NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2796455541|ref|WP_373170139|]
View 

methyltransferase domain-containing protein [Klebsiella sp. Q11]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 19424246)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 23-141 6.61e-26

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


:

Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 98.85  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  23 EKYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEE 102
Cdd:COG2230    38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2796455541 103 KCDIAACVGATWIAG--GVAGTIELLSKSLKPGGMLLIGEP 141
Cdd:COG2230   118 QFDAIVSIGMFEHVGpeNYPAYFAKVARLLKPGGRLLLHTP 158
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 4-244 1.39e-03

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.).


The actual alignment was detected with superfamily member pfam08704:

Pssm-ID: 473071  Cd Length: 242  Bit Score: 39.01  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541   4 PRIFTISESaHRIHNPFTPEkYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEE 81
Cdd:pfam08704  10 PELWTLNLP-HRTQILYTPD-ISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGhlFTFEFHEQRADKAREEFRE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  82 LGVADRVTFIHQDAA--GYVVEEKCDIAAC---VGATWIAggvagtIELLSKSLK-PGGMLLIGEPYWRQVPATeeiAQA 155
Cdd:pfam08704  88 HGIDQLVTVTHRDVCkeGFLTEVSGKADAVfldLPSPWEA------VPHAWKALKvEGGRFCSFSPCIEQVQRT---CQA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 156 CGASSLADFLTLADLVSSYDAlgyDLVEMVLADqEGWDRYEAAKwltmRRWLEENPDDEFVPEVR--AELTMAPKRHTTy 233
Cdd:pfam08704 159 LAELGFTEISTLEVLLRVYDV---RTVSLPVID-LGIDREKENE----RTRTEGLSNDDKSEDNSgnSMLGTALKPMSE- 229

                         250
                  ....*....|.
gi 2796455541 234 TREYFGWGVFA 244
Cdd:pfam08704 230 AVGHTGYLTFA 240
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 23-141 6.61e-26

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 98.85  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  23 EKYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEE 102
Cdd:COG2230    38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2796455541 103 KCDIAACVGATWIAG--GVAGTIELLSKSLKPGGMLLIGEP 141
Cdd:COG2230   118 QFDAIVSIGMFEHVGpeNYPAYFAKVARLLKPGGRLLLHTP 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-138 1.29e-12

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: 62.45  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  39 RILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKlRAEELGVADRVTFIHQDAAGYVVE--EKCDIAACVGA-TWI 115
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEadESFDVIISDPPlHHL 79

                          90       100
                  ....*....|....*....|...
gi 2796455541 116 AGGVAGTIELLSKSLKPGGMLLI 138
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-134 6.42e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  40 ILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVadRVTFIHQDAAGY-VVEEKCDIAACVGA---TWI 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpFPDGSFDLVVSSGVlhhLPD 78

                          90
                  ....*....|....*....
gi 2796455541 116 AgGVAGTIELLSKSLKPGG 134
Cdd:pfam13649  79 P-DLEAALREIARVLKPGG 96
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 33-170 7.45e-10

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 57.48  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  33 RMKAGTRILDLGSGSGEMLCTWAREH-GIRGIGVDMS--ALfsEQAKLRAEELGVaDRVTFIHQDAAGYVVEEKCD---- 105
Cdd:TIGR03534  83 RLKKGPRVLDLGTGSGAIALALAKERpDARVTAVDISpeAL--AVARKNARRLGL-ENVEFLQGDWFEPLPSGKFDlivs 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 106 ----IAACVGAT----------WIA--GGVAGT------IELLSKSLKPGGMLL--IGepyWRQVPATEEIAQACGassL 161
Cdd:TIGR03534 160 nppyIPEADIHLldpevrdfepRLAlfGGEDGLdfyrriIAQAPRLLKPGGWLLleIG---YDQGEAVRALFEAAG---F 233


                  ....*....
gi 2796455541 162 ADFLTLADL 170
Cdd:TIGR03534 234 ADVETRKDL 242
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
39-136 7.88e-07

