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Conserved domains on  [gi|1257171103|ref|NP_001343894|]
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threonine--tRNA ligase, mitochondrial isoform 5 [Mus musculus]

Protein Classification

threonine--tRNA ligase family protein( domain architecture ID 1000183)

threonine--tRNA ligase family protein such as threonine--tRNA ligase ThrRS, also termed cytoplasmic threonine--tRNA ligase, a class II aminoacyl-tRNA synthetase (aaRS) that plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr), generating aminoacyl-tRNA, and editing misacylation, and such as the large ribosomal subunit protein mL39.

Gene Ontology:  GO:0000166

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PLN02908 super family cl31949
threonyl-tRNA synthetase
 3-476 0e+00

threonyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02908:

Pssm-ID: 178496 [Multi-domain]  Cd Length: 686  Bit Score: 663.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHE 82
Cdd:PLN02908  229 VDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  83 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdgvdnsqsghpar 162
Cdd:PLN02908  309 LSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFE----------------- 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 163 CPKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCL 242
Cdd:PLN02908  372 IEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 243 DFLRCVYSVLGFSFHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQCGT 322
Cdd:PLN02908  452 DFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCAT 531

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 323 IQLDFQLPLRFDLQYKGPAGT-PECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQC 401
Cdd:PLN02908  532 VQLDFQLPIRFKLSYSAEDEAkIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQ 611

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1257171103 402 LQAAGLVSDLDAdSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLELQNAR 476
Cdd:PLN02908  612 LHAAGFYVDVDV-TDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
 
Name Accession Description Interval E-value
PLN02908 PLN02908
threonyl-tRNA synthetase
 3-476 0e+00

threonyl-tRNA synthetase


Pssm-ID: 178496 [Multi-domain]  Cd Length: 686  Bit Score: 663.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHE 82
Cdd:PLN02908  229 VDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  83 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdgvdnsqsghpar 162
Cdd:PLN02908  309 LSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFE----------------- 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 163 CPKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCL 242
Cdd:PLN02908  372 IEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 243 DFLRCVYSVLGFSFHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQCGT 322
Cdd:PLN02908  452 DFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCAT 531

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 323 IQLDFQLPLRFDLQYKGPAGT-PECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQC 401
Cdd:PLN02908  532 VQLDFQLPIRFKLSYSAEDEAkIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQ 611

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1257171103 402 LQAAGLVSDLDAdSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLELQNAR 476
Cdd:PLN02908  612 LHAAGFYVDVDV-TDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 3-471 0e+00

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


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 624.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFH- 81
Cdd:COG0441   178 VDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQe 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  82 ELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgTDGVDnsqsghpa 161
Cdd:COG0441   258 EVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPTE---SDGEE-------- 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 162 rcpkdtLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGC 241
Cdd:COG0441   327 ------YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKV 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 242 LDFLRCVYSVLGFS-FHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQC 320
Cdd:COG0441   401 IDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQC 480

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 321 GTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQ 400
Cdd:COG0441   481 GTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAK 560

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1257171103 401 CLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLE 471
Cdd:COG0441   561 KLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
thrS TIGR00418
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ...
 3-469 0e+00

threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273068 [Multi-domain]  Cd Length: 563  Bit Score: 534.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHE 82
Cdd:TIGR00418 107 VDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEP 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  83 LS-PGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdGVDNSqsghpa 161
Cdd:TIGR00418 187 EIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHWDNYKERMFPFT-----ELDNR------ 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 162 rcpkdTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGC 241
Cdd:TIGR00418 256 -----EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQ 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 242 LDFLRCVYSVLGFSFHLA-LSTRPPG-FLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQ 319
Cdd:TIGR00418 331 FRLIQKVYSDFGFSFDKYeLSTRDPEdFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQ 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 320 CGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQ 399
Cdd:TIGR00418 411 CATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVA 490

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 400 QCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRL 469
Cdd:TIGR00418 491 QKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEKL 559
ThrRS_core cd00771
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ...
 66-379 1.07e-169

Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.


Pssm-ID: 238394 [Multi-domain]  Cd Length: 298  Bit Score: 479.74  E-value: 1.07e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  66 RDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 145
Cdd:cd00771     1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 146 PPgtdgvdnsqsghparcpKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDA 225
Cdd:cd00771    81 EE-----------------DEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 226 HIFCAPHQLEAEIQGCLDFLRCVYSVLGF-SFHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGP 304
Cdd:cd00771   144 HIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGP 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1257171103 305 KIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSP 379
Cdd:cd00771   224 KIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 165-368 3.72e-34

tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.


