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Conserved domains on  [gi|1622833551|ref|XP_028692240|]
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tyrosine--tRNA ligase, cytoplasmic isoform X2 [Macaca mulatta]

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 ...
 1-273 6.93e-84

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: 261.34  E-value: 6.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNmKAPWELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYR 80
Cdd:PRK08560   51 MNKLADLQKAGFKVTVLLADWHAYLND-KGDLEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  81 LSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRVHLMNPMV 160
Cdd:PRK08560  126 LAKNTTLARARRSMTIMGRRMEEPDVSKLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 161 PGLTGS--KMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYT 238
Cdd:PRK08560  206 TGLDGGgiKMSKSKPGSAIFVHDSPEEIRRKIKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYE 285

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622833551 239 DLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF 273
Cdd:PRK08560  286 ELERDYAEGKLHPMDLKNAVAEYLIEILEPVREYL 320
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
 272-473 9.23e-69

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 234.29  E-value: 9.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 272 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 351
Cdd:PLN02610  602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 352 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGERVFVKGYEkGQPDEELKPKKK 431
Cdd:PLN02610  682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622833551 432 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 473
Cdd:PLN02610  760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
 
Name Accession Description Interval E-value
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 1-273 6.93e-84

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 261.34  E-value: 6.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNmKAPWELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYR 80
Cdd:PRK08560   51 MNKLADLQKAGFKVTVLLADWHAYLND-KGDLEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  81 LSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRVHLMNPMV 160
Cdd:PRK08560  126 LAKNTTLARARRSMTIMGRRMEEPDVSKLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 161 PGLTGS--KMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYT 238
Cdd:PRK08560  206 TGLDGGgiKMSKSKPGSAIFVHDSPEEIRRKIKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYE 285

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622833551 239 DLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF 273
Cdd:PRK08560  286 ELERDYAEGKLHPMDLKNAVAEYLIEILEPVREYL 320
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 1-265 1.06e-75

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: 238.27  E-value: 1.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNMK--------APWELLELRVSYYENVIKAMLESIgvPLEKLKFIKGTDYQLsK 72
Cdd:cd00805    22 LMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILDFI--PPEKAKFVNNSDWLL-S 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  73 EYTLDVYRLSSVVTQHDSKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYS 150
Cdd:cd00805    99 LYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQRGNITLGRDLIRKLGYK 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 151 KRVHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSFIKHVLFPLksefvilrdekwg 229
Cdd:cd00805   179 KVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEFLKLFTFLD------------- 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622833551 230 gnktYTAYTDLEKDFAAEvVHPGDLKNSVEVALNKL 265
Cdd:cd00805   239 ----YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 272-473 9.23e-69

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 234.29  E-value: 9.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 272 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 351
Cdd:PLN02610  602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 352 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGERVFVKGYEkGQPDEELKPKKK 431
Cdd:PLN02610  682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622833551 432 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 473
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 ...
 308-413 2.87e-62

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: 197.84  E-value: 2.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 308 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 387
Cdd:cd02799     1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                          90       100
                  ....*....|....*....|....*.
gi 1622833551 388 ASIEGInRQVEPLDPPAGSAPGERVF 413
Cdd:cd02799    81 ASNADH-EKVELLEPPEGAKPGERVT 105
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
1-266 8.26e-62

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 203.28  E-value: 8.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYL-DNMKAPWELLELRVSYYENVIKAMLeSIGVPLEKLKFIKGTDYQLSKEYTLDVY 79
Cdd:pfam00579  26 LMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACGLDPEKAEIVNNSDWLEHLELAWLLR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  80 RLSSVVTQHD--SKKagaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYS---K 151
Cdd:pfam00579 105 DLGKHFSLNRmlQFK---DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIELGRDLARRFNKKifkK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 152 RVHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGVLSFIKHVLFPlkseFVILRDEKWGG 230
Cdd:pfam00579 182 PVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRKDLKLFTFLSN----EEIEILEAELG 255

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622833551 231 NKTYTAYTDLEKDFAAEVVHPGDLKNSVEVALNKLL 266
Cdd:pfam00579 256 KSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 315-411 1.51e-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: 132.37  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 315 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 394
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*..
gi 1622833551 395 rQVEPLDPPAGSAPGER 411
Cdd:pfam01588  81 -SVGLLEPPADVPPGTK 96
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 1-273 1.46e-36

