREEDVVEVKSVT--------DGTGVDVV 235
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 92-165 6.66e-05

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. 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. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has 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. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 44.53  E-value: 6.66e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356361  92 GKTVLDVGCGT-GILSMFAAKA-GAAQVIAVDCS-NIIEFARQVVIDnnlqDVITVVKGKIEEIELPNGIEGVDIII 165
Cdd:cd08236 160 GDTVVVIGAGTiGLLAIQWLKIlGAKRVIAVDIDdEKLAVARELGAD----DTINPKEEDVEKVRELTEGRGADLVI 232
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 92-166 1.18e-04

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: 42.19  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    92 GKTVLDVGCGTGILSMFAAKAGaaQVIAVDCSNI----IEFARQVVIDNNLqDVITVVKGkieeielpNGIEGV-----D 162
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKES--PDAELTMVDInaraLESARENLAANGL-ENGEVVAS--------DVYSGVedgkfD 100


                  ....
gi 21356361   163 IIIS 166
Cdd:pfam05175 101 LIIS 104
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 96-195 1.40e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 40.43  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    96 LDVGCGTG-ILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITVVKGKIEEIELPngIEGVDIIIsewMGYCL 173
Cdd:pfam08242   1 LEIGCGTGtLLRALLEALPGLEYTGLDISpAALEAARERLAALGLLNAVRVELFQLDLGELD--PGSFDVVV---ASNVL 75

                          90       100
                  ....*....|....*....|..
gi 21356361   174 FYESMLDTVLYARDKWLKKDGM 195
Cdd:pfam08242  76 HHLADPRAVLRNIRRLLKPGGV 97
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 87-121 2.26e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 41.42  E-value: 2.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 21356361    87 KHLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVD 121
Cdd:pfam01728  17 GLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVD 51
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
62-156 2.66e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 42.20  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   62 HFGIHEEMLKdevRTVTYRNamyhnkhLFQGKTVLDVGCGTGILSMFAAKAgAAQVIAV--DcSNIIEFARQVVIDNNLq 139
Cdd:PRK14896  10 HFLIDDRVVD---RIVEYAE-------DTDGDPVLEIGPGKGALTDELAKR-AKKVYAIelD-PRLAEFLRDDEIAAGN- 76

                         90
                 ....*....|....*..
gi 21356361  140 dvITVVKGKIEEIELPN 156
Cdd:PRK14896  77 --VEIIEGDALKVDLPE 91
PRK08317 PRK08317
hypothetical protein; Provisional
 88-167 3.08e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 41.85  E-value: 3.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   88 HLFQGKTVLDVGCGTGILSM-FAAKAGAA-QVIAVDCS-NIIEFARQVVIDNNLQdvITVVKGKIEEIELPNgiEGVDII 164
Cdd:PRK08317  16 AVQPGDRVLDVGCGPGNDAReLARRVGPEgRVVGIDRSeAMLALAKERAAGLGPN--VEFVRGDADGLPFPD--GSFDAV 91


                 ...
gi 21356361  165 ISE 167
Cdd:PRK08317  92 RSD 94
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 88-196 4.48e-04

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: 41.54  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    88 HLFQGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITVVKGKIEEIElpngiEGVDIIIS 166
Cdd:pfam02353  58 GLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSkNQYKLARKRVAAEGLARKVEVLLQDYRDFD-----EPFDRIVS 132

                          90       100       110
                  ....*....|....*....|....*....|
gi 21356361   167 EWMGYCLFYESmLDTVLYARDKWLKKDGMM 196
Cdd:pfam02353 133 VGMFEHVGHEN-YDTFFKKLYNLLPPGGLM 161
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 58-158 5.28e-04

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


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 41.69  E-value: 5.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  58 DSYAHFGIHeeMLKDEVRTVTYrNAMyhnkHLFQGKTVLDVGCGTGILSMFAAKAG-AAQVIAVD-----CSNIIEFARQ 131
Cdd:COG2242 221 EAFERDKGP--ITKREVRALTL-AKL----ALRPGDVLWDIGAGSGSVSIEAARLApGGRVYAIErdperAALIRANARR 293

                        90       100       110
                ....*....|....*....|....*....|.
gi 21356361 132 VVIDNnlqdvITVVKGK----IEEIELPNGI 158
Cdd:COG2242 294 FGVPN-----VEVVEGEapeaLADLPDPDAV 319
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
101-196 5.66e-04

