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Conserved domains on  [gi|27806349|ref|NP_776645|]
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tyrosine--tRNA ligase, cytoplasmic [Bos taurus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 8-328 2.37e-100

nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.


The actual alignment was detected with superfamily member PRK08560:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 329  Bit Score: 305.64  E-value: 2.37e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    8 EEKLSLITRNLQEVLGEEKLKEILKERE-LKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560   2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   87 WDVLELRTSYYENVIKAMlesiGVPLEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560  81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  167 PGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRIHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  245 LKKAFCEPGNVENNGVLAFIRHVLFPLKSEFVILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316


                 ....
gi 27806349  325 REKF 328
Cdd:PRK08560 317 REYL 320
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
 334-528 3.19e-67

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 231.59  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  334 KKLSSAAYPDPSKQKPAVKGPAKNSEPEEVIpSRLDIRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKE 413
Cdd:PLN02610 610 KALSDGGKKKQGKKAGGGGKSKAAAEREIDV-SRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLE 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  414 ELQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGvNRKVEPLDPPAGSAPGERVFVKGYEkGQPDEELKPKKKVFEKLQA 493
Cdd:PLN02610 689 EMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSD-HTKVELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKKVWETLQP 766

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 27806349  494 DFKISDEYIAQWKQTNFMTKMGSVSCKSLKGGNIS 528
Cdd:PLN02610 767 DLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
 
Name Accession Description Interval E-value
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 8-328 2.37e-100

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 305.64  E-value: 2.37e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    8 EEKLSLITRNLQEVLGEEKLKEILKERE-LKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560   2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   87 WDVLELRTSYYENVIKAMlesiGVPLEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560  81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  167 PGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRIHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  245 LKKAFCEPGNVENNGVLAFIRHVLFPLKSEFVILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316


                 ....
gi 27806349  325 REKF 328
Cdd:PRK08560 317 REYL 320
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 36-320 4.53e-86

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 266.78  E-value: 4.53e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  36 LKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMK--------APWDVLELRTSYYENVIKAMLE 106
Cdd:cd00805   1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 107 SIgvPLEKLRFIKGTDYQLsKEYTLDVYRLSSVVTQHDAKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:cd00805  81 FI--PPEKAKFVNNSDWLL-SLYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 185 GVDQRKIFTFAEKYLPALGYSKRIHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLAF 263
Cdd:cd00805 158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27806349 264 IRHVLFPLksefvilrdekwggnktYTAYLDLEKDFADEvVHPGDLKNSVEVALNKL 320
Cdd:cd00805 231 LKLFTFLD-----------------YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
31-321 1.59e-73

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 235.25  E-value: 1.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    31 LKERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL-DNMKAPWDVLELRTSYYENVIKAMLeSIG 109
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   110 VPLEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFGGV 186
Cdd:pfam00579  80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFK-DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPGGS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   187 DQRKIFTFAEKYLPALGYS---KRIHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGVLA 262
Cdd:pfam00579 159 DQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRKDL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27806349   263 FIRHVLFPlkseFVILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKNSVEVALNKLL 321
Cdd:pfam00579 237 KLFTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 334-528 3.19e-67

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 231.59  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  334 KKLSSAAYPDPSKQKPAVKGPAKNSEPEEVIpSRLDIRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKE 413
Cdd:PLN02610 610 KALSDGGKKKQGKKAGGGGKSKAAAEREIDV-SRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLE 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  414 ELQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGvNRKVEPLDPPAGSAPGERVFVKGYEkGQPDEELKPKKKVFEKLQA 493
Cdd:PLN02610 689 EMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSD-HTKVELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKKVWETLQP 766

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 27806349  494 DFKISDEYIAQWKQTNFMTKMGSVSCKSLKGGNIS 528
Cdd:PLN02610 767 DLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 363-468 4.84e-61

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 195.91  E-value: 4.84e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 363 VIPSRLDIRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLC 442
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                        90       100
                ....*....|....*....|....*.
gi 27806349 443 ASVEGvNRKVEPLDPPAGSAPGERVF 468
Cdd:cd02799  81 ASNAD-HEKVELLEPPEGAKPGERVT 105
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 9-328 4.69e-50