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 48.81  E-value: 7.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  39 RILDLGSGSGEMLCTWArEHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIH---QDAAGYvVEEKCDIA---ACVga 112
Cdd:PRK11036   47 RVLDAGGGEGQTAIKLA-ELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHcaaQDIAQH-LETPVDLIlfhAVL-- 122

                          90       100
                  ....*....|....*....|....
gi 2796455541 113 TWIAGGVAgTIELLSKSLKPGGML 136
Cdd:PRK11036  123 EWVADPKS-VLQTLWSVLRPGGAL 145
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
38-190 1.18e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 47.80  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541   38 TRILDLGSGSGEMLCTWAREHG-IRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEEKCDIA-ACVGATWI 115
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVfGFEVIHHI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796455541  116 A--GGVAGTIellSKSLKPGGMLLIGEPYWRQVPATEEiaqacgASSLADFLTLADLVSSYDALGYDLVEMVLADQE 190
Cdd:smart00828  81 KdkMDLFSNI---SRHLKDGGHLVLADFIANLLSAIEH------EETTSYLVTREEWAELLARNNLRVVEGVDASLE 148
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 4-244 1.39e-03

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 39.01  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541   4 PRIFTISESaHRIHNPFTPEkYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEE 81
Cdd:pfam08704  10 PELWTLNLP-HRTQILYTPD-ISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGhlFTFEFHEQRADKAREEFRE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  82 LGVADRVTFIHQDAA--GYVVEEKCDIAAC---VGATWIAggvagtIELLSKSLK-PGGMLLIGEPYWRQVPATeeiAQA 155
Cdd:pfam08704  88 HGIDQLVTVTHRDVCkeGFLTEVSGKADAVfldLPSPWEA------VPHAWKALKvEGGRFCSFSPCIEQVQRT---CQA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 156 CGASSLADFLTLADLVSSYDAlgyDLVEMVLADqEGWDRYEAAKwltmRRWLEENPDDEFVPEVR--AELTMAPKRHTTy 233
Cdd:pfam08704 159 LAELGFTEISTLEVLLRVYDV---RTVSLPVID-LGIDREKENE----RTRTEGLSNDDKSEDNSgnSMLGTALKPMSE- 229

                         250
                  ....*....|.
gi 2796455541 234 TREYFGWGVFA 244
Cdd:pfam08704 230 AVGHTGYLTFA 240
 
Name Accession Description Interval E-value
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 23-141 6.61e-26

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 98.85  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  23 EKYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEE 102
Cdd:COG2230    38 AKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADG 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2796455541 103 KCDIAACVGATWIAG--GVAGTIELLSKSLKPGGMLLIGEP 141
Cdd:COG2230   118 QFDAIVSIGMFEHVGpeNYPAYFAKVARLLKPGGRLLLHTP 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 23-157 7.79e-14

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: 66.56  E-value: 7.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  23 EKYAALGRALRMKAGTRILDLGSGSGEMLCTWAReHGIRGIGVDMSALFSEQAKLRAEELGVadRVTFIHQDAAGY-VVE 101
Cdd:COG2226     9 DGREALLAALGLRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpFPD 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2796455541 102 EKCDIAACVGATWIAGGVAGTIELLSKSLKPGGMLLIGEPYWRQVPATEEIAQACG 157
Cdd:COG2226    86 GSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAG 141
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-138 1.29e-12

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: 62.45  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  39 RILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKlRAEELGVADRVTFIHQDAAGYVVE--EKCDIAACVGA-TWI 115
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEadESFDVIISDPPlHHL 79

                          90       100
                  ....*....|....*....|...
gi 2796455541 116 AGGVAGTIELLSKSLKPGGMLLI 138
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVLVL 102
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 33-141 2.26e-12

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: 62.34  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  33 RMKAGTRILDLGSGSGEMLCTWAReHGIRGIGVDMSALFSEQAKLRAEELgvadRVTFIHQDAAGYVVE-EKCDIAACVG 111
Cdd:COG2227    21 LLPAGGRVLDVGCGTGRLALALAR-RGADVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEdGSFDLVICSE 95

