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Conserved domains on  [gi|654546765|ref|WP_028014471|]
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MULTISPECIES: tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD [Enterobacter]

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]; ...
 1-331 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: 622.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:COG0533    1 MLILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDD 160
Cdd:COG0533   81 GPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLEDPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 161 AAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNN--DDSDQTRADIARA 238
Cdd:COG0533  161 AAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEKLkqKGEEQDKADIAAS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 239 FEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGAT 318
Cdd:COG0533  241 FQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERLKAGEF 320

                        330
                 ....*....|...
gi 654546765 319 SDLSVSVRPRWPL 331
Cdd:COG0533  321 SDLDLNARPRLPL 333
 
Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-331 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: 622.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:COG0533    1 MLILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDD 160
Cdd:COG0533   81 GPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLEDPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 161 AAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNN--DDSDQTRADIARA 238
Cdd:COG0533  161 AAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEKLkqKGEEQDKADIAAS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 239 FEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGAT 318
Cdd:COG0533  241 FQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERLKAGEF 320

                        330
                 ....*....|...
gi 654546765 319 SDLSVSVRPRWPL 331
Cdd:COG0533  321 SDLDLNARPRLPL 333
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-337 0e+00

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 603.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:PRK09604   1 MLILGIETSCDETSVAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAIAVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEEnPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDD 160
Cdd:PRK09604  81 GPGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEE-EPEFPFLALLVSGGHTQLVLVKGIGDYELLGETLDD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 161 AAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMtDRPGLDFSFSGLKTFAANTIRNNddsDQTRADIARAFE 240
Cdd:PRK09604 160 AAGEAFDKVAKLLGLGYPGGPAIDKLAKQGDPDAFKFPRPM-DRPGLDFSFSGLKTAVLNTIEKS---EQTKADIAASFQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGATSD 320
Cdd:PRK09604 236 AAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDNAAMIAAAGYERLKAGEFSD 315

                        330
                 ....*....|....*..
gi 654546765 321 LSVSVRPRWPLAELPEA 337
Cdd:PRK09604 316 LDLNARPRWPLDELSAL 332
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 3-314 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: 567.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765    3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKGLLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLeENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAA 162
Cdd:TIGR03723  81 GLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFL-EKPLEFPFLALLVSGGHTQLVLVKGVGDYELLGETLDDAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  163 GEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNNDDS--DQTRADIARAFE 240
Cdd:TIGR03723 160 GEAFDKVARLLGLGYPGGPAIDRLAKQGDPKAFKFPRPMLDRPGLDFSFSGLKTAVLNLIEKLKQKgeELTKADIAASFQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546765  241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLN 314
Cdd:TIGR03723 240 AAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAAMIAAAGYERLK 313
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 3-328 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: 555.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24133    1 ILGIETSCDETAVAVVDDGGKILSNVVSSQIDLHAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAA 162
Cdd:cd24133   81 GLIGALLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLEDPPPEFPFLALLVSGGHTQLVLVKDFGRYELLGETRDDAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 163 GEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNN--DDSDQTRADIARAFE 240
Cdd:cd24133  161 GEAFDKVAKLLGLGYPGGPAIDKLAKEGDPTAFVFPRPMLKRDGYDFSFSGLKTAVLNYLEKNkqDGIEQNKADIAASFQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGATSD 320
Cdd:cd24133  241 EAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDNAAMIAAAGYYRYKRGKFAD 320


                 ....*...
gi 654546765 321 LSVSVRPR 328
Cdd:cd24133  321 LDLNARPR 328
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 23-307 2.80e-126

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: 362.47  E-value: 2.80e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   23 GLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGPGLVGALLVGATVGRSLAFAW 102
Cdd:pfam00814   1 EILANVILSQKDLHAPYGGVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  103 DVPAIPVHHMEGHLLAPMLEEnPPEFPfVALLVSGGHTQLISVTGiGKYELLGESIDDAAGEAFDKTAKLLGLDYPGGPM 182
Cdd:pfam00814  81 NKPLVGVNHLEAHALAARLET-GLEFP-VVLLVSGGHTQVYAAKD-GRYEILGETLDDAAGEAFDKVARLLGLPYPGGPK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  183 LSKMASqgtEGRFVFPRPMTdrpGLDFSFSGLKTFAANTIRNNddsdQTRADIARAFEDAVVDTLMIKCKRALDQTGFKR 262
Cdd:pfam00814 158 IEKLAK---EGAFEFPRPVK---GMDFSFSGLKTAVLRLIEKK----EPKEDIAASFQEAVFDHLAEKTERALKLPGAKE 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 654546765  263 LVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAY 307
Cdd:pfam00814 228 LVILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIAW 272
 