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: 138.68  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELR-----VSYYENVIKAMLESIGVplEKLKFIKGTDYQLSKEYT 75
Cdd:TIGR00234  53 LLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  76 LDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQ----RKIFTFAEKYLPALGYSK 151
Cdd:TIGR00234 131 DFIRLLGKIFTVNRMLRRDAFSSRFEENISLHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 152 RVHLMNP---MVPGLTGS-KM--SSSEEESKIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLSFI 209
Cdd:TIGR00234 211 TVPLLTPadgEKMGKSLGgAVslDEGKYDFYQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEIT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 210 KHVLFP------------------LKSEFVILRDEKWGGNKTYTAYTDLEKDFAAEVVHPGDLKN-SVEVA--LNKLLDP 268
Cdd:TIGR00234 291 KYVHGPeaalaaeeiseaifsgglNPDEVPIFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEP 370


                  ....*
gi 1622833551 269 IREKF 273
Cdd:TIGR00234 371 IRKEL 375
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
315-409 8.11e-23

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 101.85  E-value: 8.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 315 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 389
Cdd:COG0073    44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121

                          90       100
                  ....*....|....*....|.
gi 1622833551 390 IEGINRQVE-PLDPPAGSAPG 409
Cdd:COG0073   122 ELGLGEDHDgILELPEDAPPG 142
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 312-412 7.60e-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: 88.25  E-value: 7.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 312 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 391
Cdd:TIGR00399  39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117

                          90       100
                  ....*....|....*....|.
gi 1622833551 392 GINRQVepLDPPAGSAPGERV 412
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
 
Name Accession Description Interval E-value
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 1-273 6.93e-84

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 261.34  E-value: 6.93e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNmKAPWELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYR 80
Cdd:PRK08560   51 MNKLADLQKAGFKVTVLLADWHAYLND-KGDLEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  81 LSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKRVHLMNPMV 160
Cdd:PRK08560  126 LAKNTTLARARRSMTIMGRRMEEPDVSKLVYPLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLL 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 161 PGLTGS--KMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYT 238
Cdd:PRK08560  206 TGLDGGgiKMSKSKPGSAIFVHDSPEEIRRKIKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYE 285

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622833551 239 DLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF 273
Cdd:PRK08560  286 ELERDYAEGKLHPMDLKNAVAEYLIEILEPVREYL 320
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 1-265 1.06e-75

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: 238.27  E-value: 1.06e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNMK--------APWELLELRVSYYENVIKAMLESIgvPLEKLKFIKGTDYQLsK 72
Cdd:cd00805    22 LMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILDFI--PPEKAKFVNNSDWLL-S 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  73 EYTLDVYRLSSVVTQHDSKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYS 150
Cdd:cd00805    99 LYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLGGSDQRGNITLGRDLIRKLGYK 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 151 KRVHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSFIKHVLFPLksefvilrdekwg 229
Cdd:cd00805   179 KVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEFLKLFTFLD------------- 238

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622833551 230 gnktYTAYTDLEKDFAAEvVHPGDLKNSVEVALNKL 265
Cdd:cd00805   239 ----YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 272-473 9.23e-69

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 234.29  E-value: 9.23e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 272 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 351
Cdd:PLN02610  602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 352 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGERVFVKGYEkGQPDEELKPKKK 431
Cdd:PLN02610  682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622833551 432 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 473
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 ...
 308-413 2.87e-62

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: 197.84  E-value: 2.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 308 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 387
Cdd:cd02799     1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                          90       100
                  ....*....|....*....|....*.
gi 1622833551 388 ASIEGInRQVEPLDPPAGSAPGERVF 413
Cdd:cd02799    81 ASNADH-EKVELLEPPEGAKPGERVT 105
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
1-266 8.26e-62

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 203.28  E-value: 8.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYL-DNMKAPWELLELRVSYYENVIKAMLeSIGVPLEKLKFIKGTDYQLSKEYTLDVY 79
Cdd:pfam00579  26 LMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACGLDPEKAEIVNNSDWLEHLELAWLLR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  80 RLSSVVTQHD--SKKagaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYS---K 151
Cdd:pfam00579 105 DLGKHFSLNRmlQFK---DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPGGSDQWGNIELGRDLARRFNKKifkK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 152 RVHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGVLSFIKHVLFPlkseFVILRDEKWGG 230
Cdd:pfam00579 182 PVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRKDLKLFTFLSN----EEIEILEAELG 255

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1622833551 231 NKTYTAYTDLEKDFAAEVVHPGDLKNSVEVALNKLL 266
Cdd:pfam00579 256 KSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 8-283 2.70e-43

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 156.77  E-value: 2.70e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   8 LKAGCEVTILFADLHAYLDNmKAPWELLELRV--SYYENVIKAmlesIGVPLEKLKFIKGTDY--QLSKEYTLDVYRLSS 83
Cdd:PTZ00126   95 TKAGCVFVFWVADWFALLNN-KMGGDLEKIRKvgEYFIEVWKA----AGMDMDNVRFLWASEEinKNPNDYWLRVMDIAR 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  84 VVTQHDSKKAGAEVVKQV--EHPLlSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYSKR-VHLMNPMV 160
Cdd:PTZ00126  170 SFNITRIKRCSQIMGRSEgdEQPC-AQILYPCMQCADIFYLKADICQLGMDQRKVNMLAREYCDKKKIKKKpIILSHHML 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 161 PGLT--GSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYT 238
Cdd:PTZ00126  249 PGLLegQEKMSKSDPNSAIFMEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTTYE 328