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2796455541 112 A-TWIAgGVAGTIELLSKSLKPGGMLLIGEP 141
Cdd:COG2227    96 VlEHLP-DPAALLRELARLLKPGGLLLLSTP 125
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
36-138 2.98e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 58.30  E-value: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  36 AGTRILDLGSGSGEMLCTWA-REHGIRGIGVDMSALFSEQAKLRaeelgvADRVTFIHQDAAGYVVEEKCDIAACVGA-T 113
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAeRFPGARVTGVDLSPEMLARARAR------LPNVRFVVADLRDLDPPEPFDLVVSNAAlH 74

                          90       100
                  ....*....|....*....|....*
gi 2796455541 114 WIAgGVAGTIELLSKSLKPGGMLLI 138
Cdd:COG4106    75 WLP-DHAALLARLAAALAPGGVLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 17-192 6.01e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.93  E-value: 6.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  17 HNPFTPEKYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGvADRVTFIHQDAA 96
Cdd:COG0500     7 SDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  97 GY--VVEEKCDIAACVGA-TWIAGGV-AGTIELLSKSLKPGGMLLIgepywrQVPATEEIAQACGASSLADFLTLADLVS 172
Cdd:COG0500    86 ELdpLPAESFDLVVAFGVlHHLPPEErEALLRELARALKPGGVLLL------SASDAAAALSLARLLLLATASLLELLLL 159

                         170       180
                  ....*....|....*....|
gi 2796455541 173 SYDAlgydLVEMVLADQEGW 192
Cdd:COG0500   160 LRLL----ALELYLRALLAA 175
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 40-134 6.42e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.57  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  40 ILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVadRVTFIHQDAAGY-VVEEKCDIAACVGA---TWI 115
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpFPDGSFDLVVSSGVlhhLPD 78

                          90
                  ....*....|....*....
gi 2796455541 116 AgGVAGTIELLSKSLKPGG 134
Cdd:pfam13649  79 P-DLEAALREIARVLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 34-143 2.25e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.43  E-value: 2.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  34 MKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEELGVaDRVTFIHQDA---AGYVVEEKCDIAA 108
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAevVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIeelPELLEDDKFDVVI 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2796455541 109 CVGATWIAGGVAGTIELLSKSLKPGGMLLIGEPYW 143
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDS 114
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 33-170 7.45e-10

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 57.48  E-value: 7.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  33 RMKAGTRILDLGSGSGEMLCTWAREH-GIRGIGVDMS--ALfsEQAKLRAEELGVaDRVTFIHQDAAGYVVEEKCD---- 105
Cdd:TIGR03534  83 RLKKGPRVLDLGTGSGAIALALAKERpDARVTAVDISpeAL--AVARKNARRLGL-ENVEFLQGDWFEPLPSGKFDlivs 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 106 ----IAACVGAT----------WIA--GGVAGT------IELLSKSLKPGGMLL--IGepyWRQVPATEEIAQACGassL 161
Cdd:TIGR03534 160 nppyIPEADIHLldpevrdfepRLAlfGGEDGLdfyrriIAQAPRLLKPGGWLLleIG---YDQGEAVRALFEAAG---F 233


                  ....*....
gi 2796455541 162 ADFLTLADL 170
Cdd:TIGR03534 234 ADVETRKDL 242
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 28-94 1.04e-08

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: 54.00  E-value: 1.04e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796455541  28 LGRALRMKAGTRILDLGSGSGE-MLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQD 94
Cdd:COG4123    29 LAAFAPVKKGGRVLDLGTGTGViALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGD 96
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 31-170 3.67e-08