Name Accession Description Interval E-value
TsaD COG0533
tRNA A37 threonylcarbamoyltransferase TsaD [Translation, ribosomal structure and biogenesis]; ...
 1-331 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: 622.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:COG0533    1 MLILGIETSCDETAAAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHLENILPLVEEALEEAGVTLKDIDAIAVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDD 160
Cdd:COG0533   81 GPGLIGALLVGVSFAKALALALGKPLIGVNHLEGHLLAPFLEDPPPEFPFLALLVSGGHTQLVLVKGVGDYELLGETIDD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 161 AAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNN--DDSDQTRADIARA 238
Cdd:COG0533  161 AAGEAFDKVAKLLGLGYPGGPAIDKLAKEGDPKAFRFPRPMLDRPGLDFSFSGLKTAVLNYIEKLkqKGEEQDKADIAAS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 239 FEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGAT 318
Cdd:COG0533  241 FQEAVVDVLVEKTRRALKETGVKRLVVAGGVAANSRLRERLEELAEKRGIRLFFPPLELCTDNAAMIAAAGYERLKAGEF 320

                        330
                 ....*....|...
gi 654546765 319 SDLSVSVRPRWPL 331
Cdd:COG0533  321 SDLDLNARPRLPL 333
PRK09604 PRK09604
tRNA (adenosine(37)-N6)-threonylcarbamoyltransferase complex transferase subunit TsaD;
1-337 0e+00

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


Pssm-ID: 236585  Cd Length: 332  Bit Score: 603.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:PRK09604   1 MLILGIETSCDETSVAVVDDGRGLLSNVVASQIDLHARYGGVVPELASRAHVENIVPLIEEALKEAGLTLEDIDAIAVTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEEnPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDD 160
Cdd:PRK09604  81 GPGLVGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFLEE-EPEFPFLALLVSGGHTQLVLVKGIGDYELLGETLDD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 161 AAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMtDRPGLDFSFSGLKTFAANTIRNNddsDQTRADIARAFE 240
Cdd:PRK09604 160 AAGEAFDKVAKLLGLGYPGGPAIDKLAKQGDPDAFKFPRPM-DRPGLDFSFSGLKTAVLNTIEKS---EQTKADIAASFQ 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGATSD 320
Cdd:PRK09604 236 AAVVDVLVIKTKRALKQTGVKTLVVAGGVAANSGLRERLAELAKKRGIEVFIPPLKLCTDNAAMIAAAGYERLKAGEFSD 315

                        330
                 ....*....|....*..
gi 654546765 321 LSVSVRPRWPLAELPEA 337
Cdd:PRK09604 316 LDLNARPRWPLDELSAL 332
T6A_TsaD_YgjD TIGR03723
tRNA threonylcarbamoyl adenosine modification protein TsaD; This model represents bacterial ...
 3-314 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: 567.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765    3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:TIGR03723   1 ILGIETSCDETAVAIVDDGKGLLSNVVASQIDLHARYGGVVPELASRAHLENIPPLIEEALAEAGLTLSDIDAIAVTAGP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLeENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAA 162
Cdd:TIGR03723  81 GLIGALLVGVSFAKALALALNKPLIGVNHLEGHLLAPFL-EKPLEFPFLALLVSGGHTQLVLVKGVGDYELLGETLDDAA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  163 GEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNNDDS--DQTRADIARAFE 240
Cdd:TIGR03723 160 GEAFDKVARLLGLGYPGGPAIDRLAKQGDPKAFKFPRPMLDRPGLDFSFSGLKTAVLNLIEKLKQKgeELTKADIAASFQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 654546765  241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLN 314
Cdd:TIGR03723 240 AAVVDVLVEKTKRALKKTGLKTLVVAGGVAANSRLRERLEELAEKRGLEVFFPPLELCTDNAAMIAAAGYERLK 313
ASKHA_NBD_TsaD_bac cd24133
nucleotide-binding domain (NBD) of bacterial tRNA N6-adenosine threonylcarbamoyltransferase ...
 3-328 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: 555.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24133    1 ILGIETSCDETAVAVVDDGGKILSNVVSSQIDLHAKYGGVVPEIASRAHLENIIPVVEEALEEAGLTLDDIDAIAVTYGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAA 162
Cdd:cd24133   81 GLIGALLVGVSFAKALAFALNKPLIGVNHLEGHILAPFLEDPPPEFPFLALLVSGGHTQLVLVKDFGRYELLGETRDDAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 163 GEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNN--DDSDQTRADIARAFE 240
Cdd:cd24133  161 GEAFDKVAKLLGLGYPGGPAIDKLAKEGDPTAFVFPRPMLKRDGYDFSFSGLKTAVLNYLEKNkqDGIEQNKADIAASFQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNAGATSD 320
Cdd:cd24133  241 EAVVDVLVEKTLRAAKETGIKRLVVAGGVAANSRLREKLEEAAEKRGLEVYIPPPELCTDNAAMIAAAGYYRYKRGKFAD 320


