NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034616942|ref|XP_016860539|]
View 

THUMP domain-containing protein 2 isoform X1 [Homo sapiens]

Protein Classification

THUMP domain-containing protein( domain architecture ID 10185027)

THUMP domain-containing protein is a SAM-dependent RNA methyltransferase containing a THUMP domain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 258-403 1.04e-28

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 pfam01170:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 184  Bit Score: 111.68  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 258 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 326
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 327 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 402
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 1034616942 403 C 403
Cdd:pfam01170 162 A 162
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 18-76 1.75e-05

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


:

Pssm-ID: 212584  Cd Length: 152  Bit Score: 44.88  E-value: 1.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616942  18 FFCTAGRGLEPFVMREVRArLAATQVEYISGKVFFTTcsDLNMLKK----LKSAERLFLLIKK 76
Cdd:cd11715     1 FFATCPPGLEELLAAELKA-LGAEDVEVGPGGVSFEG--DLEDAYRanlwLRTAHRVLLLLAE 60
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-248 3.65e-03

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


:

Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 36.48  E-value: 3.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616942  186 EEEFQNDIEKAIDTHNQN---DLTFREVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVVGI 248
Cdd:smart00981  16 EKIFKEGKTFAVRAKRRGknhEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYLSI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 258-403 1.04e-28

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 111.68  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 258 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 326
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 327 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 402
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 1034616942 403 C 403
Cdd:pfam01170 162 A 162
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 270-402 1.73e-25

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: 102.33  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 270 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPS 349
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLAD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034616942 350 ESVDIIISDIPFGKKFKLGKD-----IKSILQEMERVLHVGGTIVLLLSEDHHRRLTD 402
Cdd:COG1041    91 ESVDAIVTDPPYGRSSKISGEellelYEKALEEAARVLKPGGRVVIVTPRDIDELLEE 148
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 212-389 6.85e-19

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 87.49  E-value: 6.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 212 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 283
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 284 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIISDIPFGK 363
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGR 260

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034616942 364 KFKLGKD-----IKSILQEMERVLHVGGTIV 389
Cdd:TIGR01177 261 STTAAGDgleslYERSLEEFHEVLKSEGWIV 291
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
258-395 4.86e-15

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 76.64  E-value: 4.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 258 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY- 309
Cdd:NF040721  167 RVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELk 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 310 -VGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPLPSESVDIIISDIPFG----KKFKLGKDIKSILQEMERVLHV 384
Cdd:NF040721  247 iYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGlrigKKRIIKKLYNNFLRSAKKILHK 326

                         170
                  ....*....|.
gi 1034616942 385 GGTIVLLLSED 395
Cdd:NF040721  327 RSRIVVITAEK 337
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 286-390 4.20e-10

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: 57.05  E-value: 4.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 286 VLDPMCGLGTILLEAAkEWPDVYYVGADVSDSQLlGTWDNLKAAGLEDKIELLKISVIELPL-PSESVDIIISDIPFgkk 364
Cdd:cd02440     2 VLDLGCGTGALALALA-SGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPL--- 76

                          90       100
                  ....*....|....*....|....*.
gi 1034616942 365 FKLGKDIKSILQEMERVLHVGGTIVL 390
Cdd:cd02440    77 HHLVEDLARFLEEARRLLKPGGVLVL 102
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 267-391 1.19e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.54  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 267 RSTIAWAmaslaDIKAGAFVLDPMCGLGTILLEAAKEWPDV-YYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEL 345
Cdd:PRK00216   41 RKTIKWL-----GVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034616942 346 PLPSESVDII-ISdipFGkkfkLG--KDIKSILQEMERVLHVGGTIVLL 391
Cdd:PRK00216  116 PFPDNSFDAVtIA---FG----LRnvPDIDKALREMYRVLKPGGRLVIL 157
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 18-76 1.75e-05

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 44.88  E-value: 1.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616942  18 FFCTAGRGLEPFVMREVRArLAATQVEYISGKVFFTTcsDLNMLKK----LKSAERLFLLIKK 76
Cdd:cd11715     1 FFATCPPGLEELLAAELKA-LGAEDVEVGPGGVSFEG--DLEDAYRanlwLRTAHRVLLLLAE 60
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-248 3.65e-03

