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Conserved domains on  [gi|151301096|ref|NP_079107|]
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trimethylguanosine synthase isoform 1 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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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; ...
691-843 1.19e-49

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 pfam09445:

Pssm-ID: 473071  Cd Length: 165  Bit Score: 172.52  E-value: 1.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  691 CDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLK-----ADVVFLSPP 765
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKfekikYDCVFASPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  766 WGGPDYATAETFDIRTMMSPDGFE-IFRLSKKITNNIVYFLPRNADIDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 840
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160

                  ...
gi 151301096  841 YFG 843
Cdd:pfam09445 161 YFG 163
MSCRAMM_ClfA super family cl41352
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 7.87e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


The actual alignment was detected with superfamily member NF033609:

Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.44  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 657 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 736
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGDeSEEDPPEHKP 421
Cdd:NF033609 737 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSD 815
                        170       180
                 ....*....|....*....|....*
gi 151301096 422 SKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 816 SDSDSDSDSDSDSDSDSDSDsDSDS 840
 
Name Accession Description Interval E-value
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
691-843 1.19e-49

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 172.52  E-value: 1.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  691 CDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLK-----ADVVFLSPP 765
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKfekikYDCVFASPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  766 WGGPDYATAETFDIRTMMSPDGFE-IFRLSKKITNNIVYFLPRNADIDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 840
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160

                  ...
gi 151301096  841 YFG 843
Cdd:pfam09445 161 YFG 163
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
692-767 1.21e-11

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: 63.81  E-value: 1.21e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151301096 692 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFLLLA-SFLKADVVFLSPPWG 767
Cdd:COG1041   28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPlADESVDAIVTDPPYG 103
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
694-787 2.27e-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: 58.21  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 694 VVDAFCGVGGNTIQFALT-GMRVIAIDIDPVKIALARNNAEvYGIADKIEFICGDF--LLLASFLKADVVFLSPPWGGPD 770
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80
                         90
                 ....*....|....*...
gi 151301096 771 YATAETFD-IRTMMSPDG 787
Cdd:cd02440   81 EDLARFLEeARRLLKPGG 98
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
689-762 1.27e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 49.80  E-value: 1.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151301096 689 FKCDVVVDAFCGVGGNTIQFAL---TGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFL--KADVVFL 762
Cdd:PRK00377  39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
692-770 3.50e-06

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 50.21  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  692 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDflLLASFLK-------ADVVFLSP 764
Cdd:TIGR00479 294 ERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIAN-VTFYHGT--LETVLPKqpwagngFDKVLLDP 370

                  ....*.
gi 151301096  765 PWGGPD 770
Cdd:TIGR00479 371 PRKGCA 376
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 7.87e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.44  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 657 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 736
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGDeSEEDPPEHKP 421
Cdd:NF033609 737 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSD 815
                        170       180
                 ....*....|....*....|....*
gi 151301096 422 SKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 816 SDSDSDSDSDSDSDSDSDSDsDSDS 840
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 1.11e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.06  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 651 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 730
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 731 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 810
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 811 DSDSDSDSDSDSDSDSDSDSDsDSDS 836
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 1.34e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 621 DSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 700
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQlSEVSSKRECPASGQSEprnggTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 701 DSDSD-SDSDSDSDSDSDSDSD-----SDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 774
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 775 DSDSDSDSDSDSDSDSDSDSDsDSDS 800
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 1.40e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 683 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 762
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 763 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 842
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 843 DSDSDSDSDSDSDSESDSNSDsESGS 868
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 3.17e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 627 DSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 707 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 786
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 787 DSDSDSDSDSDSDSDSDSDSDsDSDS 812
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-443 3.64e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.13  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 663 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 743 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 822
                        170       180
                 ....*....|....*....|...
gi 151301096 421 PSKLKRSHELDIDENPASDFDDS 443
Cdd:NF033609 823 DSDSDSDSDSDSDSDSDSDSDSD 845
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-441 9.11e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 669 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 748
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE---DSQKSSGANTSKDRPHASGTDGD-ESEEDPPE 418
Cdd:NF033609 749 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDS 828
                        170       180
                 ....*....|....*....|...
gi 151301096 419 HKPSKLKRSHELDIDENPASDFD 441
Cdd:NF033609 829 DSDSDSDSDSDSDSDSDSDSDSD 851
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-415 1.99e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 753 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPP--AEDSQKSSGANTSKDRPHASGTDGDESEED 415
Cdd:NF033609 833 DSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPnsPKNGTNASNKNEAKDSKEPLPDTGSEDEAN 907
 