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 176.05  E-value: 4.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349     9 EKLSLITRNLQEVLGEEKLKEILK--ERELKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKA 85
Cdd:TIGR00234   3 NILLLLTKRGLEVQTPEEEKDLLKllERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    86 PWDVLELRT-----SYYENVIKAMLESIGVplEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPL 160
Cdd:TIGR00234  83 KSEVRKILTreevqENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENIS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   161 LSGLLYPGLQALDEEYLKVDAQFGGVDQ----RKIFTFAEKYLPALGYSKRIHLMNP---MVPGLTGS-KM--SSSEEES 230
Cdd:TIGR00234 161 LHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVslDEGKYDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   231 KIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLAFIRHVLFP------------------LKSEFV 276
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDEVP 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27806349   277 ILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKN-SVEVA--LNKLLDPIREKF 328
Cdd:TIGR00234 321 IFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEPIRKEL 375
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 370-466 5.64e-37

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 131.98  E-value: 5.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   370 IRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCASvEGVN 449
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAE-ELDG 79

                          90
                  ....*....|....*..
gi 27806349   450 RKVEPLDPPAGSAPGER 466
Cdd:pfam01588  80 GSVGLLEPPADVPPGTK 96
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 345-467 2.74e-21

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 89.79  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   345 SKQKPAVKGPAKNSEPEEVIP----------SRLDIRVGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEE 414
Cdd:TIGR00399   7 LKLKGAKKKEKKDEGEKALEPqketitiddfEKVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEE 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27806349   415 LQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGVNRKVepLDPPAGSAPGERV 467
Cdd:TIGR00399  86 LVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFL--LSPDQEAIAGERI 136
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
370-464 6.35e-21

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 96.85  E-value: 6.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 370 IRVGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVKSQGMLLCAS 444
Cdd:COG0073  44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121

                        90       100
                ....*....|....*....|.
gi 27806349 445 VEGVNRKVE-PLDPPAGSAPG 464
Cdd:COG0073 122 ELGLGEDHDgILELPEDAPPG 142
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 13-72 1.52e-03

Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 41.17  E-value: 1.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27806349  13 LITRNLQEVLGEEKLKEILKERELKVYWG---TAttgkP--HVAYFVPMSKIADFLKAGCEVTIL 72
Cdd:COG0162   7 LIWRGLIEQITDEELREKLAGGPLTIYLGfdpTA----PslHLGHLVPLMKLRRFQDLGHRPIAL 67
 
Name Accession Description Interval E-value
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 8-328 2.37e-100

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 305.64  E-value: 2.37e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    8 EEKLSLITRNLQEVLGEEKLKEILKERE-LKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560   2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   87 WDVLELRTSYYENVIKAMlesiGVPLEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560  81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  167 PGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRIHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  245 LKKAFCEPGNVENNGVLAFIRHVLFPLKSEFVILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316


                 ....
gi 27806349  325 REKF 328
Cdd:PRK08560 317 REYL 320
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 36-320 4.53e-86

catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it aminoacylates the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173902 [Multi-domain]  Cd Length: 269  Bit Score: 266.78  E-value: 4.53e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  36 LKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMK--------APWDVLELRTSYYENVIKAMLE 106
Cdd:cd00805   1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 107 SIgvPLEKLRFIKGTDYQLsKEYTLDVYRLSSVVTQHDAKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:cd00805  81 FI--PPEKAKFVNNSDWLL-SLYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 185 GVDQRKIFTFAEKYLPALGYSKRIHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLAF 263
Cdd:cd00805 158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 27806349 264 IRHVLFPLksefvilrdekwggnktYTAYLDLEKDFADEvVHPGDLKNSVEVALNKL 320
Cdd:cd00805 231 LKLFTFLD-----------------YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
31-321 1.59e-73

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 235.25  E-value: 1.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    31 LKERELKVYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL-DNMKAPWDVLELRTSYYENVIKAMLeSIG 109
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   110 VPLEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFGGV 186
Cdd:pfam00579  80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRMLQFK-DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPGGS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   187 DQRKIFTFAEKYLPALGYS---KRIHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGVLA 262
Cdd:pfam00579 159 DQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRKDL 236

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 27806349   263 FIRHVLFPlkseFVILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKNSVEVALNKLL 321
Cdd:pfam00579 237 KLFTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 334-528 3.19e-67

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 231.59  E-value: 3.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  334 KKLSSAAYPDPSKQKPAVKGPAKNSEPEEVIpSRLDIRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKE 413
Cdd:PLN02610 610 KALSDGGKKKQGKKAGGGGKSKAAAEREIDV-SRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLE 688

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  414 ELQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGvNRKVEPLDPPAGSAPGERVFVKGYEkGQPDEELKPKKKVFEKLQA 493
Cdd:PLN02610 689 EMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSD-HTKVELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKKVWETLQP 766

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 27806349  494 DFKISDEYIAQWKQTNFMTKMGSVSCKSLKGGNIS 528
Cdd:PLN02610 767 DLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 363-468 4.84e-61

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 195.91  E-value: 4.84e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 363 VIPSRLDIRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLC 442
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                        90       100
                ....*....|....*....|....*.
gi 27806349 443 ASVEGvNRKVEPLDPPAGSAPGERVF 468
Cdd:cd02799  81 ASNAD-HEKVELLEPPEGAKPGERVT 105
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 9-328 4.69e-50

tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272976 [Multi-domain]  Cd Length: 378  Bit Score: 176.05  E-value: 4.69e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349     9 EKLSLITRNLQEVLGEEKLKEILK--ERELKVYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKA 85
Cdd:TIGR00234   3 NILLLLTKRGLEVQTPEEEKDLLKllERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    86 PWDVLELRT-----SYYENVIKAMLESIGVplEKLRFIKGTDYQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPL 160
Cdd:TIGR00234  83 KSEVRKILTreevqENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENIS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   161 LSGLLYPGLQALDEEYLKVDAQFGGVDQ----RKIFTFAEKYLPALGYSKRIHLMNP---MVPGLTGS-KM--SSSEEES 230
Cdd:TIGR00234 161 LHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVslDEGKYDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   231 KIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLAFIRHVLFP------------------LKSEFV 276
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDEVP 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 27806349   277 ILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKN-SVEVA--LNKLLDPIREKF 328
Cdd:TIGR00234 321 IFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEPIRKEL 375
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 5-336 1.84e-48

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 172.18  E-value: 1.84e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    5 LSPEEKLSLITRNLQEVLGEEKLKEILKERE-LKVYWGTATTGKPHVAYFVPMSKIADFL-KAGCEVTILFADLHAYLDN 82
Cdd:PTZ00126  35 LSLEERVKLCLSIGEECIQPEELRELLKLKErPICYDGFEPSGRMHIAQGILKAINVNKLtKAGCVFVFWVADWFALLNN 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   83 mKAPWDVLELRT--SYYENVIKAmlesIGVPLEKLRFIKGTDY--QLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQV-- 156
Cdd:PTZ00126 115 -KMGGDLEKIRKvgEYFIEVWKA----AGMDMDNVRFLWASEEinKNPNDYWLRVMDIARSFNITRIKRCSQIMGRSEgd 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  157 EHPLlSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKR-IHLMNPMVPGLT--GSKMSSSEEESKID 233
Cdd:PTZ00126 190 EQPC-AQILYPCMQCADIFYLKADICQLGMDQRKVNMLAREYCDKKKIKKKpIILSHHMLPGLLegQEKMSKSDPNSAIF 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  234 LLDRKEDVKKKLKKAFCEPGNVENNGVLAFIRHVLFPLKSEFVILRDEKWGGNKTYTAYLDLEKDFADEVVHPGDLKNSV 313
Cdd:PTZ00126 269 MEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTTYEELEKDYLSGALHPGDLKPAL 348

                        330       340
                 ....*....|....*....|....
gi 27806349  314 EVALNKLLDPIREKF-NTPALKKL 336
Cdd:PTZ00126 349 AKYLNLMLQPVRDHFqNNPEAKSL 372
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 370-467 4.30e-39

The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.


Pssm-ID: 239066 [Multi-domain]  Cd Length: 99  Bit Score: 137.65  E-value: 4.30e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 370 IRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGV- 448
Cdd:cd02153   1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGLe 80

                        90
                ....*....|....*....
gi 27806349 449 NRKVEPLDPPAGSAPGERV 467
Cdd:cd02153  81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 370-466 5.64e-37

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 131.98  E-value: 5.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   370 IRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCASvEGVN 449
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAE-ELDG 79

                          90
                  ....*....|....*..
gi 27806349   450 RKVEPLDPPAGSAPGER 466
Cdd:pfam01588  80 GSVGLLEPPADVPPGTK 96
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 338-467 2.77e-28

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 119.10  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  338 SAAYPDPSKQKPAVKGPAKNSEPEEVIP----SRLDIRVGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKE 413
Cdd:PRK00133 542 SKEAAAAKAAAAAAAAPLAEEPIAETISfddfAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIKSAYDPE 620

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 27806349  414 ELQDRLVVVLCNLKPQKMR-GVkSQGMLLCASVEGVNRKVepLDPPAGSAPGERV 467
Cdd:PRK00133 621 ELVGKLVVMVANLAPRKMKfGV-SEGMVLAAGPGGGDLFL--LEPDEGAKPGMRV 672
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 366-467 5.46e-27

tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.


