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Conserved domains on  [gi|1159732543|ref|WP_079283860|]
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tRNA lysidine(34) synthetase TilS [Acinetobacter baumannii]

Protein Classification

tRNA lysidine(34) synthetase( domain architecture ID 18389937)

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

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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 ...
 15-240 2.01e-69

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: 220.86  E-value: 2.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  15 KFRRgVLKQAQEFSEKSSFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYII 91
Cdd:COG0037     1 KVRK-AIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRlgfELVAVHVDHGLREESDEDAEFVAELCEELGIPLHV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  92 QKVQIA------NGNLEAQARQARYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDyRKDMTI 163
Cdd:COG0037    80 VRVDVPaiakkeGKSPEAAARRARYGALYELARELgaDKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSR-GGGVRL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159732543 164 WRPFLDLTREQIALWTAQLEVKYIDDPMNYDTHYDRVWCREALWPFLTSRFPKMQQALSRTSYLMQDASEILEEVLK 240
Cdd:COG0037   159 IRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 373-443 1.36e-11

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: 59.89  E-value: 1.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159732543  373 LKIIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDNVMLGVftpKGFWLAQSPYCEEGGW 443
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWV---VGLRVDARFKAKETTK 68
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 254-319 2.59e-10

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


:

Pssm-ID: 462708  Cd Length: 66  Bit Score: 56.10  E-value: 2.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159732543 254 LTKLYELSFARQRQLLSAWMKGQGQYRPAFEMVERLRAEVIESKSDAQAALHWNQFYYVRYQNILY 319
Cdd:pfam09179   1 IAALAALSPARRRRLLRRWLAQLGLPMPSAAHLEEILRQLLLARPDAQPRLQLPDGGVRRYRGRLY 66
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 15-240 2.01e-69

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: 220.86  E-value: 2.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  15 KFRRgVLKQAQEFSEKSSFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYII 91
Cdd:COG0037     1 KVRK-AIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRlgfELVAVHVDHGLREESDEDAEFVAELCEELGIPLHV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  92 QKVQIA------NGNLEAQARQARYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDyRKDMTI 163
Cdd:COG0037    80 VRVDVPaiakkeGKSPEAAARRARYGALYELARELgaDKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSR-GGGVRL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159732543 164 WRPFLDLTREQIALWTAQLEVKYIDDPMNYDTHYDRVWCREALWPFLTSRFPKMQQALSRTSYLMQDASEILEEVLK 240
Cdd:COG0037   159 IRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 32-208 3.36e-65

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: 207.83  E-value: 3.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  32 SFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIA---NGNLEAQA 105
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKlglKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEApksGGNLEAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 106 RQARYQAYQQHLQENEI--LLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKDMTIWRPFLDLTREQIALWTAQLE 183
Cdd:cd01992    81 REARYAFLERAAKEHGIdvLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCRENG 160

                         170       180
                  ....*....|....*....|....*
gi 1159732543 184 VKYIDDPMNYDTHYDRVWCREALWP 208
Cdd:cd01992   161 LPWVEDPSNADLKYTRNRIRHELLP 185
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 24-444 8.83e-65

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 215.26  E-value: 8.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  24 AQEFSEKSSFLIGCSGGMDSMLLLHLM----AQIFPQKIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIA-- 97
Cdd:PRK10660    9 NRQLLTSRQILVAFSGGLDSTVLLHLLvqwrTENPGVTLRAIHVHHGLSPNADSWVKHCEQVCQQWQVPLVVERVQLDqr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  98 NGNLEAQARQARYQAYQQHLQENEILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKDMTIWRPFLDLTREQIAL 177
Cdd:PRK10660   89 GLGIEAAARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELEQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 178 WTAQLEVKYIDDPMNYDTHYDRVWCREALWPFLTSRFPKMQQALSRTSYLMQDASEILEEVLKDDWQYSGSAD-YLNLTK 256
Cdd:PRK10660  169 YAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDgTLSIDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 257 LYELSFARQRQLLSAWMKGQGQYRPAFEMVERLRAEVIESKSDAQAALHWNQFYYVRYQNILYRLSKQVYLAETL---NP 333
Cdd:PRK10660  249 LLAMSDARRAAILRRWLAGQGAPMPSRDQLQRIWQEVALAREDAEPCLRLGAFEIRRYQSQLWLIKSVAGQSETIlpwQT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 334 VDAELEHSFKLEEkWQGAAGLfHVECKRIGLSHSllnkklkiIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQ 413
Cdd:PRK10660  329 WLQPLELPAGLGS-LQLVAGG-DVRPPRADEAVS--------VRFKAQGLLHIVGRNHGRKLKKIWQELGVPPWLRDRTP 398