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 36.48  E-value: 3.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616942  186 EEEFQNDIEKAIDTHNQN---DLTFREVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVVGI 248
Cdd:smart00981  16 EKIFKEGKTFAVRAKRRGknhEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYLSI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 258-403 1.04e-28

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 111.68  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 258 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 326
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 327 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 402
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 1034616942 403 C 403
Cdd:pfam01170 162 A 162
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 270-402 1.73e-25

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: 102.33  E-value: 1.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 270 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPS 349
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLAD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034616942 350 ESVDIIISDIPFGKKFKLGKD-----IKSILQEMERVLHVGGTIVLLLSEDHHRRLTD 402
Cdd:COG1041    91 ESVDAIVTDPPYGRSSKISGEellelYEKALEEAARVLKPGGRVVIVTPRDIDELLEE 148
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 212-389 6.85e-19

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 87.49  E-value: 6.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 212 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 283
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 284 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIISDIPFGK 363
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGR 260

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034616942 364 KFKLGKD-----IKSILQEMERVLHVGGTIV 389
Cdd:TIGR01177 261 STTAAGDgleslYERSLEEFHEVLKSEGWIV 291
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
258-395 4.86e-15

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 76.64  E-value: 4.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 258 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY- 309
Cdd:NF040721  167 RVYQHPAHLNPTIASSLIYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELk 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 310 -VGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPLPSESVDIIISDIPFG----KKFKLGKDIKSILQEMERVLHV 384
Cdd:NF040721  247 iYGIEKFRKHLEGAKKNAENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGlrigKKRIIKKLYNNFLRSAKKILHK 326

                         170
                  ....*....|.
gi 1034616942 385 GGTIVLLLSED 395
Cdd:NF040721  327 RSRIVVITAEK 337
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 227-382 2.31e-12

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 68.20  E-value: 2.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 227 DLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasRAYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILL 298
Cdd:COG0116   130 DEDGPDVRIHVHLlKDRATLsldtSGESLHK-----RGYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILI 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 299 EAA----------------KEWPD----------------------VYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKI 340
Cdd:COG0116   205 EAAliaaniapglnrdfafEKWPDfdaelwqelreeaearikrdppLPIFGSDIDPRAIEAARENAERAGVADLIEFEQA 284

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034616942 341 SVIELPLPSESvDIIISDIPFGKKFKLGKDIKSILQEMERVL 382
Cdd:COG0116   285 DFRDLEPPAEP-GLIITNPPYGERLGEEEELEALYRELGDVL 325
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 273-402 5.18e-12

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: 63.47  E-value: 5.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 273 AMASLADIKAGAFVLDPMCGLGTILLEAAKEwpDVYYVGADVSDSQLLGTWDNLKAAGLedKIELLKISVIELPLPSESV 352
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSF 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616942 353 DIIIS-----DIPfgkkfklgkDIKSILQEMERVLHVGGTIVLL-LSEDHHRRLTD 402
Cdd:COG2226    89 DLVISsfvlhHLP---------DPERALAEIARVLKPGGRLVVVdFSPPDLAELEE 135
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 286-390 4.20e-10

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: 57.05  E-value: 4.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 286 VLDPMCGLGTILLEAAkEWPDVYYVGADVSDSQLlGTWDNLKAAGLEDKIELLKISVIELPL-PSESVDIIISDIPFgkk 364
Cdd:cd02440     2 VLDLGCGTGALALALA-SGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPL--- 76

                          90       100
                  ....*....|....*....|....*.
gi 1034616942 365 FKLGKDIKSILQEMERVLHVGGTIVL 390
Cdd:cd02440    77 HHLVEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 287-390 4.25e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.44  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 287 LDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLlgtwDNLKAAGLEDKIELLKISVIELPLPSESVDIIISdipfgkKFK 366
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVT--GVDISPEML----ELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLS------SEV 68

                          90       100
                  ....*....|....*....|....*.
gi 1034616942 367 LG--KDIKSILQEMERVLHVGGTIVL 390
Cdd:pfam08241  69 LHhvEDPERALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 267-391 1.19e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.54  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 267 RSTIAWAmaslaDIKAGAFVLDPMCGLGTILLEAAKEWPDV-YYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEL 345
Cdd:PRK00216   41 RKTIKWL-----GVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034616942 346 PLPSESVDII-ISdipFGkkfkLG--KDIKSILQEMERVLHVGGTIVLL 391
Cdd:PRK00216  116 PFPDNSFDAVtIA---FG----LRnvPDIDKALREMYRVLKPGGRLVIL 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 286-386 2.51e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.41  E-value: 2.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 286 VLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLedKIELLKISVIELPLPSESVDIIISDIPFGkkF 365
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLH--H 75

