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Conserved domains on  [gi|1622318219|ref|WP_136282807|]
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tRNA lysidine(34) synthetase TilS [Streptococcus pyogenes]

Protein Classification

tRNA lysidine(34) synthetase TilS( domain architecture ID 10798083)

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 Symbol:  tilS
Gene Ontology:  GO:0005524|GO:0016879|GO:0006400
PubMed:  18073113|12012333|15894617
SCOP:  3001593|4002775

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 22-195 1.18e-76

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: 236.37  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  22 HVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNFE--------GIFSE 93
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDvkalakgkKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  94 KAARDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFA-NGQLIRPFLTFSKKDLPE-- 170
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGsGIQIIRPLLGISKSEIEEyl 160

                         170       180
                  ....*....|....*....|....*....
gi 1622318219 171 ----IFHFEDSSNRELSFLRNRVRNNYLP 195
Cdd:TIGR02432 161 kengLPWFEDETNQDDKYLRNRIRHELLP 189
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 350-399 3.42e-07

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: 47.18  E-value: 3.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622318219  350 IKLRSRQSGD--YISFGHFSKKIRRLFIDEKFTIAERQNAIIGEQDEQIIFV 399
Cdd:smart00977   1 LTVRFRQPGDrlRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWV 52
 
Name Accession Description Interval E-value
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 22-195 1.18e-76

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: 236.37  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  22 HVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNFE--------GIFSE 93
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDvkalakgkKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  94 KAARDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFA-NGQLIRPFLTFSKKDLPE-- 170
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGsGIQIIRPLLGISKSEIEEyl 160

                         170       180
                  ....*....|....*....|....*....
gi 1622318219 171 ----IFHFEDSSNRELSFLRNRVRNNYLP 195
Cdd:TIGR02432 161 kengLPWFEDETNQDDKYLRNRIRHELLP 189
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 22-195 1.76e-75

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: 233.25  E-value: 1.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  22 HVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNFEGIFS-----EKAA 96
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEAPKsggnlEAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  97 RDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFANGQLIRPFLTFSKKDLPEIFH--- 173
Cdd:cd01992    81 REARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCReng 160

                         170       180
                  ....*....|....*....|....*
gi 1622318219 174 ---FEDSSNRELSFLRNRVRNNYLP 195
Cdd:cd01992   161 lpwVEDPSNADLKYTRNRIRHELLP 185
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 6-212 5.93e-68

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: 215.85  E-value: 5.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219   6 EIFNEIKNKAYFKNHRHVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVS 85
Cdd:COG0037     1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  86 NF--------EGIFSEKAARDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFaNGQLI 157
Cdd:COG0037    81 RVdvpaiakkEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGG-GVRLI 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622318219 158 RPFLTFSKKDLPE------IFHFEDSSNRELSFLRNRVRNNYLPLLKQENPRFIQGLNQLA 212
Cdd:COG0037   160 RPLLYVSRKEIEAyakengLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSA 220
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 25-191 2.93e-59

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 191.30  E-value: 2.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  25 IAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNF-----EGIFSEKAARDW 99
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVdvakkSGENLEAAAREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219 100 RYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFANGQLIRPFLTFSKKDLPE------IFH 173
Cdd:pfam01171  81 RYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAyakehkIPW 160

                         170
                  ....*....|....*...
gi 1622318219 174 FEDSSNRELSFLRNRVRN 191
Cdd:pfam01171 161 FEDESNADDKYTRNRIRH 178
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 20-206 2.80e-30

