NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1864361956|ref|WP_176743843|]
View 

MULTISPECIES: tRNA lysidine(34) synthetase TilS [Staphylococcus]

Protein Classification

tRNA lysidine(34) synthetase( domain architecture ID 17564802)

tRNA lysidine(34) synthetase TilS converts cytidine to lysidine by ligating lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner and thus changing the amino acid specificity of the tRNA from methionine to isoleucine

CATH:  3.40.50.620
EC:  6.3.4.19
Gene Ontology:  GO:0005524|GO:0032267|GO:0006400
PubMed:  18073113|12012333|15894617|10447505
SCOP:  3000688|3001593

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 6-203 9.34e-70

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


:

Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 220.47  E-value: 9.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956   6 SLWSNTDHVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTDVVA 85
Cdd:COG0037    10 RLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDVPAIAK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  86 -QGKSIQADARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHyTICRPLLEVSKE 164
Cdd:COG0037    90 kEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGGV-RLIRPLLYVSRK 168

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1864361956 165 DIRDYQHKYQVPYYEDSSNSDNKYVRNDIRNRLLPAINQ 203
Cdd:COG0037   169 EIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEE 207
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 357-418 7.50e-18

TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.


:

Pssm-ID: 198045 [Multi-domain]  Cd Length: 69  Bit Score: 77.22  E-value: 7.50e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864361956  357 LLIRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQyHQIIAVGNLYIAKAY 418
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYG-DEIVWVVGLRVDARF 61
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 6-203 9.34e-70

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 220.47  E-value: 9.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956   6 SLWSNTDHVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTDVVA 85
Cdd:COG0037    10 RLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDVPAIAK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  86 -QGKSIQADARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHyTICRPLLEVSKE 164
Cdd:COG0037    90 kEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGGV-RLIRPLLYVSRK 168

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1864361956 165 DIRDYQHKYQVPYYEDSSNSDNKYVRNDIRNRLLPAINQ 203
Cdd:COG0037   169 EIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEE 207
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 16-195 1.77e-69

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 217.49  E-value: 1.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  16 IAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTdvVAQGKSIQADAR 95
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVA--KKSGENLEAAAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  96 QLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHYTICRPLLEVSKEDIRDYQHKYQV 175
Cdd:pfam01171  79 EARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEHKI 158

                         170       180
                  ....*....|....*....|
gi 1864361956 176 PYYEDSSNSDNKYVRNDIRN 195
Cdd:pfam01171 159 PWFEDESNADDKYTRNRIRH 178
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 13-199 3.33e-69

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 217.08  E-value: 3.33e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  13 HVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLnlTDVVAQGKSIQA 92
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTV--TEAPKSGGNLEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  93 DARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHYTICRPLLEVSKEDIRDYQHK 172
Cdd:cd01992    79 AAREARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCRE 158

                         170       180
                  ....*....|....*....|....*..
gi 1864361956 173 YQVPYYEDSSNSDNKYVRNDIRNRLLP 199
Cdd:cd01992   159 NGLPWVEDPSNADLKYTRNRIRHELLP 185
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 13-199 1.40e-67

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 213.26  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  13 HVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTDV-VAQGKSIQ 91
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDVKALaKGKKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  92 ADARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNH-YTICRPLLEVSKEDIRDYQ 170
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSgIQIIRPLLGISKSEIEEYL 160

                         170       180
                  ....*....|....*....|....*....
gi 1864361956 171 HKYQVPYYEDSSNSDNKYVRNDIRNRLLP 199
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHELLP 189
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 13-203 1.59e-28

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 116.26  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  13 HVVIAVSTGIDSMSLLHNLLS-QSSRTYKQLTCLHVNHGLreaSHKEEAFIE---AFCKQYEIPCYVKRLNLTdvvAQGK 88
Cdd:PRK10660   17 QILVAFSGGLDSTVLLHLLVQwRTENPGVTLRAIHVHHGL---SPNADSWVKhceQVCQQWQVPLVVERVQLD---QRGL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  89 SIQADARQLRYEWFDEMmkrLDAD-VLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHYTICRPLLEVSKEDIR 167
Cdd:PRK10660   91 GIEAAARQARYQAFART---LLPGeVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELE 167

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1864361956 168 DYQHKYQVPYYEDSSNSDNKYVRNDIRNRLLPAINQ 203
Cdd:PRK10660  168 QYAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQ 203
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 357-418 7.50e-18

TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.


Pssm-ID: 198045 [Multi-domain]  Cd Length: 69  Bit Score: 77.22  E-value: 7.50e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864361956  357 LLIRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQyHQIIAVGNLYIAKAY 418
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYG-DEIVWVVGLRVDARF 61
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 357-402 1.72e-12

tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the family of the N-terminal domain of tRNA(Ile)-lysidine synthetase. This family (TIGR02433) describes a small C-terminal domain of about 50 residues present in about half the members of family TIGR02432,and in no other protein. Characterized examples of tRNA(Ile)-lysidine synthetase from E. coli and Bacillus subtilis both contain this domain. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274130 [Multi-domain]  Cd Length: 47  Bit Score: 61.40  E-value: 1.72e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1864361956 357 LLIRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQ 402
Cdd:TIGR02433   1 LTVRFRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYG 46
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 359-418 2.12e-09

TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.