Name Accession Description Interval E-value
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
691-843 1.19e-49

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 172.52  E-value: 1.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  691 CDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLK-----ADVVFLSPP 765
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKfekikYDCVFASPP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  766 WGGPDYATAETFDIRTMMSPDGFE-IFRLSKKITNNIVYFLPRNADIDQVAS----LAGPGGQVEIEQNFLNNKLKTITA 840
Cdd:pfam09445  81 WGGPSYKKQNVYDLENKLQPYGLSqLLKEFTKISKNVILFLPRNSDLNQLSAltreVLGPEAKCKVLYIKENGYMKGLLC 160

                  ...
gi 151301096  841 YFG 843
Cdd:pfam09445 161 YFG 163
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
692-767 1.21e-11

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: 63.81  E-value: 1.21e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151301096 692 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFLLLA-SFLKADVVFLSPPWG 767
Cdd:COG1041   28 DTVLDPFCGTGTILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPlADESVDAIVTDPPYG 103
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
668-765 6.73e-11

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: 64.81  E-value: 6.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 668 GWFSVTPEkIAEHIAGRVS---QSFKCDVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFI 744
Cdd:COG2265  209 SFFQVNPE-QAEALYAAALewlDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFV 286
                         90       100
                 ....*....|....*....|....*
gi 151301096 745 CGD-FLLLASFL---KADVVFLSPP 765
Cdd:COG2265  287 AGDlEEVLPELLwggRPDVVVLDPP 311
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
694-787 2.27e-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: 58.21  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 694 VVDAFCGVGGNTIQFALT-GMRVIAIDIDPVKIALARNNAEvYGIADKIEFICGDF--LLLASFLKADVVFLSPPWGGPD 770
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAeeLPPEADESFDVIISDPPLHHLV 80
                         90
                 ....*....|....*...
gi 151301096 771 YATAETFD-IRTMMSPDG 787
Cdd:cd02440   81 EDLARFLEeARRLLKPGG 98
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
684-760 2.54e-10

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


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 62.96  E-value: 2.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 684 RVSQSFKCD-VVVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFL--KADV 759
Cdd:COG2520  173 RIAELVKPGeRVLDMFAGVGPFSIPIAkRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVAPELegKADR 252

                 .
gi 151301096 760 V 760
Cdd:COG2520  253 I 253
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
694-763 6.23e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.80  E-value: 6.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301096  694 VVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIadKIEFICGDFLLL----ASFlkaDVVFLS 763
Cdd:pfam13649   1 VLDLGCGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpfpdGSF---DLVVSS 70
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
694-763 8.88e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.16  E-value: 8.88e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301096 694 VVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFICGDF-----LLLASFlkaDVVFLS 763
Cdd:COG0500   30 VLDLGCGTGRNLLALAaRFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLaeldpLPAESF---DLVVAF 101
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
692-767 1.67e-09

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: 58.14  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  692 DVVVDAFCGVGGNTIQFALTGMRVI-------------AIDIDPVKIALARNNAEVYGIADKIEFICGDFLLL-ASFLKA 757
Cdd:pfam01170  30 DPLLDPMCGSGTILIEAALMGANIApgkfdarvraplyGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLpLLEGSV 109
                          90
                  ....*....|
gi 151301096  758 DVVFLSPPWG 767
Cdd:pfam01170 110 DVIVTNPPYG 119
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
694-763 2.12e-09

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.18  E-value: 2.12e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 151301096 694 VVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEvygiADKIEFICGDFLLLASFL-KADVVFLS 763
Cdd:COG2227   28 VLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAA----ELNVDFVQGDLEDLPLEDgSFDLVICS 94
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
662-768 9.79e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 56.07  E-value: 9.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 662 IKLDREGWFS---------VTPEKIAEHI--AGRVSQSFKCDVVVDAFCGVGGNTIQFALTGM-RVIAIDIDPVKIALAR 729
Cdd:COG2263    6 IILEKLPGFSnpkveleqyPTPAELAAELlhLAYLRGDIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIAR 85
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 151301096 730 NNAEvyGIADKIEFICGDFLLLASFLKADVVFLSPPWGG 768
Cdd:COG2263   86 ENAE--RLGVRVDFIRADVTRIPLGGSVDTVVMNPPFGA 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
692-763 3.12e-08