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1622833551 239 DLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF-NTPALKKLAS 283
Cdd:PTZ00126  329 ELEKDYLSGALHPGDLKPALAKYLNLMLQPVRDHFqNNPEAKSLLS 374
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 315-412 1.97e-40

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: 140.35  E-value: 1.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 315 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGI- 393
Cdd:cd02153     1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGLe 80

                          90
                  ....*....|....*....
gi 1622833551 394 NRQVEPLDPPAGSAPGERV 412
Cdd:cd02153    81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 315-411 1.51e-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: 132.37  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 315 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 394
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*..
gi 1622833551 395 rQVEPLDPPAGSAPGER 411
Cdd:pfam01588  81 -SVGLLEPPADVPPGTK 96
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 1-273 1.46e-36

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: 138.68  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   1 MSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELR-----VSYYENVIKAMLESIGVplEKLKFIKGTDYQLSKEYT 75
Cdd:TIGR00234  53 LLKLRDFQQAGHEVIVLLGDFTALIGDPTGKSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  76 LDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQ----RKIFTFAEKYLPALGYSK 151
Cdd:TIGR00234 131 DFIRLLGKIFTVNRMLRRDAFSSRFEENISLHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 152 RVHLMNP---MVPGLTGS-KM--SSSEEESKIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLSFI 209
Cdd:TIGR00234 211 TVPLLTPadgEKMGKSLGgAVslDEGKYDFYQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEIT 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 210 KHVLFP------------------LKSEFVILRDEKWGGNKTYTAYTDLEKDFAAEVVHPGDLKN-SVEVA--LNKLLDP 268
Cdd:TIGR00234 291 KYVHGPeaalaaeeiseaifsgglNPDEVPIFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEP 370


                  ....*
gi 1622833551 269 IREKF 273
Cdd:TIGR00234 371 IRKEL 375
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 277-412 1.12e-29

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 122.57  E-value: 1.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 277 ALKKLASAAYPDPSKQKPMAKGPAKnsepeEVIP----SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLV 352
Cdd:PRK00133  541 ASKEAAAAKAAAAAAAAPLAEEPIA-----ETISfddfAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIK 614

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 353 QFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVepLDPPAGSAPGERV 412
Cdd:PRK00133  615 SAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGPGGGDLFL--LEPDEGAKPGMRV 672
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 276-406 5.41e-28

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 117.21  E-value: 5.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 276 PALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIP------SRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVS 349
Cdd:PRK12267  508 PRIDVEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEitiddfDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVS 587

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833551 350 GLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDP-PAGS 406
Cdd:PRK12267  588 GIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLTLLTVDKEvPNGS 645
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 311-412 2.23e-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: 105.28  E-value: 2.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 311 SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 390
Cdd:cd02800     7 AKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAED 85

                          90       100
                  ....*....|....*....|..
gi 1622833551 391 EGinrQVEPLDPPAGSAPGERV 412
Cdd:cd02800    86 GG---KLKLLTPDEEVEPGSRV 104
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 312-412 3.82e-24

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: 96.54  E-value: 3.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 312 RLDIRVGKIITVEKHPDA-DSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 390
Cdd:cd02798     8 KVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGADD 87

                          90       100
                  ....*....|....*....|..
gi 1622833551 391 EGinRQVEPLDPPAGSAPGERV 412
Cdd:cd02798    88 EG--GEVVLLVPDREVPNGAKV 107
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
315-409 8.11e-23

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 101.85  E-value: 8.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 315 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 389
Cdd:COG0073    44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121

                          90       100
                  ....*....|....*....|.
gi 1622833551 390 IEGINRQVE-PLDPPAGSAPG 409
Cdd:COG0073   122 ELGLGEDHDgILELPEDAPPG 142
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 312-412 7.60e-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: 88.25  E-value: 7.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 312 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 391
Cdd:TIGR00399  39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117

                          90       100
                  ....*....|....*....|.
gi 1622833551 392 GINRQVepLDPPAGSAPGERV 412
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 315-391 1.30e-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: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 315 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------LKPQKMRGVESQGMlL 386
Cdd:cd02796     1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG----APNVRAGDKVVVALPGavlpgglkIKKRKLRGVESEGM-L 75


                  ....*
gi 1622833551 387 CASIE 391
Cdd:cd02796    76 CSAKE 80
PRK10089 PRK10089
chaperone CsaA;
312-413 1.92e-14

