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Conserved domains on  [gi|767906539|ref|XP_011540649|]
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tyrosine--tRNA ligase, cytoplasmic isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
 117-318 8.21e-69

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 228.90  E-value: 8.21e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 117 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 196
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 197 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 276
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767906539 277 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 318
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 4-128 1.64e-32

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 PTZ00126:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 383  Bit Score: 124.03  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   4 MVPGLT--GSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTA 81
Cdd:PTZ00126 247 MLPGLLegQEKMSKSDPNSAIFMEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTT 326

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767906539  82 YVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF-NTPALKKLAS 128
Cdd:PTZ00126 327 YEELEKDYLSGALHPGDLKPALAKYLNLMLQPVRDHFqNNPEAKSLLS 374
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 117-318 8.21e-69

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 228.90  E-value: 8.21e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 117 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 196
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 197 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 276
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767906539 277 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 318
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 ...
 153-258 7.39e-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: 191.67  E-value: 7.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 153 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 232
Cdd:cd02799    1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                         90       100
                 ....*....|....*....|....*.
gi 767906539 233 ASIEGInRQVEPLDPPAGSAPGEHVF 258
Cdd:cd02799   81 ASNADH-EKVELLEPPEGAKPGERVT 105
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 160-255 2.90e-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: 128.51  E-value: 2.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539  160 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 239
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*.
gi 767906539  240 rQVEPLDPPAGSAPGE 255
Cdd:pfam01588  81 -SVGLLEPPADVPPGT 95
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 4-128 1.64e-32

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 124.03  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   4 MVPGLT--GSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTA 81
Cdd:PTZ00126 247 MLPGLLegQEKMSKSDPNSAIFMEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTT 326

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767906539  82 YVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF-NTPALKKLAS 128
Cdd:PTZ00126 327 YEELEKDYLSGALHPGDLKPALAKYLNLMLQPVRDHFqNNPEAKSLLS 374
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
160-254 7.28e-24

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 101.85  E-value: 7.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 160 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 234
Cdd:COG0073   44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121

                         90       100
                 ....*....|....*....|.
gi 767906539 235 IEGINRQVE-PLDPPAGSAPG 254
Cdd:COG0073  122 ELGLGEDHDgILELPEDAPPG 142
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 157-257 7.01e-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: 84.02  E-value: 7.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539  157 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 236
Cdd:TIGR00399  39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117

                          90       100
                  ....*....|....*....|.
gi 767906539  237 GINRQVepLDPPAGSAPGEHV 257
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
1-111 1.45e-16

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 78.47  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539    1 MNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGVLSFIKHVLFPlkseFVILRDEKWGGNKTY 79
Cdd:pfam00579 186 TNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRKDLKLFTFLSN----EEIEILEAELGKSPY 259

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767906539   80 TAYVDLEKDFAAEVVHPGDLKNSVEVALNKLL 111
Cdd:pfam00579 260 REAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 1-110 2.03e-08

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: 54.15  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   1 MNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSFIKHVLFPLksefvilrdekwggnktY 79
Cdd:cd00805  184 TTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEFLKLFTFLD-----------------Y 239

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767906539  80 TAYVDLEKDFAAEvVHPGDLKNSVEVALNKL 110
Cdd:cd00805  240 EEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 117-318 8.21e-69

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 228.90  E-value: 8.21e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 117 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 196
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 197 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 276
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767906539 277 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 318
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 ...
 153-258 7.39e-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: 191.67  E-value: 7.39e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 153 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 232
Cdd:cd02799    1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                         90       100
                 ....*....|....*....|....*.
gi 767906539 233 ASIEGInRQVEPLDPPAGSAPGEHVF 258
Cdd:cd02799   81 ASNADH-EKVELLEPPEGAKPGERVT 105
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 160-257 1.04e-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: 134.95  E-value: 1.04e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 160 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGI- 238
Cdd:cd02153    1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGLe 80

                         90
                 ....*....|....*....
gi 767906539 239 NRQVEPLDPPAGSAPGEHV 257
Cdd:cd02153   81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 160-255 2.90e-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: 128.51  E-value: 2.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539  160 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 239
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*.
gi 767906539  240 rQVEPLDPPAGSAPGE 255
Cdd:pfam01588  81 -SVGLLEPPADVPPGT 95
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 4-128 1.64e-32

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 124.03  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   4 MVPGLT--GSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTA 81
Cdd:PTZ00126 247 MLPGLLegQEKMSKSDPNSAIFMEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTT 326

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767906539  82 YVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF-NTPALKKLAS 128
Cdd:PTZ00126 327 YEELEKDYLSGALHPGDLKPALAKYLNLMLQPVRDHFqNNPEAKSLLS 374
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 2-118 1.75e-31

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 119.97  E-value: 1.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   2 NPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTY 79
Cdd:PRK08560 202 TPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRKIKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEY 281

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767906539  80 TAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF 118
Cdd:PRK08560 282 ESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPVREYL 320
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 122-257 1.20e-29

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 118.72  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 122 ALKKLASAAYPDPSKQKPMAKGPAKnsepeEVIP----SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLV 197
Cdd:PRK00133 541 ASKEAAAAKAAAAAAAAPLAEEPIA-----ETISfddfAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIK 614

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 198 QFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVepLDPPAGSAPGEHV 257
Cdd:PRK00133 615 SAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGPGGGDLFL--LEPDEGAKPGMRV 672
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 121-251 2.40e-29

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 117.98  E-value: 2.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 121 PALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIP------SRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVS 194
Cdd:PRK12267 508 PRIDVEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEitiddfDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVS 587

