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Conserved domains on  [gi|498409035|ref|WP_010718855|]
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tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD [Enterococcus hirae]

Protein Classification

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD( domain architecture ID 11425234)

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD is part of the enzyme complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine

CATH:  3.30.420.40
EC:  2.3.1.234
Gene Ontology:  GO:0002949|GO:0061711|GO:0005506
SCOP:  4002236

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 5-333 0e+00

tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 440299  Cd Length: 333  Bit Score: 559.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:COG0533    2 LILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARF-QKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDA 163
Cdd:COG0533   82 PGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLeDPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDDA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 164 AGEAYDKVGRVLGLSYPSGKEIDQLAHRGE-DTYHFPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASF 242
Cdd:COG0533  162 AGEAFDKVAKLLGLGYPGGPAIDKLAKEGDpKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEKLKQKGEEQDKADIAASF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 243 QASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQAN 322
Cdd:COG0533  242 QEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRG--IRLFFPPLELCTDNAAMIAAAGYERLKAGE 319

                        330
                 ....*....|.
gi 498409035 323 FADLRLNAKPS 333
Cdd:COG0533  320 FSDLDLNARPR 330
 
Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 5-333 0e+00

tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440299  Cd Length: 333  Bit Score: 559.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:COG0533    2 LILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARF-QKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDA 163
Cdd:COG0533   82 PGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLeDPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDDA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 164 AGEAYDKVGRVLGLSYPSGKEIDQLAHRGE-DTYHFPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASF 242
Cdd:COG0533  162 AGEAFDKVAKLLGLGYPGGPAIDKLAKEGDpKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEKLKQKGEEQDKADIAASF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 243 QASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQAN 322
Cdd:COG0533  242 QEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRG--IRLFFPPLELCTDNAAMIAAAGYERLKAGE 319

                        330
                 ....*....|.
gi 498409035 323 FADLRLNAKPS 333
Cdd:COG0533  320 FSDLDLNARPR 330
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
5-336 0e+00

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;


Pssm-ID: 236585  Cd Length: 332  Bit Score: 545.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:PRK09604   2 LILGIETSCDETSVAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAIAVTAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAA 164
Cdd:PRK09604  82 PGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEEEPEFPFLALLVSGGHTQLVLVKGIGDYELLGETLDDAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRGE-DTYHFPRAMiHESNYDFSFSGLKSAFINLVHNAQQrgetlDTNNLAASFQ 243
Cdd:PRK09604 162 GEAFDKVAKLLGLGYPGGPAIDKLAKQGDpDAFKFPRPM-DRPGLDFSFSGLKTAVLNTIEKSEQ-----TKADIAASFQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQANF 323
Cdd:PRK09604 236 AAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRG--IEVFIPPLKLCTDNAAMIAAAGYERLKAGEF 313

                        330
                 ....*....|...
gi 498409035 324 ADLRLNAKPSVVL 336
Cdd:PRK09604 314 SDLDLNARPRWPL 326
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 6-319 0e+00

tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial members of a protein family that is widely distributed. In a few pathogenic species, the protein is exported in a way that may represent an exceptional secondary function. This model plus companion (archaeal) model TIGR03722 together span the prokaryotic member sequences of TIGR00329, a protein family that appears universal in life, and whose broad function is unknown. A member of TIGR03722 has been characterized as a DNA-binding protein with apurinic endopeptidase activity. In contrast, the rare characterized members of the present family show O-sialoglycoprotein endopeptidase (EC. 3.4.24.57) activity after export. These include glycoprotease (gcp) from Pasteurella haemolytica A1 and a cohemolysin from Riemerella anatipestifer (GB|AAG39646.1). The member from Staphylococcus aureus is essential and is related to cell wall dynamics and the modulation of autolysis, but members are also found in the Mycoplasmas (which lack a cell wall). A reasonable hypothesis is that virulence-related activities after export are secondary to a bacterial domain-wide unknown function. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274748  Cd Length: 313  Bit Score: 538.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035    6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKGLLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAAG 165
Cdd:TIGR03723  81 GLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEKPLEFPFLALLVSGGHTQLVLVKGVGDYELLGETLDDAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  166 EAYDKVGRVLGLSYPSGKEIDQLAHRG-EDTYHFPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASFQA 244
Cdd:TIGR03723 161 EAFDKVARLLGLGYPGGPAIDRLAKQGdPKAFKFPRPMLDRPGLDFSFSGLKTAVLNLIEKLKQKGEELTKADIAASFQA 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498409035  245 SVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELK 319
Cdd:TIGR03723 241 AVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRG--LEVFFPPLELCTDNAAMIAAAGYERLK 313
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 6-333 0e+00

nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.


Pssm-ID: 466983  Cd Length: 328  Bit Score: 526.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24133    1 ILGIETSCDETAVAVVDDGGKILSNVVSSQIDLHAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARF-QKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAA 164
Cdd:cd24133   81 GLIGALLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLeDPPPEFPFLALLVSGGHTQLVLVKDFGRYELLGETRDDAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRGEDTYH-FPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASFQ 243
Cdd:cd24133  161 GEAFDKVAKLLGLGYPGGPAIDKLAKEGDPTAFvFPRPMLKRDGYDFSFSGLKTAVLNYLEKNKQDGIEQNKADIAASFQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQANF 323
Cdd:cd24133  241 EAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRG--LEVYIPPPELCTDNAAMIAAAGYYRYKRGKF 318