Pssm-ID: 395469 [Multi-domain]  Cd Length: 181  Bit Score: 126.76  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 165 KDTLALKPMNCPAHCLMFA-HRPRSWReLPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLD 243
Cdd:pfam00587   8 GDELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 244 FLRCVYSVLGFSFH-LALSTRPpgflgeprlwdqaeqvlqqalekfgepwdlnpgDGAFYGPKIDVHLHD-ALGRPHQCG 321
Cdd:pfam00587  87 LIDRVYSRLGLEVRvVRLSNSD---------------------------------GSAFYGPKLDFEVVFpSLGKQRQTG 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1257171103 322 TIQLD-FQLPLRFDLQYKGPAGTPECPVLIHRAVLGsVERLLGVLAES 368
Cdd:pfam00587 134 TIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILEN 180
tRNA_SAD smart00863
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ...
 2-42 2.83e-10

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 197931 [Multi-domain]  Cd Length: 43  Bit Score: 55.47  E-value: 2.83e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1257171103    2 SVDLCRGPHLRHTGQIGALKLLTNSSALWRslgapetLQRV 42
Cdd:smart00863  10 SVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
 
Name Accession Description Interval E-value
PLN02908 PLN02908
threonyl-tRNA synthetase
 3-476 0e+00

threonyl-tRNA synthetase


Pssm-ID: 178496 [Multi-domain]  Cd Length: 686  Bit Score: 663.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHE 82
Cdd:PLN02908  229 VDLCRGPHIPNTSFVKAFACLKASSAYWRGDVDRESLQRVYGISFPDKKLLKEYKHRIEEAKKRDHRLLGQKQELFFFHE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  83 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdgvdnsqsghpar 162
Cdd:PLN02908  309 LSPGSCFFLPHGARIYNKLMDFIREQYWERGYDEVITPNIYNMDLWETSGHAAHYKENMFVFE----------------- 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 163 CPKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCL 242
Cdd:PLN02908  372 IEKQEFGLKPMNCPGHCLMFAHRVRSYRELPLRLADFGVLHRNELSGALTGLTRVRRFQQDDAHIFCREDQIKDEVKGVL 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 243 DFLRCVYSVLGFSFHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQCGT 322
Cdd:PLN02908  452 DFLDYVYEVFGFTYELKLSTRPEKYLGDLETWDKAEAALTEALNAFGKPWQLNEGDGAFYGPKIDITVSDALKRKFQCAT 531

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 323 IQLDFQLPLRFDLQYKGPAGT-PECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQC 401
Cdd:PLN02908  532 VQLDFQLPIRFKLSYSAEDEAkIERPVMIHRAILGSVERMFAILLEHYAGKWPFWLSPRQAIVVPISEKSQDYAEEVRAQ 611

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1257171103 402 LQAAGLVSDLDAdSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLELQNAR 476
Cdd:PLN02908  612 LHAAGFYVDVDV-TDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEELLTEFKEERAEF 685
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 3-471 0e+00

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


Pssm-ID: 440210 [Multi-domain]  Cd Length: 639  Bit Score: 624.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFH- 81
Cdd:COG0441   178 VDLCRGPHVPSTGKIKAFKLLSVAGAYWRGDEKNKMLQRIYGTAFPKKKELDAYLHRLEEAKKRDHRKLGKELDLFHFQe 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  82 ELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgTDGVDnsqsghpa 161
Cdd:COG0441   258 EVGPGLPFWHPKGAIIRRELEDYIREKHRKAGYQEVKTPHILDRELWETSGHWDHYRENMFPTE---SDGEE-------- 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 162 rcpkdtLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGC 241
Cdd:COG0441   327 ------YALKPMNCPGHILIYKSGLRSYRDLPLRLAEFGTVHRYEPSGALHGLMRVRGFTQDDAHIFCTPDQIEDEIKKV 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 242 LDFLRCVYSVLGFS-FHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQC 320
Cdd:COG0441   401 IDLVLEVYKDFGFEdYYVKLSTRPEKRIGSDEIWDKAEAALREALEELGLEYVINPGEGAFYGPKIDFQLKDAIGREWQC 480

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 321 GTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQQ 400
Cdd:COG0441   481 GTIQLDFNLPERFDLTYVGEDGEKHRPVMIHRAILGSIERFIGILIEHYAGAFPLWLAPVQVVVLPISDKHADYAKEVAK 560

