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Conserved domains on  [gi|24649468|ref|NP_732925|]
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Glutamyl-prolyl-tRNA synthetase, isoform B [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
proS_fam_I super family cl36641
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
 501-996 0e+00

prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]


The actual alignment was detected with superfamily member TIGR00408:

Pssm-ID: 273062 [Multi-domain]  Cd Length: 472  Bit Score: 575.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   501 ATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADF 580
Cdd:TIGR00408   2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   581 APEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFA 660
Cdd:TIGR00408  82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   661 DKEEAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIVYE 740
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   741 DPeTQQKKYVYQNSWGITTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPcgitVNTKDDERAQLLDACKALEKRLVGGG 820
Cdd:TIGR00408 241 TP-TGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIP----IIFKKKENEKVMEAAREVRSRLKKAG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   821 VRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLETIHESMLNKAQE 900
Cdd:TIGR00408 316 FRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWE 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   901 DMTSHTKKVTNWTDFCGFLEQKN-ILLAPFCGEISCEDKIKADSArgeeaepgapamgAKSLCIPFDQPAPiaasDKCIN 979
Cdd:TIGR00408 395 RFEQKIVIVETLEEIKQALNEKRgVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDGDVL----QLCIF 457

                         490
                  ....*....|....*..
gi 24649468   980 psCTNKPKFYTLFGRSY 996
Cdd:TIGR00408 458 --CGRKAPDYVLIARTY 472
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 30-79 1.51e-20

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


:

Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 85.75  E-value: 1.51e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468  30 LDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPG 79
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 176-225 1.86e-19

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


:

Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 82.67  E-value: 1.86e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 176 ILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPG 225
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
103-152 5.91e-19

WHEP-TRS domain;


:

Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 81.00  E-value: 5.91e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 24649468   103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGT 152
Cdd:pfam00458   2 TEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGA 51
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 255-304 3.35e-17

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


:

Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 76.12  E-value: 3.35e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 255 LLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPG 304
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 330-379 1.39e-16

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


:

Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 74.19  E-value: 1.39e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 330 VLSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPD 379
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 404-451 1.66e-15

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


:

Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 71.11  E-value: 1.66e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24649468 404 LTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFP 451
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYK 48
 
Name Accession Description Interval E-value
proS_fam_I TIGR00408
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
 501-996 0e+00

prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273062 [Multi-domain]  Cd Length: 472  Bit Score: 575.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   501 ATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADF 580
Cdd:TIGR00408   2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   581 APEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFA 660
Cdd:TIGR00408  82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   661 DKEEAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIVYE 740
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   741 DPeTQQKKYVYQNSWGITTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPcgitVNTKDDERAQLLDACKALEKRLVGGG 820
Cdd:TIGR00408 241 TP-TGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIP----IIFKKKENEKVMEAAREVRSRLKKAG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   821 VRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLETIHESMLNKAQE 900
Cdd:TIGR00408 316 FRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWE 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   901 DMTSHTKKVTNWTDFCGFLEQKN-ILLAPFCGEISCEDKIKADSArgeeaepgapamgAKSLCIPFDQPAPiaasDKCIN 979
Cdd:TIGR00408 395 RFEQKIVIVETLEEIKQALNEKRgVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDGDVL----QLCIF 457

                         490
                  ....*....|....*..
gi 24649468   980 psCTNKPKFYTLFGRSY 996
Cdd:TIGR00408 458 --CGRKAPDYVLIARTY 472
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 506-768 2.14e-171

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 archaea, the cytoplasm of eukaryotes and some bacteria.


Pssm-ID: 238401 [Multi-domain]  Cd Length: 261  Bit Score: 500.20  E-value: 2.14e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 506 NLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADFAPEVA 585
Cdd:cd00778   1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 586 WVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKEEA 665
Cdd:cd00778  81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 666 AKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIVYEDPEtQ 745
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-G 238

                       250       260
                ....*....|....*....|...
gi 24649468 746 QKKYVYQNSWGITTRTIGVMIMV 768
Cdd:cd00778 239 QKEYVHQTSWGISTRLIGAIIMI 261
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
 493-887 9.35e-90