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 121.27  E-value: 2.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  20 HRHVLIAVSGGVDSMNLLHFLYLF-QDKLKIRIGIAHVNHKQRSESDSeeaylkcWAKkH--------DIPIYV------ 84
Cdd:PRK10660   15 SRQILVAFSGGLDSTVLLHLLVQWrTENPGVTLRAIHVHHGLSPNADS-------WVK-HceqvcqqwQVPLVVervqld 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  85 SNFEGIfsEKAARDWRYAFFKSIMLKNnySALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFANGQLIRPFLTFS 164
Cdd:PRK10660   87 QRGLGI--EAAARQARYQAFARTLLPG--EVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622318219 165 KKDLpEIF---H----FEDSSNRELSFLRNRVRNNYLPLLKQENPRFIQ 206
Cdd:PRK10660  163 REEL-EQYaqaHglrwIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAE 210
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 350-399 3.42e-07

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: 47.18  E-value: 3.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622318219  350 IKLRSRQSGD--YISFGHFSKKIRRLFIDEKFTIAERQNAIIGEQDEQIIFV 399
Cdd:smart00977   1 LTVRFRQPGDrlRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWV 52
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 350-394 1.56e-03

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: 36.37  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622318219 350 IKLRSRQSGDYIS---FGHfSKKIRRLFIDEKFTIAERQNAIIGEQDE 394
Cdd:TIGR02433   1 LTVRFRQGGDRIKllgRKG-SKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
 
Name Accession Description Interval E-value
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 22-195 1.18e-76

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: 236.37  E-value: 1.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  22 HVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNFE--------GIFSE 93
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDvkalakgkKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  94 KAARDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFA-NGQLIRPFLTFSKKDLPE-- 170
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGsGIQIIRPLLGISKSEIEEyl 160

                         170       180
                  ....*....|....*....|....*....
gi 1622318219 171 ----IFHFEDSSNRELSFLRNRVRNNYLP 195
Cdd:TIGR02432 161 kengLPWFEDETNQDDKYLRNRIRHELLP 189
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 22-195 1.76e-75

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: 233.25  E-value: 1.76e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  22 HVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNFEGIFS-----EKAA 96
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEAPKsggnlEAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  97 RDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFANGQLIRPFLTFSKKDLPEIFH--- 173
Cdd:cd01992    81 REARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCReng 160

                         170       180
                  ....*....|....*....|....*
gi 1622318219 174 ---FEDSSNRELSFLRNRVRNNYLP 195
Cdd:cd01992   161 lpwVEDPSNADLKYTRNRIRHELLP 185
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 6-212 5.93e-68

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: 215.85  E-value: 5.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219   6 EIFNEIKNKAYFKNHRHVLIAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVS 85
Cdd:COG0037     1 KVRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  86 NF--------EGIFSEKAARDWRYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFaNGQLI 157
Cdd:COG0037    81 RVdvpaiakkEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGG-GVRLI 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622318219 158 RPFLTFSKKDLPE------IFHFEDSSNRELSFLRNRVRNNYLPLLKQENPRFIQGLNQLA 212
Cdd:COG0037   160 RPLLYVSRKEIEAyakengLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSA 220
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 25-191 2.93e-59

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 191.30  E-value: 2.93e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  25 IAVSGGVDSMNLLHFLYLFQDKLKIRIGIAHVNHKQRSESDSEEAYLKCWAKKHDIPIYVSNF-----EGIFSEKAARDW 99
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVdvakkSGENLEAAAREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219 100 RYAFFKSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFANGQLIRPFLTFSKKDLPE------IFH 173
Cdd:pfam01171  81 RYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAyakehkIPW 160

                         170
                  ....*....|....*...
gi 1622318219 174 FEDSSNRELSFLRNRVRN 191
Cdd:pfam01171 161 FEDESNADDKYTRNRIRH 178
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 20-206 2.80e-30