                 ....*...
gi 654546765 321 LSVSVRPR 328
Cdd:cd24133  321 LDLNARPR 328
ASKHA_NBD_TsaD-like cd24097
nucleotide-binding domain (NBD) of TsaD and similar proteins; TsaD (EC 2.3.1.234), also called ...
 3-315 0e+00

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: 553.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24097    1 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAA 162
Cdd:cd24097   81 GLVGALLVGATVGRSLAFAWNVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 163 GEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNNDDSDQTRADIARAFEDA 242
Cdd:cd24097  161 GEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDEQTRADIARAFEDA 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546765 243 VVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNA 315
Cdd:cd24097  241 VVDTLMIKCKRALDSTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKA 313
gcp_kae1 TIGR00329
metallohydrolase, glycoprotease/Kae1 family; This subfamily includes the well-studied secreted ...
 4-306 1.14e-177

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: 494.18  E-value: 1.14e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765    4 LGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGPG 83
Cdd:TIGR00329   1 LGIETSCDDTGVAIVDEEGNVLANIKISQIPLHAKYGGVVPEEASRHHAENIPPLLERALIESNVDKSEIDLIAVTRGPG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   84 LVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAAG 163
Cdd:TIGR00329  81 LGGSLRVGATFARSLALALNKPLIGVNHLLGHIYIPRLDTNIPQFPFVSLLVSGGHTQIILVKGIGDYEVLGETLDDAVG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  164 EAFDKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRNN--DDSDQTRADIARAFED 241
Cdd:TIGR00329 161 EAFDKVARLLGLGYPGGPKIEELAKKGDALPFYFPLPYTVKPMLDFSFSGLKTAARRKIEKLgkNLNEATKEDIAYSFQE 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 654546765  242 AVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIA 306
Cdd:TIGR00329 241 TAFDHLIEKTKRALKDTNPKELVLVGGVSANKRLREKLETLCQELNVEFYYPPLEFCSDNGAMIA 305
ASKHA_NBD_Kae1_TsaD cd24031
nucleotide-binding domain (NBD) of the Kae1/TsaD family tRNA N6-adenosine ...
 3-315 5.51e-164

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: 459.25  E-value: 5.51e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHAdyGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24031    1 VLGIEGSADKTGVGIVDDEGKVLANQLDTYVTPKA--GGIVPEEAARHHARKIVPLIQEALKESGLTAKDIDLIAYTQGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLeeNPPEFPFVALLVSGGHTQLISVTGiGKYELLGESIDDAA 162
Cdd:cd24031   79 GLGGALRVGATVARTLAVAWNKPIIGVNHCIGHLEIPKL--NTPAFPPVALYVSGGNTQVIAYTG-GRYRVFGETIDIAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 163 GEAFDKTAKLLGLDYPGGPMLSKMASQGTEGRfvfpRPMTDRPGLDFSFSGLKTFAANTIRNNDDSDQTRADIARAFEDA 242
Cdd:cd24031  156 GNALDKFARELGLDYPGGPLIEKMAAQGKKLV----ELPYTVKGMDFSFSGLLTAAARTYRDGGTDEQTREDIAYSFQET 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546765 243 VVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNA 315
Cdd:cd24031  232 VFDMLVEKTERALAHTNKKEVVLVGGVSANNRLREMLATMCEKRGGEFFYPPPEFCTDNGAMIAYAGLEMFKA 304
ASKHA_NBD_OSGEPL1_QRI7_euk cd24134
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase-like protein 1 (OSGEPL1) ...
 3-315 2.18e-129

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: 372.62  E-value: 2.18e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24134    1 VLGIETSCDDTGAAVVDSDGRILGEALASQKEIHEQYGGIVPTLAADLHRANIPRVVEEALEQAGLSLSDLDAVAVTVGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEENPPEFPFVALLVSGGHTQLISVTGIGKYELLGESIDDAA 162
Cdd:cd24134   81 GLALCLRVGLEFAKGLAAAHNKPLIPVHHMEAHALTARLTEEPVEFPFLVLLVSGGHCLLVLARGVGDYTILGTTLDDAP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 163 GEAFDKTAKLLGLDYP-----GGPMLSKMASQGTEGRF-VFPRPMTDRPGLDFSFSGLKTFAANTIR------NNDDSDQ 230
Cdd:cd24134  161 GEAFDKVARLLGLKPLcdglsGGAALEALAKEGDPAAFkPFPVPMSKRKDCDFSFSGLKTAVRRLIEklekeeGVGLSLP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 231 TRADIARAFEDAVVDTLMIKCKRALDQTG-----FKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMI 305
Cdd:cd24134  241 ERADIAASFQHAAVRHLEDRLRRALKYCRelppePKTLVVSGGVASNQYLRKRLETLAEEHGLQLVCPPPRLCTDNGVMI 320