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1159732543 414 ILVLDNVM---LGVFTPKGFWLAQspycEEGGWQ 444
Cdd:PRK10660  399 LLFYGETLiaaAGVFVTQEGQAEE----GENGVS 428
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 32-208 1.61e-58

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: 190.92  E-value: 1.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  32 SFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIAN------GNLE 102
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKikiKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDVKAlakgkkKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 103 AQARQARYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKD-MTIWRPFLDLTREQIALWT 179
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHgaDYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSgIQIIRPLLGISKSEIEEYL 160

                         170       180
                  ....*....|....*....|....*....
gi 1159732543 180 AQLEVKYIDDPMNYDTHYDRVWCREALWP 208
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHELLP 189
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 35-203 1.05e-53

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 177.82  E-value: 1.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  35 IGCSGGMDSMLLLHLMAQI---FPQKIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIAN---GNLEAQARQA 108
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLkikLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVAKksgENLEAAAREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 109 RYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKDMTIWRPFLDLTREQIALWTAQLEVKY 186
Cdd:pfam01171  81 RYDFFEEALKKHgaDVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEHKIPW 160

                         170
                  ....*....|....*..
gi 1159732543 187 IDDPMNYDTHYDRVWCR 203
Cdd:pfam01171 161 FEDESNADDKYTRNRIR 177
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 373-443 1.36e-11

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: 59.89  E-value: 1.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159732543  373 LKIIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDNVMLGVftpKGFWLAQSPYCEEGGW 443
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWV---VGLRVDARFKAKETTK 68
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 375-419 1.47e-10

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: 56.40  E-value: 1.47e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1159732543 375 IIR-RQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDN 419
Cdd:TIGR02433   2 TVRfRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 254-319 2.59e-10

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


Pssm-ID: 462708  Cd Length: 66  Bit Score: 56.10  E-value: 2.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159732543 254 LTKLYELSFARQRQLLSAWMKGQGQYRPAFEMVERLRAEVIESKSDAQAALHWNQFYYVRYQNILY 319
Cdd:pfam09179   1 IAALAALSPARRRRLLRRWLAQLGLPMPSAAHLEEILRQLLLARPDAQPRLQLPDGGVRRYRGRLY 66
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 373-443 8.87e-07

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: 46.43  E-value: 8.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159732543 373 LKIIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDNVMLGVftpKGFWLAQSPYCEEGGW 443
Cdd:pfam11734   1 LSVRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYGDQLVAV---AGLGVAAGFEAQPGEA 68
 
Name Accession Description Interval E-value
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 15-240 2.01e-69

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: 220.86  E-value: 2.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  15 KFRRgVLKQAQEFSEKSSFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYII 91
Cdd:COG0037     1 KVRK-AIRDYRLLEPGDRILVAVSGGKDSLALLHLLAKLRRRlgfELVAVHVDHGLREESDEDAEFVAELCEELGIPLHV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  92 QKVQIA------NGNLEAQARQARYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDyRKDMTI 163
Cdd:COG0037    80 VRVDVPaiakkeGKSPEAAARRARYGALYELARELgaDKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSR-GGGVRL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1159732543 164 WRPFLDLTREQIALWTAQLEVKYIDDPMNYDTHYDRVWCREALWPFLTSRFPKMQQALSRTSYLMQDASEILEEVLK 240
Cdd:COG0037   159 IRPLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 32-208 3.36e-65

