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Conserved domains on  [gi|515166630|ref|WP_016795152|]
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tRNA lysidine(34) synthetase TilS [Vibrio cyclitrophicus]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 21-440 6.64e-151

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member PRK10660:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 436  Bit Score: 435.98  E-value: 6.64e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  21 RLIVAFSGGVDSRVLLELAAQYAQTH-DIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGeSVEKL 99
Cdd:PRK10660  17 QILVAFSGGLDSTVLLHLLVQWRTENpGVTLRAIHVHHGLSPNADSWVKHCEQVCQQWQVPLVVERVQLDQRGL-GIEAA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 100 ARDARYKAFEQHVRSGDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMGL 179
Cdd:PRK10660  96 ARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELEQYAQAHGL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 180 TWVEDESNQDLRYDRNFIRHQVTPTLIERWPSFRESVSRSAQLCAEQEFLLDELLESHFQQALRGSKSLSLSLSIEAlsq 259
Cdd:PRK10660 176 RWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDGTLSIDPLLAM--- 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 260 hSDLLRARLLRMWLNHCNQPMPSQKQLKLIWDEVACAQADANPKLVLNDVEIRRFNNQLYLVQDTQDLS----SWQSDIs 335
Cdd:PRK10660 253 -SDARRAAILRRWLAGQGAPMPSRDQLQRIWQEVALAREDAEPCLRLGAFEIRRYQSQLWLIKSVAGQSetilPWQTWL- 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 336 aeGSLVLPDGLGELHLSSAMSegVSSNRdlqsfslSDKSVTLRviFNPEGLsAHPVGRGHSRKLKKLFQEYQVPSWLRRR 415
Cdd:PRK10660 331 --QPLELPAGLGSLQLVAGGD--VRPPR-------ADEAVSVR--FKAQGL-LHIVGRNHGRKLKKIWQELGVPPWLRDR 396

                        410       420
                 ....*....|....*....|....*
gi 515166630 416 TPILMDGDRVIAVLGLFVDKnyEGQ 440
Cdd:PRK10660 397 TPLLFYGETLIAAAGVFVTQ--EGQ 419
 
Name Accession Description Interval E-value
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 21-440 6.64e-151

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 435.98  E-value: 6.64e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  21 RLIVAFSGGVDSRVLLELAAQYAQTH-DIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGeSVEKL 99
Cdd:PRK10660  17 QILVAFSGGLDSTVLLHLLVQWRTENpGVTLRAIHVHHGLSPNADSWVKHCEQVCQQWQVPLVVERVQLDQRGL-GIEAA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 100 ARDARYKAFEQHVRSGDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMGL 179
Cdd:PRK10660  96 ARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELEQYAQAHGL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 180 TWVEDESNQDLRYDRNFIRHQVTPTLIERWPSFRESVSRSAQLCAEQEFLLDELLESHFQQALRGSKSLSLSLSIEAlsq 259
Cdd:PRK10660 176 RWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDGTLSIDPLLAM--- 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 260 hSDLLRARLLRMWLNHCNQPMPSQKQLKLIWDEVACAQADANPKLVLNDVEIRRFNNQLYLVQDTQDLS----SWQSDIs 335
Cdd:PRK10660 253 -SDARRAAILRRWLAGQGAPMPSRDQLQRIWQEVALAREDAEPCLRLGAFEIRRYQSQLWLIKSVAGQSetilPWQTWL- 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 336 aeGSLVLPDGLGELHLSSAMSegVSSNRdlqsfslSDKSVTLRviFNPEGLsAHPVGRGHSRKLKKLFQEYQVPSWLRRR 415
Cdd:PRK10660 331 --QPLELPAGLGSLQLVAGGD--VRPPR-------ADEAVSVR--FKAQGL-LHIVGRNHGRKLKKIWQELGVPPWLRDR 396

                        410       420
                 ....*....|....*....|....*
gi 515166630 416 TPILMDGDRVIAVLGLFVDKnyEGQ 440
Cdd:PRK10660 397 TPLLFYGETLIAAAGVFVTQ--EGQ 419
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 8-235 6.76e-82

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: 252.06  E-value: 6.76e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   8 FTSALHQSAL--KPSRLIVAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVER 85
Cdd:COG0037    2 VRKAIRDYRLlePGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  86 VSLD---LNSGESVEKLARDARYKAFEQHVRS--GDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGkAFMLR 160
Cdd:COG0037   82 VDVPaiaKKEGKSPEAAARRARYGALYELARElgADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGG-VRLIR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515166630 161 PLLSVTRSDIETSAHNMGLTWVEDESNQDLRYDRNFIRHQVTPTLIERWPSFRESVSRSAQLCAEQEFLLDELLE 235
Cdd:COG0037  161 PLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 21-203 3.67e-68

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: 215.15  E-value: 3.67e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  21 RLIVAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGESVEKLA 100
Cdd:cd01992    1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEAPKSGGNLEAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 101 RDARYKAFEQHVRS--GDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMG 178
Cdd:cd01992   81 REARYAFLERAAKEhgIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCRENG 160

                        170       180
                 ....*....|....*....|....*
gi 515166630 179 LTWVEDESNQDLRYDRNFIRHQVTP 203
Cdd:cd01992  161 LPWVEDPSNADLKYTRNRIRHELLP 185
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 24-199 1.15e-67

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 213.64  E-value: 1.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   24 VAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGESVEKLARDA 103
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVAKKSGENLEAAAREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  104 RYKAFEQHVRSG--DVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMGLTW 181
Cdd:pfam01171  81 RYDFFEEALKKHgaDVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEHKIPW 160

                         170
                  ....*....|....*...
gi 515166630  182 VEDESNQDLRYDRNFIRH 199
Cdd:pfam01171 161 FEDESNADDKYTRNRIRH 178
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 21-203 2.31e-62

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: 200.17  E-value: 2.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   21 RLIVAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERV---SLDLNSGESVE 97
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVdvkALAKGKKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   98 KLARDARYKAFEQHVRS--GDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFML-RPLLSVTRSDIETSA 174
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKhgADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSGIQIiRPLLGISKSEIEEYL 160

                         170       180
                  ....*....|....*....|....*....
gi 515166630  175 HNMGLTWVEDESNQDLRYDRNFIRHQVTP 203
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHELLP 189
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 377-437 4.77e-22

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: 89.17  E-value: 4.77e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515166630   377 LRVIFNPEGLSAHPVGRGHSRKLKKLFQEYQVPSWLRRRTPILMDGDRVIAVLGLFVDKNY 437
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWVVGLRVDARF 61
 
Name Accession Description Interval E-value
tilS PRK10660
tRNA(Ile)-lysidine synthetase; Provisional
 21-440 6.64e-151

tRNA(Ile)-lysidine synthetase; Provisional


Pssm-ID: 182626 [Multi-domain]  Cd Length: 436  Bit Score: 435.98  E-value: 6.64e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  21 RLIVAFSGGVDSRVLLELAAQYAQTH-DIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGeSVEKL 99
Cdd:PRK10660  17 QILVAFSGGLDSTVLLHLLVQWRTENpGVTLRAIHVHHGLSPNADSWVKHCEQVCQQWQVPLVVERVQLDQRGL-GIEAA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 100 ARDARYKAFEQHVRSGDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMGL 179
Cdd:PRK10660  96 ARQARYQAFARTLLPGEVLVTAQHLDDQCETFLLALKRGSGPAGLSAMAEVSPFAGTRLIRPLLARSREELEQYAQAHGL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 180 TWVEDESNQDLRYDRNFIRHQVTPTLIERWPSFRESVSRSAQLCAEQEFLLDELLESHFQQALRGSKSLSLSLSIEAlsq 259
Cdd:PRK10660 176 RWIEDDSNQDDRYDRNFLRLRVLPLLQQRWPHFAEATARSAALCAEQEQLLDELLAEDLAHLQTPDGTLSIDPLLAM--- 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 260 hSDLLRARLLRMWLNHCNQPMPSQKQLKLIWDEVACAQADANPKLVLNDVEIRRFNNQLYLVQDTQDLS----SWQSDIs 335
Cdd:PRK10660 253 -SDARRAAILRRWLAGQGAPMPSRDQLQRIWQEVALAREDAEPCLRLGAFEIRRYQSQLWLIKSVAGQSetilPWQTWL- 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 336 aeGSLVLPDGLGELHLSSAMSegVSSNRdlqsfslSDKSVTLRviFNPEGLsAHPVGRGHSRKLKKLFQEYQVPSWLRRR 415
Cdd:PRK10660 331 --QPLELPAGLGSLQLVAGGD--VRPPR-------ADEAVSVR--FKAQGL-LHIVGRNHGRKLKKIWQELGVPPWLRDR 396

                        410       420
                 ....*....|....*....|....*
gi 515166630 416 TPILMDGDRVIAVLGLFVDKnyEGQ 440
Cdd:PRK10660 397 TPLLFYGETLIAAAGVFVTQ--EGQ 419
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 8-235 6.76e-82

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: 252.06  E-value: 6.76e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   8 FTSALHQSAL--KPSRLIVAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVER 85
Cdd:COG0037    2 VRKAIRDYRLlePGDRILVAVSGGKDSLALLHLLAKLRRRLGFELVAVHVDHGLREESDEDAEFVAELCEELGIPLHVVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  86 VSLD---LNSGESVEKLARDARYKAFEQHVRS--GDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGkAFMLR 160
Cdd:COG0037   82 VDVPaiaKKEGKSPEAAARRARYGALYELARElgADKIATGHHLDDQAETFLLNLLRGSGLAGLAGMPPSRGGG-VRLIR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515166630 161 PLLSVTRSDIETSAHNMGLTWVEDESNQDLRYDRNFIRHQVTPTLIERWPSFRESVSRSAQLCAEQEFLLDELLE 235
Cdd:COG0037  161 PLLYVSRKEIEAYAKENGLPWIEDPCNYDPRYTRNRIRHLVLPELEERNPGFKENLARSAENLAEEEDLLDELAE 235
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 21-203 3.67e-68

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: 215.15  E-value: 3.67e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  21 RLIVAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGESVEKLA 100
Cdd:cd01992    1 KILVAVSGGPDSMALLHLLKELRPKLGLKLVAVHVDHGLREESAEEAQFVAKLCKKLGIPLHILTVTEAPKSGGNLEAAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630 101 RDARYKAFEQHVRS--GDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMG 178
Cdd:cd01992   81 REARYAFLERAAKEhgIDVLLTAHHLDDQAETVLMRLLRGSGLSGLAGMAARSKAGGIRLIRPLLGISKAELLAYCRENG 160

                        170       180
                 ....*....|....*....|....*
gi 515166630 179 LTWVEDESNQDLRYDRNFIRHQVTP 203
Cdd:cd01992  161 LPWVEDPSNADLKYTRNRIRHELLP 185
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 24-199 1.15e-67

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 213.64  E-value: 1.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   24 VAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERVSLDLNSGESVEKLARDA 103
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKLKIKLGIELTAAHVNHGLREESDREAEHVQALCRQLGIPLEILRVDVAKKSGENLEAAAREA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  104 RYKAFEQHVRSG--DVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFMLRPLLSVTRSDIETSAHNMGLTW 181
Cdd:pfam01171  81 RYDFFEEALKKHgaDVLLTAHHLDDQLETFLMRLKRGSGLAGLAGIPPVREFAGGRIIRPLLKVSKAEIEAYAKEHKIPW 160

                         170
                  ....*....|....*...
gi 515166630  182 VEDESNQDLRYDRNFIRH 199
Cdd:pfam01171 161 FEDESNADDKYTRNRIRH 178
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 21-203 2.31e-62

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: 200.17  E-value: 2.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   21 RLIVAFSGGVDSRVLLELAAQYAQTHDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVERV---SLDLNSGESVE 97
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKIKIKLIAAHVDHGLRPESDEEAEFVQQFCRKLNIPLEIKKVdvkALAKGKKKNLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630   98 KLARDARYKAFEQHVRS--GDVLVTGQHIDDQLETFLLALKRGSGPKGLSSMAKIMPFGKAFML-RPLLSVTRSDIETSA 174
Cdd:TIGR02432  81 EAAREARYDFFEEIAKKhgADYILTAHHADDQAETILMRLLRGSGLRGLSGMKPIRILGSGIQIiRPLLGISKSEIEEYL 160

                         170       180
                  ....*....|....*....|....*....
gi 515166630  175 HNMGLTWVEDESNQDLRYDRNFIRHQVTP 203
Cdd:TIGR02432 161 KENGLPWFEDETNQDDKYLRNRIRHELLP 189
TilS_C pfam11734
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 377-444 4.50e-27

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: 103.05  E-value: 4.50e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515166630  377 LRVIFNPEGLSAHPVGRGHSRKLKKLFQEYQVPSWLRRRTPILMDGDRVIAVLGLFVDKNYEGQDCEA 444
Cdd:pfam11734   1 LSVRFRRGGERLRPAGRGGSRKLKKLFQEAGVPPWLRDRLPLLFYGDQLVAVAGLGVAAGFEAQPGEA 68
TilS_C smart00977
TilS substrate C-terminal domain; This domain is found in the tRNA(Ile) lysidine synthetase ...
 377-437 4.77e-22

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: 89.17  E-value: 4.77e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515166630   377 LRVIFNPEGLSAHPVGRGHSRKLKKLFQEYQVPSWLRRRTPILMDGDRVIAVLGLFVDKNY 437
Cdd:smart00977   1 LTVRFRQPGDRLRPLGRGGSKKLKKLFQDAKVPPWERDRIPLLFYGDEIVWVVGLRVDARF 61
TilS pfam09179
TilS substrate binding domain; This domain is found in the tRNA(Ile) lysidine synthetase (TilS) ...
 259-319 2.78e-16

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


Pssm-ID: 462708  Cd Length: 66  Bit Score: 73.04  E-value: 2.78e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515166630  259 QHSDLLRARLLRMWLNHCNQPMPSQKQLKLIWDEVACAQADANPKLVLNDVEIRRFNNQLY 319
Cdd:pfam09179   6 ALSPARRRRLLRRWLAQLGLPMPSAAHLEEILRQLLLARPDAQPRLQLPDGGVRRYRGRLY 66
lysidine_TilS_C TIGR02433
tRNA(Ile)-lysidine synthetase, C-terminal domain; TIGRFAMs model TIGR02432 describes the ...
 377-423 5.94e-15

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: 68.72  E-value: 5.94e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 515166630  377 LRVIFNPEGLSAHPVGRGHSRKLKKLFQEYQVPSWLRRRTPILMDGD 423
Cdd:TIGR02433   1 LTVRFRQGGDRIKLLGRKGSKKLKKLFIDAKVPPWLRDRIPLLFYGD 47
TtcA-like cd24138
tRNA-cytidine(32) 2-sulfurtransferase and similar proteins; tRNA-cytidine(32) ...
 20-179 7.99e-12

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: 63.83  E-value: 7.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  20 SRLIVAFSGGVDSRVLLELAAQYAQTHDIECR--AVHVHHGLSENADYWvERCQAWCDVLSVSL----AVERVSLDLNSG 93
Cdd:cd24138    9 DRILVGLSGGKDSLTLLHLLEELKRRAPIKFElvAVTVDPGYPGYRPPR-EELAEILEELGEILedeeSEIIIIEKEREE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  94 ESVEKL-ARDARYKAFEQHVRSG-DVLVTGQHIDDQLETFLLALKRGSgpkGLSSM--AKIMPFGKAFMLRPLLSVTRSD 169
Cdd:cd24138   88 KSPCSLcSRLRRGILYSLAKELGcNKLALGHHLDDAVETLLMNLLYGG---RLKTMppKVTMDRGGLTVIRPLIYVREKD 164

                        170
                 ....*....|
gi 515166630 170 IETSAHNMGL 179
Cdd:cd24138  165 IRAFAEENGL 174
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 18-185 2.36e-06

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


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 48.09  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  18 KPSRLIVAFSGGVDSRVLLELAAQYaqthDIECRAVHVHHGLSENADYWVERCQAWCDVLSVSLAVerVSLDLNSGESVE 97
Cdd:cd01993    7 KDDKILVAVSGGKDSLALLAVLKKL----GYNVEALYINLGIGEYSEKSEEVVKKLAEKLNLPLHV--VDLKEEYGLGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515166630  98 KLARDARYKA------FEQHV-------RSGDVLVTGQHIDDQLeTFLL---------ALKRGsGPKGLSSMAKIMPfgk 155
Cdd:cd01993   81 ELAKKSRRPPcsvcglVKRYImnkfaveNGFDVVATGHNLDDEA-AFLLgnilnwneeYLAKQ-GPFLLPEHGGLVT--- 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 515166630 156 afMLRPLLSVTRSDIETSAHNMGLTWVEDE 185
Cdd:cd01993  156 --RVKPLYEITEEEIALYALLNGIPYLEEE 183
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 23-70 3.39e-04

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: 38.97  E-value: 3.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 515166630  23 IVAFSGGVDSRVLLELAAQYAQTHDIEcrAVHVHHGL--SENADYWVERC 70
Cdd:cd01986    2 VVGYSGGKDSSVALHLASRLGRKAEVA--VVHIDHGIgfKEEAESVASIA 49
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
21-41 2.06e-03

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 39.71  E-value: 2.06e-03
                         10        20
                 ....*....|....*....|.
gi 515166630  21 RLIVAFSGGVDSRVLLELAAQ 41
Cdd:COG1606   17 SVLVAFSGGVDSTLLAKVAHD 37
 
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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