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: 297.84  E-value: 9.35e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 493 KQTRLGLEATKEDnlPD----WYSQVITKGEMIEYYdVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKA 568
Cdd:COG0442   2 RASKLFIPTLKER--PAdaevWSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 569 VLEKEKtHIADFAPEVAWVTksgdsD-LAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRT 647
Cdd:COG0442  79 LWEESG-RWEGFGPELARVT-----DrLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRT 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 648 REFLWQEGHTAFADKEEAAKEVLDILDLYALVYTHlLAIPVVKGRKT-------EKEKFA--------------GGDYTT 706
Cdd:COG0442 153 REFLMKDAYSFHATEEELDEEYQKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYAA 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 707 TVEA---------------------------------------------------------------------------- 710
Cdd:COG0442 232 NIEKaealappaeraeptkeleavatpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllga 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 711 --------------------FISASG------------------------------------------------------ 716
Cdd:COG0442 312 selelateeeieaalgavpgFLGPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpc 391

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 717 ----------RAIQGATSHHLGQNFSKMFEIVYEDpETQQKKYVYQNSWGIT-TRTIGVMIMVHADNQGLVLPPHVACIQ 785
Cdd:COG0442 392 pdcggllqdgRGIEVGHIFKLGTKYSKAMDATFLD-ENGKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQ 470

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 786 AIVVPcgitVNTKDDEraqLLDACKALEKRLVGGGVRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVR 865
Cdd:COG0442 471 VVIVP----INMKDEA---VLEAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKR 542

                       570       580
                ....*....|....*....|..
gi 24649468 866 RDTVEKITIPLADVEKKIPALL 887
Cdd:COG0442 543 RDTGEKEEVPLDELVETVKELL 564
ProRS-C_1 pfam09180
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 912-996 2.42e-23

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 462709  Cd Length: 67  Bit Score: 94.12  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   912 WTDFCGFLEQKNILLAPFCGEISCEDKIKADSargeeaepgapamGAKSLCIPFDQPapiAASDKCINpsCTNKPKFYTL 991
Cdd:pfam09180   1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFDQE---EEGGKCIV--CGKPAKKWVL 62


                  ....*
gi 24649468   992 FGRSY 996
Cdd:pfam09180  63 FARSY 67
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 30-79 1.51e-20

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 85.75  E-value: 1.51e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468  30 LDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPG 79
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
30-81 1.54e-19

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 82.93  E-value: 1.54e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24649468    30 LDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPGQT 81
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAA 52
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 176-225 1.86e-19

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 82.67  E-value: 1.86e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 176 ILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPG 225
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
103-152 5.91e-19

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 81.00  E-value: 5.91e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 24649468   103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGT 152
Cdd:pfam00458   2 TEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGA 51
WHEP-TRS pfam00458
WHEP-TRS domain;
176-227 7.18e-19

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 81.00  E-value: 7.18e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24649468   176 ILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGTT 227
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAA 52
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 102-151 7.94e-19

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 80.74  E-value: 7.94e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 102 VNASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPG 151
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
ProRS-C_1 smart00946
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 912-996 2.19e-18

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 198014  Cd Length: 67  Bit Score: 79.92  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468    912 WTDFCGFLEQKNILLAPFCGEISCEDKIKADSargeeaepgapamGAKSLCIPFDQPAPiaaSDKCINpsCTNKPKFYTL 991
Cdd:smart00946   1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFDQDEE---PGKCVV--CGKPAKKWVL 62


                   ....*
gi 24649468    992 FGRSY 996
Cdd:smart00946  63 FARSY 67
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 255-304 3.35e-17

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 76.12  E-value: 3.35e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 255 LLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPG 304
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 330-379 1.39e-16

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 74.19  E-value: 1.39e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 330 VLSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPD 379
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
255-307 2.09e-16

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 74.07  E-value: 2.09e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24649468   255 LLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPGTVA 307
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
WHEP-TRS pfam00458
WHEP-TRS domain;
332-382 2.80e-16

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 73.68  E-value: 2.80e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24649468   332 SKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPDAKS 382
Cdd:pfam00458   3 EKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 103-153 8.53e-16

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 72.37  E-value: 8.53e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24649468    103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGTV 153
Cdd:smart00991   1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAP 51
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 404-451 1.66e-15