                        330
                 ....*....|
gi 498409035 324 ADLRLNAKPS 333
Cdd:cd24133  319 ADLDLNARPR 328
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 26-312 1.72e-124

tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated. EC:2.3.1.234


Pssm-ID: 395656  Cd Length: 272  Bit Score: 358.23  E-value: 1.72e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   26 EILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGPGLVGSLLIGISAAKAFAWAN 105
Cdd:pfam00814   1 EILANVILSQKDLHAPYGGVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  106 NLPLIPVNHMAGHIYAARFQKPFEFPlLALLVSGGHTELVYMKeDGNYQIIGETRDDAAGEAYDKVGRVLGLSYPSGKEI 185
Cdd:pfam00814  81 NKPLVGVNHLEAHALAARLETGLEFP-VVLLVSGGHTQVYAAK-DGRYEILGETLDDAAGEAFDKVARLLGLPYPGGPKI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  186 DQLAHRGedTYHFPRAMIhesNYDFSFSGLKSAFINLVHNAQqrgetlDTNNLAASFQASVVDVLVNKTLRACNEYPVKQ 265
Cdd:pfam00814 159 EKLAKEG--AFEFPRPVK---GMDFSFSGLKTAVLRLIEKKE------PKEDIAASFQEAVFDHLAEKTERALKLPGAKE 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 498409035  266 LIVAGGVAANQGLRETLEEAlkKEHPEIELLIPPLKLCGDNAAMIGA 312
Cdd:pfam00814 228 LVILGGVAANKRLREALTEM--AEERGVKLFAPPLEYCTDNGAMIAW 272
 
Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 5-333 0e+00

tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyltransferase TsaD is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440299  Cd Length: 333  Bit Score: 559.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:COG0533    2 LILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARF-QKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDA 163
Cdd:COG0533   82 PGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLeDPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDDA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 164 AGEAYDKVGRVLGLSYPSGKEIDQLAHRGE-DTYHFPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASF 242
Cdd:COG0533  162 AGEAFDKVAKLLGLGYPGGPAIDKLAKEGDpKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEKLKQKGEEQDKADIAASF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 243 QASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQAN 322
Cdd:COG0533  242 QEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRG--IRLFFPPLELCTDNAAMIAAAGYERLKAGE 319

                        330
                 ....*....|.
gi 498409035 323 FADLRLNAKPS 333
Cdd:COG0533  320 FSDLDLNARPR 330
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
5-336 0e+00

tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;


Pssm-ID: 236585  Cd Length: 332  Bit Score: 545.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:PRK09604   2 LILGIETSCDETSVAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAIAVTAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAA 164
Cdd:PRK09604  82 PGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEEEPEFPFLALLVSGGHTQLVLVKGIGDYELLGETLDDAA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRGE-DTYHFPRAMiHESNYDFSFSGLKSAFINLVHNAQQrgetlDTNNLAASFQ 243
Cdd:PRK09604 162 GEAFDKVAKLLGLGYPGGPAIDKLAKQGDpDAFKFPRPM-DRPGLDFSFSGLKTAVLNTIEKSEQ-----TKADIAASFQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQANF 323
Cdd:PRK09604 236 AAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRG--IEVFIPPLKLCTDNAAMIAAAGYERLKAGEF 313

                        330
                 ....*....|...
gi 498409035 324 ADLRLNAKPSVVL 336
Cdd:PRK09604 314 SDLDLNARPRWPL 326
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 6-319 0e+00

tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial members of a protein family that is widely distributed. In a few pathogenic species, the protein is exported in a way that may represent an exceptional secondary function. This model plus companion (archaeal) model TIGR03722 together span the prokaryotic member sequences of TIGR00329, a protein family that appears universal in life, and whose broad function is unknown. A member of TIGR03722 has been characterized as a DNA-binding protein with apurinic endopeptidase activity. In contrast, the rare characterized members of the present family show O-sialoglycoprotein endopeptidase (EC. 3.4.24.57) activity after export. These include glycoprotease (gcp) from Pasteurella haemolytica A1 and a cohemolysin from Riemerella anatipestifer (GB|AAG39646.1). The member from Staphylococcus aureus is essential and is related to cell wall dynamics and the modulation of autolysis, but members are also found in the Mycoplasmas (which lack a cell wall). A reasonable hypothesis is that virulence-related activities after export are secondary to a bacterial domain-wide unknown function. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274748  Cd Length: 313  Bit Score: 538.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035    6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKGLLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAAG 165
Cdd:TIGR03723  81 GLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEKPLEFPFLALLVSGGHTQLVLVKGVGDYELLGETLDDAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  166 EAYDKVGRVLGLSYPSGKEIDQLAHRG-EDTYHFPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASFQA 244
Cdd:TIGR03723 161 EAFDKVARLLGLGYPGGPAIDRLAKQGdPKAFKFPRPMLDRPGLDFSFSGLKTAVLNLIEKLKQKGEELTKADIAASFQA 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498409035  245 SVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELK 319
Cdd:TIGR03723 241 AVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRG--LEVFFPPLELCTDNAAMIAAAGYERLK 313
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 6-333 0e+00

nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.


Pssm-ID: 466983  Cd Length: 328  Bit Score: 526.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24133    1 ILGIETSCDETAVAVVDDGGKILSNVVSSQIDLHAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARF-QKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAA 164
Cdd:cd24133   81 GLIGALLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLeDPPPEFPFLALLVSGGHTQLVLVKDFGRYELLGETRDDAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRGEDTYH-FPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASFQ 243
Cdd:cd24133  161 GEAFDKVAKLLGLGYPGGPAIDKLAKEGDPTAFvFPRPMLKRDGYDFSFSGLKTAVLNYLEKNKQDGIEQNKADIAASFQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELKQANF 323
Cdd:cd24133  241 EAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRG--LEVYIPPPELCTDNAAMIAAAGYYRYKRGKF 318

                        330
                 ....*....|
gi 498409035 324 ADLRLNAKPS 333
Cdd:cd24133  319 ADLDLNARPR 328
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 26-312 1.72e-124

tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, products of COG0533 that belong to a small group of 60 proteins that are present in all three domains of life. COG0533 proteins are suggest to play a role in a post translational modification of certain tRNAs. For example, YgjD along with YeaZ, YjeE, and YrdC have been deemed necessary and sufficient for the tRNA modification. This modification involves the formation of N6-threonyl carbamoyl adenosine (t6A) at position 37 in the anti-codon stem loop which is critical for translational speed and accuracy. Structural analysis indicate that YeaZ lacks resemblance to any known protease active site. Together with the absence of a putative zinc-binding motif. Thus the likelyhood of it being a protease, as previously thought, has been negated. EC:2.3.1.234