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.84  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  31 ALRMKAGTRILDLGSGSGEMLCTWAREH-GIRGIGVDMS--ALfsEQAKLRAEELGVADRVTFIHQDAAGYVVE-EKCDI 106
Cdd:COG2890   107 LLPAGAPPRVLDLGTGSGAIALALAKERpDARVTAVDISpdAL--AVARRNAERLGLEDRVRFLQGDLFEPLPGdGRFDL 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 107 AAC----VGATWIA----------------GGVAG------TIELLSKSLKPGGMLLIgEPYWRQVPATEEIAQACGass 160
Cdd:COG2890   185 IVSnppyIPEDEIAllppevrdheprlaldGGEDGldfyrrIIAQAPRLLKPGGWLLL-EIGEDQGEAVRALLEAAG--- 260

                         170
                  ....*....|
gi 2796455541 161 LADFLTLADL 170
Cdd:COG2890   261 FADVETHKDL 270
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 37-163 1.30e-07

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 50.93  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  37 GTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEEKCD-IAACVGAT 113
Cdd:COG2519    92 GARVLEAGTGSGALTLALARAVGPEGkvYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIDEGDVDaVFLDMPDP 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2796455541 114 WIAggvagtIELLSKSLKPGGMLLIGEPYWRQVpatEEIAQACGASSLAD 163
Cdd:COG2519   172 WEA------LEAVAKALKPGGVLVAYVPTVNQV---SKLVEALRESGFTD 212
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
30-138 2.55e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 49.23  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  30 RALRMKAGTRILDLGSGSGemLCT-WAREHGIRGIGVDMSALFSEQAKLRaeelGVADRvtFIHQDAAG-YVVEEKCDIA 107
Cdd:COG4976    40 ARLPPGPFGRVLDLGCGTG--LLGeALRPRGYRLTGVDLSEEMLAKAREK----GVYDR--LLVADLADlAEPDGRFDLI 111

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2796455541 108 ACVGATWIAGGVAGTIELLSKSLKPGGMLLI 138
Cdd:COG4976   112 VAADVLTYLGDLAAVFAGVARALKPGGLFIF 142
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 38-182 5.85e-07

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: 48.82  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  38 TRILDLGSGSGEMLCTWAREH-GIRGIGVDMSALFSEQAKLRAEElgvadRVTFIHQDAAGYVVEE-KCD-IAACVGATW 114
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTKLSE-----NVQFICGDAEKLPLEDsSFDlIVSNLALQW 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796455541 115 iAGGVAGTIELLSKSLKPGGMLLIGEPywrqVPAT-EEIAQACGASSLaDFLTLADLVSSYDALGYDLV 182
Cdd:TIGR02072 111 -CDDLSQALSELARVLKPGGLLAFSTF----GPGTlHELRQSFGQHGL-RYLSLDELKALLKNSFELLT 173
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
39-136 7.88e-07

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 48.81  E-value: 7.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  39 RILDLGSGSGEMLCTWArEHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIH---QDAAGYvVEEKCDIA---ACVga 112
Cdd:PRK11036   47 RVLDAGGGEGQTAIKLA-ELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHcaaQDIAQH-LETPVDLIlfhAVL-- 122

                          90       100
                  ....*....|....*....|....
gi 2796455541 113 TWIAGGVAgTIELLSKSLKPGGML 136
Cdd:PRK11036  123 EWVADPKS-VLQTLWSVLRPGGAL 145
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
38-190 1.18e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 47.80  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541   38 TRILDLGSGSGEMLCTWAREHG-IRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEEKCDIA-ACVGATWI 115
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHPhLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVfGFEVIHHI 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796455541  116 A--GGVAGTIellSKSLKPGGMLLIGEPYWRQVPATEEiaqacgASSLADFLTLADLVSSYDALGYDLVEMVLADQE 190
Cdd:smart00828  81 KdkMDLFSNI---SRHLKDGGHLVLADFIANLLSAIEH------EETTSYLVTREEWAELLARNNLRVVEGVDASLE 148
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 30-95 2.06e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 47.46  E-value: 2.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796455541  30 RALRMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDmsalFSEQ----AKLRAEELGVADRVTFIHQDA 95
Cdd:PRK00216   45 KWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGevVGLD----FSEGmlavGREKLRDLGLSGNVEFVQGDA 112
PRK08317 PRK08317
hypothetical protein; Provisional
 30-143 5.04e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 46.08  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  30 RALRMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEELGvaDRVTFIHQDAAGYVVeEKCDIA 107
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEGrvVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGLPF-PDGSFD 89

