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Conserved domains on  [gi|4507947|ref|NP_003671|]
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tyrosine--tRNA ligase, cytoplasmic [Homo sapiens]

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 3.16e-99

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: 302.94  E-value: 3.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     8 EEKLHLITRNLQEVLGEEKLKEILKERE-LKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560   2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    87 WELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560  81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   167 PGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   245 LKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316

                 ....
gi 4507947   325 REKF 328
Cdd:PRK08560 317 REYL 320
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
327-528 7.55e-67

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 230.82  E-value: 7.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   327 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 406
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   407 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 486
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4507947   487 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 528
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
 
Name Accession Description Interval E-value
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
8-328 3.16e-99

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 302.94  E-value: 3.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     8 EEKLHLITRNLQEVLGEEKLKEILKERE-LKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560   2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    87 WELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560  81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   167 PGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   245 LKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316

                 ....
gi 4507947   325 REKF 328
Cdd:PRK08560 317 REYL 320
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
36-320 4.58e-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: 4.58e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   36 LKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMK--------APWELLELRVSYYENVIKAMLE 106
Cdd:cd00805   1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  107 SIgvPLEKLKFIKGTDYQLsKEYTLDVYRLSSVVTQHDSKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:cd00805  81 FI--PPEKAKFVNNSDWLL-SLYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  185 GIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSF 263
Cdd:cd00805 158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947  264 IKHVLFPLksefvilrdekwggnktYTAYVDLEKDFAAEvVHPGDLKNSVEVALNKL 320
Cdd:cd00805 231 LKLFTFLD-----------------YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
31-321 1.69e-74

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 237.56  E-value: 1.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     31 LKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL-DNMKAPWELLELRVSYYENVIKAMLeSIG 109
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    110 VPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHD--SKKagaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:pfam00579  80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRmlQFK---DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    185 GIDQRKIFTFAEKYLPALGYS---KRVHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGV 260
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRK 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507947    261 LSFIKHVLFPlkseFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLL 321
Cdd:pfam00579 235 DLKLFTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PLN02610 PLN02610
probable methionyl-tRNA synthetase
327-528 7.55e-67

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 230.82  E-value: 7.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   327 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 406
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   407 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 486
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4507947   487 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 528
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
363-468 7.17e-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: 195.52  E-value: 7.17e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  363 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 442
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
                        90       100
                ....*....|....*....|....*.
gi 4507947  443 ASIEGInRQVEPLDPPAGSAPGEHVF 468
Cdd:cd02799  81 ASNADH-EKVELLEPPEGAKPGERVT 105
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
9-328 1.23e-49

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: 174.89  E-value: 1.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947      9 EKLHLITRNLQEVLGEEKLKEILK--ERELKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKA 85
Cdd:TIGR00234   3 NILLLLTKRGLEVQTPEEEKDLLKllERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     86 PWELLELR-----VSYYENVIKAMLESIGVplEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPL 160
Cdd:TIGR00234  83 KSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    161 LSGLLYPGLQALDEEYLKVDAQFGGIDQ----RKIFTFAEKYLPALGYSKRVHLMNP---MVPGLTGS-KM--SSSEEES 230
Cdd:TIGR00234 161 LHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVslDEGKYDF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    231 KIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLSFIKHVLFP------------------LKSEFV 276
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDEVP 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4507947    277 ILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKN-SVEVA--LNKLLDPIREKF 328
Cdd:TIGR00234 321 IFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEPIRKEL 375
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
370-465 9.50e-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: 131.21  E-value: 9.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 449
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80
                          90
                  ....*....|....*.
gi 4507947    450 rQVEPLDPPAGSAPGE 465
Cdd:pfam01588  81 -SVGLLEPPADVPPGT 95
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
370-464 1.68e-22

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 101.47  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  370 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 444
Cdd:COG0073  44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121
                        90       100
                ....*....|....*....|.
gi 4507947  445 IEGINRQVE-PLDPPAGSAPG 464
Cdd:COG0073 122 ELGLGEDHDgILELPEDAPPG 142
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
367-467 9.43e-20

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: 85.56  E-value: 9.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    367 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 446
Cdd:TIGR00399  39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117
                          90       100
                  ....*....|....*....|.
gi 4507947    447 GINRQVepLDPPAGSAPGEHV 467
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
11-72 1.21e-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: 1.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947   11 LHLITRNLQEVLGEEKLKEILKERELKIYWG---TAttgkP--HVAYFVPMSKIADFLKAGCEVTIL 72
Cdd:COG0162   5 LELIWRGLIEQITDEELREKLAGGPLTIYLGfdpTA----PslHLGHLVPLMKLRRFQDLGHRPIAL 67
 