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: 53.46  E-value: 3.12e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301096 692 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIadKIEFICGDFLLL----ASFlkaDVVFLS 763
Cdd:COG2226   24 ARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfpdGSF---DLVISS 94
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
700-762 8.57e-08

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


Pssm-ID: 443298  Cd Length: 173  Bit Score: 52.88  E-value: 8.57e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 700 GVGGNTIQFALtGM----RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFL-LLASFLKA--DVVFL 762
Cdd:COG4122   26 GTGYSTLWLAR-ALpddgRLTTIEIDPERAAIARENFARAGLADRIRLILGDALeVLPRLADGpfDLVFI 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
694-748 2.78e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.08  E-value: 2.78e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 151301096 694 VVDAFCGVGGNTIQFA-LTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDF 748
Cdd:COG2230   55 VLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY 110
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
693-765 4.96e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 52.07  E-value: 4.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151301096 693 VVVDAFCGVG--GNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFL-LLASFLKADVVfLS-PP 765
Cdd:COG2890  115 RVLDLGTGSGaiALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFePLPGDGRFDLI-VSnPP 190
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
689-762 1.27e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 49.80  E-value: 1.27e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 151301096 689 FKCDVVVDAFCGVGGNTIQFAL---TGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFL--KADVVFL 762
Cdd:PRK00377  39 RKGDMILDIGCGTGSVTVEASLlvgETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTIneKFDRIFI 117
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
690-766 2.17e-06

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: 49.76  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 690 KCDVVVDAFCGVGgnTIQFALT----GMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKA---DVVFL 762
Cdd:COG4123   37 KGGRVLDLGTGTG--VIALMLAqrspGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPgsfDLVVS 114

                 ....
gi 151301096 763 SPPW 766
Cdd:COG4123  115 NPPY 118
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
692-770 3.50e-06

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 50.21  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  692 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDflLLASFLK-------ADVVFLSP 764
Cdd:TIGR00479 294 ERVLDAYCGMGTFTLPLAKQAKSVVGVEGVPESVEKAQQNAELNGIAN-VTFYHGT--LETVLPKqpwagngFDKVLLDP 370

                  ....*.
gi 151301096  765 PWGGPD 770
Cdd:TIGR00479 371 PRKGCA 376
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
714-761 7.23e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 48.63  E-value: 7.23e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 151301096 714 RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDfllLASFLKADVVF 761
Cdd:COG2264  173 RVLAVDIDPVAVEAARENAELNGVEDRIEVVLGD---LLEDGPYDLVV 217
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
695-763 7.73e-06

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.96  E-value: 7.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 151301096  695 VDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEvygiADKIEFICGDFLLL----ASFlkaDVVFLS 763
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP----REGLTFVVGDAEDLpfpdNSF---DLVLSS 66
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
694-747 3.20e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 45.98  E-value: 3.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 151301096 694 VVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGD 747
Cdd:PRK07580  67 ILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
713-767 6.88e-05

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: 45.86  E-value: 6.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 151301096 713 MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWG 767
Cdd:COG0116  251 LPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEPGLIITNPPYG 305
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 7.87e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.44  E-value: 7.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 657 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 736
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGDeSEEDPPEHKP 421
Cdd:NF033609 737 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSD-SDSDSDSDSD 815
                        170       180
                 ....*....|....*....|....*
gi 151301096 422 SKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 816 SDSDSDSDSDSDSDSDSDSDsDSDS 840
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
693-761 8.60e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 43.56  E-value: 8.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301096  693 VVVDAFCGVGGNTIQFAL---TGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFICGDFLLLASFL---KADVVF 761
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEelgPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPELLeddKFDVVI 79
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 1.11e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 46.06  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 651 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 730
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 731 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 810
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 811 DSDSDSDSDSDSDSDSDSDSDsDSDS 836
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 1.34e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 621 DSDSASDSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 700
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQlSEVSSKRECPASGQSEprnggTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 701 DSDSD-SDSDSDSDSDSDSDSD-----SDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 774
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 775 DSDSDSDSDSDSDSDSDSDSDsDSDS 800
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 1.40e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.67  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 683 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 762
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 763 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 842
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 843 DSDSDSDSDSDSDSESDSNSDsESGS 868
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
690-760 1.52e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.26  E-value: 1.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 151301096 690 KCDVVVDAFCGVGgntiqfALTGM-------RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVV 760
Cdd:COG4076   35 PGDVVLDIGTGSG------LLSMLaaragakKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKADVI 106
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
694-765 2.01e-04