Pssm-ID: 395656  Cd Length: 272  Bit Score: 358.23  E-value: 1.72e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   26 EILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGPGLVGSLLIGISAAKAFAWAN 105
Cdd:pfam00814   1 EILANVILSQKDLHAPYGGVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  106 NLPLIPVNHMAGHIYAARFQKPFEFPlLALLVSGGHTELVYMKeDGNYQIIGETRDDAAGEAYDKVGRVLGLSYPSGKEI 185
Cdd:pfam00814  81 NKPLVGVNHLEAHALAARLETGLEFP-VVLLVSGGHTQVYAAK-DGRYEILGETLDDAAGEAFDKVARLLGLPYPGGPKI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  186 DQLAHRGedTYHFPRAMIhesNYDFSFSGLKSAFINLVHNAQqrgetlDTNNLAASFQASVVDVLVNKTLRACNEYPVKQ 265
Cdd:pfam00814 159 EKLAKEG--AFEFPRPVK---GMDFSFSGLKTAVLRLIEKKE------PKEDIAASFQEAVFDHLAEKTERALKLPGAKE 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 498409035  266 LIVAGGVAANQGLRETLEEAlkKEHPEIELLIPPLKLCGDNAAMIGA 312
Cdd:pfam00814 228 LVILGGVAANKRLREALTEM--AEERGVKLFAPPLEYCTDNGAMIAW 272
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 7-311 2.80e-124

metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted O-sialoglycoprotein endopeptidase (glycoprotease, EC 3.4.24.57) of Pasteurella haemolytica, a pathogen. A member from Riemerella anatipestifer, associated with cohemolysin activity, likewise is exported without benefit of a classical signal peptide and shows glycoprotease activity on the test substrate glycophorin. However, archaeal members of this subfamily show unrelated activities as demonstrated in Pyrococcus abyssi: DNA binding, iron binding, apurinic endonuclease activity, genomic association with a kinase domain, and no glycoprotease activity. This family thus pulls together a set of proteins as a homology group that appears to be near-universal in life, yet heterogeneous in assayed function between bacteria and archaea. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 129429 [Multi-domain]  Cd Length: 305  Bit Score: 358.98  E-value: 2.80e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035    7 LAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGPG 86
Cdd:TIGR00329   1 LGIETSCDDTGVAIVDEEGNVLANIKISQIPLHAKYGGVVPEEASRHHAENIPPLLERALIESNVDKSEIDLIAVTRGPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   87 LVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARF-QKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAAG 165
Cdd:TIGR00329  81 LGGSLRVGATFARSLALALNKPLIGVNHLLGHIYIPRLdTNIPQFPFVSLLVSGGHTQIILVKGIGDYEVLGETLDDAVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  166 EAYDKVGRVLGLSYPSGKEIDQLAHRG-EDTYHFPRAMIHESNYDFSFSGLKSAFINLVHNAQQRGETLDTNNLAASFQA 244
Cdd:TIGR00329 161 EAFDKVARLLGLGYPGGPKIEELAKKGdALPFYFPLPYTVKPMLDFSFSGLKTAARRKIEKLGKNLNEATKEDIAYSFQE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498409035  245 SVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIG 311
Cdd:TIGR00329 241 TAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLETLCQELN--VEFYYPPLEFCSDNGAMIA 305
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 6-320 2.85e-116

nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) and similar proteins from eukayotes; The family includes mammalian OSGEPL1 and yeast QRI7, which are the mitochondrial orthologs of the universal Kae1/ TsaD (also known as YgjD) protein. OSGEPL1/QRI7 (EC 2.3.1.234), also called mitochondrial tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. It is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. It is involved in mitochondrial genome maintenance.


Pssm-ID: 466984  Cd Length: 330  Bit Score: 339.50  E-value: 2.85e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24134    1 VLGIETSCDDTGAAVVDSDGRILGEALASQKEIHEQYGGIVPTLAADLHRANIPRVVEEALEQAGLSLSDLDAVAVTVGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAAR-FQKPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAA 164
Cdd:cd24134   81 GLALCLRVGLEFAKGLAAAHNKPLIPVHHMEAHALTARlTEEPVEFPFLVLLVSGGHCLLVLARGVGDYTILGTTLDDAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPS-----GKEIDQLAHRG--EDTYHFPRAMIHESNYDFSFSGLKSAFINLVhnaQQRGETLDT-- 235
Cdd:cd24134  161 GEAFDKVARLLGLKPLCdglsgGAALEALAKEGdpAAFKPFPVPMSKRKDCDFSFSGLKTAVRRLI---EKLEKEEGVgl 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 236 -----NNLAASFQASVVDVLVNKTLRA---CNEYP--VKQLIVAGGVAANQGLRETLEEALkkEHPEIELLIPPLKLCGD 305
Cdd:cd24134  238 slperADIAASFQHAAVRHLEDRLRRAlkyCRELPpePKTLVVSGGVASNQYLRKRLETLA--EEHGLQLVCPPPRLCTD 315

                        330
                 ....*....|....*
gi 498409035 306 NAAMIGAAAHVELKQ 320
Cdd:cd24134  316 NGVMIAWAGIERLRA 330
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 6-319 5.35e-95

nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD, or tRNA threonylcarbamoyladenosine biosynthesis protein TsaD, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. The family also includes mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.