Name Accession Description Interval E-value
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
8-328 3.16e-99

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 302.94  E-value: 3.16e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     8 EEKLHLITRNLQEVLGEEKLKEILKERE-LKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560   2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    87 WELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560  81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   167 PGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   245 LKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316

                 ....
gi 4507947   325 REKF 328
Cdd:PRK08560 317 REYL 320
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
36-320 4.58e-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: 4.58e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   36 LKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMK--------APWELLELRVSYYENVIKAMLE 106
Cdd:cd00805   1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  107 SIgvPLEKLKFIKGTDYQLsKEYTLDVYRLSSVVTQHDSKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:cd00805  81 FI--PPEKAKFVNNSDWLL-SLYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  185 GIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSF 263
Cdd:cd00805 158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947  264 IKHVLFPLksefvilrdekwggnktYTAYVDLEKDFAAEvVHPGDLKNSVEVALNKL 320
Cdd:cd00805 231 LKLFTFLD-----------------YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
31-321 1.69e-74

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 237.56  E-value: 1.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     31 LKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL-DNMKAPWELLELRVSYYENVIKAMLeSIG 109
Cdd:pfam00579   1 KKNRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    110 VPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHD--SKKagaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:pfam00579  80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRmlQFK---DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    185 GIDQRKIFTFAEKYLPALGYS---KRVHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGV 260
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRK 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507947    261 LSFIKHVLFPlkseFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLL 321
Cdd:pfam00579 235 DLKLFTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PLN02610 PLN02610
probable methionyl-tRNA synthetase
327-528 7.55e-67

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 230.82  E-value: 7.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   327 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 406
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   407 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 486
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4507947   487 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 528
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
363-468 7.17e-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: 195.52  E-value: 7.17e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  363 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 442
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
                        90       100
                ....*....|....*....|....*.
gi 4507947  443 ASIEGInRQVEPLDPPAGSAPGEHVF 468
Cdd:cd02799  81 ASNADH-EKVELLEPPEGAKPGERVT 105
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
9-328 1.23e-49

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: 174.89  E-value: 1.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947      9 EKLHLITRNLQEVLGEEKLKEILK--ERELKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKA 85
Cdd:TIGR00234   3 NILLLLTKRGLEVQTPEEEKDLLKllERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     86 PWELLELR-----VSYYENVIKAMLESIGVplEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPL 160
Cdd:TIGR00234  83 KSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENIS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    161 LSGLLYPGLQALDEEYLKVDAQFGGIDQ----RKIFTFAEKYLPALGYSKRVHLMNP---MVPGLTGS-KM--SSSEEES 230
Cdd:TIGR00234 161 LHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVslDEGKYDF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    231 KIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLSFIKHVLFP------------------LKSEFV 276
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDEVP 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 4507947    277 ILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKN-SVEVA--LNKLLDPIREKF 328
Cdd:TIGR00234 321 IFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEPIRKEL 375
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
5-338 1.32e-48

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 172.57  E-value: 1.32e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     5 PSPEEKLHLITRNLQEVLGEEKLKEILKERELKI-YWGTATTGKPHVAYFVPMSKIADFL-KAGCEVTILFADLHAYLDN 82
Cdd:PTZ00126  35 LSLEERVKLCLSIGEECIQPEELRELLKLKERPIcYDGFEPSGRMHIAQGILKAINVNKLtKAGCVFVFWVADWFALLNN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    83 mKAPWELLELRV--SYYENVIKAmlesIGVPLEKLKFIKGTDY--QLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQV-- 156
Cdd:PTZ00126 115 -KMGGDLEKIRKvgEYFIEVWKA----AGMDMDNVRFLWASEEinKNPNDYWLRVMDIARSFNITRIKRCSQIMGRSEgd 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   157 EHPLlSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKR-VHLMNPMVPGLT--GSKMSSSEEESKID 233
Cdd:PTZ00126 190 EQPC-AQILYPCMQCADIFYLKADICQLGMDQRKVNMLAREYCDKKKIKKKpIILSHHMLPGLLegQEKMSKSDPNSAIF 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   234 LLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSV 313
Cdd:PTZ00126 269 MEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTTYEELEKDYLSGALHPGDLKPAL 348
                        330       340
                 ....*....|....*....|....*.
gi 4507947   314 EVALNKLLDPIREKF-NTPALKKLAS 338
Cdd:PTZ00126 349 AKYLNLMLQPVRDHFqNNPEAKSLLS 374
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
370-467 5.28e-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: 137.27  E-value: 5.28e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGI- 448
Cdd:cd02153   1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGLe 80
                        90
                ....*....|....*....
gi 4507947  449 NRQVEPLDPPAGSAPGEHV 467
Cdd:cd02153  81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
370-465 9.50e-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: 131.21  E-value: 9.50e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 449
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80
                          90
                  ....*....|....*.
gi 4507947    450 rQVEPLDPPAGSAPGE 465
Cdd:pfam01588  81 -SVGLLEPPADVPPGT 95
metG PRK00133
methionyl-tRNA synthetase; Reviewed
332-467 5.80e-28