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2796455541 108 ACVG---ATWIAgGVAGTIELLSKSLKPGGMLLIGEPYW 143
Cdd:PRK08317   90 AVRSdrvLQHLE-DPARALAEIARVLRPGGRVVVLDTDW 127
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-138 5.87e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.81  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  41 LDLGSGSGEMLCtWAREHGIRGIGVDMSALFSEQAKLRAEELGvadrVTFIHQDAAGYVVEEK-CDIAACVGATWIAGGV 119
Cdd:pfam08241   1 LDVGCGTGLLTE-LLARLGARVTGVDISPEMLELAREKAPREG----LTFVVGDAEDLPFPDNsFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|....*....
gi 2796455541 120 AGTIELLSKSLKPGGMLLI 138
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 26-170 6.56e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.92  E-value: 6.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  26 AALGRALRmKAGTRILDLGSGSGEMLCTWAREH-GIRGIGVDMS--ALfsEQAKLRAeELGVADRVTFIHQDAAGYVVEE 102
Cdd:PRK09328   99 WALEALLL-KEPLRVLDLGTGSGAIALALAKERpDAEVTAVDISpeAL--AVARRNA-KHGLGARVEFLQGDWFEPLPGG 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 103 KCD--------IAACVGAT----------WIA--GGVAGT------IELLSKSLKPGGMLL--IGepyWRQVPATEEIAQ 154
Cdd:PRK09328  175 RFDlivsnppyIPEADIHLlqpevrdhepHLAlfGGEDGLdfyrriIEQAPRYLKPGGWLLleIG---YDQGEAVRALLA 251

                         170
                  ....*....|....*.
gi 2796455541 155 ACGassLADFLTLADL 170
Cdd:PRK09328  252 AAG---FADVETRKDL 264
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 32-138 9.11e-06

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: 45.78  E-value: 9.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  32 LRMKAGTRILDLGSGSGEMLCTWAREHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDaagYV-VEEKCDIAACV 110
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQD---YRdFDEPFDRIVSV 133

                          90       100       110
                  ....*....|....*....|....*....|
gi 2796455541 111 GATWIAG--GVAGTIELLSKSLKPGGMLLI 138
Cdd:pfam02353 134 GMFEHVGheNYDTFFKKLYNLLPPGGLMLL 163
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
26-109 3.19e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.87  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  26 AALGRALRMKA--GTRILDLGSGSGeMLCTWAREHG-IRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQDAAGYVVEE 102
Cdd:COG4076    23 DAFKAAIERVVkpGDVVLDIGTGSG-LLSMLAARAGaKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPE 101


                  ....*..
gi 2796455541 103 KCDIAAC 109
Cdd:COG4076   102 KADVIIS 108
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-136 4.95e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.20  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  41 LDLGSGSGEMLCTWARE-HGIRGIGVDMSALFSEQA--KLRAEELGVADRVTFIHQDAAGyVVEEKCDIAACVGATWIAG 117
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlPGLEYTGLDISPAALEAAreRLAALGLLNAVRVELFQLDLGE-LDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 2796455541 118 GVAGTIELLSKSLKPGGML 136
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 36-94 1.16e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 42.13  E-value: 1.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2796455541  36 AGTRILDLGSGSGEMLCTWAReHGIRGIGVDMSALFSEQAKLRAEELGVADRVTFIHQD 94
Cdd:PRK07580   63 TGLRILDAGCGVGSLSIPLAR-RGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 4-244 1.39e-03