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 39.51  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   101 GTGILSMFAAKAGAAQVIAVDCS-NIIEFARQ----VVIDNNLQDVITVVKgkieeiELPNGiEGVDIIISewmgyCLFY 175
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSeEKLELAKElgadHVINPKETDLVEEIK------ELTGG-KGVDVVFD-----CVGS 68

                          90       100
                  ....*....|....*....|.
gi 21356361   176 ESMLDTVLYArdkwLKKDGMM 196
Cdd:pfam00107  69 PATLEQALKL----LRPGGRV 85
arsM PRK11873
arsenite methyltransferase;
92-166 6.45e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 41.09  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   92 GKTVLDVGCGTGILSMFAAKA-GA-AQVIAVDCS-NIIEFARqvviDNNLQDVITVV---KGKIEEIELPNGIegVDIII 165
Cdd:PRK11873  78 GETVLDLGSGGGFDCFLAARRvGPtGKVIGVDMTpEMLAKAR----ANARKAGYTNVefrLGEIEALPVADNS--VDVII 151


                 .
gi 21356361  166 S 166
Cdd:PRK11873 152 S 152
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 87-179 6.77e-04

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: 40.01  E-value: 6.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    87 KHLFQGKTVLDVGCGTGILS-MFAAKAGAAQVIAVDCSNIIEFARQVVIDNNLQDVITVvkgKI----EEIElPNGIEG- 160
Cdd:pfam10294  42 ANNLSGLNVLELGSGTGLVGiAVALLLPGASVTITDLEEALELLKKNIELNALSSKVVV---KVldwgENLP-PDLFDGh 117

                          90       100
                  ....*....|....*....|
gi 21356361   161 -VDIIIsewMGYCLFYESML 179
Cdd:pfam10294 118 pVDLIL---AADCVYNEDSF 134
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 69-165 6.81e-04

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 39.24  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    69 MLKDEVRTVTYRNAmyhnkHLFQGKTVLDVGCGTGILSMFAAKA-GAAQVIAVD-----CSNIIEFARQVVIDNnlqdvI 142
Cdd:TIGR02469   2 MTKREVRALTLAKL-----RLRPGDVLWDIGAGTGSVTIEAARLvPNGRVYAIErnpeaLDLIERNLRRFGVSN-----I 71

                          90       100
                  ....*....|....*....|...
gi 21356361   143 TVVKGKIEEIeLPNGIEGVDIII 165
Cdd:TIGR02469  72 VIVEGDAPEA-PEALLPDPDAVF 93
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 92-165 7.73e-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: 41.32  E-value: 7.73e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21356361  92 GKTVLDVGCGTGILSMFAAKAgAAQVIAVDCS-NIIEFARQVVIDNNLQDViTVVKGKIEEI--ELPNGiEGVDIII 165
Cdd:COG2265 234 GERVLDLYCGVGTFALPLARR-AKKVIGVEIVpEAVEDARENARLNGLKNV-EFVAGDLEEVlpELLWG-GRPDVVV 307
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 91-165 8.23e-04

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-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) to highlight its broad range of activities and to distinguish 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. Active site zinc has a catalytic role, while structural zinc aids in stability. 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: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 41.04  E-value: 8.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  91 QGKTVLDVGCG-TGILSMFAAKA-GAAQVIAVDCS-NIIEFARQV----VIDNNLQDVITVVKgkieeiELPNGiEGVDI 163
Cdd:cd08235 165 PGDTVLVIGAGpIGLLHAMLAKAsGARKVIVSDLNeFRLEFAKKLgadyTIDAAEEDLVEKVR------ELTDG-RGADV 237


                ..
gi 21356361 164 II 165
Cdd:cd08235 238 VI 239
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 86-166 1.01e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 40.35  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    86 NKHLFQGKTVLDVGCGTGILS-MFAAKAGAAQVIAVD-CSNIIEFARQvviDNNLQdvITVVKGKIEEIELPNGIegVDI 163
Cdd:TIGR02072  29 EKGIFIPASVLDIGCGTGYLTrALLKRFPQAEFIALDiSAGMLAQAKT---KLSEN--VQFICGDAEKLPLEDSS--FDL 101


                  ...
gi 21356361   164 IIS 166
Cdd:TIGR02072 102 IVS 104
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 92-165 1.03e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (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 includes various 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. 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 40.64  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCG-TGILSMFAAKAGAAQVIAVDCS-NIIEFARQV----VIDNNLQDVITVVKgkieeiELPNGiEGVDIII 165
Cdd:cd08261 160 GDTVLVVGAGpIGLGVIQVAKARGARVIVVDIDdERLEFARELgaddTINVGDEDVAARLR------ELTDG-EGADVVI 232
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 92-165 1.05e-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: 40.55  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCGT-GILSMFAAKA-GAAQVIAVDCS-NIIEFARQV----VIDNNLQDVITVVKGKIEEIelpnGIEGVDII 164
Cdd:cd05285 163 GDTVLVFGAGPiGLLTAAVAKAfGATKVVVTDIDpSRLEFAKELgathTVNVRTEDTPESAEKIAELL----GGKGPDVV 238