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: 207.83  E-value: 3.36e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  32 SFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIA---NGNLEAQA 105
Cdd:cd01992     1 KILVAVSGGPDSMALLHLLKELRPKlglKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEApksGGNLEAAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 106 RQARYQAYQQHLQENEI--LLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKDMTIWRPFLDLTREQIALWTAQLE 183
Cdd:cd01992    81 REARYAFLERAAKEHGIdvLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCRENG 160

                         170       180
                  ....*....|....*....|....*
gi 1159732543 184 VKYIDDPMNYDTHYDRVWCREALWP 208
Cdd:cd01992   161 LPWVEDPSNADLKYTRNRIRHELLP 185
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 24-444 8.83e-65

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 215.26  E-value: 8.83e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  24 AQEFSEKSSFLIGCSGGMDSMLLLHLM----AQIFPQKIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIA-- 97
Cdd:PRK10660    9 NRQLLTSRQILVAFSGGLDSTVLLHLLvqwrTENPGVTLRAIHVHHGLSPNADSWVKHCEQVCQQWQVPLVVERVQLDqr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  98 NGNLEAQARQARYQAYQQHLQENEILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKDMTIWRPFLDLTREQIAL 177
Cdd:PRK10660   89 GLGIEAAARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELEQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 178 WTAQLEVKYIDDPMNYDTHYDRVWCREALWPFLTSRFPKMQQALSRTSYLMQDASEILEEVLKDDWQYSGSAD-YLNLTK 256
Cdd:PRK10660  169 YAQAHGLRWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDgTLSIDP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 257 LYELSFARQRQLLSAWMKGQGQYRPAFEMVERLRAEVIESKSDAQAALHWNQFYYVRYQNILYRLSKQVYLAETL---NP 333
Cdd:PRK10660  249 LLAMSDARRAAILRRWLAGQGAPMPSRDQLQRIWQEVALAREDAEPCLRLGAFEIRRYQSQLWLIKSVAGQSETIlpwQT 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 334 VDAELEHSFKLEEkWQGAAGLfHVECKRIGLSHSllnkklkiIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQ 413
Cdd:PRK10660  329 WLQPLELPAGLGS-LQLVAGG-DVRPPRADEAVS--------VRFKAQGLLHIVGRNHGRKLKKIWQELGVPPWLRDRTP 398

                         410       420       430
                  ....*....|....*....|....*....|....
gi 1159732543 414 ILVLDNVM---LGVFTPKGFWLAQspycEEGGWQ 444
Cdd:PRK10660  399 LLFYGETLiaaAGVFVTQEGQAEE----GENGVS 428
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 32-208 1.61e-58

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: 190.92  E-value: 1.61e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  32 SFLIGCSGGMDSMLLLHLMAQIFPQ---KIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIAN------GNLE 102
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKikiKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVDVKAlakgkkKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 103 AQARQARYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKD-MTIWRPFLDLTREQIALWT 179
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHgaDYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSgIQIIRPLLGISKSEIEEYL 160

                         170       180
                  ....*....|....*....|....*....
gi 1159732543 180 AQLEVKYIDDPMNYDTHYDRVWCREALWP 208
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHELLP 189
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 35-203 1.05e-53

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 177.82  E-value: 1.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  35 IGCSGGMDSMLLLHLMAQI---FPQKIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIAN---GNLEAQARQA 108
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLkikLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVAKksgENLEAAAREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 109 RYQAYQQHLQEN--EILLLAHHQQDQAETVILRLLSGAGVDGLAAMQAIDYRKDMTIWRPFLDLTREQIALWTAQLEVKY 186
Cdd:pfam01171  81 RYDFFEEALKKHgaDVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEHKIPW 160