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 118.33  E-value: 5.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   332 ALKKLASAAYPDPSKQKPMAKGPAKnsepeEVIP----SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLV 407
Cdd:PRK00133 541 ASKEAAAAKAAAAAAAAPLAEEPIA-----ETISfddfAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIK 614
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   408 QFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVepLDPPAGSAPGEHV 467
Cdd:PRK00133 615 SAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGPGGGDLFL--LEPDEGAKPGMRV 672
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
331-461 1.39e-27

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 116.82  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   331 PALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIP------SRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVS 404
Cdd:PRK12267 508 PRIDVEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEitiddfDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVS 587
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4507947   405 GLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDP-PAGS 461
Cdd:PRK12267 588 GIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLTLLTVDKEvPNGS 645
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
366-467 4.27e-26

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: 102.19  E-value: 4.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  366 SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 445
Cdd:cd02800   7 AKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAED 85
                        90       100
                ....*....|....*....|..
gi 4507947  446 EGinrQVEPLDPPAGSAPGEHV 467
Cdd:cd02800  86 GG---KLKLLTPDEEVEPGSRV 104
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
367-464 3.74e-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: 94.23  E-value: 3.74e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  367 RLDIRVGKIITVEKHPDA-DSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 445
Cdd:cd02798   8 KVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGADD 87
                        90
                ....*....|....*....
gi 4507947  446 EGinRQVEPLDPPAGSAPG 464
Cdd:cd02798  88 EG--GEVVLLVPDREVPNG 104
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
370-464 1.68e-22

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 101.47  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  370 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 444
Cdd:COG0073  44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121
                        90       100
                ....*....|....*....|.
gi 4507947  445 IEGINRQVE-PLDPPAGSAPG 464
Cdd:COG0073 122 ELGLGEDHDgILELPEDAPPG 142
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
367-467 9.43e-20

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: 85.56  E-value: 9.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    367 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 446
Cdd:TIGR00399  39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117
                          90       100
                  ....*....|....*....|.
gi 4507947    447 GINRQVepLDPPAGSAPGEHV 467
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
6-328 5.11e-16

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 81.10  E-value: 5.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     6 SPEEKLHLITRNLQEVLGEEKLKEIL-KERELKIYWGTATTGKPHVAYFVPMS-KIADFLKAGCEVTILFADLHAyLDNM 83
Cdd:PTZ00348   2 NTDERYKLLRSVGEECIQESELRNLIeKKPLIRCYDGFEPSGRMHIAQGIFKAvNVNKCTQAGCEFVFWVADWFA-LMND 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    84 KAPWELLELRV--SYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYT-----LDVYRLSSVVTqhdSKKAGAEVVKQV 156
Cdd:PTZ00348  81 KVGGELEKIRIvgRYLIEVWKAA----GMDMDKVLFLWSSEEITNHANTywrtvLDIGRQNTIAR---IKKCCTIMGKTE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   157 EHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYS-KRVHLMNPMVPGLT--GSKMSSSEEESKID 233
Cdd:PTZ00348 154 GTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKqgQAKMSKSDPDSAIF 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   234 LLDRKEDVKKKLKKAFC-----------EPG----NVENNGVLSFIKHVLFPLKSEFVILrdekwgGNKTYTAYVDLEKD 298
Cdd:PTZ00348 234 MEDTEEDVARKIRQAYCprvkqsaseitDDGapvaTDDRNPVLDYFQCVVYARPGAVATI------DGTTYATYEDLEQA 307
                        330       340       350
                 ....*....|....*....|....*....|
gi 4507947   299 FAAEVVHPGDLKNSVEVALNKLLDPIREKF 328
Cdd:PTZ00348 308 FVSDEVSEEALKSCLIDEVNALLEPVRQHF 337
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
370-446 1.55e-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: 69.46  E-value: 1.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------LKPQKMRGVESQGMlL 441
Cdd:cd02796   1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG----APNVRAGDKVVVALPGavlpgglkIKKRKLRGVESEGM-L 75

                ....*
gi 4507947  442 CASIE 446
Cdd:cd02796  76 CSAKE 80
PRK10089 PRK10089
chaperone CsaA;
367-443 3.59e-14

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 68.70  E-value: 3.59e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507947   367 RLDIRVGKIITVEKHPDADSL-YVEKIDVG-EAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCA 443
Cdd:PRK10089  11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGF 89
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
358-446 1.20e-12