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1257171103 401 CLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLE 471
Cdd:COG0441   561 KLRAAGIRVEVD-LRNEKIGYKIREAQLQKVPYMLVVGDKEVENGTVSVRRRGGGDLGTMSLDEFIARLKE 630
thrS TIGR00418
threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most ...
 3-469 0e+00

threonyl-tRNA synthetase; This model represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. . [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273068 [Multi-domain]  Cd Length: 563  Bit Score: 534.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHE 82
Cdd:TIGR00418 107 VDLCKGPHLPNTSFIKAFKLEKVAGAYWRGDSKNKMLQRIYGTAWADKKQLAAYLLRLEEAKKRDHRKLGKELELFSFEP 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  83 LS-PGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKppgtdGVDNSqsghpa 161
Cdd:TIGR00418 187 EIgPGLPFWLPKGATIRNLLEDFVRQKQIKYGYMEVETPIMYDLELWEISGHWDNYKERMFPFT-----ELDNR------ 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 162 rcpkdTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGC 241
Cdd:TIGR00418 256 -----EFMLKPMNCPGHFLIFKSSLRSYRDLPLRIAELGYSHRYEQSGELHGLMRVRGFTQDDAHIFCTEDQIKEEFKNQ 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 242 LDFLRCVYSVLGFSFHLA-LSTRPPG-FLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQ 319
Cdd:TIGR00418 331 FRLIQKVYSDFGFSFDKYeLSTRDPEdFIGEDELWEKAEAALEEALKELGVPYEIDPGRGAFYGPKIDFAFKDALGREWQ 410

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 320 CGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQ 399
Cdd:TIGR00418 411 CATVQLDFELPERFDLTYVDEDNEEKRPVMIHRAILGSIERFIAILLEKYAGNFPLWLAPVQVVVIPVNERHLDYAKKVA 490

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 400 QCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRL 469
Cdd:TIGR00418 491 QKLKKAGIRVDVD-DRNERLGKKIREAQKQKIPYMLVVGDKEMESLAVNVRTRKGQKLEKMSLDEFLEKL 559
ThrRS_core cd00771
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ...
 66-379 1.07e-169

Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.


Pssm-ID: 238394 [Multi-domain]  Cd Length: 298  Bit Score: 479.74  E-value: 1.07e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  66 RDHRRIGKEQELFFFHELSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 145
Cdd:cd00771     1 DHRRLGGELELFFFFDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFPFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 146 PPgtdgvdnsqsghparcpKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDA 225
Cdd:cd00771    81 EE-----------------DEEYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQSGALHGLTRVRGFTQDDA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 226 HIFCAPHQLEAEIQGCLDFLRCVYSVLGF-SFHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGP 304
Cdd:cd00771   144 HIFCTPDQIKEEIKGVLDLIKEVYSDFGFfDYKVELSTRPEKFIGSDEVWEKAEAALREALEEIGLPYEINEGEGAFYGP 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1257171103 305 KIDVHLHDALGRPHQCGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSP 379
Cdd:cd00771   224 KIDFHVKDALGREWQCSTIQLDFNLPERFDLTYIGEDGEKKRPVMIHRAILGSIERFIGILIEHYAGKFPLWLAP 298
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
 3-476 2.36e-159

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 466.15  E-value: 2.36e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   3 VDLCRGPHLRHTGQIGALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFHE 82
Cdd:PRK12444  182 VDLCRGPHLPSTGYLKAFQLTHVSGAYWRGDSNNQVLQRIYGVAFSSQKELEEYLHFVEEAAKRNHRKLGKELELFMFSE 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  83 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADM-FSlkppgtdGVDNSqsghpa 161
Cdd:PRK12444  262 EAPGMPFYLPKGQIIRNELEAFLREIQKEYNYQEVRTPFMMNQELWERSGHWDHYKDNMyFS-------EVDNK------ 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 162 rcpkdTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGC 241
Cdd:PRK12444  329 -----SFALKPMNCPGHMLMFKNKLHSYRELPIRMCEFGQVHRHEFSGALNGLLRVRTFCQDDAHLFVTPDQIEDEIKSV 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 242 LDFLRCVYSVLGFSFHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQCG 321
Cdd:PRK12444  404 MAQIDYVYKTFGFEYEVELSTRPEDSMGDDELWEQAEASLENVLQSLNYKYRLNEGDGAFYGPKIDFHIKDALNRSHQCG 483