                        330
                 ....*....|
gi 654546765 306 AYAGMVRLNA 315
Cdd:cd24134  321 AWAGIERLRA 330
TsaD pfam00814
tRNA N6-adenosine threonylcarbamoyltransferase; This domain can be found in Kae1/Qri7/YgjD, ...
 23-307 2.80e-126

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: 362.47  E-value: 2.80e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   23 GLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGPGLVGALLVGATVGRSLAFAW 102
Cdd:pfam00814   1 EILANVILSQKDLHAPYGGVVPELASRHHSERLMPLIDEALAEAGLSLEDLDAIAVTKGPGLFTGLRVGASFAKGLALAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  103 DVPAIPVHHMEGHLLAPMLEEnPPEFPfVALLVSGGHTQLISVTGiGKYELLGESIDDAAGEAFDKTAKLLGLDYPGGPM 182
Cdd:pfam00814  81 NKPLVGVNHLEAHALAARLET-GLEFP-VVLLVSGGHTQVYAAKD-GRYEILGETLDDAAGEAFDKVARLLGLPYPGGPK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  183 LSKMASqgtEGRFVFPRPMTdrpGLDFSFSGLKTFAANTIRNNddsdQTRADIARAFEDAVVDTLMIKCKRALDQTGFKR 262
Cdd:pfam00814 158 IEKLAK---EGAFEFPRPVK---GMDFSFSGLKTAVLRLIEKK----EPKEDIAASFQEAVFDHLAEKTERALKLPGAKE 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 654546765  263 LVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAY 307
Cdd:pfam00814 228 LVILGGVAANKRLREALTEMAEERGVKLFAPPLEYCTDNGAMIAW 272
ASKHA_NBD_Kae1_arch_bac cd24131
nucleotide-binding domain (NBD) of tRNA N6-adenosine threonylcarbamoyltransferase (Kae1) and ...
 1-335 1.04e-76

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: 238.32  E-value: 1.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLAN--QLYSQVKlhadyGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAY 78
Cdd:cd24131    1 MIVLGIEGTAHTFGVGIVDSEGEVLANvtDTYVPEK-----GGIHPREAAEHHSEVAPELIKKALEEAGVSLNDIDLIAF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  79 TAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLE---ENPpefpfVALLVSGGHTQLISVTGiGKYELLG 155
Cdd:cd24131   76 SQGPGLGPCLRVVATAARALALKLDKPLVGVNHCIAHIEIGRLTtgaKDP-----VTLYVSGGNTQVIAYVN-GRYRVFG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 156 ESIDDAAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEgrfVFPRPMTDRpGLDFSFSGLKTFAANTIRNNddsdQTRADI 235
Cdd:cd24131  150 ETLDIGIGNALDKFAREVGLGHPGGPKIEKLAEKGKK---YVELPYTVK-GMDLSFSGLLTAALRAYKSG----ARLEDV 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 236 ARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGMVRLNA 315
Cdd:cd24131  222 CYSLQETAFAMLVEVTERALAHTGKDEVLLVGGVAANNRLREMLREMCEERGAKFYVPPPELCGDNGAMIAWTGLLMYKH 301

                        330       340
                 ....*....|....*....|.
gi 654546765 316 GATSDLSVS-VRPRWPLAELP 335
Cdd:cd24131  302 GIRMSLEETiVRPRFRTDEVD 322
arch_KAE1 TIGR03722
universal archaeal protein Kae1; This family represents the archaeal protein Kae1. Its partner ...
 4-335 3.89e-76

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: 236.77  E-value: 3.89e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765    4 LGIETSCDETGIAIYDDEKGLLANQlysQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGPG 83
Cdd:TIGR03722   1 LGIEGTAHTFGVGIVDEDGEILANV---SDTYVPEKGGIHPREAAEHHAEVAPKLIKEALEEAGVSLEDIDAVAFSQGPG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   84 LVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLE---ENPpefpfVALLVSGGHTQLISVTGiGKYELLGESIDD 160
Cdd:TIGR03722  78 LGPCLRVGATAARALALKLNKPLVGVNHCVAHIEIGRLTtgaKDP-----VVLYVSGGNTQVIAYRN-GRYRVFGETLDI 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  161 AAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEgrfVFPRPMTDRpGLDFSFSGLKTFAANTIRNNDDsdqtRADIARAFE 240
Cdd:TIGR03722 152 GLGNALDKFAREVGLGHPGGPKIEELAEKGKE---YIELPYTVK-GMDLSFSGLLTAALRAYKKGAR----LEDVCYSLQ 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLaEMMQKRRGEVFYARP-EFCTDNGAMIAYAGMVRLNAGATS 319
Cdd:TIGR03722 224 ETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREML-ELMAEDRGAKFYVPPpEYAGDNGAMIAYTGLLMYKHGVTI 302

                         330
                  ....*....|....*..
gi 654546765  320 DLSVS-VRPRWPLAELP 335
Cdd:TIGR03722 303 PVEESrVRQRWRTDEVE 319
ASKHA_NBD_Kae1-like cd24096
nucleotide-binding domain (NBD) of Kae1 and similar proteins; Kae1 (EC 2.3.1.234), also called ...
 3-316 7.26e-70