                .
gi 21356361 165 I 165
Cdd:cd05285 239 I 239
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 69-152 1.24e-03

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 39.78  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   69 MLKDEVRTVTYRNAmyhnkHLFQGKTVLDVGCGTGILSMFAA--KAGAAQVIAVDCS-NIIEFARQVVIDNNLQDVITVV 145
Cdd:PRK00377  23 MTKEEIRALALSKL-----RLRKGDMILDIGCGTGSVTVEASllVGETGKVYAVDKDeKAINLTRRNAEKFGVLNNIVLI 97


                 ....*..
gi 21356361  146 KGKIEEI 152
Cdd:PRK00377  98 KGEAPEI 104
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 91-166 1.26e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361   91 QGKTVLDVGCGTGILS-MFAAKAGAAQVIAVDCSNI-IEFARQvVIDNNLQDVITVVKGkieeiELPNGIEG--VDIIIS 166
Cdd:PRK09328 108 EPLRVLDLGTGSGAIAlALAKERPDAEVTAVDISPEaLAVARR-NAKHGLGARVEFLQG-----DWFEPLPGgrFDLIVS 181
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 91-123 1.82e-03

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 39.84  E-value: 1.82e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 21356361   91 QGKTVLDVGCGTGILSMFAAKAGAAqVIAVDCS 123
Cdd:PLN02585 144 AGVTVCDAGCGTGSLAIPLALEGAI-VSASDIS 175
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 91-132 3.03e-03

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: 39.14  E-value: 3.03e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 21356361  91 QGKTVLDVGCGT-GILSMFAAK-AGAAQVIAVDCSNI-IEFARQV 132
Cdd:cd08232 165 AGKRVLVTGAGPiGALVVAAARrAGAAEIVATDLADApLAVARAM 209
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 92-167 3.05e-03

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: 38.01  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  92 GKTVLDVGCGTGILSMFAAKAGaAQVIAVDCS-NIIEFARQvvidnNLQ----DVITVVKGKIEEIELPNgiEGVDIIIS 166
Cdd:COG1041  27 GDTVLDPFCGTGTILIEAGLLG-RRVIGSDIDpKMVEGARE-----NLEhygyEDADVIRGDARDLPLAD--ESVDAIVT 98


                .
gi 21356361 167 E 167
Cdd:COG1041  99 D 99
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
91-165 3.13e-03

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 39.12  E-value: 3.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  91 QGKTVLDVGCGTGILSMFAAKAGAAQVIAVDCS-NIIEFARQ---------VVIDNNLQDVITVVKgkieeiELPNgiEG 160
Cdd:COG2521 132 RGDRVLDTCTGLGYTAIEALKRGAREVITVEKDpNVLELAELnpwsrelanERIKIILGDASEVIK------TFPD--ES 203


                ....*
gi 21356361 161 VDIII 165
Cdd:COG2521 204 FDAII 208
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 89-222 4.90e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.41  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361    89 LFQGKTVLDVGCGTGILSMFAAKAGaAQVIAVD--CSNIIEFARQVVIDNNLQDVITVVKGKIeeielpngiegvDIIIS 166
Cdd:pfam13489  20 LPSPGRVLDFGCGTGIFLRLLRAQG-FSVTGVDpsPIAIERALLNVRFDQFDEQEAAVPAGKF------------DVIVA 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21356361   167 eWMGYC--LFYESMLDTVLyardKWLKKDGMMF---PDRGTLYITAIEDRQY---KDEKINWWD 222
Cdd:pfam13489  87 -REVLEhvPDPPALLRQIA----ALLKPGGLLLlstPLASDEADRLLLEWPYlrpRNGHISLFS 145
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 91-165 9.69e-03

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. 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: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 37.64  E-value: 9.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356361  91 QGKTVLDVGCG-TGILSMFAAKA-GAAQVIAVDCSNI-IEFARQVVIDnnlqDVITVVKGKIEE--IELPNGiEGVDIII 165
Cdd:cd05278 167 PGSTVAVIGAGpVGLCAVAGARLlGAARIIAVDSNPErLDLAKEAGAT----DIINPKNGDIVEqiLELTGG-RGVDCVI 241
 
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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