Pssm-ID: 239199 [Multi-domain]  Cd Length: 105  Bit Score: 104.89  E-value: 5.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 366 SRLDIRVGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCASV 445
Cdd:cd02800   7 AKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAED 85

                        90       100
                ....*....|....*....|..
gi 27806349 446 EGvnrKVEPLDPPAGSAPGERV 467
Cdd:cd02800  86 GG---KLKLLTPDEEVEPGSRV 104
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 331-461 5.56e-27

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 114.90  E-value: 5.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  331 PALKKLSSAAYPDPSKQKPAVKGPAKNSEPEEVIP------SRLDIRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVS 404
Cdd:PRK12267 508 PRIDVEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEitiddfDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVS 587

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 27806349  405 GLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGVNRKVEPLDP-PAGS 461
Cdd:PRK12267 588 GIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLTLLTVDKEvPNGS 645
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 367-467 1.33e-23

tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.


Pssm-ID: 239197 [Multi-domain]  Cd Length: 107  Bit Score: 95.39  E-value: 1.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 367 RLDIRVGKVISVDKHPDA-DSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCASV 445
Cdd:cd02798   8 KVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGADD 87

                        90       100
                ....*....|....*....|..
gi 27806349 446 EGvnRKVEPLDPPAGSAPGERV 467
Cdd:cd02798  88 EG--GEVVLLVPDREVPNGAKV 107
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 345-467 2.74e-21

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 89.79  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   345 SKQKPAVKGPAKNSEPEEVIP----------SRLDIRVGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEE 414
Cdd:TIGR00399   7 LKLKGAKKKEKKDEGEKALEPqketitiddfEKVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEE 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 27806349   415 LQDRLVVVLCNLKPQKMRGVKSQGMLLCASVEGVNRKVepLDPPAGSAPGERV 467
Cdd:TIGR00399  86 LVGKKVIVVANLKPAKLFGVKSEGMILAAEDDGKVLFL--LSPDQEAIAGERI 136
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
370-464 6.35e-21

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 96.85  E-value: 6.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 370 IRVGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVKSQGMLLCAS 444
Cdd:COG0073  44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121

                        90       100
                ....*....|....*....|.
gi 27806349 445 VEGVNRKVE-PLDPPAGSAPG 464
Cdd:COG0073 122 ELGLGEDHDgILELPEDAPPG 142
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 5-328 1.17e-15

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 79.95  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    5 LSPEEKLSLITRNLQEVLGEEKLKEIL-KERELKVYWGTATTGKPHVAYFVPMS-KIADFLKAGCEVTILFADLHAYL-D 81
Cdd:PTZ00348   1 MNTDERYKLLRSVGEECIQESELRNLIeKKPLIRCYDGFEPSGRMHIAQGIFKAvNVNKCTQAGCEFVFWVADWFALMnD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   82 NMKAPWDVLELRTSYYENVIKAMlesiGVPLEKLRFIKGTDYQLSKEYT-----LDVYRLSSVVTqhdAKKAGAEVVKQV 156
Cdd:PTZ00348  81 KVGGELEKIRIVGRYLIEVWKAA----GMDMDKVLFLWSSEEITNHANTywrtvLDIGRQNTIAR---IKKCCTIMGKTE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  157 EHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYS-KRIHLMNPMVPGLT--GSKMSSSEEESKID 233
Cdd:PTZ00348 154 GTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKqgQAKMSKSDPDSAIF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  234 LLDRKEDVKKKLKKAFC-----------EPG----NVENNGVLAFIRHVLFPLKSEFVILrdekwgGNKTYTAYLDLEKD 298
Cdd:PTZ00348 234 MEDTEEDVARKIRQAYCprvkqsaseitDDGapvaTDDRNPVLDYFQCVVYARPGAVATI------DGTTYATYEDLEQA 307

                        330       340       350
                 ....*....|....*....|....*....|
gi 27806349  299 FADEVVHPGDLKNSVEVALNKLLDPIREKF 328
Cdd:PTZ00348 308 FVSDEVSEEALKSCLIDEVNALLEPVRQHF 337
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 370-446 5.59e-14

tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.