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 44.47  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 694 VVDAFCGVGGntiqFAL----TGMRVIAIDIDPVKIALARNNAEVYGIaDKIEFICGDfllLASFLKA-----DVVFLSP 764
Cdd:PRK03522 177 MWDLFCGVGG----FGLhcatPGMQLTGIEISAEAIACAKQSAAELGL-TNVQFQALD---STQFATAqgevpDLVLVNP 248

                 .
gi 151301096 765 P 765
Cdd:PRK03522 249 P 249
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
694-787 2.53e-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: 42.87  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 694 VVDAFCGVG--GNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFLLLASFLKADVVFLSPPW---GG 768
Cdd:COG2813   53 VLDLGCGYGviGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPDGSFDLILSNPPFhagRA 131
                         90       100
                 ....*....|....*....|.
gi 151301096 769 PDYATAETF--DIRTMMSPDG 787
Cdd:COG2813  132 VDKEVAHALiaDAARHLRPGG 152
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-445 3.17e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 627 DSDSASDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 706
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 707 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 786
                        170       180
                 ....*....|....*....|....*.
gi 151301096 421 PSKLKRSHELDIDENPASDFD-DSGS 445
Cdd:NF033609 787 DSDSDSDSDSDSDSDSDSDSDsDSDS 812
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-443 3.64e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.13  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 663 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 742
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE-DSQKSSGANTSKDRPHASGTDGD-ESEEDPPEHK 420
Cdd:NF033609 743 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDSDS 822
                        170       180
                 ....*....|....*....|...
gi 151301096 421 PSKLKRSHELDIDENPASDFDDS 443
Cdd:NF033609 823 DSDSDSDSDSDSDSDSDSDSDSD 845
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
693-765 4.72e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 42.84  E-value: 4.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 151301096 693 VVVDAFCGVG--GNTIQFALTGMRVIAIDIDPVKIALARNNAEvYGIADKIEFICGDFLLLASFLKADVVfLS-PP 765
Cdd:PRK09328 111 RVLDLGTGSGaiALALAKERPDAEVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFEPLPGGRFDLI-VSnPP 184
PRK14968 PRK14968
putative methyltransferase; Provisional
692-765 5.29e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.81  E-value: 5.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151301096 692 DVVVDAFCGVGGNTIQFALTGMRVIAIDIDPVKIALARNNAEVYGIAD-KIEFICGDflLLASF--LKADVVFLSPP 765
Cdd:PRK14968  25 DRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNnGVEVIRSD--LFEPFrgDKFDVILFNPP 99
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
692-768 7.14e-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: 42.85  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 692 DVVVDAFCGVGGNTIQFALT--GMRVIAIDIDPVKIALARNNAEVYGIADkIEFICGDFL-LLASFLKADVVFLsppwGG 768
Cdd:COG2242  249 DVLWDIGAGSGSVSIEAARLapGGRVYAIERDPERAALIRANARRFGVPN-VEVVEGEAPeALADLPDPDAVFI----GG 323
Met_10 pfam02475
Met-10+ like-protein; The methionine-10 mutant allele of N. crassa codes for a protein of ...
692-747 7.31e-04

