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Conserved domains on  [gi|489336487|ref|WP_003243704|]
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MULTISPECIES: tRNA lysidine(34) synthetase TilS [Bacillus]

Protein Classification

tRNA lysidine(34) synthetase TilS( domain architecture ID 10798081)

tRNA lysidine(34) synthetase TilS ligates 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

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
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-238 2.80e-91

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: 277.10  E-value: 2.80e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   4 VKDFLNKHNLTLKGATIIVGVSGGPDSMALLHALHTLCGRSA-NVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCETA 82
Cdd:COG0037    2 VRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGfELVAVHVDHGLR-EESDEDAEFVAELCEELGIPLHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  83 QINVTAYAQEKGLNKQAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGtGRII 162
Cdd:COG0037   81 RVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGG-VRLI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489336487 163 RPFLTITKEEILHYCHENGLSYRTDESNAKDDYTRNRFRKTVLPFLKQESPDVHKRFQKVSEALTEDEQFLQSLTK 238
Cdd:COG0037  160 RPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 385-456 2.36e-23

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: 93.02  E-value: 2.36e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336487   385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDaSGEIIWIPGLKKSifEDLVIPNSDRI 456
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFY-GDEIVWVVGLRVD--ARFKAKETTKR 69
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 258-325 5.99e-03

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


:

Pssm-ID: 462708  Cd Length: 66  Bit Score: 35.30  E-value: 5.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  258 SQLLALPMPLQRRGVQLILNYLYENVPssfSAHHIQQFLD-WAENGG-PSGVLDFPKGlkVVKSYQTCLF 325
Cdd:pfam09179   2 AALAALSPARRRRLLRRWLAQLGLPMP---SAAHLEEILRqLLLARPdAQPRLQLPDG--GVRRYRGRLY 66
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-238 2.80e-91

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: 277.10  E-value: 2.80e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   4 VKDFLNKHNLTLKGATIIVGVSGGPDSMALLHALHTLCGRSA-NVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCETA 82
Cdd:COG0037    2 VRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGfELVAVHVDHGLR-EESDEDAEFVAELCEELGIPLHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  83 QINVTAYAQEKGLNKQAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGtGRII 162
Cdd:COG0037   81 RVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGG-VRLI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489336487 163 RPFLTITKEEILHYCHENGLSYRTDESNAKDDYTRNRFRKTVLPFLKQESPDVHKRFQKVSEALTEDEQFLQSLTK 238
Cdd:COG0037  160 RPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 19-206 2.68e-88

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: 267.58  E-value: 2.68e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   19 TIIVGVSGGPDSMALLHALHTLCGR-SANVIAAHVDHRFRGaESEEDMRFVQAYCKAEQLVCETAQINVTAYAQEKGLNK 97
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKiKIKLIAAHVDHGLRP-ESDEEAEFVQQFCRKLNIPLEIKKVDVKALAKGKKKNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   98 QAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGT-GRIIRPFLTITKEEILHY 176
Cdd:TIGR02432  80 EEAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSgIQIIRPLLGISKSEIEEY 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 489336487  177 CHENGLSYRTDESNAKDDYTRNRFRKTVLP 206
Cdd:TIGR02432 160 LKENGLPWFEDETNQDDKYLRNRIRHELLP 189
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 22-202 5.61e-85

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 258.71  E-value: 5.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   22 VGVSGGPDSMALLHALHTLCGRSA-NVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCETAQINVtayAQEKGLNKQAA 100
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGiELTAAHVNHGLR-EESDREAEHVQALCRQLGIPLEILRVDV---AKKSGENLEAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  101 ARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGTGRIIRPFLTITKEEILHYCHEN 180
Cdd:pfam01171  77 AREARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEH 156

                         170       180
                  ....*....|....*....|..
gi 489336487  181 GLSYRTDESNAKDDYTRNRFRK 202
Cdd:pfam01171 157 KIPWFEDESNADDKYTRNRIRH 178
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 19-206 4.57e-83

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: 254.06  E-value: 4.57e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  19 TIIVGVSGGPDSMALLHALHTLCG-RSANVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCEtaqINVTAYAQEKGLNK 97
Cdd:cd01992    1 KILVAVSGGPDSMALLHLLKELRPkLGLKLVAVHVDHGLR-EESAEEAQFVAKLCKKLGIPLH---ILTVTEAPKSGGNL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  98 QAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGTGRIIRPFLTITKEEILHYC 177
Cdd:cd01992   77 EAAAREARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYC 156