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 71.11  E-value: 1.66e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24649468 404 LTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFP 451
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYK 48
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 32-80 1.77e-15

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 71.22  E-value: 1.77e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24649468     32 SQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPGQ 80
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGA 50
WHEP-TRS pfam00458
WHEP-TRS domain;
404-451 4.97e-15

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 69.83  E-value: 4.97e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 24649468   404 LTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFP 451
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYK 48
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 178-226 8.21e-15

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 69.68  E-value: 8.21e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24649468    178 SQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGT 226
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGA 50
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 257-310 1.27e-13

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 66.21  E-value: 1.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24649468    257 NKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPGTVAPAP 310
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 332-382 2.60e-13

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 65.44  E-value: 2.60e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24649468    332 SKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPDAKS 382
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPP 52
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 727-883 3.29e-13

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 73.58  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  727 LGQNFSKMFEIVYEDpETQQKKYVYQNSWGI-TTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPcgitVNTKDDEraqL 805
Cdd:PRK09194 412 LGTKYSEAMNATVLD-ENGKAQPLIMGCYGIgVSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVP----VNMKDEE---V 483

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649468  806 LDACKALEKRLVGGGVRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKI 883
Cdd:PRK09194 484 KELAEKLYAELQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 406-450 1.67e-11

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 60.05  E-value: 1.67e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 24649468    406 QEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDF 450
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDY 46
PLN02734 PLN02734
glycyl-tRNA synthetase
 171-220 6.28e-06

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 50.13  E-value: 6.28e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649468  171 DSVAQILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLK-------ADYKAATGS 220
Cdd:PLN02734   7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKleksaleKELQAAVGA 63
PLN02734 PLN02734
glycyl-tRNA synthetase
 103-137 2.00e-05

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 48.59  E-value: 2.00e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 24649468  103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELK 137
Cdd:PLN02734  13 QAAVTAQGNAVRALKASKADKAEIDAAIEKLKALK 47
PLN02734 PLN02734
glycyl-tRNA synthetase
 28-75 3.77e-05

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 47.82  E-value: 3.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24649468   28 SELDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADyKSATGKD 75
Cdd:PLN02734  10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKE 56
PLN02734 PLN02734
glycyl-tRNA synthetase
 402-439 6.45e-04

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 43.58  E-value: 6.45e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 24649468  402 DELTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALK 439
Cdd:PLN02734  10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALK 47
 
Name Accession Description Interval E-value
proS_fam_I TIGR00408
prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is ...
 501-996 0e+00

prolyl-tRNA synthetase, family I; Prolyl-tRNA synthetase is a class II tRNA synthetase and is recognized by pfam model tRNA-synt_2b, which recognizes tRNA synthetases for Gly, His, Ser, and Pro. The prolyl-tRNA synthetases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human multifunctional tRNA ligase, and the enzyme from the spirochete Borrelia burgdorferi. The other family includes enzymes from Escherichia coli, Bacillus subtilis, Synechocystis PCC6803, and one of the two prolyL-tRNA synthetases of Saccharomyces cerevisiae. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273062 [Multi-domain]  Cd Length: 472  Bit Score: 575.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   501 ATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADF 580
Cdd:TIGR00408   2 ASKMQDFSEWYHQILEKAEIIDYYPVKGCYVWLPYGFKIWKNIQKILRNILDEIGHEEVYFPMLIPESELAKEKDHIKGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   581 APEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFA 660
Cdd:TIGR00408  82 EPEVYWITHGGLSKLDEPLALRPTSETAMYPMFKKWVKSYTDLPLKINQWVNVFRYETKHTRPFLRTREFTWQEAHTAHA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   661 DKEEAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIVYE 740
Cdd:TIGR00408 162 TAEEAEEQVLRALDIYKEFIENSLAIPYFVGRKPEWEKFAGAEYTWAFETIMP-DGRTLQIATSHNLGQNFAKTFEIKFE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   741 DPeTQQKKYVYQNSWGITTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPcgitVNTKDDERAQLLDACKALEKRLVGGG 820
Cdd:TIGR00408 241 TP-TGDKEYAYQTSYGISTRVIGALIAIHSDEKGLVLPPRVAPIQVVIIP----IIFKKKENEKVMEAAREVRSRLKKAG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   821 VRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLETIHESMLNKAQE 900
Cdd:TIGR00408 316 FRVHIDDRDN-RPGRKFYQWEIKGIPLRIEVGPNDIEKNIAVISRRDTGEKYQVSLDQLEERVVELLNNIQENLRNRAWE 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   901 DMTSHTKKVTNWTDFCGFLEQKN-ILLAPFCGEISCEDKIKADSArgeeaepgapamgAKSLCIPFDQPAPiaasDKCIN 979
Cdd:TIGR00408 395 RFEQKIVIVETLEEIKQALNEKRgVVLVPWCGEEECEEDLKEKVQ-------------VTILCIPEDGDVL----QLCIF 457