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 39.01  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541   4 PRIFTISESaHRIHNPFTPEkYAALGRALRMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEE 81
Cdd:pfam08704  10 PELWTLNLP-HRTQILYTPD-ISLITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGhlFTFEFHEQRADKAREEFRE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  82 LGVADRVTFIHQDAA--GYVVEEKCDIAAC---VGATWIAggvagtIELLSKSLK-PGGMLLIGEPYWRQVPATeeiAQA 155
Cdd:pfam08704  88 HGIDQLVTVTHRDVCkeGFLTEVSGKADAVfldLPSPWEA------VPHAWKALKvEGGRFCSFSPCIEQVQRT---CQA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 156 CGASSLADFLTLADLVSSYDAlgyDLVEMVLADqEGWDRYEAAKwltmRRWLEENPDDEFVPEVR--AELTMAPKRHTTy 233
Cdd:pfam08704 159 LAELGFTEISTLEVLLRVYDV---RTVSLPVID-LGIDREKENE----RTRTEGLSNDDKSEDNSgnSMLGTALKPMSE- 229

                         250
                  ....*....|.
gi 2796455541 234 TREYFGWGVFA 244
Cdd:pfam08704 230 AVGHTGYLTFA 240
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 31-183 1.48e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.18  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  31 ALRMKAGTRILDLGSGSGEMlCTWAREHGIRGIGVDMSALFSEQAKLraeelgVADRVTFIHQDAAgyVVEEKCDIAACV 110
Cdd:pfam13489  17 LPKLPSPGRVLDFGCGTGIF-LRLLRAQGFSVTGVDPSPIAIERALL------NVRFDQFDEQEAA--VPAGKFDVIVAR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541 111 GAT-----WIAggvagTIELLSKSLKPGGMLLIGEP--YWRQVPATEEIAQACGASSLADFLTLADLVSSYDALGYDLVE 183
Cdd:pfam13489  88 EVLehvpdPPA-----LLRQIAALLKPGGLLLLSTPlaSDEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFEVVS 162
arsM PRK11873
arsenite methyltransferase;
33-94 2.25e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 38.39  E-value: 2.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796455541  33 RMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEELGVADrVTFIHQD 94
Cdd:PRK11873   74 ELKPGETVLDLGSGGGFDCFLAARRVGPTGkvIGVDMTPEMLAKARANARKAGYTN-VEFRLGE 136
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
32-109 2.46e-03

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


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 38.39  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  32 LRMKAGTRILDLGSGSGEMLCTWAR--EHGIRGIGVDMSALFSEQAKLRAEELGVAdrVTFIHQDAAGYVVEEKCDIAAC 109
Cdd:COG0827   111 FTKKEGLRILDPAVGTGNLLTTVLNqlKKKVNAYGVEVDDLLIRLAAVLANLQGHP--VELFHQDALQPLLIDPVDVVIS 188
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 19-138 2.77e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 37.85  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  19 PFTPEKYAALGRA-LRMKAGTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEELGVADRVTFIHQDA 95
Cdd:PRK00377   22 PMTKEEIRALALSkLRLRKGDMILDIGCGTGSVTVEASLLVGETGkvYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEA 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2796455541  96 AGYV--VEEKCDiaacvgATWIAGGVAGTIELLSKS---LKPGGMLLI 138
Cdd:PRK00377  102 PEILftINEKFD------RIFIGGGSEKLKEIISASweiIKKGGRIVI 143
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 37-138 3.58e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 37.90  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796455541  37 GTRILDLGSGSGEMLCTWAREHGIRG--IGVDMSALFSEQAKLRAEELGVaDRVTFIHQDAAgYVVEEkcdiAACVGATW 114
Cdd:PRK13943   81 GMRVLEIGGGTGYNAAVMSRVVGEKGlvVSVEYSRKICEIAKRNVRRLGI-ENVIFVCGDGY-YGVPE----FAPYDVIF 154

                          90       100
                  ....*....|....*....|....
gi 2796455541 115 IAGGVAGTIELLSKSLKPGGMLLI 138
Cdd:PRK13943  155 VTVGVDEVPETWFTQLKEGGRVIV 178
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH