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Conserved domains on  [gi|3860612|emb|CAA14513|]
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CELL CYCLE PROTEIN MESJ (mesJ) [Rickettsia prowazekii str. Madrid E]

Protein Classification

tRNA lysidine(34) synthetase( domain architecture ID 11112495)

tRNA lysidine(34) synthetase 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 Ontology:  GO:0005524|GO:0016879|GO:0006400
SCOP:  3001593

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
24-199 8.61e-70

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


:

Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 218.65  E-value: 8.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     24 IAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFDH-QNNFSNLQERAREG 102
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVaKKSGENLEAAAREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    103 RYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSsnIHWYN---NIQIIRPLYNIPKSELVEYLVNHKI 179
Cdd:pfam01171  81 RYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAG--IPPVRefaGGRIIRPLLKVSKAEIEAYAKEHKI 158
                         170       180
                  ....*....|....*....|
gi 3860612    180 KWFEDESNLSDKYRRNIIRQ 199
Cdd:pfam01171 159 PWFEDESNADDKYTRNRIRH 178
 
Name Accession Description Interval E-value
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
24-199 8.61e-70

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 218.65  E-value: 8.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     24 IAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFDH-QNNFSNLQERAREG 102
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVaKKSGENLEAAAREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    103 RYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSsnIHWYN---NIQIIRPLYNIPKSELVEYLVNHKI 179
Cdd:pfam01171  81 RYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAG--IPPVRefaGGRIIRPLLKVSKAEIEAYAKEHKI 158
                         170       180
                  ....*....|....*....|
gi 3860612    180 KWFEDESNLSDKYRRNIIRQ 199
Cdd:pfam01171 159 PWFEDESNADDKYTRNRIRH 178
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
21-202 1.89e-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: 207.45  E-value: 1.89e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   21 KIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFDHQ-NNFSNLQERA 99
Cdd:cd01992   1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEApKSGGNLEAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612  100 REGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSS-SNIHWYNNIQIIRPLYNIPKSELVEYLVNHK 178
Cdd:cd01992  81 REARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGmAARSKAGGIRLIRPLLGISKAELLAYCRENG 160
                       170       180
                ....*....|....*....|....
gi 3860612  179 IKWFEDESNLSDKYRRNIIRQKLF 202
Cdd:cd01992 161 LPWVEDPSNADLKYTRNRIRHELL 184
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
21-201 1.04e-60

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: 195.54  E-value: 1.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     21 KIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYY----NLSFDHQNNFSNLQ 96
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEikkvDVKALAKGKKKNLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     97 ERAREGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSSNIHWY--NNIQIIRPLYNIPKSELVEYL 174
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRIlgSGIQIIRPLLGISKSEIEEYL 160
                         170       180
                  ....*....|....*....|....*..
gi 3860612    175 VNHKIKWFEDESNLSDKYRRNIIRQKL 201
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHEL 187
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
20-204 4.95e-51

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: 171.94  E-value: 4.95e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   20 SKIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFD----HQNNFSNL 95
Cdd:COG0037  16 DRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDvpaiAKKEGKSP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   96 QERAREGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSSNIHWYNNIQIIRPLYNIPKSELVEYLV 175
Cdd:COG0037  96 EAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGGVRLIRPLLYVSRKEIEAYAK 175
                       170       180
                ....*....|....*....|....*....
gi 3860612  176 NHKIKWFEDESNLSDKYRRNIIRQKLFKE 204
Cdd:COG0037 176 ENGLPWIEDPCNYDPRYTRNRIRHLVLPE 204
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
21-198 2.36e-19

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 89.68  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    21 KIAIAVSGGSDSISLLYLANIWARKN-NIELFVISVDHNLRPQSKQ---------ENYYIHTISSNLNrkyynlsFDHQN 90
Cdd:PRK10660  17 QILVAFSGGLDSTVLLHLLVQWRTENpGVTLRAIHVHHGLSPNADSwvkhceqvcQQWQVPLVVERVQ-------LDQRG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    91 NfsNLQERAREGRYDLMTNLCLELDVLVllTAHHEDDYVENFCLRLERNSGIFGLSS-SNIHWYNNIQIIRPLYNIPKSE 169
Cdd:PRK10660  90 L--GIEAAARQARYQAFARTLLPGEVLV--TAQHLDDQCETFLLALKRGSGPAGLSAmAEVSPFAGTRLIRPLLARSREE 165
                        170       180
                 ....*....|....*....|....*....
gi 3860612   170 LVEYLVNHKIKWFEDESNLSDKYRRNIIR 198
Cdd:PRK10660 166 LEQYAQAHGLRWIEDDSNQDDRYDRNFLR 194
 
Name Accession Description Interval E-value
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
24-199 8.61e-70

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 218.65  E-value: 8.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     24 IAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFDH-QNNFSNLQERAREG 102
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVaKKSGENLEAAAREA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    103 RYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSsnIHWYN---NIQIIRPLYNIPKSELVEYLVNHKI 179
Cdd:pfam01171  81 RYDFFEEALKKHGADVLLTAHHLDDQLETFLMRLKRGSGLAGLAG--IPPVRefaGGRIIRPLLKVSKAEIEAYAKEHKI 158
                         170       180
                  ....*....|....*....|
gi 3860612    180 KWFEDESNLSDKYRRNIIRQ 199
Cdd:pfam01171 159 PWFEDESNADDKYTRNRIRH 178
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
21-202 1.89e-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: 207.45  E-value: 1.89e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   21 KIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFDHQ-NNFSNLQERA 99
Cdd:cd01992   1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEApKSGGNLEAAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612  100 REGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSS-SNIHWYNNIQIIRPLYNIPKSELVEYLVNHK 178
Cdd:cd01992  81 REARYAFLERAAKEHGIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGmAARSKAGGIRLIRPLLGISKAELLAYCRENG 160
                       170       180
                ....*....|....*....|....
gi 3860612  179 IKWFEDESNLSDKYRRNIIRQKLF 202
Cdd:cd01992 161 LPWVEDPSNADLKYTRNRIRHELL 184
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
21-201 1.04e-60

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: 195.54  E-value: 1.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     21 KIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYY----NLSFDHQNNFSNLQ 96
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEikkvDVKALAKGKKKNLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612     97 ERAREGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSSNIHWY--NNIQIIRPLYNIPKSELVEYL 174
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKHGADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRIlgSGIQIIRPLLGISKSEIEEYL 160
                         170       180
                  ....*....|....*....|....*..
gi 3860612    175 VNHKIKWFEDESNLSDKYRRNIIRQKL 201
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHEL 187
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
20-204 4.95e-51

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: 171.94  E-value: 4.95e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   20 SKIAIAVSGGSDSISLLYLANIWARKNNIELFVISVDHNLRPQSKQENYYIHTISSNLNRKYYNLSFD----HQNNFSNL 95
Cdd:COG0037  16 DRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVRVDvpaiAKKEGKSP 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   96 QERAREGRYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSSNIHWYNNIQIIRPLYNIPKSELVEYLV 175
Cdd:COG0037  96 EAAARRARYGALYELARELGADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGGVRLIRPLLYVSRKEIEAYAK 175
                       170       180
                ....*....|....*....|....*....
gi 3860612  176 NHKIKWFEDESNLSDKYRRNIIRQKLFKE 204
Cdd:COG0037 176 ENGLPWIEDPCNYDPRYTRNRIRHLVLPE 204
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
21-198 2.36e-19

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 89.68  E-value: 2.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    21 KIAIAVSGGSDSISLLYLANIWARKN-NIELFVISVDHNLRPQSKQ---------ENYYIHTISSNLNrkyynlsFDHQN 90
Cdd:PRK10660  17 QILVAFSGGLDSTVLLHLLVQWRTENpGVTLRAIHVHHGLSPNADSwvkhceqvcQQWQVPLVVERVQ-------LDQRG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    91 NfsNLQERAREGRYDLMTNLCLELDVLVllTAHHEDDYVENFCLRLERNSGIFGLSS-SNIHWYNNIQIIRPLYNIPKSE 169
Cdd:PRK10660  90 L--GIEAAARQARYQAFARTLLPGEVLV--TAQHLDDQCETFLLALKRGSGPAGLSAmAEVSPFAGTRLIRPLLARSREE 165
                        170       180
                 ....*....|....*....|....*....
gi 3860612   170 LVEYLVNHKIKWFEDESNLSDKYRRNIIR 198
Cdd:PRK10660 166 LEQYAQAHGLRWIEDDSNQDDRYDRNFLR 194
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
20-173 2.16e-09

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: 56.51  E-value: 2.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   20 SKIAIAVSGGSDSISLLYLANIWARKNNIELFVISV------DHNLRPQSKQENY-----YIHTISSNLNRKyyNLSFDH 88
Cdd:cd24138   9 DRILVGLSGGKDSLTLLHLLEELKRRAPIKFELVAVtvdpgyPGYRPPREELAEIleelgEILEDEESEIII--IEKERE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   89 QNNFSNLQERARegRYDLMTnLCLELDVLVLLTAHHEDDYVENFCLRLERNSGIFGLSSSNIHWYNNIQIIRPLYNIPKS 168
Cdd:cd24138  87 EKSPCSLCSRLR--RGILYS-LAKELGCNKLALGHHLDDAVETLLMNLLYGGRLKTMPPKVTMDRGGLTVIRPLIYVREK 163

                ....*
gi 3860612  169 ELVEY 173
Cdd:cd24138 164 DIRAF 168
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
6-185 2.79e-08

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: 53.75  E-value: 2.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612    6 FEYNINNLIGNFGL----SKIAIAVSGGSDSISLLY-LANIWARKN-NIELFVISVD---HNLRPQS-----KQENYY-- 69
Cdd:cd01713   1 IERRVHRTIRKYRLikpgDRVAVGLSGGKDSTVLLYvLKELNKRHDyGVELIAVTIDegiKGYRDDSleaarKLAEEYgi 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3860612   70 IHTISSnlNRKYYNLSFDHqnnfsNLQERAREG---------RYDLMTNLCLELDVLVLLTAHHEDDYVENFCLRLERN- 139
Cdd:cd01713  81 PLEIVS--FEDEFGFTLDE-----LIVGKGGKKnactycgvfRRRALNRGARELGADKLATGHNLDDEAETILMNLLRGd 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 3860612  140 ---SGIFGLSSSNIHwYNNIQIIRPLYNIPKSELVEYLVNHKIKWFEDE 185
Cdd:cd01713 154 varLLRTGPEPRSEG-EGLVPRIKPLRYIPEKEIVLYAHLNGLPYFSTE 201
 
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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