Pssm-ID: 239196 [Multi-domain]  Cd Length: 103  Bit Score: 67.92  E-value: 5.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349 370 IRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------LKPQKMRGVKSQGMlL 441
Cdd:cd02796   1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG----APNVRAGDKVVVALPGavlpgglkIKKRKLRGVESEGM-L 75


                ....*
gi 27806349 442 CASVE 446
Cdd:cd02796  76 CSAKE 80
PRK10089 PRK10089
chaperone CsaA;
367-468 5.66e-14

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 68.32  E-value: 5.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  367 RLDIRVGKVISVDKHPDADSL-YVEKIDVG-EAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVKSQGMLLCAS 444
Cdd:PRK10089  11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGFE 90

                         90       100
                 ....*....|....*....|....
gi 27806349  445 VEgvNRKVEPLDPPAGSAPGERVF 468
Cdd:PRK10089  91 DE--DGEVVLLTPDRPVPNGVKLV 112
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 358-446 6.78e-13

phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273097 [Multi-domain]  Cd Length: 797  Bit Score: 71.17  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   358 SEPEEVIPSRLD---IRVGKVISVDKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------L 426
Cdd:TIGR00472  31 LEVEAVIPFSKPlkgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCG----APNVEAGKKVAVALPGaklpnglkI 106

                          90       100
                  ....*....|....*....|
gi 27806349   427 KPQKMRGVKSQGMlLCASVE 446
Cdd:TIGR00472 107 KKSKLRGVESEGM-LCSESE 125
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 361-446 2.15e-10

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 63.27  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  361 EEVIPSRLDIR---VGKVISVDKHPDADSLYVEKIDVGEaEPRTVVSG-----LVQFVPkeelqdrlvVVLCN------- 425
Cdd:PRK00629  33 EGVEDVAAGLSgvvVGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGapnvrAGDKVP---------VALPGavlpggf 102

                         90       100
                 ....*....|....*....|..
gi 27806349  426 -LKPQKMRGVKSQGMlLCASVE 446
Cdd:PRK00629 103 kIKKAKLRGVESEGM-LCSASE 123
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 38-328 3.02e-07

tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 272975 [Multi-domain]  Cd Length: 327  Bit Score: 52.33  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349    38 VYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLdnmkAPWDVLELRTSYYENVIKAMLeSIGVPLEKLRF 117
Cdd:TIGR00233   5 VLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAIT----VKQTDPDALRKAREELAADYL-AVGLDPEKTFI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   118 IKGTDYQlskEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLL-YPGLQALDEEYLKVDAQFGGVDQRKIF---- 192
Cdd:TIGR00233  80 FLQSDYP---EHYELAWLLSCQVTFGELKRMTQFKDKSQAENVPIGLLsYPVLQAADILLYQADLVPVGIDQDQHLeltr 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   193 ----TFAEKY-----LPALGYSKrihlMNPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNV------EN 257
Cdd:TIGR00233 157 dlaeRFNKKFknffpKPESLISK----FFPRLMGLSGKKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGGRVtlfehrEK 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806349   258 NGVLAFIrhVLFPLKSEFVILRDEKWGgnktytaylDLEKDFADEVVHpGDLKNSVEVALNKLLDPIREKF 328
Cdd:TIGR00233 233 PGVPNLL--VIYQYLSFFLIDDDKLKE---------IYEAYKSGKLGY-GECKKALIEVLQEFLKEIQERR 291
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 38-241 1.23e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 41.39  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349   38 VYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAPWDvlELRTSYYENvIKAMLeSIGVPLEKLRF 117
Cdd:PRK12285  69 VYTGFMPSGPMHIGHKMVFDELKWHQEFGANVYIPIADDEAYAAR-GLSWE--ETREWAYEY-ILDLI-ALGFDPDKTEI 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27806349  118 IKGTDYQlskeytlDVYRLSSVVtqhdAKKAGAEVVKQV----EHPLLSGLLYPGLQALDEEYLKVDAQFG------GVD 187
Cdd:PRK12285 144 YFQSENI-------KVYDLAFEL----AKKVNFSELKAIygftGETNIGHIFYPATQAADILHPQLEEGPKptlvpvGID 212

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27806349  188 Q-------RKIftfAEKYLPALGYSKRIHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDV 241
Cdd:PRK12285 213 QdphirltRDI---AERLHGGYGFIKPSSTYHKFMPGLTGGKMSSSKPESAIYLTDDPETV 270
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
 13-72 1.52e-03

Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439932 [Multi-domain]  Cd Length: 409  Bit Score: 41.17  E-value: 1.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27806349  13 LITRNLQEVLGEEKLKEILKERELKVYWG---TAttgkP--HVAYFVPMSKIADFLKAGCEVTIL 72
Cdd:COG0162   7 LIWRGLIEQITDEELREKLAGGPLTIYLGfdpTA----PslHLGHLVPLMKLRRFQDLGHRPIAL 67
 
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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