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: 220.00  E-value: 7.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLAN--QLYSQVKlhadyGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:cd24096    2 CLGIEGTAHTFGVGIVDSDGKVLANvrDMYTPPK-----GGIHPREAADHHAEVFDKLLSEALEEAGVTINDIDLIAFSQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHL-LAPMLE--ENPpefpfVALLVSGGHTQLISVTGiGKYELLGES 157
Cdd:cd24096   77 GPGLGPSLRVTATVARTLAVLLNKPIIGVNHCIAHIeIGKLTTgaKDP-----VVLYVSGGNTQVIAYVG-KRYRVFGET 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 158 IDDAAGEAFDKTAKLLGLDYPGGPMLSKMASQGTEgrfVFPRPMTDRpGLDFSFSGLKTFAANTIRnnddSDQTRADIAR 237
Cdd:cd24096  151 LDIGIGNCLDQFARELGLPFPGGPKIEKLAEKGKK---LIDLPYTVK-GMDVSFSGLLTAAERAYK----SGYRKEDLCY 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 238 AFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMqKRRGEVFYARP-EFCTDNGAMIAYAGMVRLNAG 316
Cdd:cd24096  223 SLQETAFAMLVEITERALAHTGKDEVLLVGGVAANNRLREMLKAMC-EDRGIKFFVPPkEYCGDNGAMIAWTGLLMYKAG 301
PRK14878 PRK14878
UGMP family protein; Provisional
 4-335 1.80e-68

UGMP family protein; Provisional


Pssm-ID: 184878  Cd Length: 323  Bit Score: 217.10  E-value: 1.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   4 LGIETSCDETGIAIYDDEKgLLANqLYSQvkLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGPG 83
Cdd:PRK14878   1 LGIESTAHTLGVGIVKEDK-VLAN-VRDT--YVPEKGGIHPREAAQHHAEVAPELLRKALEKAGISIEDIDAVAVSQGPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  84 LVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLE---ENPpefpfVALLVSGGHTQLISVTGiGKYELLGESIDD 160
Cdd:PRK14878  77 LGPALRVGATAARALALKYNKPLVPVNHCIAHIEIGRLTtgaKDP-----VVLYVSGGNTQVLAFRG-GRYRVFGETLDI 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 161 AAGEAFDKTAKLLGLDYPGGPMLSKMASqgtEGRFVFPRPMTDRpGLDFSFSGLKTFAANTIrnndDSDQTRADIARAFE 240
Cdd:PRK14878 151 AIGNALDTFAREVGLAPPGGPAIEKCAE---KGEKYIELPYVVK-GQDLSFSGLLTAALRLY----KGKERLEDVCYSLR 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 241 DAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLaEMMQKRRGEVFYARP-EFCTDNGAMIAYAGMVRLNAGATS 319
Cdd:PRK14878 223 ETAFAMLVEVTERALAHTGKKEVLLVGGVAANRRLREKL-EIMAEDRGAKFYVVPpEYAGDNGAMIAYTGLLAYKHGVTI 301

                        330
                 ....*....|....*..
gi 654546765 320 DLSVS-VRPRWPLAELP 335
Cdd:PRK14878 302 PPEESfVRQRWRLDEVD 318
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
1-328 1.43e-64

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 212.83  E-value: 1.43e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQlysQVKLHADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:PRK09605   1 MIVLGIEGTAWKTSAGIVDSDGDVLFNE---SDPYKPPSGGIHPREAAEHHAEAIPKVIKEALEEAGLKPEDIDLVAFSQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLlapmlE--------ENPpefpfVALLVSGGHTQLISVTGiGKYE 152
Cdd:PRK09605  78 GPGLGPCLRVVATAARALALSLDVPLIGVNHCVAHV-----EigrlttgaEDP-----VTLYVSGGNTQVLAYLN-GRYR 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 153 LLGESIDDAAGEAFDKTAKLLGLDYPGGPMLSKMAsqgTEGRFVFPRPMTDRpGLDFSFSGLKTFAANTIrnndDSDQTR 232
Cdd:PRK09605 147 VFGETLDIGVGNALDKFARHVGLPHPGGPKIEKLA---KDGKKYIDLPYVVK-GMDFSFSGLLTAAKRAY----DAGEPL 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 233 ADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRrGEVFYA-RPEFCTDNGAMIAYAGMV 311
Cdd:PRK09605 219 EDVCYSLQETAFAMLTEVTERALAHTGKDEVLLVGGVAANNRLREMLKEMCEER-GADFYVpEPRFCGDNGAMIAWLGLL 297