                        170       180
                 ....*....|....*....|....*....
gi 489336487 178 HENGLSYRTDESNAKDDYTRNRFRKTVLP 206
Cdd:cd01992  157 RENGLPWVEDPSNADLKYTRNRIRHELLP 185
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 20-254 2.39e-32

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 127.82  E-value: 2.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  20 IIVGVSGGPDSMALLHALHTLCGRSANVI--AAHVDHrfrGAESEEDmrfvqAYCKAEQLVCETAQI-----NVTAYAQE 92
Cdd:PRK10660  18 ILVAFSGGLDSTVLLHLLVQWRTENPGVTlrAIHVHH---GLSPNAD-----SWVKHCEQVCQQWQVplvveRVQLDQRG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  93 KGLnkQAAARDCRYQFFEEIMSKHQAdyLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGTGRIIRPFLTITKEE 172
Cdd:PRK10660  90 LGI--EAAARQARYQAFARTLLPGEV--LVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487 173 ILHYCHENGLSYRTDESNAKDDYTRNRFRKTVLPFLKQESPDVHKRFQKVSEALTEDEQFLQSLTKDEMNKVITSQSNTS 252
Cdd:PRK10660 166 LEQYAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDGTLS 245


                 ..
gi 489336487 253 VE 254
Cdd:PRK10660 246 ID 247
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 385-456 2.36e-23

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: 93.02  E-value: 2.36e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336487   385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDaSGEIIWIPGLKKSifEDLVIPNSDRI 456
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFY-GDEIVWVVGLRVD--ARFKAKETTKR 69
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 385-431 1.16e-18

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: 79.12  E-value: 1.16e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489336487  385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDAS 431
Cdd:TIGR02433   1 LTVRFRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 385-443 3.75e-18

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: 78.40  E-value: 3.75e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336487  385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDAsGEIIWIPGLKKS 443
Cdd:pfam11734   1 LSVRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYG-DQLVAVAGLGVA 58
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 258-325 5.99e-03

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


Pssm-ID: 462708  Cd Length: 66  Bit Score: 35.30  E-value: 5.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  258 SQLLALPMPLQRRGVQLILNYLYENVPssfSAHHIQQFLD-WAENGG-PSGVLDFPKGlkVVKSYQTCLF 325
Cdd:pfam09179   2 AALAALSPARRRRLLRRWLAQLGLPMP---SAAHLEEILRqLLLARPdAQPRLQLPDG--GVRRYRGRLY 66
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-238 2.80e-91

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: 277.10  E-value: 2.80e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   4 VKDFLNKHNLTLKGATIIVGVSGGPDSMALLHALHTLCGRSA-NVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCETA 82
Cdd:COG0037    2 VRKAIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRLGfELVAVHVDHGLR-EESDEDAEFVAELCEELGIPLHVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  83 QINVTAYAQEKGLNKQAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGtGRII 162
Cdd:COG0037   81 RVDVPAIAKKEGKSPEAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGG-VRLI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489336487 163 RPFLTITKEEILHYCHENGLSYRTDESNAKDDYTRNRFRKTVLPFLKQESPDVHKRFQKVSEALTEDEQFLQSLTK 238
Cdd:COG0037  160 RPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 19-206 2.68e-88

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: 267.58  E-value: 2.68e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   19 TIIVGVSGGPDSMALLHALHTLCGR-SANVIAAHVDHRFRGaESEEDMRFVQAYCKAEQLVCETAQINVTAYAQEKGLNK 97
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKiKIKLIAAHVDHGLRP-ESDEEAEFVQQFCRKLNIPLEIKKVDVKALAKGKKKNL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   98 QAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGT-GRIIRPFLTITKEEILHY 176
Cdd:TIGR02432  80 EEAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSgIQIIRPLLGISKSEIEEY 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 489336487  177 CHENGLSYRTDESNAKDDYTRNRFRKTVLP 206
Cdd:TIGR02432 160 LKENGLPWFEDETNQDDKYLRNRIRHELLP 189
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 22-202 5.61e-85

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 258.71  E-value: 5.61e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   22 VGVSGGPDSMALLHALHTLCGRSA-NVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCETAQINVtayAQEKGLNKQAA 100
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGiELTAAHVNHGLR-EESDREAEHVQALCRQLGIPLEILRVDV---AKKSGENLEAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  101 ARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGTGRIIRPFLTITKEEILHYCHEN 180
Cdd:pfam01171  77 AREARYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEH 156