Pssm-ID: 466947  Cd Length: 313  Bit Score: 284.95  E-value: 5.35e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24097    1 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQ-KPFEFPLLALLVSGGHTELVYMKEDGNYQIIGETRDDAA 164
Cdd:cd24097   81 GLVGALLVGATVGRSLAFAWNVPAIPVHHMEGHLLAPMLEdNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRG-EDTYHFPRAMIHESNYDFSFSGLKSAFINlvhNAQQRGETLDT-NNLAASF 242
Cdd:cd24097  161 GEAFDKTAKLLGLDYPGGPLLSKMAAQGtAGRFVFPRPMTDRPGLDFSFSGLKTFAAN---TIRDNGTDEQTrADIARAF 237

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498409035 243 QASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAAAHVELK 319
Cdd:cd24097  238 EDAVVDTLMIKCKRALDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRR--GEVFYARPEFCTDNGAMIAYAGMVRFK 312
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 6-313 9.53e-88

nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine threonylcarbamoyltransferase; tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein, or tRNA threonylcarbamoyladenosine biosynthesis protein, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. The family includes different orthologous of tRNA N6-adenosine threonylcarbamoyltransferase, such as bacterial kinase-associated endopeptidase 1 (Kae1) and TsaD (also known as YgjD) protein, mammalian O-sialoglycoprotein endopeptidase (OSGEP) and yeast protein Kae1, as well as mammalian OSGEP-like protein 1 (OSGEPL1) and yeast protein Qri7, which are the mitochondrial versions of the universal Kae1/TsaD (also known as YgjD) protein and essential for mitochondrial genome maintenance.


Pssm-ID: 466881  Cd Length: 304  Bit Score: 265.88  E-value: 9.53e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKNGDEILANVIASQINSHKrfGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24031    1 VLGIEGSADKTGVGIVDDEGKVLANQLDTYVTPKA--GGIVPEEAARHHARKIVPLIQEALKESGLTAKDIDLIAYTQGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPfEFPLLALLVSGGHTELVYMKEdGNYQIIGETRDDAAG 165
Cdd:cd24031   79 GLGGALRVGATVARTLAVAWNKPIIGVNHCIGHLEIPKLNTP-AFPPVALYVSGGNTQVIAYTG-GRYRVFGETIDIAVG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 166 EAYDKVGRVLGLSYPSGKEIDQLAHRGEDTYHFPRAMiheSNYDFSFSGLKSAFINLVHNAQQRGETLDtnNLAASFQAS 245
Cdd:cd24031  157 NALDKFARELGLDYPGGPLIEKMAAQGKKLVELPYTV---KGMDFSFSGLLTAAARTYRDGGTDEQTRE--DIAYSFQET 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498409035 246 VVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKEHpeIELLIPPLKLCGDNAAMIGAA 313
Cdd:cd24031  232 VFDMLVEKTERALAHTNKKEVVLVGGVSANNRLREMLATMCEKRG--GEFFYPPPEFCTDNGAMIAYA 297
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 5-311 2.67e-65

nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and similar proteins mainly from archaea and bacteria; Kae1 (EC 2.3.1.234), also called N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.


Pssm-ID: 466981  Cd Length: 323  Bit Score: 209.05  E-value: 2.67e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQInshKRFGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:cd24131    2 IVLGIEGTAHTFGVGIVDSEGEVLANVTDTYV---PEKGGIHPREAAEHHSEVAPELIKKALEEAGVSLNDIDLIAFSQG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLaLLVSGGHTELVYMkEDGNYQIIGETRDDAA 164
Cdd:cd24131   79 PGLGPCLRVVATAARALALKLDKPLVGVNHCIAHIEIGRLTTGAKDPVT-LYVSGGNTQVIAY-VNGRYRVFGETLDIGI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRGEDTYHFP---RAMihesnyDFSFSGLKSAFINLVhnaqQRGETLDtnNLAAS 241
Cdd:cd24131  157 GNALDKFAREVGLGHPGGPKIEKLAEKGKKYVELPytvKGM------DLSFSGLLTAALRAY----KSGARLE--DVCYS 224

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 242 FQASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEaLKKEHpEIELLIPPLKLCGDNAAMIG 311
Cdd:cd24131  225 LQETAFAMLVEVTERALAHTGKDEVLLVGGVAANNRLREMLRE-MCEER-GAKFYVPPPELCGDNGAMIA 292
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 7-310 6.61e-64

universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner Bud32 is fused with it in about half of the known archaeal genomes. The pair, which appears universal in the archaea, corresponds to EKC/KEOPS complex in eukaryotes. A recent characterization of the member from Pyrococcus abyssi, as an iron-binding, atypical DNA-binding protein with an apurinic lyase activity, challenges the common annotation of close homologs as O-sialoglycoprotein endopeptidase. The latter annotation is based on a characterized protein from the bacterium Pasteurella haemolytica. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274747  Cd Length: 322  Bit Score: 205.57  E-value: 6.61e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035    7 LAIESSCDETSVAVVKNGDEILANVIASQINSHkrfGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGPG 86
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVDEDGEILANVSDTYVPEK---GGIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   87 LVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPlLALLVSGGHTeLVYMKEDGNYQIIGETRDDAAGE 166
Cdd:TIGR03722  78 LGPCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTTGAKDP-VVLYVSGGNT-QVIAYRNGRYRVFGETLDIGLGN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  167 AYDKVGRVLGLSYPSGKEIDQLAHRGEDTYHFP---RAMihesnyDFSFSGLKSAFINLVhnaqQRGETLDtnNLAASFQ 243
Cdd:TIGR03722 156 ALDKFAREVGLGHPGGPKIEELAEKGKEYIELPytvKGM------DLSFSGLLTAALRAY----KKGARLE--DVCYSLQ 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498409035  244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEaLKKEHpEIELLIPPLKLCGDNAAMI 310
Cdd:TIGR03722 224 ETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREMLEL-MAEDR-GAKFYVPPPEYAGDNGAMI 288
PRK14878 PRK14878
UGMP family protein; Provisional
 7-310 7.97e-61