                         170
                  ....*....|....*..
gi 1159732543 187 IDDPMNYDTHYDRVWCR 203
Cdd:pfam01171 161 FEDESNADDKYTRNRIR 177
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 373-443 1.36e-11

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: 59.89  E-value: 1.36e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159732543  373 LKIIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDNVMLGVftpKGFWLAQSPYCEEGGW 443
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWV---VGLRVDARFKAKETTK 68
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 375-419 1.47e-10

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: 56.40  E-value: 1.47e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1159732543 375 IIR-RQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDN 419
Cdd:TIGR02433   2 TVRfRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 254-319 2.59e-10

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


Pssm-ID: 462708  Cd Length: 66  Bit Score: 56.10  E-value: 2.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1159732543 254 LTKLYELSFARQRQLLSAWMKGQGQYRPAFEMVERLRAEVIESKSDAQAALHWNQFYYVRYQNILY 319
Cdd:pfam09179   1 IAALAALSPARRRRLLRRWLAQLGLPMPSAAHLEEILRQLLLARPDAQPRLQLPDGGVRRYRGRLY 66
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 27-194 1.26e-08

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: 54.59  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543  27 FSEKSSFLIGCSGGMDSMLLLHLMAQI-----FPQKIRAIYIDHQLQDQSAEWaEVVATQAAILNIPY-IIQKVQIANGN 100
Cdd:cd24138     5 IEPGDRILVGLSGGKDSLTLLHLLEELkrrapIKFELVAVTVDPGYPGYRPPR-EELAEILEELGEILeDEESEIIIIEK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1159732543 101 LEAQ-------ARQARYQAYqQHLQENEI--LLLAHHQQDQAETVILRLLSGAgvdGLAAMQAIDY--RKDMTIWRPfLD 169
Cdd:cd24138    84 EREEkspcslcSRLRRGILY-SLAKELGCnkLALGHHLDDAVETLLMNLLYGG---RLKTMPPKVTmdRGGLTVIRP-LI 158

                         170       180
                  ....*....|....*....|....*.
gi 1159732543 170 LTRE-QIALWTAQLEVKYIDDPMNYD 194
Cdd:cd24138   159 YVREkDIRAFAEENGLPKIECPCPYC 184
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 373-443 8.87e-07

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: 46.43  E-value: 8.87e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159732543 373 LKIIRRQGGEKIHLYGRVGQWPLKKAIQEAHILPWLRHTIQILVLDNVMLGVftpKGFWLAQSPYCEEGGW 443
Cdd:pfam11734   1 LSVRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYGDQLVAV---AGLGVAAGFEAQPGEA 68
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
 41-100 1.44e-04

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 41.13  E-value: 1.44e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1159732543  41 MDSMLLLHLMAQIFPQKIRAIYIDHQLQDQSAEW-AEVVATQAAILNIPYIIQKVQIANGN 100
Cdd:cd21218    41 KDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQAAEKLGCKYFLTPEDIVSGN 101
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 27-99 5.39e-04

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: 41.16  E-value: 5.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1159732543  27 FSEKSSFLIGCSGGMDSMLLLHLMAQIFPQkIRAIYIDHQLQDQSAEWAEVVATQAAILNIPYIIQKVQIANG 99
Cdd:cd01993     5 FEKDDKILVAVSGGKDSLALLAVLKKLGYN-VEALYINLGIGEYSEKSEEVVKKLAEKLNLPLHVVDLKEEYG 76
CysD COG0175
3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or ...
 20-64 9.04e-03

3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase (PAPS reductase)/FAD synthetase or related enzyme is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439945 [Multi-domain]  Cd Length: 232  Bit Score: 37.52  E-value: 9.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1159732543  20 VLKQA-QEFSEKssFLIGCSGGMDSMLLLHLMAQIFPqKIRAIYID 64
Cdd:COG0175    24 ILREAaAEFGGR--VVVSSSGGKDSTVLLHLAAKFKP-PIPVLFLD 66
 
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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