                        330
                 ....*....|....*...
gi 654546765 312 RLNAGATSDLSVS-VRPR 328
Cdd:PRK09605 298 MYKAGDTLDIEDTrVNPN 315
ASKHA_NBD_Kae1_TsaB-like cd24001
nucleotide-binding domain (NBD) of the Kae1/TsaB-like domain family; The family includes tRNA ...
 3-310 1.48e-62

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: 197.29  E-value: 1.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDeKGLLANQLYSQVKLHADYGGVVPelaSRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24001    1 VLGIEGSAEDTGVAIVDD-GGVLANHFETYVTEKTGGYPPEA---ARHHARRIVPLIQEALAESGLTLDDIDAIAFGRGP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLeeNPPEFPFVALLVSGGHTQLISVTgigkyellgesiddaa 162
Cdd:cd24001   77 GLGGALRVGATVARGLALAWDKPLIGVNHCIAHAEIAKL--KTGATRPVALIVSGGNTQVIAYE---------------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 163 geafdktakllgldypggpmlskmasqgtegrfvfprpmtdrpgldfsfsglktfaantirnnddsdqtradiarafeda 242
Cdd:cd24001      --------------------------------------------------------------------------------

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546765 243 vvdtlmikckraldqtgfkrLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAMIAYAGM 310
Cdd:cd24001  139 --------------------LVLVGGVSANNRLREKLATMCEKRGDKFFVPPGEFCIDNGAMIAYAGL 186
PTZ00340 PTZ00340
O-sialoglycoprotein endopeptidase-like protein; Provisional
 1-328 4.90e-57

O-sialoglycoprotein endopeptidase-like protein; Provisional


Pssm-ID: 240369  Cd Length: 345  Bit Score: 188.32  E-value: 4.90e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKlhADYGGVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:PTZ00340   1 FLALGIEGSANKLGVGIVTSDGEILSNVRETYIT--PPGTGFLPRETAQHHREHILSLVKEALEEAKITPSDISLICYTK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  81 GPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPML---EENPpefpfVALLVSGGHTQLISVTgIGKYELLGES 157
Cdd:PTZ00340  79 GPGMGAPLSVGAVVARTLSLLWGKPLVGVNHCVAHIEMGRLvtgAENP-----VVLYVSGGNTQVIAYS-EHRYRIFGET 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 158 IDDAAGEAFDKTAKLLGLD-YPG-GPMLSKMASqgtEGRFVFPRPMTDRpGLDFSFSGLKTFAANTIRNN---------- 225
Cdd:PTZ00340 153 IDIAVGNCLDRFARLLNLSnDPApGYNIEQLAK---KGKNLIELPYVVK-GMDMSFSGILTYIEDLVEHPqfkdvvseiv 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 226 -DDSDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYARPEFCTDNGAM 304
Cdd:PTZ00340 229 pPEEEFFTDDLCFSLQETIFAMLVEVTERAMSHCGSNEVLIVGGVGCNLRLQEMMQQMAKERGGKLFAMDERYCIDNGAM 308

                        330       340
                 ....*....|....*....|....*..
gi 654546765 305 IAYAGMVRLNAGATSDL---SVSVRPR 328
Cdd:PTZ00340 309 IAYAGLLEYLSGGFTPLkdaTVTQRFR 335
ASKHA_NBD_OSGEP_like_euk cd24132
nucleotide-binding domain (NBD) of O-sialoglycoprotein endopeptidase (OSGEP) and similar ...
 3-316 1.08e-51

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: 173.11  E-value: 1.08e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDEKGLLANQLYSQVklhADYG-GVVPELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAG 81
Cdd:cd24132    2 ALGIEGSANKLGVGIVRSDGEILSNPRHTYI---TPPGqGFLPRDTAKHHRAHILDLVKEALKEAGITPSDIDCICYTKG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  82 PGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPML---EENPpefpfVALLVSGGHTQLISVTGiGKYELLGESI 158
Cdd:cd24132   79 PGMGAPLQSVAVVARTLSQLWNKPLVGVNHCVGHIEMGRLvtgAQNP-----VVLYVSGGNTQVIAYSE-KRYRIFGETI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 159 DDAAGEAFDKTAKLLGL-DYPG-GPMLSKMASQGTegRFVfPRPMTDRpGLDFSFSGLKTFAANTIRNNDDSDQ-TRADI 235
Cdd:cd24132  153 DIAVGNCLDRFARVLKLsNDPSpGYNIEQLAKKGK--KLI-ELPYTVK-GMDVSFSGILSYIEKLAKKKLKKGEcTPEDL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 236 ARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRtlraKLAEMMQ---KRRGEVFYARPE-FCTDNGAMIAYAGMV 311
Cdd:cd24132  229 CFSLQETVFAMLVEITERAMAHCGSKEVLIVGGVGCNL----RLQEMMGimaEERGGKLFATDErYCIDNGAMIAQAGLL 304


                 ....*
gi 654546765 312 RLNAG 316
Cdd:cd24132  305 MFRSG 309
TsaB COG1214
tRNA A37 threonylcarbamoyladenosine modification protein TsaB [Translation, ribosomal ...
 1-109 1.54e-16