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 197.45  E-value: 7.97e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   7 LAIESSCDETSVAVVKnGDEILANVIASQINSHkrfGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGPG 86
Cdd:PRK14878   1 LGIESTAHTLGVGIVK-EDKVLANVRDTYVPEK---GGIHPREAAQHHAEVAPELLRKALEKAGISIEDIDAVAVSQGPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  87 LVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPlLALLVSGGHTeLVYMKEDGNYQIIGETRDDAAGE 166
Cdd:PRK14878  77 LGPALRVGATAARALALKYNKPLVPVNHCIAHIEIGRLTTGAKDP-VVLYVSGGNT-QVLAFRGGRYRVFGETLDIAIGN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 167 AYDKVGRVLGLSYPSGKEIDQLAHRGEDTYHFPRAMIHEsnyDFSFSGLKSAFINLVhnaqQRGETLDtnNLAASFQASV 246
Cdd:PRK14878 155 ALDTFAREVGLAPPGGPAIEKCAEKGEKYIELPYVVKGQ---DLSFSGLLTAALRLY----KGKERLE--DVCYSLRETA 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498409035 247 VDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEaLKKEHpEIELLIPPLKLCGDNAAMI 310
Cdd:PRK14878 226 FAMLVEVTERALAHTGKKEVLLVGGVAANRRLREKLEI-MAEDR-GAKFYVVPPEYAGDNGAMI 287
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 5-314 9.30e-60

nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called kinase-associated endopeptidase 1, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, kinase-associated endopeptidase 1 (Kae1), t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1, or tRNA threonylcarbamoyladenosine biosynthesis protein Kae1, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is a component of the KEOPS complex that is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Kae1 likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is the mammalian orthologue of kinase-associated endopeptidase Kae1. The family also includes bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein (EC 2.3.1.234/EC 2.7.11.1), which contains a Kae1 domain and a Bud32 domain. The Kae1 domain may play a catalytic role and the Bud32 domain probably displays kinase activity that regulates Kae1 function.


Pssm-ID: 466946  Cd Length: 301  Bit Score: 194.19  E-value: 9.30e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANViaSQINSHKRfGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:cd24096    1 ICLGIEGTAHTFGVGIVDSDGKVLANV--RDMYTPPK-GGIHPREAADHHAEVFDKLLSEALEEAGVTINDIDLIAFSQG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLaLLVSGGHTElVYMKEDGNYQIIGETRDDAA 164
Cdd:cd24096   78 PGLGPSLRVTATVARTLAVLLNKPIIGVNHCIAHIEIGKLTTGAKDPVV-LYVSGGNTQ-VIAYVGKRYRVFGETLDIGI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLSYPSGKEIDQLAHRGEDTYHFPRAMiheSNYDFSFSGLKSAFINLVHnaqqRGETLDtnNLAASFQA 244
Cdd:cd24096  156 GNCLDQFARELGLPFPGGPKIEKLAEKGKKLIDLPYTV---KGMDVSFSGLLTAAERAYK----SGYRKE--DLCYSLQE 226

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 245 SVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLeEALKKEHpEIELLIPPLKLCGDNAAMIGAAA 314
Cdd:cd24096  227 TAFAMLVEITERALAHTGKDEVLLVGGVAANNRLREML-KAMCEDR-GIKFFVPPKEYCGDNGAMIAWTG 294
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
5-319 9.61e-53

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 182.01  E-value: 9.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANV-IASQINShkrfGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTY 83
Cdd:PRK09605   2 IVLGIEGTAWKTSAGIVDSDGDVLFNEsDPYKPPS----GGIHPREAAEHHAEAIPKVIKEALEEAGLKPEDIDLVAFSQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  84 GPGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLaLLVSGGHTELV-YMkeDGNYQIIGETRDD 162
Cdd:PRK09605  78 GPGLGPCLRVVATAARALALSLDVPLIGVNHCVAHVEIGRLTTGAEDPVT-LYVSGGNTQVLaYL--NGRYRVFGETLDI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 163 AAGEAYDKVGRVLGLSYPSGKEIDQLAHRGEDTYHFP---RAMihesnyDFSFSGLKSAFInlvhNAQQRGETLDtnNLA 239
Cdd:PRK09605 155 GVGNALDKFARHVGLPHPGGPKIEKLAKDGKKYIDLPyvvKGM------DFSFSGLLTAAK----RAYDAGEPLE--DVC 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 240 ASFQASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEaLKKEHpEIELLIPPLKLCGDNAAMIGAAAHVELK 319
Cdd:PRK09605 223 YSLQETAFAMLTEVTERALAHTGKDEVLLVGGVAANNRLREMLKE-MCEER-GADFYVPEPRFCGDNGAMIAWLGLLMYK 300
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 5-326 4.36e-43

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 152.11  E-value: 4.36e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRfgGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:PTZ00340   2 LALGIEGSANKLGVGIVTSDGEILSNVRETYITPPGT--GFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLaLLVSGGHTElVYMKEDGNYQIIGETRDDAA 164
Cdd:PTZ00340  80 PGMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLVTGAENPVV-LYVSGGNTQ-VIAYSEHRYRIFGETIDIAV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLS-YPS-GKEIDQLAHRGEDTYHFP---RAMihesnyDFSFSGLKSAFINLVHNAQQR---------G 230
Cdd:PTZ00340 158 GNCLDRFARLLNLSnDPApGYNIEQLAKKGKNLIELPyvvKGM------DMSFSGILTYIEDLVEHPQFKdvvseivppE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 231 ETLDTNNLAASFQASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALK----KEHPEIEllipplKLCGDN 306
Cdd:PTZ00340 232 EEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKerggKLFAMDE------RYCIDN 305

                        330       340
                 ....*....|....*....|
gi 498409035 307 AAMIGAAAHVELKQANFADL 326
Cdd:PTZ00340 306 GAMIAYAGLLEYLSGGFTPL 325
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 5-313 2.47e-37

nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar proteins mainly from eukaryotes; OSGEP (EC 2.3.1.234), also called tRNA N6-adenosine threonylcarbamoyltransferase, N6-L-threonylcarbamoyladenine synthase, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein OSGEP, tRNA threonylcarbamoyladenosine biosynthesis protein OSGEP, is a component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction but requires other protein(s) of the complex to fulfill this activity. OSGEP is the mammalian orthologue of kinase-associated endopeptidase Kae1.