                         170       180
                  ....*....|....*....|..
gi 489336487  181 GLSYRTDESNAKDDYTRNRFRK 202
Cdd:pfam01171 157 KIPWFEDESNADDKYTRNRIRH 178
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 19-206 4.57e-83

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: 254.06  E-value: 4.57e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  19 TIIVGVSGGPDSMALLHALHTLCG-RSANVIAAHVDHRFRgAESEEDMRFVQAYCKAEQLVCEtaqINVTAYAQEKGLNK 97
Cdd:cd01992    1 KILVAVSGGPDSMALLHLLKELRPkLGLKLVAVHVDHGLR-EESAEEAQFVAKLCKKLGIPLH---ILTVTEAPKSGGNL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  98 QAAARDCRYQFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGTGRIIRPFLTITKEEILHYC 177
Cdd:cd01992   77 EAAAREARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYC 156

                        170       180
                 ....*....|....*....|....*....
gi 489336487 178 HENGLSYRTDESNAKDDYTRNRFRKTVLP 206
Cdd:cd01992  157 RENGLPWVEDPSNADLKYTRNRIRHELLP 185
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 20-254 2.39e-32

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 127.82  E-value: 2.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  20 IIVGVSGGPDSMALLHALHTLCGRSANVI--AAHVDHrfrGAESEEDmrfvqAYCKAEQLVCETAQI-----NVTAYAQE 92
Cdd:PRK10660  18 ILVAFSGGLDSTVLLHLLVQWRTENPGVTlrAIHVHH---GLSPNAD-----SWVKHCEQVCQQWQVplvveRVQLDQRG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  93 KGLnkQAAARDCRYQFFEEIMSKHQAdyLALAHHGDDQVETMLMKLAKGTLGTGLAGMQPVRRFGTGRIIRPFLTITKEE 172
Cdd:PRK10660  90 LGI--EAAARQARYQAFARTLLPGEV--LVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487 173 ILHYCHENGLSYRTDESNAKDDYTRNRFRKTVLPFLKQESPDVHKRFQKVSEALTEDEQFLQSLTKDEMNKVITSQSNTS 252
Cdd:PRK10660 166 LEQYAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDGTLS 245


                 ..
gi 489336487 253 VE 254
Cdd:PRK10660 246 ID 247
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 385-456 2.36e-23

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: 93.02  E-value: 2.36e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489336487   385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDaSGEIIWIPGLKKSifEDLVIPNSDRI 456
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFY-GDEIVWVVGLRVD--ARFKAKETTKR 69
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 10-182 9.13e-22

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: 92.34  E-value: 9.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  10 KHNLTLKGATIIVGVSGGPDSMALLHALHTLCGRSA---NVIAAHVDHRFRGAESEEDmrFVQAYCKAEQLVCEtaQINV 86
Cdd:cd24138    1 DFKMIEPGDRILVGLSGGKDSLTLLHLLEELKRRAPikfELVAVTVDPGYPGYRPPRE--ELAEILEELGEILE--DEES 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  87 TAYAQEKGLNKQAAARDC----RYQFFeEIMSKHQADYLALAHHGDDQVETMLMKLAKGTLgtgLAGMQPV---RRFGTg 159
Cdd:cd24138   77 EIIIIEKEREEKSPCSLCsrlrRGILY-SLAKELGCNKLALGHHLDDAVETLLMNLLYGGR---LKTMPPKvtmDRGGL- 151

                        170       180
                 ....*....|....*....|...
gi 489336487 160 RIIRPFLTITKEEILHYCHENGL 182
Cdd:cd24138  152 TVIRPLIYVREKDIRAFAEENGL 174
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 385-431 1.16e-18

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: 79.12  E-value: 1.16e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 489336487  385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDAS 431
Cdd:TIGR02433   1 LTVRFRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 385-443 3.75e-18

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: 78.40  E-value: 3.75e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489336487  385 LTIRTRKAGDRIKLKGMNGSKKVKDIFIDKKLPLQERDNWPIVTDAsGEIIWIPGLKKS 443
Cdd:pfam11734   1 LSVRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYG-DQLVAVAGLGVA 58
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 2-188 3.42e-16