                          90       100
                  ....*....|....*....|.
gi 1034616942 366 KLGKDIKSILQEMERVLHVGG 386
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 276-391 2.59e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 2.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 276 SLADIKAGAFVLDPMCGLGTILLEAAKE-WPDVYYVGADVSDSQLLGTwdNLKAAGLEDKIELLKISVIELPLPSESVDI 354
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALA--KERAAGLGPNVEFVRGDADGLPFPDGSFDA 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034616942 355 IISDipfgKKFKLGKDIKSILQEMERVLHVGGTIVLL 391
Cdd:PRK08317   91 VRSD----RVLQHLEDPARALAEIARVLRPGGRVVVL 123
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 274-390 2.40e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.31  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 274 MASLADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPlPSESVD 353
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFD 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034616942 354 IIISdipfgkkfkLG-------KDIKSILQEMERVLHVGGTIVL 390
Cdd:COG2230   121 AIVS---------IGmfehvgpENYPAYFAKVARLLKPGGRLLL 155
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 227-362 3.62e-07

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 52.88  E-value: 3.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 227 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA- 301
Cdd:PRK11783  131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAAm 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 302 -----------KEW------------------------------PDVYYVGADvSDSQLLGT-WDNLKAAGLEDKIELLK 339
Cdd:PRK11783  211 maadiapglhrERWgfsgwlghdealwqelleeaqeraraglaeLPSKFYGSD-IDPRVIQAaRKNARRAGVAELITFEV 289

                         170       180
                  ....*....|....*....|....*
gi 1034616942 340 ISVIEL--PLPSESVDIIISDIPFG 362
Cdd:PRK11783  290 KDVADLknPLPKGPTGLVISNPPYG 314
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 280-390 5.13e-07

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: 48.48  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 280 IKAGAFVLDPMCGLGTILLEAAKEWPDVyyVGADVSDSQLlgtwDNLKAAGLEDKIELLKISVIELPLPSESVDIIIS-- 357
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGADV--TGVDISPEAL----EIARERAAELNVDFVQGDLEDLPLEDGSFDLVICse 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034616942 358 ---DIPfgkkfklgkDIKSILQEMERVLHVGGTIVL 390
Cdd:COG2227    96 vleHLP---------DPAALLRELARLLKPGGLLLL 122
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 275-421 5.80e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 5.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 275 ASLADIKAGAFVLDPMCGLGTILLEAAKEwPDVYYVGADVSDSQLLGTWDNLKAAGLeDKIELLKISVIEL-PLPSESVD 353
Cdd:COG0500    19 ALLERLPKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELdPLPAESFD 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616942 354 IIIS-----DIPFGKkfklgkdIKSILQEMERVLHVGGtIVLLLSEDHHRRLTDCKESNIPFNSKDSHTDEPG 421
Cdd:COG0500    97 LVVAfgvlhHLPPEE-------REALLRELARALKPGG-VLLLSASDAAAALSLARLLLLATASLLELLLLLR 161
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 18-76 1.75e-05