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


Pssm-ID: 396850 [Multi-domain]  Cd Length: 198  Bit Score: 41.57  E-value: 7.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 151301096  692 DVVVDAFCGVGGNTIQFALTG--MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGD 747
Cdd:pfam02475 101 EVVVDMFAGIGPFSIPIAKHSkaRRVYAIELNPESYKYLKENIKLNKVEDVVKPILGD 158
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-441 9.11e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 42.97  E-value: 9.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 669 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 748
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPPAE---DSQKSSGANTSKDRPHASGTDGD-ESEEDPPE 418
Cdd:NF033609 749 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDsdsDSDSDSDSDSDSDSDSDSDSDSDsDSDSDSDS 828
                        170       180
                 ....*....|....*....|...
gi 151301096 419 HKPSKLKRSHELDIDENPASDFD 441
Cdd:NF033609 829 DSDSDSDSDSDSDSDSDSDSDSD 851
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
675-808 9.49e-04

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 41.96  E-value: 9.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096  675 EKIAEHIAGRVSQSFKCDVVVDAFCGVGGNTIQFALT--GMRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLA 752
Cdd:TIGR00536  99 EELVEKALASLISQPPILHILDLGTGSGCIALALAYEfpNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPL 178
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 151301096  753 SFLKADVVFLSPPwggpdYATAETFDIRTMM-----------SPDGFEIfrlSKKITNNIVYFLPRN 808
Cdd:TIGR00536 179 AGQKIDIIVSNPP-----YIDEEDLADLPNVvrfepllalvgGDDGLNI---LRQIIELAPDYLKPN 237
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
263-415 1.99e-03

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 41.82  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 263 DASQSCDTDTYTSKTEADDKNDEKCMKVDLVSFPSSPIMVDNDSSGTSDKDHSEILDGISNIKLNSEEVTQSQLDSCTSH 342
Cdd:NF033609 753 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 832
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301096 343 DGHQQLSEVSSKRECPASGQSEPRNGGTNEESNSSGNTNTDPP--AEDSQKSSGANTSKDRPHASGTDGDESEED 415
Cdd:NF033609 833 DSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPnsPKNGTNASNKNEAKDSKEPLPDTGSEDEAN 907
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
714-767 5.56e-03

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: 40.17  E-value: 5.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 151301096 714 RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKAD---VVFLSPPWG 767
Cdd:PRK11783 258 KFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKGptgLVISNPPYG 314
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
643-763 5.61e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.83  E-value: 5.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 151301096 643 ELAKYWAQRYRLFS-RFDDGIkldREGWFSVTPEKIAEHIAGRVsQSFKCDVVVDAFCGVGGNTIQFALTGMRVIAIDID 721
Cdd:COG4976    2 ALDAYVEALFDQYAdSYDAAL---VEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLS 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 151301096 722 PVKIALARNNAeVYgiadkIEFICGDFLLLASFL-KADVVFLS 763
Cdd:COG4976   78 EEMLAKAREKG-VY-----DRLLVADLADLAEPDgRFDLIVAA 114
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
700-729 5.99e-03

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and 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. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 39.92  E-value: 5.99e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 151301096 700 GVGGNTIQFA-LTGMRVIAIDIDPVKIALAR 729
Cdd:cd08254  176 GLGLNAVQIAkAMGAAVIAVDIKEEKLELAK 206
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
714-760 6.55e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 39.36  E-value: 6.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 151301096 714 RVIAIDIDPVKIALARNNAEVYGIADKIEFICGDflllasfLKADVV 760
Cdd:PRK00517 144 KVLAVDIDPQAVEAARENAELNGVELNVYLPQGD-------LKADVI 183
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
693-764 8.38e-03

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 39.51  E-value: 8.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 151301096 693 VVVDAFCGVGGNTIQFAL-TGM-RVIAIDIDPVKIALARNNAEVYGIaDKIEFICGDF-LLLASFLKADVVFLSP 764
Cdd:PRK04338  60 SVLDALSASGIRGIRYALeTGVeKVTLNDINPDAVELIKKNLELNGL-ENEKVFNKDAnALLHEERKFDVVDIDP 133
PRK08317 PRK08317
hypothetical protein; Provisional
690-747 9.40e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 38.76  E-value: 9.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 151301096 690 KCDVVVDAFCGVGGNTIQFAL----TGmRVIAIDIDPVKIALARNNAEvyGIADKIEFICGD 747
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELARrvgpEG-RVVGIDRSEAMLALAKERAA--GLGPNVEFVRGD 77
 
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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