Pssm-ID: 463335 [Multi-domain]  Cd Length: 73  Bit Score: 53.75  E-value: 2.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956 359 IRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQyHQIIAVGNLYIAKAY 418
Cdd:pfam11734   3 VRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYG-DQLVAVAGLGVAAGF 61
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 6-203 9.34e-70

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 220.47  E-value: 9.34e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956   6 SLWSNTDHVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTDVVA 85
Cdd:COG0037    10 RLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDVPAIAK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  86 -QGKSIQADARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHyTICRPLLEVSKE 164
Cdd:COG0037    90 kEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGGV-RLIRPLLYVSRK 168

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1864361956 165 DIRDYQHKYQVPYYEDSSNSDNKYVRNDIRNRLLPAINQ 203
Cdd:COG0037   169 EIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEE 207
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 16-195 1.77e-69

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 217.49  E-value: 1.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  16 IAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTdvVAQGKSIQADAR 95
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVA--KKSGENLEAAAR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  96 QLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHYTICRPLLEVSKEDIRDYQHKYQV 175
Cdd:pfam01171  79 EARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEHKI 158

                         170       180
                  ....*....|....*....|
gi 1864361956 176 PYYEDSSNSDNKYVRNDIRN 195
Cdd:pfam01171 159 PWFEDESNADDKYTRNRIRH 178
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 13-199 3.33e-69

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 217.08  E-value: 3.33e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  13 HVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLnlTDVVAQGKSIQA 92
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTV--TEAPKSGGNLEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  93 DARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHYTICRPLLEVSKEDIRDYQHK 172
Cdd:cd01992    79 AAREARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCRE 158

                         170       180
                  ....*....|....*....|....*..
gi 1864361956 173 YQVPYYEDSSNSDNKYVRNDIRNRLLP 199
Cdd:cd01992   159 NGLPWVEDPSNADLKYTRNRIRHELLP 185
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 13-199 1.40e-67

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 213.26  E-value: 1.40e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  13 HVVIAVSTGIDSMSLLHNLLSQSSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNLTDV-VAQGKSIQ 91
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDVKALaKGKKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  92 ADARQLRYEWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNH-YTICRPLLEVSKEDIRDYQ 170
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSgIQIIRPLLGISKSEIEEYL 160

                         170       180
                  ....*....|....*....|....*....
gi 1864361956 171 HKYQVPYYEDSSNSDNKYVRNDIRNRLLP 199
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHELLP 189
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 13-203 1.59e-28

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 116.26  E-value: 1.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  13 HVVIAVSTGIDSMSLLHNLLS-QSSRTYKQLTCLHVNHGLreaSHKEEAFIE---AFCKQYEIPCYVKRLNLTdvvAQGK 88
Cdd:PRK10660   17 QILVAFSGGLDSTVLLHLLVQwRTENPGVTLRAIHVHHGL---SPNADSWVKhceQVCQQWQVPLVVERVQLD---QRGL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  89 SIQADARQLRYEWFDEMmkrLDAD-VLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHYTICRPLLEVSKEDIR 167
Cdd:PRK10660   91 GIEAAARQARYQAFART---LLPGeVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELE 167

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1864361956 168 DYQHKYQVPYYEDSSNSDNKYVRNDIRNRLLPAINQ 203
Cdd:PRK10660  168 QYAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQ 203
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 357-418 7.50e-18

TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.


Pssm-ID: 198045 [Multi-domain]  Cd Length: 69  Bit Score: 77.22  E-value: 7.50e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864361956  357 LLIRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQyHQIIAVGNLYIAKAY 418
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYG-DEIVWVVGLRVDARF 61
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 357-402 1.72e-12

tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the family of the N-terminal domain of tRNA(Ile)-lysidine synthetase. This family (TIGR02433) describes a small C-terminal domain of about 50 residues present in about half the members of family TIGR02432,and in no other protein. Characterized examples of tRNA(Ile)-lysidine synthetase from E. coli and Bacillus subtilis both contain this domain. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274130 [Multi-domain]  Cd Length: 47  Bit Score: 61.40  E-value: 1.72e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1864361956 357 LLIRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQ 402
Cdd:TIGR02433   1 LTVRFRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYG 46
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 7-180 3.65e-12