                         490
                  ....*....|....*..
gi 24649468   980 psCTNKPKFYTLFGRSY 996
Cdd:TIGR00408 458 --CGRKAPDYVLIARTY 472
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 506-768 2.14e-171

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 archaea, the cytoplasm of eukaryotes and some bacteria.


Pssm-ID: 238401 [Multi-domain]  Cd Length: 261  Bit Score: 500.20  E-value: 2.14e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 506 NLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADFAPEVA 585
Cdd:cd00778   1 DFSEWYTEVITKAELIDYGPVKGCMVFRPYGYAIWENIQKILDKEIKETGHENVYFPLLIPESELEKEKEHIEGFAPEVA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 586 WVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKEEA 665
Cdd:cd00778  81 WVTHGGLEELEEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWETKTTRPFLRTREFLWQEGHTAHATEEEA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 666 AKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISaSGRAIQGATSHHLGQNFSKMFEIVYEDPEtQ 745
Cdd:cd00778 161 EEEVLQILDLYKEFYEDLLAIPVVKGRKTEWEKFAGADYTYTIEAMMP-DGRALQSGTSHNLGQNFSKAFDIKYQDKD-G 238

                       250       260
                ....*....|....*....|...
gi 24649468 746 QKKYVYQNSWGITTRTIGVMIMV 768
Cdd:cd00778 239 QKEYVHQTSWGISTRLIGAIIMI 261
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
 774-996 6.57e-91

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: 288.04  E-value: 6.57e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 774 GLVLPPHVACIQAIVVPCGItvntKDDERAQLLDACKALEKRLVGGGVRCEGDYRDNYSPGWKFNHWELKGVPLRLEVGP 853
Cdd:cd00862   1 GLVLPPRVAPIQVVIVPIGI----KDEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 854 KDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLETIHESMLNKAQEDMTShTKKVTNWTDFCGFLEQKNILLAPFCGEI 933
Cdd:cd00862  77 RDLEKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDA-TRIVDTWEEFKEALNEKGIVLAPWCGEE 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24649468 934 SCEDKIKADSArgeeaepgapamgAKSLCIPFDQPApIAASDKCINpsCTNKPKFYTLFGRSY 996
Cdd:cd00862 156 ECEEEIKEETA-------------ATILCIPFDEAK-LEEGGKCVV--CGRPAKAYARFAKSY 202
ProS COG0442
Prolyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Prolyl-tRNA ...
 493-887 9.35e-90

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: 297.84  E-value: 9.35e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 493 KQTRLGLEATKEDnlPD----WYSQVITKGEMIEYYdVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKA 568
Cdd:COG0442   2 RASKLFIPTLKER--PAdaevWSHQLMLRAGLIRKL-ASGIYTYLPLGYRVLEKIEAIVREEMKRTGAQEVLMPLLQPAE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 569 VLEKEKtHIADFAPEVAWVTksgdsD-LAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRT 647
Cdd:COG0442  79 LWEESG-RWEGFGPELARVT-----DrLEREFCLGPTHEEVITDLVRNEIKSYRDLPLLLYQIQTKFRDEIRPRFGLLRT 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 648 REFLWQEGHTAFADKEEAAKEVLDILDLYALVYTHlLAIPVVKGRKT-------EKEKFA--------------GGDYTT 706
Cdd:COG0442 153 REFLMKDAYSFHATEEELDEEYQKMLDAYERIFER-LGLPVRAVEADsgaiggsESHEFMvladsgedtivycdACDYAA 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 707 TVEA---------------------------------------------------------------------------- 710
Cdd:COG0442 232 NIEKaealappaeraeptkeleavatpgaktieevaeflgvpaektvktlvykadgelvavlvrgdhelneiklenllga 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 711 --------------------FISASG------------------------------------------------------ 716
Cdd:COG0442 312 selelateeeieaalgavpgFLGPVGlgvpyiadrsvagmsnfvcganeddyhytnvnwgrdfpvdevadlrnvvegdpc 391