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 322 TIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTE-QEEYARQVQQ 400
Cdd:PRK12444  484 TIQLDFQMPEKFDLNYIDEKNEKRRPVVIHRAVLGSLDRFLAILIEHFGGAFPAWLAPVQVKVIPVSNAvHVQYADEVAD 563

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1257171103 401 CLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRLLELQNAR 476
Cdd:PRK12444  564 KLAQAGIRVERD-ERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDMFVESIKEEIKNR 638
PLN02837 PLN02837
threonine-tRNA ligase
 4-469 3.21e-114

threonine-tRNA ligase


Pssm-ID: 215450 [Multi-domain]  Cd Length: 614  Bit Score: 349.58  E-value: 3.21e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103   4 DLCRGPHLRHTGQIG--ALKLLTNSSALWRSLGAPETLQRVSGISFPKVELLRNWEARREAAELRDHRRIGKEQELFFFH 81
Cdd:PLN02837  153 DLCAGPHVERTGKINkkAVELESVAGAYWRGDEKNQMLQRIYGTAWESEEQLKAYLHFKEEAKRRDHRRLGQDLDLFSIQ 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  82 ELSPGS-CFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSlkppgtdgvdnsqsghP 160
Cdd:PLN02837  233 DDAGGGlVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYD----------------Q 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 161 ARCPKDTLALKPMNCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQG 240
Cdd:PLN02837  297 MDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHGLFRVRGFTQDDAHIFCLEDQIKDEIRG 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 241 CLDFLRCVYSVLGFS-FHLALSTRPPGFLGEPRLWDQAEQVLQQALEKFGEPWDLNPGDGAFYGPKIDVHLHDALGRPHQ 319
Cdd:PLN02837  377 VLDLTEEILKQFGFSkYEINLSTRPEKSVGSDDIWEKATTALRDALDDKGWEYKVDEGGGAFYGPKIDLKIEDALGRKWQ 456

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 320 CGTIQLDFQLPLRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAESCGGKWPLWLSPLQVVVIPVRTEQEEYARQVQ 399
Cdd:PLN02837  457 CSTIQVDFNLPERFDITYVDSNSEKKRPIMIHRAILGSLERFFGVLIEHYAGDFPLWLAPVQARVLPVTDNELEYCKEVV 536

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 400 QCLQAAGLVSDLdaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLGERDLAESVQRL 469
Cdd:PLN02837  537 AKLKAKGIRAEV--CHGERLPKLIRNAETQKIPLMAVVGPKEVETRTLTVRSRHGGELGTMPVDDFINRI 604
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 165-368 3.72e-34

tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.


Pssm-ID: 395469 [Multi-domain]  Cd Length: 181  Bit Score: 126.76  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 165 KDTLALKPMNCPAHCLMFA-HRPRSWReLPVRLADFGALHRAEASGSLGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLD 243
Cdd:pfam00587   8 GDELALKPTNEPGHTLLFReEGLRSKD-LPLKLAQFGTCFRHEASGDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 244 FLRCVYSVLGFSFH-LALSTRPpgflgeprlwdqaeqvlqqalekfgepwdlnpgDGAFYGPKIDVHLHD-ALGRPHQCG 321
Cdd:pfam00587  87 LIDRVYSRLGLEVRvVRLSNSD---------------------------------GSAFYGPKLDFEVVFpSLGKQRQTG 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1257171103 322 TIQLD-FQLPLRFDLQYKGPAGTPECPVLIHRAVLGsVERLLGVLAES 368
Cdd:pfam00587 134 TIQNDgFRLPRRLGIRYKDEDNESKFPYMIHRAGLG-VERFLAAILEN 180
PRK03991 PRK03991
threonyl-tRNA synthetase; Validated
 188-471 4.87e-31

threonyl-tRNA synthetase; Validated


Pssm-ID: 235190 [Multi-domain]  Cd Length: 613  Bit Score: 126.52  E-value: 4.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 188 SWRELPVR---LADFGalHRAEASGSLGGLTRLWRFQQDDAHIFC-----APHQLEAEIQGCLDFLRCV---YSVLgFSF 256
Cdd:PRK03991  303 SYKNLPLKmyeLSTYS--FRLEQRGELVGLKRLRAFTMPDMHTLCkdmeqAMEEFEKQYEMILETGEDLgrdYEVA-IRF 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 257 hlalsTRppGFlgeprlWDQAEQVLQQALEKFGEP-----WDlnpgDGAFYGP-KIDVHLHDALGRPHQCGTIQLDFQLP 330
Cdd:PRK03991  380 -----TE--DF------YEENKDWIVELVKREGKPvlleiLP----ERKHYWVlKVEFAFIDSLGRPIENPTVQIDVENA 442