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: 77.24  E-value: 3.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   2 KSVKDFLNKHNLTLKGATIIVGVSGGPDSMALLHALHTLCGR---SANVIAAHVD---HRFRgaesEEDMRFVQAYCKAE 75
Cdd:cd01713    3 RRVHRTIRKYRLIKPGDRVAVGLSGGKDSTVLLYVLKELNKRhdyGVELIAVTIDegiKGYR----DDSLEAARKLAEEY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  76 QLVCETAQ----INVTAY--AQEKGLNKQAaardCRY------QFFEEIMSKHQADYLALAHHGDDQVETMLMKLAKGTL 143
Cdd:cd01713   79 GIPLEIVSfedeFGFTLDelIVGKGGKKNA----CTYcgvfrrRALNRGARELGADKLATGHNLDDEAETILMNLLRGDV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 489336487 144 GTGLAGMQPVRRFGTGRI--IRPFLTITKEEILHYCHENGLSYRTDE 188
Cdd:cd01713  155 ARLLRTGPEPRSEGEGLVprIKPLRYIPEKEIVLYAHLNGLPYFSTE 201
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 10-188 7.27e-15

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: 72.74  E-value: 7.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  10 KHNLTLKGATIIVGVSGGPDSMALLHALHTLcgrSANVIAAHVDHRFrGAESEEDMRFVQAYCKAEQLvcetaQINVTAY 89
Cdd:cd01993    1 RYKMFEKDDKILVAVSGGKDSLALLAVLKKL---GYNVEALYINLGI-GEYSEKSEEVVKKLAEKLNL-----PLHVVDL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  90 AQEKGLNKQAAARD-----C-------RYqffeeIMSK----HQADYLALAHHGDDQVETMLMKLAKGTLGTgLAGMQPV 153
Cdd:cd01993   72 KEEYGLGIPELAKKsrrppCsvcglvkRY-----IMNKfaveNGFDVVATGHNLDDEAAFLLGNILNWNEEY-LAKQGPF 145

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489336487 154 RRFGTGRII---RPFLTITKEEILHYCHENGLSYRTDE 188
Cdd:cd01993  146 LLPEHGGLVtrvKPLYEITEEEIALYALLNGIPYLEEE 183
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 20-66 5.77e-06

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 43.98  E-value: 5.77e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489336487  20 IIVGVSGGPDSMALLHALHtLCGRSANVIAAHVDHRFRGAESEEDMR 66
Cdd:cd01986    1 VVVGYSGGKDSSVALHLAS-RLGRKAEVAVVHIDHGIGFKEEAESVA 46
PRK10696 PRK10696
tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional
 2-179 7.71e-06

tRNA 2-thiocytidine biosynthesis protein TtcA; Provisional


Pssm-ID: 236737 [Multi-domain]  Cd Length: 258  Bit Score: 47.16  E-value: 7.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487   2 KSVKDFlnkhNLTLKGATIIVGVSGGPDSMALLHALHTLCGRSA---NVIAAHVDHRFRGAESEedmrFVQAYCKAEQLV 78
Cdd:PRK10696  18 QAIADF----NMIEEGDRVMVCLSGGKDSYTLLDILLNLQKRAPinfELVAVNLDQKQPGFPEH----VLPEYLESLGVP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  79 CETAQINVTAYAQEK--------GLnkqaAARDCR---YQFFEEimskHQADYLALAHHGDDQVETMLMKLAKGtlGTgL 147
Cdd:PRK10696  90 YHIEEQDTYSIVKEKipegkttcSL----CSRLRRgilYRTARE----LGATKIALGHHRDDILETLFLNMFYG--GK-L 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 489336487 148 AGMQPVRRFGTGR--IIRPfltitkeeiLHYCHE 179
Cdd:PRK10696 159 KAMPPKLLSDDGKhiVIRP---------LAYVAE 183
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 258-325 5.99e-03

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


Pssm-ID: 462708  Cd Length: 66  Bit Score: 35.30  E-value: 5.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489336487  258 SQLLALPMPLQRRGVQLILNYLYENVPssfSAHHIQQFLD-WAENGG-PSGVLDFPKGlkVVKSYQTCLF 325
Cdd:pfam09179   2 AALAALSPARRRRLLRRWLAQLGLPMP---SAAHLEEILRqLLLARPdAQPRLQLPDG--GVRRYRGRLY 66
GMP_synthase_C cd01997
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ...
 14-63 7.56e-03

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: 38.29  E-value: 7.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489336487  14 TLKGATIIVGVSGGPDSM---ALLH-ALhtlcgRSANVIAAHVDHRF-RGAESEE 63
Cdd:cd01997    4 TVGDKKVLCLVSGGVDSTvcaALLHkAL-----GDERVIAVHIDNGLmRKNESEQ 53
 
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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