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 69.47  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 312 RLDIRVGKIITVEKHPDADSL-YVEKIDVG-EAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 389
Cdd:PRK10089   11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGFE 90

                          90       100
                  ....*....|....*....|....
gi 1622833551 390 IEgiNRQVEPLDPPAGSAPGERVF 413
Cdd:PRK10089   91 DE--DGEVVLLTPDRPVPNGVKLV 112
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 9-273 4.36e-13

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 71.47  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   9 KAGCEVTILFADLHAyLDNMKAPWELLELRV--SYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYT-----LDVYRL 81
Cdd:PTZ00348   62 QAGCEFVFWVADWFA-LMNDKVGGELEKIRIvgRYLIEVWKAA----GMDMDKVLFLWSSEEITNHANTywrtvLDIGRQ 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  82 SSVVTqhdSKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYS-KRVHLMNPMV 160
Cdd:PTZ00348  137 NTIAR---IKKCCTIMGKTEGTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKlKPVILSHHML 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 161 PGLT--GSKMSSSEEESKIDLLDRKEDVKKKLKKAFC-----------EPG----NVENNGVLSFIKHVLFPLKSEFVIL 223
Cdd:PTZ00348  214 AGLKqgQAKMSKSDPDSAIFMEDTEEDVARKIRQAYCprvkqsaseitDDGapvaTDDRNPVLDYFQCVVYARPGAVATI 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622833551 224 rdekwgGNKTYTAYTDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF 273
Cdd:PTZ00348  294 ------DGTTYATYEDLEQAFVSDEVSEEALKSCLIDEVNALLEPVRQHF 337
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 303-391 8.80e-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: 70.78  E-value: 8.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 303 SEPEEVIPSRLD---IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------L 371
Cdd:TIGR00472  31 LEVEAVIPFSKPlkgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCG----APNVEAGKKVAVALPGaklpnglkI 106

                          90       100
                  ....*....|....*....|
gi 1622833551 372 KPQKMRGVESQGMlLCASIE 391
Cdd:TIGR00472 107 KKSKLRGVESEGM-LCSESE 125
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 306-391 2.62e-11

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 65.96  E-value: 2.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 306 EEVIPSRLDIR---VGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSG-----LVQFVPkeelqdrlvVVLCN------- 370
Cdd:PRK00629   33 EGVEDVAAGLSgvvVGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGapnvrAGDKVP---------VALPGavlpggf 102

                          90       100
                  ....*....|....*....|..
gi 1622833551 371 -LKPQKMRGVESQGMlLCASIE 391
Cdd:PRK00629  103 kIKKAKLRGVESEGM-LCSASE 123
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 8-296 7.06e-05

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: 44.63  E-value: 7.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551   8 LKAGCEVTILFADLHAYLdnmkAPWELLELRVSYYENVIKAMLeSIGVPLEKLKFIKGTDYQlskEYTLDVYRLSSVVTQ 87
Cdd:TIGR00233  30 QQFGVELFICIADLHAIT----VKQTDPDALRKAREELAADYL-AVGLDPEKTFIFLQSDYP---EHYELAWLLSCQVTF 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551  88 HDSKKAGAEVVKQVEHPLLSGLL-YPGLQALDEEYLKVDAQFGGVDQRKIF--------TFAEKY-----LPALGYSKRV 153
Cdd:TIGR00233 102 GELKRMTQFKDKSQAENVPIGLLsYPVLQAADILLYQADLVPVGIDQDQHLeltrdlaeRFNKKFknffpKPESLISKFF 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 154 hlmnPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNV------ENNGVLSFIkhVLFPLKSEFVILRDEk 227
Cdd:TIGR00233 182 ----PRLMGLSGKKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGGRVtlfehrEKPGVPNLL--VIYQYLSFFLIDDDK- 254

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622833551 228 wggnktytAYTDLEKDFAAEVVHpGDLKNSVEVALNKLLDPIREKFNTPALKKLASAAYPDPSKQKPMA 296
Cdd:TIGR00233 255 --------LKEIYEAYKSGKLGY-GECKKALIEVLQEFLKEIQERRAEIAEEILDKILEPGAKKARETA 314
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 303-393 2.26e-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: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622833551 303 SEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKeelqdrLVVVLC----------NLK 372
Cdd:COG0072    33 EEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVG------VVVVAApggavlpggfKIK 106

                          90       100
                  ....*....|....*....|.
gi 1622833551 373 PQKMRGVESQGMLLCASIEGI 393
Cdd:COG0072   107 KAKIRGVESSGMLCSEEELGL 127
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 181-258 3.92e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 39.89  E-value: 3.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622833551 181 DRKEDVKKKLKKAFCEPgNVENNGVLSFIKHVLFPlKSEFVILRDEKWGGNKTYTAYTDLEKDFAAEVVHPGDLKNSV 258
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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