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: 77.58  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKgLLANQLysqvklhadyggvvpELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTA 80
Cdd:COG1214    1 MLILAIDTSTEACSVALLDDGE-VLAERE---------------ENDGRGHSERLLPMIDELLAEAGLTLSDLDAIAVGI 64

                         90       100       110
                 ....*....|....*....|....*....|
gi 654546765  81 GPG-LVGaLLVGATVGRSLAFAWDVPAIPV 109
Cdd:COG1214   65 GPGsFTG-LRIGVATAKGLALALGIPLVGV 93
T6A_YeaZ TIGR03725
tRNA threonylcarbamoyl adenosine modification protein YeaZ; This family describes a protein ...
 3-134 1.99e-14

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: 71.14  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765    3 VLGIETSCDETGIAIYDDEKgllanqLYSQVKlhadyggvvpELASRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:TIGR03725   1 ILAIDTSTEALSVALLDDGK------VLAERT----------EPAGRNHSERLLPMIEELLAEAGLSLQDLDAIAVGVGP 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 654546765   83 GLVGALLVGATVGRSLAFAWDVPAIPVHHMEghLLAPMLEENPPEFPFVALL 134
Cdd:TIGR03725  65 GSFTGLRIGLATAKGLALALGIPLVGVSSLE--ALAAQAAAQDGGGPVLVAI 114
ASKHA_NBD_TsaB cd24032
nucleotide-binding domain (NBD) of tRNA threonylcarbamoyladenosine biosynthesis protein TsaB ...
 3-109 3.96e-14

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: 70.00  E-value: 3.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   3 VLGIETSCDETGIAIYDDekgllaNQLYSQVKLHADyggvvpelasRDHVRKTVPLIQAALKEAGLSSTDIDAVAYTAGP 82
Cdd:cd24032    1 ILAIDTSTSACSVALLKG------GKILAEYELDLG----------RRHSERLLPMIDELLKEAGLSLKDLDAIAVGIGP 64

                         90       100
                 ....*....|....*....|....*..
gi 654546765  83 GLVGALLVGATVGRSLAFAWDVPAIPV 109
Cdd:cd24032   65 GSFTGLRIGLATAKGLALALGIPLVGV 91
COG2192 COG2192
Predicted carbamoyl transferase, NodU family [General function prediction only];
1-277 1.40e-09

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


Pssm-ID: 441795 [Multi-domain]  Cd Length: 568  Bit Score: 59.02  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765   1 MRVLGIETSCDETGIAIYDDEKGLLANQL--YSQVKLHADYggvvPELAsrdhvrktvplIQAALKEAGLSSTDIDAVAY 78
Cdd:COG2192    1 MYILGISAFYHDSAAALVVDGEIVAAAEEerFTRIKHDKAF----PRNA-----------IRYCLAEAGITLADVDAVAF 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  79 TAGPGLVGALLVGATVGRSLAFAWD-VPAIPVHHME----GHLLAPMLEENPPEFPFV---------ALLVSG-GHTQLI 143
Cdd:COG2192   66 YWKPLLKFERLLETYLARAPRGLRSfLRALPGWLREklflKRLLRRELDGPRPKVLFVehhlahaasAFFPSPfEEAAVL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 144 SVTGIG-------------KYELLGEsIDDAAG-----EAFdkTA-----------KLLGL-DYpGGP-----MLSKMAS 188
Cdd:COG2192  146 TIDGVGewattsighgrggRIELLKE-IRFPHSlgllySAF--TYylgfkvnsgeyKVMGLaPY-GKPryvdlLLRELID 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 189 QGTEGRFVFPRPMTDRPGLDFSFSGL--KTFAANTIRNNDDSDQTRADIARA----FEDAVVDTLmikcKRALDQTGFKR 262
Cdd:COG2192  222 LKDDGSFRLNMDYFNYATGLRMTSEKleELFGGPPRRPEDPLTQRHADLAASvqavLEEVVLHLA----RHLHERTGSRN 297

                        330
                 ....*....|....*....
gi 654546765 263 LVMAGGV----SANRTLRA 277
Cdd:COG2192  298 LCLAGGValncVANGRILR 316
HypF COG0068
Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, ...
 232-308 5.65e-06

Hydrogenase maturation factor HypF (carbamoyltransferase) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439838 [Multi-domain]  Cd Length: 757  Bit Score: 48.18  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 232 RADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMQKRRGEVFYAR--PefCTDNG-----AM 304
Cdd:COG0068  672 PAEIAARFHNTLAEAIAELALRLAERTGIDTVALSGGVFQNRLLLELLRARLEAAGFKVLLHRqvP--PNDGGislgqAA 749