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 331 LRFDLQYKGPAGTPECPVLIHRAVLGSVERLLGVLAE-----SCGGK---WPLWLSPLQVVVIPVRTEQEEYARQVQQCL 402
Cdd:PRK03991  443 ERFGIKYVDENGEEKYPIILHCSPTGSIERVIYALLEkaakeEEEGKvpmLPTWLSPTQVRVIPVSERHLDYAEEVADKL 522

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 403 QAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTR-DNRQLgERDLAESVQRLLE 471
Cdd:PRK03991  523 EAAGIRVDVD-DRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIReESEKV-EMTLEELIERIKE 590
Gly_His_Pro_Ser_Thr_tRS_core cd00670
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ...
 94-365 6.67e-27

Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238359 [Multi-domain]  Cd Length: 235  Bit Score: 108.25  E-value: 6.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  94 GTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLKPPGTDGVDNSqsghparcpkdtLALKPM 173
Cdd:cd00670     1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRELRDTD------------LVLRPA 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 174 NCPAHCLMFAHRPRSWRELPVRLADFGALHRAEASGSlGGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLG 253
Cdd:cd00670    69 ACEPIYQIFSGEILSYRALPLRLDQIGPCFRHEPSGR-RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 254 FSFHLALSTRPpgFLGEPRlwdqaeqvlqqalekfgepwdlNPGDGAFYGPKIDVHLHDAL-GRPHQCGTIQLDFQLPLR 332
Cdd:cd00670   148 LPVRVVVADDP--FFGRGG----------------------KRGLDAGRETVVEFELLLPLpGRAKETAVGSANVHLDHF 203

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1257171103 333 FDLQYKGPAGTPECPVLIHRAvlGSVERLLGVL 365
Cdd:cd00670   204 GASFKIDEDGGGRAHTGCGGA--GGEERLVLAL 234
ThrRS_anticodon cd00860
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ...
 379-470 1.11e-26

ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238437 [Multi-domain]  Cd Length: 91  Bit Score: 102.97  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 379 PLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQLG 458
Cdd:cd00860     1 PVQVVVIPVTDEHLDYAKEVAKKLSDAGIRVEVD-LRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLG 79

                          90
                  ....*....|..
gi 1257171103 459 ERDLAESVQRLL 470
Cdd:cd00860    80 SMSLDEFIEKLK 91
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 381-472 8.11e-19

Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.


Pssm-ID: 460819 [Multi-domain]  Cd Length: 94  Bit Score: 81.09  E-value: 8.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 381 QVVVIPV---RTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNRQL 457
Cdd:pfam03129   1 QVVVIPLgekAEELEEYAQKLAEELRAAGIRVELD-DRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79

                          90
                  ....*....|....*
gi 1257171103 458 GERDLAESVQRLLEL 472
Cdd:pfam03129  80 ETVSLDELVEKLKEL 94
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 99-361 2.89e-12

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 65.99  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103  99 NALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRAdmfslkpPGTDGVDNSqsghparcpkdtLALKPMNCPAH 178
Cdd:cd00768     3 SKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLL-------PVGAENEED------------LYLRPTLEPGL 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 179 CLMFAHRPRSwreLPVRLADFGALHRAEASGSlgGLTRLWRFQQDDAHIFCAPHQLEAEIQGCLDFLRCVYSVLGfsfhl 258
Cdd:cd00768    64 VRLFVSHIRK---LPLRLAEIGPAFRNEGGRR--GLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALG----- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 259 alstrppgfLGEPRLWdqaeqVLQQAlekfGEPWDlnpgdgAFYGPKIDVHLHDALGRPHQCGTIQLDFQLPLR-FDLQY 337
Cdd:cd00768   134 ---------IKLDIVF-----VEKTP----GEFSP------GGAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARaADLYF 189

                         250       260
                  ....*....|....*....|....
gi 1257171103 338 KGPAGTPECPVLIHRAvlGSVERL 361
Cdd:cd00768   190 LDEALEYRYPPTIGFG--LGLERL 211
tRNA_SAD smart00863
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ...
 2-42 2.83e-10

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 197931 [Multi-domain]  Cd Length: 43  Bit Score: 55.47  E-value: 2.83e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1257171103    2 SVDLCRGPHLRHTGQIGALKLLTNSSALWRslgapetLQRV 42
Cdd:smart00863  10 SVELCGGTHVPNTGEIGAFKILSVSGAYWG-------LQRI 43
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 83-145 2.24e-08

Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.