Pssm-ID: 466982  Cd Length: 309  Bit Score: 135.75  E-value: 2.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGDEILANVIASQINSHKRfgGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:cd24132    1 IALGIEGSANKLGVGIVRSDGEILSNPRHTYITPPGQ--GFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  85 PGLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFQKPFEFPLLaLLVSGGHTELVYMKEdGNYQIIGETRDDAA 164
Cdd:cd24132   79 PGMGAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLVTGAQNPVV-LYVSGGNTQVIAYSE-KRYRIFGETIDIAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 165 GEAYDKVGRVLGLS-YPS-GKEIDQLAHRGEDTYHFP---RAMihesnyDFSFSGLKSAFINLVHNAQQRGEtLDTNNLA 239
Cdd:cd24132  157 GNCLDRFARVLKLSnDPSpGYNIEQLAKKGKKLIELPytvKGM------DVSFSGILSYIEKLAKKKLKKGE-CTPEDLC 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 240 ASFQASVVDVLVNKTLRA---CNEYPVkqLIVaGGVAANQGLRETLEEALK----KEHPEIEllipplKLCGDNAAMIGA 312
Cdd:cd24132  230 FSLQETVFAMLVEITERAmahCGSKEV--LIV-GGVGCNLRLQEMMGIMAEerggKLFATDE------RYCIDNGAMIAQ 300


                 .
gi 498409035 313 A 313
Cdd:cd24132  301 A 301
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 6-145 1.05e-35

nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA N6-adenosine threonylcarbamoyltransferase Kae1/TsaD, tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ), as well as proteins from the NodU/CmcH subfamily. tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. TsaB is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7) is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2) functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12) acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. nodulation protein NolNO (EC 2.1.3.-) is involved in the O-carbamoylation of nod factors. The NodU/CmcH subfamily proteins consist of two domains. Only the N-terminal domain shows similarity with Kae1/TsaB-like domain, which belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466851 [Multi-domain]  Cd Length: 186  Bit Score: 127.95  E-value: 1.05e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKNGdEILANVIASQINSHkrfGGVVPEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24001    1 VLGIEGSAEDTGVAIVDDG-GVLANHFETYVTEK---TGGYPPEAARHHARRIVPLIQEALAESGLTLDDIDAIAFGRGP 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNHMAGHIYAARFqKPFEFPLLALLVSGGHTELV 145
Cdd:cd24001   77 GLGGALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKL-KTGATRPVALIVSGGNTQVI 135
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 5-113 5.93e-19

tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine modification protein TsaB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440827  Cd Length: 227  Bit Score: 84.13  E-value: 5.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   5 LILAIESSCDETSVAVVKNGdEILANVIasqinshkrfggvvpEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYG 84
Cdd:COG1214    2 LILAIDTSTEACSVALLDDG-EVLAERE---------------ENDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGIG 65

                         90       100       110
                 ....*....|....*....|....*....|..
gi 498409035  85 PglvGS---LLIGISAAKAFAWANNLPLIPVN 113
Cdd:COG1214   66 P---GSftgLRIGVATAKGLALALGIPLVGVS 94
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 6-192 1.09e-18

nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB (previously known as YeaZ) and similar proteins; TsaB, also called t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaB, is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. It may be involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, it can act as a protease that specifically degrades TsaD in vitro; therefore, TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. TsaB does not show sialoglycoprotease activity against glycophorin A.


Pssm-ID: 466882 [Multi-domain]  Cd Length: 205  Bit Score: 83.10  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDETSVAVVKnGDEILAnviasQINSHKRfggvvpevasRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:cd24032    1 ILAIDTSTSACSVALLK-GGKILA-----EYELDLG----------RRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGP 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  86 GLVGSLLIGISAAKAFAWANNLPLIPVNH---MA------------------GHIYAARFQKPFEFPLL---ALLVSGGH 141
Cdd:cd24032   65 GSFTGLRIGLATAKGLALALGIPLVGVSTleaLAqnapradgrvlpaidarrGEVYWALYERDKGGLILeeeEAVLPPEE 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 498409035 142 TELVYMKEDgNYQIIGETRDDAAGEAYDKVGRVLGLSYPSGKEIDQLAHRG 192
Cdd:cd24032  145 LEEILLLKK-PAILVGDGWDKYPDLIKENPVLPIELLLPSAADLAPLALAK 194
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 6-128 4.00e-18

tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein family, YeaZ, now associated with the threonylcarbamoyl adenosine (t6A) tRNA modification. Members of this family may occur as fusions with ygjD (previously gcp) or the ribosomal protein N-acetyltransferase rimI, and is frequently encoded next to rimI. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274750 [Multi-domain]  Cd Length: 204  Bit Score: 81.54  E-value: 4.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035    6 ILAIESSCDETSVAVVKNGdeilaNVIASQInshkrfggvvpEVASRHHVEQITLCIEDALAEAGTSVEQLSAVAVTYGP 85
Cdd:TIGR03725   1 ILAIDTSTEALSVALLDDG-----KVLAERT-----------EPAGRNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGP 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 498409035   86 GlvgS---LLIGISAAKAFAWANNLPLIPVN---HMAGHIYAARFQKPF 128
Cdd:TIGR03725  65 G---SftgLRIGLATAKGLALALGIPLVGVSsleALAAQAAAQDGGGPV 110
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 16-316 5.17e-06