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767906539 195 GLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDP-PAGS 251
Cdd:PRK12267 588 GIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLTLLTVDKEvPNGS 645
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 156-257 9.28e-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: 101.42  E-value: 9.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 156 SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 235
Cdd:cd02800    7 AKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAED 85

                         90       100
                 ....*....|....*....|..
gi 767906539 236 EGinrQVEPLDPPAGSAPGEHV 257
Cdd:cd02800   86 GG---KLKLLTPDEEVEPGSRV 104
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
160-254 7.28e-24

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 101.85  E-value: 7.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 160 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 234
Cdd:COG0073   44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121

                         90       100
                 ....*....|....*....|.
gi 767906539 235 IEGINRQVE-PLDPPAGSAPG 254
Cdd:COG0073  122 ELGLGEDHDgILELPEDAPPG 142
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 157-254 1.12e-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: 93.07  E-value: 1.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 157 RLDIRVGKIITVEKHPDA-DSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 235
Cdd:cd02798    8 KVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGADD 87

                         90
                 ....*....|....*....
gi 767906539 236 EGinRQVEPLDPPAGSAPG 254
Cdd:cd02798   88 EG--GEVVLLVPDREVPNG 104
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 157-257 7.01e-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: 84.02  E-value: 7.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539  157 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 236
Cdd:TIGR00399  39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117

                          90       100
                  ....*....|....*....|.
gi 767906539  237 GINRQVepLDPPAGSAPGEHV 257
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
1-111 1.45e-16

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 78.47  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539    1 MNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGVLSFIKHVLFPlkseFVILRDEKWGGNKTY 79
Cdd:pfam00579 186 TNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRKDLKLFTFLSN----EEIEILEAELGKSPY 259

                          90       100       110
                  ....*....|....*....|....*....|..
gi 767906539   80 TAYVDLEKDFAAEVVHPGDLKNSVEVALNKLL 111
Cdd:pfam00579 260 REAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
PRK10089 PRK10089
chaperone CsaA;
157-233 2.72e-14

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 67.93  E-value: 2.72e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767906539 157 RLDIRVGKIITVEKHPDADSL-YVEKIDVG-EAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCA 233
Cdd:PRK10089  11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGF 89
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 160-236 2.84e-14

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


Pssm-ID: 239196 [Multi-domain]  Cd Length: 103  Bit Score: 67.53  E-value: 2.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 160 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------LKPQKMRGVESQGMlL 231
Cdd:cd02796    1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG----APNVRAGDKVVVALPGavlpgglkIKKRKLRGVESEGM-L 75


                 ....*
gi 767906539 232 CASIE 236
Cdd:cd02796   76 CSAKE 80
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 148-236 2.65e-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: 70.40  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539  148 SEPEEVIPSRLD---IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------L 216
Cdd:TIGR00472  31 LEVEAVIPFSKPlkgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCG----APNVEAGKKVAVALPGaklpnglkI 106

                          90       100
                  ....*....|....*....|
gi 767906539  217 KPQKMRGVESQGMlLCASIE 236
Cdd:TIGR00472 107 KKSKLRGVESEGM-LCSESE 125
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 151-236 7.99e-12

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 65.96  E-value: 7.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 151 EEVIPSRLDIR---VGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSG-----LVQFVPkeelqdrlvVVLCN------- 215
Cdd:PRK00629  33 EGVEDVAAGLSgvvVGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGapnvrAGDKVP---------VALPGavlpggf 102

                         90       100
                 ....*....|....*....|..
gi 767906539 216 -LKPQKMRGVESQGMlLCASIE 236
Cdd:PRK00629 103 kIKKAKLRGVESEGM-LCSASE 123
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 1-110 2.03e-08

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: 54.15  E-value: 2.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   1 MNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSFIKHVLFPLksefvilrdekwggnktY 79
Cdd:cd00805  184 TTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEFLKLFTFLD-----------------Y 239

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767906539  80 TAYVDLEKDFAAEvVHPGDLKNSVEVALNKL 110
Cdd:cd00805  240 EEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 148-238 1.20e-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: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539 148 SEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKeelqdrLVVVLC----------NLK 217
Cdd:COG0072   33 EEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVG------VVVVAApggavlpggfKIK 106

                         90       100
                 ....*....|....*....|.
gi 767906539 218 PQKMRGVESQGMLLCASIEGI 238
Cdd:COG0072  107 KAKIRGVESSGMLCSEEELGL 127
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 26-103 3.02e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 39.11  E-value: 3.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767906539  26 DRKEDVKKKLKKAFCEPgNVENNGVLSFIKHVLFPlKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSV 103
Cdd:PTZ00348 570 DNDMDIRRKIKKAYSAP-NEEANPVISVAQHLLAQ-QGALSIERGEANGGNVAYNTPEALVADCGSGALHPADLKAAV 645
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 4-118 4.73e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 38.73  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906539   4 MVPGLT--GSKMSSSEEESKIDLLDRKEDVKKKLKKAFC-----------EPG----NVENNGVLSFIKHVLFPLKSEFV 66
Cdd:PTZ00348 212 MLAGLKqgQAKMSKSDPDSAIFMEDTEEDVARKIRQAYCprvkqsaseitDDGapvaTDDRNPVLDYFQCVVYARPGAVA 291

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767906539  67 ILrdekwgGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPIREKF 118
Cdd:PTZ00348 292 TI------DGTTYATYEDLEQAFVSDEVSEEALKSCLIDEVNALLEPVRQHF 337
 
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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