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 121.27  E-value: 2.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  20 HRHVLIAVSGGVDSMNLLHFLYLF-QDKLKIRIGIAHVNHKQRSESDSeeaylkcWAKkH--------DIPIYV------ 84
Cdd:PRK10660   15 SRQILVAFSGGLDSTVLLHLLVQWrTENPGVTLRAIHVHHGLSPNADS-------WVK-HceqvcqqwQVPLVVervqld 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  85 SNFEGIfsEKAARDWRYAFFKSIMLKNnySALVTAHHSDDQAETILMRLIRGSRLRHLSGIKSVQPFANGQLIRPFLTFS 164
Cdd:PRK10660   87 QRGLGI--EAAARQARYQAFARTLLPG--EVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARS 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622318219 165 KKDLpEIF---H----FEDSSNRELSFLRNRVRNNYLPLLKQENPRFIQ 206
Cdd:PRK10660  163 REEL-EQYaqaHglrwIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAE 210
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 17-168 2.10e-13

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: 68.45  E-value: 2.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  17 FKNHRHVLIAVSGGVDSMNLLHFL--YLFQDKLKIRIGIAHVNHKQRSESDSEEaYLKCWAKKHDIPIYVSNFEGIFSEK 94
Cdd:cd24138     5 IEPGDRILVGLSGGKDSLTLLHLLeeLKRRAPIKFELVAVTVDPGYPGYRPPRE-ELAEILEELGEILEDEESEIIIIEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  95 A----------ARDWRYAFFkSIMLKNNYSALVTAHHSDDQAETILMRLIRGSRLRHLSGiKSVQPFANGQLIRPFLTFS 164
Cdd:cd24138    84 EreekspcslcSRLRRGILY-SLAKELGCNKLALGHHLDDAVETLLMNLLYGGRLKTMPP-KVTMDRGGLTVIRPLIYVR 161


                  ....
gi 1622318219 165 KKDL 168
Cdd:cd24138   162 EKDI 165
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 6-160 2.98e-09

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: 56.83  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219   6 EIFNEIKNKAYFKNHRHVLIAVSGGVDSMNLLHFLYLFQDKLKIRI---------GIahvnHKQRSESdseEAYLKCWAK 76
Cdd:cd01713     4 RVHRTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRHDYGVeliavtideGI----KGYRDDS---LEAARKLAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  77 KHDIPIYVSNFEGIF-----SEKAARDWRYA-------FFKSIM----LKNNYSALVTAHHSDDQAETILMRLIRGsRLR 140
Cdd:cd01713    77 EYGIPLEIVSFEDEFgftldELIVGKGGKKNactycgvFRRRALnrgaRELGADKLATGHNLDDEAETILMNLLRG-DVA 155

                         170       180
                  ....*....|....*....|...
gi 1622318219 141 HLSGIKSVQPFANGQL---IRPF 160
Cdd:cd01713   156 RLLRTGPEPRSEGEGLvprIKPL 178
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 350-399 3.42e-07

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: 47.18  E-value: 3.42e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622318219  350 IKLRSRQSGD--YISFGHFSKKIRRLFIDEKFTIAERQNAIIGEQDEQIIFV 399
Cdd:smart00977   1 LTVRFRQPGDrlRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWV 52
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 23-130 3.91e-06

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: 47.32  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622318219  23 VLIAVSGGVDSMNLLHFL---YLFQDKLKIRIGIAHVnhkqrSEsDSEEAYLKcWAKKHDIPIYVSN---FEGIFSEKAA 96
Cdd:cd01993    11 ILVAVSGGKDSLALLAVLkklGYNVEALYINLGIGEY-----SE-KSEEVVKK-LAEKLNLPLHVVDlkeEYGLGIPELA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622318219  97 RDW------------RYaFFKSIMLKNNYSALVTAHHSDDQAETIL 130
Cdd:cd01993    84 KKSrrppcsvcglvkRY-IMNKFAVENGFDVVATGHNLDDEAAFLL 128
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 350-394 1.56e-03

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: 36.37  E-value: 1.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622318219 350 IKLRSRQSGDYIS---FGHfSKKIRRLFIDEKFTIAERQNAIIGEQDE 394
Cdd:TIGR02433   1 LTVRFRQGGDRIKllgRKG-SKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
 
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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