N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH family includes NodU from Rhizobium, CmcH from Amycolatopsis lactamdurans, the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius, NovN from Streptomyces niveus and NolNO from Sinorhizobium fredii. NodU is a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. 3'-hydroxymethylcephem-O-carbamoyltransferase CmcH (EC 2.1.3.7), also called 3'-hydroxymethylcephem-O-CASE (CCT), is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity. nebramycin 5' synthase TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. Novobiocin biosynthesis protein NovN (EC 2.1.3.12), also called decarbamoylnovobiocin carbamoyltransferase, acts as a carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. Nodulation protein NolNO (EC 2.1.3.-), also called NolO or Y4hD, is involved in the O-carbamoylation of nod factors. Members in this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466883 [Multi-domain]  Cd Length: 268  Bit Score: 47.29  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  16 TSVAVVKNGdEILANVIAsqinshKRFGGVvpevasRHHVEQITLCIEDALAEAGtsVEQLSAVAVTYGPGLVGSLLIGI 95
Cdd:cd24033   12 ASAALLDDG-ELVFALEE------ERFTRI------KHDKGFPEEALEELLEEAG--LEDIDDVDVVVVSNNDLDRLDLL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  96 SAAKAFAWANNL-------------PLIPVNHMAGHIYAARFQKPFEfplLALLVS---GGHTE--LVYMKEDGNYQIIG 157
Cdd:cd24033   77 LRLLAPAVGLRLylkkkllflgkevPIYYVDHHLAHAASAFYTSPFE---EALVLVidgGGDDEsfSIYYGDGGKLKLLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 158 ETRDDAA-GEAYDKVGRVLGLSYPS--GKeidqlahrgedtyhfpramihesnydfsFSGLKSAfinlvhnaqqrGEtld 234
Cdd:cd24033  154 KFSPPLSlGLLYSAITSLLGFKGLSgaGK----------------------------LMGLAAY-----------GA--- 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 235 tnNLAASFQASVVDVLVNKTLRACNEYPVKQLIVAGGVA----ANQglretleeALKKEHPEIELLIPPlkLCGD--NAa 308
Cdd:cd24033  192 --DLAATVQKVFEEALLELIKKLLERTGSDNLCLSGGCAlncvANS--------KLAEEGLFKNVFVPP--APGDsgLS- 258


                 ....*...
gi 498409035 309 mIGAAAHV 316
Cdd:cd24033  259 -LGAALYV 265
COG2192 COG2192
Predicted carbamoyl transferase, NodU family [General function prediction only];
62-316 9.99e-06

Predicted carbamoyl transferase, NodU family [General function prediction only];


Pssm-ID: 441795 [Multi-domain]  Cd Length: 568  Bit Score: 47.08  E-value: 9.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  62 IEDALAEAGTSVEQLSAVAVTYGPGLVGSLLIGISAAKA----FAWANNLP-----------------------LIPVNH 114
Cdd:COG2192   46 IRYCLAEAGITLADVDAVAFYWKPLLKFERLLETYLARAprglRSFLRALPgwlreklflkrllrreldgprpkVLFVEH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 115 MAGHIYAARFQKPFEFPllALLVSGG----HTELVYMKEDGNYQIIGETRD-----------------DAAGEAYdkvgR 173
Cdd:COG2192  126 HLAHAASAFFPSPFEEA--AVLTIDGvgewATTSIGHGRGGRIELLKEIRFphslgllysaftyylgfKVNSGEY----K 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 174 VLGLSyPSGKE------IDQLAHRGED-TYHFPRAMIhesNYDFSFSGLKSAFINLV-HNAQQRGETLDTN--NLAASFQ 243
Cdd:COG2192  200 VMGLA-PYGKPryvdllLRELIDLKDDgSFRLNMDYF---NYATGLRMTSEKLEELFgGPPRRPEDPLTQRhaDLAASVQ 275

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498409035 244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVA----ANQGLREtleealkkEHPEIELLIPPlklC-GDNAAMIGAAAHV 316
Cdd:COG2192  276 AVLEEVVLHLARHLHERTGSRNLCLAGGVAlncvANGRILR--------EGPFEDVWVQP---AaGDAGTALGAALAV 342
Carbam_trans_N pfam02543
Carbamoyltransferase N-terminus; This domain is found in NodU from Rhizobium, CmcH from ...
 108-313 3.14e-04

Carbamoyltransferase N-terminus; This domain is found in NodU from Rhizobium, CmcH from Nocardia lactamdurans and the bifunctional carbamoyltransferase TobZ from Streptoalloteichus tenebrarius. NodU a Rhizobium nodulation protein involved in the synthesis of nodulation factors has 6-O-carbamoyltransferase-like activity. CmcH is involved in cephamycin (antibiotic) biosynthesis and has 3-hydroxymethylcephem carbamoyltransferase activity, EC:2.1.3.7 catalysing the reaction: Carbamoyl phosphate + 3-hydroxymethylceph-3-EM-4-carboxylate <=> phosphate + 3-carbamoyloxymethylcephem. TobZ functions as an ATP carbamoyltransferase and tobramycin carbamoyltransferase. These proteins contain two domains, this is the larger, N-terminal, domain.


Pssm-ID: 426823 [Multi-domain]  Cd Length: 352  Bit Score: 42.25  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  108 PLIPVNHMAGHIYAARFQKPF---EFPLLALLVSGG-HTELVYMKEDGNYQIIGETRDDAA-GEAYDKVGRVLGLSYPSG 182
Cdd:pfam02543 126 DVSSYEHHLGHAASAYYTSPFapkETLVLCLDGDGDwKPRSLWLFKGGDRRIHWLFPYSASiGHAYSAFTEHFGFYPNSD 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  183 K-EIDQLAHRGE---------------DTYhfpRAMIHESNYDFSFSGLKSAFINL-----VHNAQQR---GETLDTNNL 238
Cdd:pfam02543 206 EgKLMALAAYGKpddlilgelqnlykkAGY---RINKEKLRWEHNINILLKKFHDFfeaprLHNKQYRqkwKEKIGDEDI 282

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498409035  239 AASFQASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQglreTLEEALKKEHPEIELLIPPLKlcGDNAAMIGAA 313
Cdd:pfam02543 283 AATIQVFLERLVVEYHNIVYEKFKIRNLCIAGGVGLNI----KWNSALRERGLFEDVWIFPAP--GDSGSAIGAA 351
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 6-316 5.53e-04