                 ....
gi 654546765 305 IAYA 308
Cdd:COG0068  750 IAAA 753
ASKHA_NBD_MJ1051-like_N cd24100
N-terminal nucleotide-binding domain (NBD) of Methanocaldococcus jannaschii protein MJ1051 and ...
 233-282 5.76e-05

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: 43.62  E-value: 5.76e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 654546765 233 ADIA----RAFEDAVVDTLmikcKRALDQTGFKRLVMAGGVSANRTLRAKLAEM 282
Cdd:cd24100  161 EDIAaavqRVLEEVVVEWV----KNALKKTGIKNLALAGGVFANVKLNQRIAEL 210
ASKHA_NBD_NovN-like_N cd24099
N-terminal nucleotide-binding domain (NBD) of Streptomyces niveus novobiocin biosynthesis ...
 59-280 8.97e-04

N-terminal nucleotide-binding domain (NBD) of Streptomyces niveus novobiocin biosynthesis protein N (NovN) and similar proteins; The family includes a group of proteins similar to Streptomyces niveus novobiocin biosynthesis protein N (NovN) and Sinorhizobium fredii nodulation protein NolNO. 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. Novobiocincin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases. NolNO (EC 2.1.3.-), also called NolO or Y4hD, is involved in the O-carbamoylation of nod factors. Members of this family consist of two domains. The model corresponds to the N-terminal Kae1-like domain.


Pssm-ID: 466949 [Multi-domain]  Cd Length: 340  Bit Score: 40.68  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765  59 IQAALKEAGLSSTDIDAVAYTAGPGLVGALL------VGATV---GRSL-------AFAWDVPAIPVHHMEGHLLAPMle 122
Cdd:cd24099   61 IRACLEAAGISLDDIDAIAFYFEEDFLDAILkllylpHRDLEykdARALirrllsdAFGYEIDPDKIVFVDHHLAHAA-- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 123 enppefpfVALLVSGGHTQLISVT-GIGKYE--------------LLGESIDDAAGEAFDKTAKLLGLDY---------- 177
Cdd:cd24099  139 --------SAYAMSGFDDSLVLTLdGSGDGEsgsvfkgsggeletLATYSVADSLGLFYLDVIKLLGYGMfdeykvmgla 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 178 PGG------PMLSKMASQGTEGRFVFPRpmtDRpgLDFSFSGLKtfaantIRNNDDSD-QTRADIA----RAFEDAVVDT 246
Cdd:cd24099  211 PYGdpskyrPLFKSLYTLLPNGRYELNF---DI--VDALFEGLP------PRRKGEPFtQVHKDIAaslqEALEDIVLHI 279

                        250       260       270
                 ....*....|....*....|....*....|....
gi 654546765 247 LMIKCKraldQTGFKRLVMAGGVSANRTLRAKLA 280
Cdd:cd24099  280 LRHWQQ----ATGHRNLCLAGGVAHNCTLNGKIL 309
ASKHA_NBD_HSP70 cd10170
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
 130-299 4.42e-03

nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466811 [Multi-domain]  Cd Length: 329  Bit Score: 38.62  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 130 FVALLVSGGHTQLISVTGIGKYELLG-ESIDDAAGEAF-----DKTAKLLGLDYPGGPMLSKMASQGTEGRFVFPRPMTD 203
Cdd:cd10170  150 LSLYEVTSGSPLLLEEVAPGGGALLGgTDIDEAFEKLLreklgDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546765 204 RPGLDFSFSGLKTFAANTIRnnddsdQTRADIARAFEDAV--VDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAE 281
Cdd:cd10170  230 VPSLLGGGLPELGLEKGTLL------LTEEEIRDLFDPVIdkILELIEEQLEAKSGTPPDAVVLVGGFSRSPYLRERLRE 303

                        170
                 ....*....|....*...
gi 654546765 282 MMQKRRGEVFYARPEFCT 299
Cdd:cd10170  304 RFGSAGIIIVLRSDDPDT 321
ASKHA_NBD_TobZ_N cd24098
N-terminal nucleotide-binding domain (NBD) of nebramycin 5' synthase (TobZ) and similar ...
 233-281 4.62e-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: 4.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 654546765 233 ADIARAFEdAVVDTLMIK-CKRALDQTGFKRLVMAGGVSANRTLRAKLAE 281
Cdd:cd24098  165 KDLAASVQ-AVLEEAVLHlARYLRKKTGERNLCLAGGVALNCVANGKLLR 213
ASKHA_NBD_NodU_CmcH-like_N cd24033
N-terminal nucleotide-binding domain (NBD) of the NodU/CmcH family proteins; The NodU/CmcH ...
 233-281 6.29e-03

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: 37.66  E-value: 6.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 654546765 233 ADIA----RAFEDAVVDTLmikcKRALDQTGFKRLVMAGGVSANRTLRAKLAE 281
Cdd:cd24033  191 ADLAatvqKVFEEALLELI----KKLLERTGSDNLCLSGGCALNCVANSKLAE 239
 
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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