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: 70.40  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    358 SEPEEVIPSRLD---IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------L 426
Cdd:TIGR00472  31 LEVEAVIPFSKPlkgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCG----APNVEAGKKVAVALPGaklpnglkI 106
                          90       100
                  ....*....|....*....|
gi 4507947    427 KPQKMRGVESQGMlLCASIE 446
Cdd:TIGR00472 107 KKSKLRGVESEGM-LCSESE 125
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
361-446 3.45e-11

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 65.96  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   361 EEVIPSRLDIR---VGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSG-----LVQFVPkeelqdrlvVVLCN------- 425
Cdd:PRK00629  33 EGVEDVAAGLSgvvVGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGapnvrAGDKVP---------VALPGavlpggf 102
                         90       100
                 ....*....|....*....|..
gi 4507947   426 -LKPQKMRGVESQGMlLCASIE 446
Cdd:PRK00629 103 kIKKAKLRGVESEGM-LCSASE 123
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
38-351 4.70e-08

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: 55.03  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947     38 IYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLdnmkAPWELLELRVSYYENVIKAMLeSIGVPLEKLKF 117
Cdd:TIGR00233   5 VLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAIT----VKQTDPDALRKAREELAADYL-AVGLDPEKTFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    118 IKGTDYQlskEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLL-YPGLQALDEEYLKVDAQFGGIDQRKIF---- 192
Cdd:TIGR00233  80 FLQSDYP---EHYELAWLLSCQVTFGELKRMTQFKDKSQAENVPIGLLsYPVLQAADILLYQADLVPVGIDQDQHLeltr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    193 ----TFAEKY-----LPALGYSKRVhlmnPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNV------EN 257
Cdd:TIGR00233 157 dlaeRFNKKFknffpKPESLISKFF----PRLMGLSGKKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGGRVtlfehrEK 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    258 NGVLSFIkhVLFPLKSEFVILRDEKWGgnktytayvDLEKDFAAEVVHpGDLKNSVEVALNKLLDPIREKFNTPALKKLA 337
Cdd:TIGR00233 233 PGVPNLL--VIYQYLSFFLIDDDKLKE---------IYEAYKSGKLGY-GECKKALIEVLQEFLKEIQERRAEIAEEILD 300
                         330
                  ....*....|....
gi 4507947    338 SAAYPDPSKQKPMA 351
Cdd:TIGR00233 301 KILEPGAKKARETA 314
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
38-241 1.14e-03

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 41.39  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947    38 IYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIkamleSIGVPLEKLKF 117
Cdd:PRK12285  69 VYTGFMPSGPMHIGHKMVFDELKWHQEFGANVYIPIADDEAYAARGLSWEETREWAYEYILDLI-----ALGFDPDKTEI 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947   118 IKGTDYQlskeytlDVYRLSSVVtqhdSKKAGAEVVKQV----EHPLLSGLLYPGLQALDEEYLKVDAQFG------GID 187
Cdd:PRK12285 144 YFQSENI-------KVYDLAFEL----AKKVNFSELKAIygftGETNIGHIFYPATQAADILHPQLEEGPKptlvpvGID 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507947   188 Q-------RKIftfAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDV 241
Cdd:PRK12285 213 QdphirltRDI---AERLHGGYGFIKPSSTYHKFMPGLTGGKMSSSKPESAIYLTDDPETV 270
TyrS COG0162
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ...
11-72 1.21e-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: 1.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947   11 LHLITRNLQEVLGEEKLKEILKERELKIYWG---TAttgkP--HVAYFVPMSKIADFLKAGCEVTIL 72
Cdd:COG0162   5 LELIWRGLIEQITDEELREKLAGGPLTIYLGfdpTA----PslHLGHLVPLMKLRRFQDLGHRPIAL 67
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
358-448 2.85e-03

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


Pssm-ID: 439842 [Multi-domain]  Cd Length: 793  Bit Score: 40.53  E-value: 2.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947  358 SEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKeelqdrLVVVLC----------NLK 427
Cdd:COG0072  33 EEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVG------VVVVAApggavlpggfKIK 106
                        90       100
                ....*....|....*....|.
gi 4507947  428 PQKMRGVESQGMLLCASIEGI 448
Cdd:COG0072 107 KAKIRGVESSGMLCSEEELGL 127
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
236-313 6.12e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 39.50  E-value: 6.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507947   236 DRKEDVKKKLKKAFCEPgNVENNGVLSFIKHVLFPlKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSV 313
Cdd:PTZ00348 570 DNDMDIRRKIKKAYSAP-NEEANPVISVAQHLLAQ-QGALSIERGEANGGNVAYNTPEALVADCGSGALHPADLKAAV 645
 
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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