N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and similar proteins; The family includes a group of uncharacterized proteins similar to Methanocaldococcus jannaschii protein MJ1051 and protein MJ1058. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466950 [Multi-domain]  Cd Length: 238  Bit Score: 40.92  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035   6 ILAIESSCDeTSVAVVKNGDEILAnviASQinshKRFggvvpevaSR--HHVEQITLCIEDALAEAGTSVEQLSAVAVTY 83
Cdd:cd24100    2 ILGIHDGHD-SSAALLEDGKIVAA---VSE----ERF--------TRvkNDGGFPYRAIEEVLKLAGISPSDIDAVAVAG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  84 gpglvgslligisaakafaWANNLPLIPVNHMAGHIYAA-RFQKPFEfPLLALLVSG---GHTELVYMKEDGNYQIIGET 159
Cdd:cd24100   66 -------------------LFSKAKIIFVDHHLAHAASAyYTSPGFD-DALVITLDGggdGLSGTVSIGEGGKLERLATS 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 160 RDDAA-GEAYDKVGRVLGLSYPS--GKeIDQLAHRGEDtyhfpramihesnydfsfsglksafinlvhnaqqrgetldtn 236
Cdd:cd24100  126 PALASlGLFYSYVTELLGFKPNRheGK-VMGLAAYGED------------------------------------------ 162

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 237 nLAASFQASVVDVLVnKTLRAC-NEYPVKQLIVAGGVAAN----QGLRETleealkkehPEIE-LLIPPlkLCGDNAAMI 310
Cdd:cd24100  163 -IAAAVQRVLEEVVV-EWVKNAlKKTGIKNLALAGGVFANvklnQRIAEL---------PEVEnLFVFP--SMGDGGLAL 229


                 ....*.
gi 498409035 311 GAAAHV 316
Cdd:cd24100  230 GAALLA 235
ASKHA_NBD_TobZ_N cd24098
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
 237-316 4.31e-03

N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar proteins; TobZ (EC 6.1.2.2), also called kanamycin A carbamoyltransferase, or tobramycin carbamoyltransferase, is involved in the biosynthesis of the 2-deoxystreptamine-containing aminoglycoside antibiotics such as nebramycin 5 and 6-O-carbamoylkanamycin. It catalyzes the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP to yield O-carbamoyladenylate. Then it catalyzes the transfer of the carbamoyl moiety from O-carbamoyladenylate to the tobramycin 6-hydroxy group to yield nebramycin 5'. It catalyzes the same reaction with kanamycin A. These reactions are considerably slower in the presence of deoxy-ATP. TobZ consists of two major domains: the N-terminal Kae1-like domain is involved in the transfer of carbamoyl from O-carbamoyladenylate to tobramycin or kanamycin; the C-terminal YrdC-like domain is involved in the hydrolysis of carbamoyl phosphate and its subsequent adenylation by ATP. The model corresponds to the N-terminal domain.


Pssm-ID: 466948 [Multi-domain]  Cd Length: 243  Bit Score: 38.21  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 237 NLAASFQASVVDVLVNKTLRACNEYPVKQLIVAGGVA----ANQGLretLEEALKKehpeiELLIPPlkLCGDNAAMIGA 312
Cdd:cd24098  166 DLAASVQAVLEEAVLHLARYLRKKTGERNLCLAGGVAlncvANGKL---LREGPFD-----NIFIQP--AAGDAGTALGA 235


                 ....
gi 498409035 313 AAHV 316
Cdd:cd24098  236 ALAV 239
ASKHA_NBD_O66634-like_rpt1 cd24034
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
 43-313 6.51e-03

nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.


Pssm-ID: 466884 [Multi-domain]  Cd Length: 258  Bit Score: 37.57  E-value: 6.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035  43 GGVVPEVASRHHVEQITLCIEDALAEAGT-SVEQLSAVAVTygpglvgslliGiSAAKAFAWANNLPliPVNHMAGHIYA 121
Cdd:cd24034   19 KGNIVFSDYERHFGNPREALLELLEEIKErLGDEIARIAVT-----------G-SGGRGLAELLGLP--FVQEVVAIEAA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 122 ARFQKPfefPLLALLVSGGHTELVY-MKEDGNYQIIGETRDDAA--GEAYDKVGRVLGLSypsGKEIDQLAHRGEDTYHF 198
Cdd:cd24034   85 VKHLHP---DARTVIEIGGEDFKLIeLDGDGKLKDFRMNSKCAAgtGAFIDQQARRLGLS---LEELAELALKAEPPAPI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 199 pramihesnydfsfSGLKSAFI--NLVHnAQQRGETLDtNNLAASFQASVVDVlvnKTLRACNEYPVKQLIVAGGVAA-N 275
Cdd:cd24034  159 --------------AGRCSVFAksDMIH-LQNKGVPKE-DIAAGLCRAVARNV---IATLAKGREIEGPVILVGGVATnN 219

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 498409035 276 QGLRETLEEALkkehPEIELLIPPLklcGDNAAMIGAA 313
Cdd:cd24034  220 AVLREAFEELL----GDEELIVPEH---AEYFEALGAA 250
ASKHA_NBD_YjiL-like cd24109
nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The ...
 244-313 7.07e-03

nucleotide-binding domain (NBD) of Escherichia coli protein YjiL and similar proteins; The subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YjiL, which belongs to the BcrAD/BadFG-like ATPase family that also includes the BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins, which are subunits of benzoyl-CoA reductase that may be involved in ATP hydrolysis.


Pssm-ID: 466959 [Multi-domain]  Cd Length: 243  Bit Score: 37.56  E-value: 7.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498409035 244 ASVVDVLVNKTLRACNEYPVKQLIVAGGVAANQGLRETLEEALKKehpeiELLIPPLklcGDNAAMIGAA 313
Cdd:cd24109  180 AGVNYSIAKRVAPLLNRLKSPPIVLTGGVARNKAIIELLEKRLGA-----EVIVPEL---PQFAGAIGAA 241
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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