Pssm-ID: 238402 [Multi-domain]  Cd Length: 255  Bit Score: 54.89  E-value: 2.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1257171103  83 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 145
Cdd:cd00779    19 TSSGLYSWLPLGLRVLKKIENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLK 81
PRK14938 PRK14938
Ser-tRNA(Thr) hydrolase; Provisional
 374-474 1.70e-07

Ser-tRNA(Thr) hydrolase; Provisional


Pssm-ID: 184902 [Multi-domain]  Cd Length: 387  Bit Score: 53.31  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 374 PLWLSPLQVVVIPVRTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRD 453
Cdd:PRK14938  269 PDWLNPIQVRILPVKKDFLDFSIQVAERLRKEGIRVNVD-DLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRA 347

                          90       100
                  ....*....|....*....|....*..
gi 1257171103 454 N---RQLGERDLAESVQR---LLELQN 474
Cdd:PRK14938  348 NneqKSMTVEELVKEIKRadeLKERSN 374
tRNA_SAD pfam07973
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ...
 2-27 3.54e-07

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 429764 [Multi-domain]  Cd Length: 43  Bit Score: 46.67  E-value: 3.54e-07
                          10        20
                  ....*....|....*....|....*.
gi 1257171103   2 SVDLCRGPHLRHTGQIGALKLLTNSS 27
Cdd:pfam07973  10 DVDLCGGTHVPNTGEIGAFKILKGES 35
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
 379-470 6.83e-06

HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).


Pssm-ID: 238379 [Multi-domain]  Cd Length: 94  Bit Score: 44.31  E-value: 6.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 379 PLQVVVIPV---RTEQEEYARQVQQCLQAAGLVSDLDaDSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRTRDNR 455
Cdd:cd00738     1 PIDVAIVPLtdpRVEAREYAQKLLNALLANGIRVLYD-DRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79

                          90
                  ....*....|....*
gi 1257171103 456 QLGERDLAESVQRLL 470
Cdd:cd00738    80 ESETLHVDELPEFLV 94
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
 90-145 1.40e-05

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


Pssm-ID: 440211 [Multi-domain]  Cd Length: 564  Bit Score: 47.46  E-value: 1.40e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1257171103  90 FLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 145
Cdd:COG0442    42 YLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAELWEESGRWEGFGPELARVT 97
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 83-145 6.06e-05

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 45.46  E-value: 6.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1257171103  83 LSPGSCFFLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 145
Cdd:PRK09194   35 LASGIYTYLPLGLRVLRKIENIVREEMNKIGAQEVLMPALQPAELWQESGRWEEYGPELLRLK 97
PRK12325 PRK12325
prolyl-tRNA synthetase; Provisional
 90-145 2.08e-04

prolyl-tRNA synthetase; Provisional


Pssm-ID: 237059 [Multi-domain]  Cd Length: 439  Bit Score: 43.69  E-value: 2.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1257171103  90 FLPRGTRVYNALVAFIRAEYARRGFSEVKTPTLFSTKLWEQSGHWEHYRADMFSLK 145
Cdd:PRK12325   42 WLPLGLKVLKKIENIVREEQNRAGAIEILMPTIQPADLWRESGRYDAYGKEMLRIK 97
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
 378-484 7.90e-04

ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.


Pssm-ID: 238439 [Multi-domain]  Cd Length: 202  Bit Score: 40.74  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1257171103 378 SPLQVVVIPV------RTEQEEYARQVQQCLQAAGLVSDLDADSGLTLSRRVRRAQLAHYNFQFVVGQREQSQRTVNVRT 451
Cdd:cd00862     9 APIQVVIVPIgikdekREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDLEKNTVVIVR 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1257171103 452 RDNR---QLGERDLAESVQRLLEL-QNARVPNAEEVF 484
Cdd:cd00862    89 RDTGekkTVPLAELVEKVPELLDEiQEDLYERALEFR 125
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
 374-426 4.70e-03

GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238435 [Multi-domain]  Cd Length: 121  Bit Score: 37.15  E-value: 4.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1257171103 374 PLWLSPLQVVVIPV--RTEQEEYARQVQQCLQAAGLVSDLDaDSGlTLSRRVRRA 426
Cdd:cd00858    21 PPALAPIKVAVLPLvkRDELVEIAKEISEELRELGFSVKYD-DSG-SIGRRYARQ 73
 
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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