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 64.65  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956   7 LWSNTDHVVIAVSTGIDSMSLLHNLlsqsSRTYKQLTCLHVNHGLREASHKEEAFIEAFCKQYEIPCYVKRLNltdvVAQ 86
Cdd:cd01993     4 MFEKDDKILVAVSGGKDSLALLAVL----KKLGYNVEALYINLGIGEYSEKSEEVVKKLAEKLNLPLHVVDLK----EEY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  87 GKSIQADARQL------------RYeWFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTG-RSTRSTLGIDVQSIR-NHY 152
Cdd:cd01993    76 GLGIPELAKKSrrppcsvcglvkRY-IMNKFAVENGFDVVATGHNLDDEAAFLLGNILNWnEEYLAKQGPFLLPEHgGLV 154

                         170       180
                  ....*....|....*....|....*...
gi 1864361956 153 TICRPLLEVSKEDIRDYQHKYQVPYYED 180
Cdd:cd01993   155 TRVKPLYEITEEEIALYALLNGIPYLEE 182
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 7-180 2.13e-11

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 62.99  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956   7 LWSNTDHVVIAVSTGIDSMSLLHNLLSQSSRTY--KQLTCLHVN---HGLREAShkeEAFIEAFCKQYEIPCYVKR---- 77
Cdd:cd01713    14 LIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDygVELIAVTIDegiKGYRDDS---LEAARKLAEEYGIPLEIVSfede 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  78 LNLT-DVVAQGKSIQADA--------RQLryewFDEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTR-STLGIDVQS 147
Cdd:cd01713    91 FGFTlDELIVGKGGKKNActycgvfrRRA----LNRGARELGADKLATGHNLDDEAETILMNLLRGDVARlLRTGPEPRS 166

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1864361956 148 IRNHYTI-CRPLLEVSKEDIRDYQHKYQVPYYED 180
Cdd:cd01713   167 EGEGLVPrIKPLRYIPEKEIVLYAHLNGLPYFST 200
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 12-176 9.27e-11

tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) 2-sulfurtransferase, also called two-thiocytidine biosynthesis protein A or tRNA 2-thiocytidine biosynthesis protein TtcA, catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). TtcA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467514 [Multi-domain]  Cd Length: 187  Bit Score: 60.75  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  12 DHVVIAVSTGIDSMSLLHnLLSQSSRTYK---QLTCLHVNHGLREAShkeeaFIEAFCKQY-EIPCYVKRLNLTDVVAQG 87
Cdd:cd24138     9 DRILVGLSGGKDSLTLLH-LLEELKRRAPikfELVAVTVDPGYPGYR-----PPREELAEIlEELGEILEDEESEIIIIE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  88 KSIQAD------ARQLRYEWFdEMMKRLDADVLLTAHHLDDQLETIFYRLFTGRSTRSTLGIDVQSIRNHyTICRPLLEV 161
Cdd:cd24138    83 KEREEKspcslcSRLRRGILY-SLAKELGCNKLALGHHLDDAVETLLMNLLYGGRLKTMPPKVTMDRGGL-TVIRPLIYV 160

                         170
                  ....*....|....*
gi 1864361956 162 SKEDIRDYQHKYQVP 176
Cdd:cd24138   161 REKDIRAFAEENGLP 175
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 359-418 2.12e-09

TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein.


Pssm-ID: 463335 [Multi-domain]  Cd Length: 73  Bit Score: 53.75  E-value: 2.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956 359 IRTRHNGDKVELNGQKGHKKVSRLFIDHKIPNDVRMQMPLIEDQyHQIIAVGNLYIAKAY 418
Cdd:pfam11734   3 VRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYG-DQLVAVAGLGVAAGF 61
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 14-101 5.57e-04

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 41.06  E-value: 5.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  14 VVIAVSTGIDSMSLLHNLLSQssrtYKQLTCLHVNHGLReASHKEEAFIEAFCKQYEIPCYVKRLN---------LTDVV 84
Cdd:cd01995     3 AVVLLSGGLDSTTLLYWALKE----GYEVHALTFDYGQR-HAKEELEAAKLIAKLLGIEHKVIDLSflgelggssLTDEG 77

                          90
                  ....*....|....*..
gi 1864361956  85 AQGKSIQADARQLRYEW 101
Cdd:cd01995    78 EEVPDGEYDEESIPSTW 94
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 10-113 9.21e-04

C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus.


Pssm-ID: 467501 [Multi-domain]  Cd Length: 311  Bit Score: 40.99  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864361956  10 NTDHVVIAVSTGIDSM---SLLHNLLSQssrtyKQLTCLHVNHGL-ReasHKEEAFIEAFCKQYEIpcyvkrLNLTDVVA 85
Cdd:cd01997     6 GDKKVLCLVSGGVDSTvcaALLHKALGD-----ERVIAVHIDNGLmR---KNESEQVEEALKKLGV------INLAKVDA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1864361956  86 QGKSIQA-----DARQLR-------YEWFDEMMKRLDADV 113
Cdd:cd01997    72 SKRFLKKlkgvtDPEEKRkiigdtfIEVFDEVAKELNLDP 111
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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