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 44.88  E-value: 1.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616942  18 FFCTAGRGLEPFVMREVRArLAATQVEYISGKVFFTTcsDLNMLKK----LKSAERLFLLIKK 76
Cdd:cd11715     1 FFATCPPGLEELLAAELKA-LGAEDVEVGPGGVSFEG--DLEDAYRanlwLRTAHRVLLLLAE 60
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 280-390 1.88e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 280 IKAGAFVLDPMCGLGTILLEAAKE-WPDVYYVGADVSDSQLLGTWDNLKAAGLED-KIELLKISVIELPLPSESVDIIIS 357
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNvEFEQGDIEELPELLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034616942 358 DipfgKKFKLGKDIKSILQEMERVLHVGGTIVL 390
Cdd:pfam13847  81 N----CVLNHIPDPDKVLQEILRVLKPGGRLII 109
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
281-391 7.32e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 43.97  E-value: 7.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 281 KAGAFVLDPMCGLGTI---LLEAAKEWPDVyyVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIIs 357
Cdd:pfam01209  41 KRGNKFLDVAGGTGDWtfgLSDSAGSSGKV--VGLDINENMLKEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVT- 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034616942 358 dIPFGkkFKLGKDIKSILQEMERVLHVGGTIVLL 391
Cdd:pfam01209 117 -ISFG--LRNFPDYLKVLKEAFRVLKPGGRVVCL 147
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 270-390 1.96e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.23  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 270 IAWAMAsLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKaAGLEDKIELLKISVIElPLPS 349
Cdd:PRK09328   97 VEWALE-ALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFE-PLPG 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034616942 350 ESVDIIISD---IPFGKKFKL---------------GKD----IKSILQEMERVLHVGGTIVL 390
Cdd:PRK09328  174 GRFDLIVSNppyIPEADIHLLqpevrdhephlalfgGEDgldfYRRIIEQAPRYLKPGGWLLL 236
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 270-357 2.47e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.83  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 270 IAWAMASLADIKAgAFVLDpmcgLGT----ILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEl 345
Cdd:COG2890   101 VELALALLPAGAP-PRVLD----LGTgsgaIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFE- 174

                          90
                  ....*....|...
gi 1034616942 346 PLPS-ESVDIIIS 357
Cdd:COG2890   175 PLPGdGRFDLIVS 187
arsM PRK11873
arsenite methyltransferase;
277-386 3.05e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 42.63  E-value: 3.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 277 LADIKAGAFVLDPMCGLG-TILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDII 355
Cdd:PRK11873   72 LAELKPGETVLDLGSGGGfDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVDVI 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1034616942 356 ISD--IpfgkkfKLGKDIKSILQEMERVLHVGG 386
Cdd:PRK11873  151 ISNcvI------NLSPDKERVFKEAFRVLKPGG 177
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 286-361 6.57e-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: 40.65  E-value: 6.57e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034616942 286 VLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIElPLPSESVDIIISDIPF 361
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLEN-GEVVASDVYS-GVEDGKFDLIISNPPF 108
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 286-390 8.16e-04

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: 40.56  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 286 VLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIElPLPSESVDIIISDIPfgkkF 365
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLS-GVPDGSFDLILSNPP----F 126

                          90       100       110
                  ....*....|....*....|....*....|
gi 1034616942 366 KLGKDI-KSILQEM----ERVLHVGGTIVL 390
Cdd:COG2813   127 HAGRAVdKEVAHALiadaARHLRPGGELWL 156
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 291-388 9.70e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.50  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 291 CGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLED--KIELLKISVIELPLPseSVDIIISdipfgkkfkLG 368
Cdd:pfam08242   5 CGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPG--SFDVVVA---------SN 73

                          90       100
                  ....*....|....*....|....*
gi 1034616942 369 -----KDIKSILQEMERVLHVGGTI 388
Cdd:pfam08242  74 vlhhlADPRAVLRNIRRLLKPGGVL 98
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
270-369 9.99e-04

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 40.94  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 270 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAK--------EWPDVYYVGADVSDSqllgTWD----NLKAAGLEDKIEL 337
Cdd:COG0286    31 VVRLMVELLDPKPGETVYDPACGSGGFLVEAAEylkehggdERKKLSLYGQEINPT----TYRlakmNLLLHGIGDPNIE 106

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1034616942 338 LKISVIELPLPSESVDIIISDIPFGKKFKLGK 369
Cdd:COG0286   107 LGDTLSNDGDELEKFDVVLANPPFGGKWKKEE 138
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 278-357 1.19e-03

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 40.77  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 278 ADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPlpsESVDIIIS 357
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGGLMRRAAERY-DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFD---EPFDRIVS 132
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-248 3.65e-03

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 36.48  E-value: 3.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034616942  186 EEEFQNDIEKAIDTHNQN---DLTFREVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVVGI 248
Cdd:smart00981  16 EKIFKEGKTFAVRAKRRGknhEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYLSI 82
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
347-390 6.39e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 38.37  E-value: 6.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034616942 347 LPSESVDIIISDIPF--GKKFKLGKD--------------IKSILQEMERVLHVGGTIVL 390
Cdd:COG0863    14 LPDESVDLIVTDPPYnlGKKYGLGRReignelsfeeylefLREWLAECYRVLKPGGSLYV 73
 
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