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 717 ----------RAIQGATSHHLGQNFSKMFEIVYEDpETQQKKYVYQNSWGIT-TRTIGVMIMVHADNQGLVLPPHVACIQ 785
Cdd:COG0442 392 pdcggllqdgRGIEVGHIFKLGTKYSKAMDATFLD-ENGKEQPVWMGCYGIGvTRLIAAAIEQHHDDKGIIWPPAIAPFQ 470

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 786 AIVVPcgitVNTKDDEraqLLDACKALEKRLVGGGVRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVR 865
Cdd:COG0442 471 VVIVP----INMKDEA---VLEAAEELYAELKAAGIDVLLDDRDE-RPGVKFADAELIGIPLRIVIGPRDLEEGQVEVKR 542

                       570       580
                ....*....|....*....|..
gi 24649468 866 RDTVEKITIPLADVEKKIPALL 887
Cdd:COG0442 543 RDTGEKEEVPLDELVETVKELL 564
ProRS_core cd00772
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 510-767 1.34e-70

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.


Pssm-ID: 238395 [Multi-domain]  Cd Length: 264  Bit Score: 235.34  E-value: 1.34e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 510 WYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADFAPEVAWVTK 589
Cdd:cd00772   5 KSLEHIGKAELADQGPGRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVFKD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 590 SGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKEEAAKEV 669
Cdd:cd00772  85 AGDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEIRPRFGFLRAREFIMKDGHSAHADAEEADEEF 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 670 LDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAfISASGRAIQGATSHHLGQNFSKMFE--IVYEDPETQQk 747
Cdd:cd00772 165 LNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREFEA-LMEDGKAKQAETGHIFGEGFARAFDlkAKFLDKDGKE- 242

                       250       260
                ....*....|....*....|.
gi 24649468 748 KYVYQNSWGIT-TRTIGVMIM 767
Cdd:cd00772 243 KFFEMGCWGIGiSRFIGAIIE 263
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 ...
 538-766 6.12e-31

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: 121.73  E-value: 6.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 538 AIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKtHIADFAPEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWV 617
Cdd:cd00670   3 ALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG-HLDGYRKEMYTFEDKGRELRDTDLVLRPAACEPIYQIFSGEI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 618 QSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTaFADKEEAAKEVLDILDLYALVYtHLLAIPVVKGRKTEKE 697
Cdd:cd00670  82 LSYRALPLRLDQIGPCFRHEPSGRRGLMRVREFRQVEYVV-FGEPEEAEEERREWLELAEEIA-RELGLPVRVVVADDPF 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649468 698 KFAGGD--------YTTTVEAFISASGRAIQGATSHHLGQNFSKMFEIvyEDPETQQKKYVYQNSW-GITTRTIGVMI 766
Cdd:cd00670 160 FGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGASF--KIDEDGGGRAHTGCGGaGGEERLVLALL 235
ProRS-C_1 pfam09180
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 912-996 2.42e-23

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 462709  Cd Length: 67  Bit Score: 94.12  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   912 WTDFCGFLEQKNILLAPFCGEISCEDKIKADSargeeaepgapamGAKSLCIPFDQPapiAASDKCINpsCTNKPKFYTL 991
Cdd:pfam09180   1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET-------------GATSRCIPFDQE---EEGGKCIV--CGKPAKKWVL 62


                  ....*
gi 24649468   992 FGRSY 996
Cdd:pfam09180  63 FARSY 67
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 30-79 1.51e-20

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 85.75  E-value: 1.51e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468  30 LDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPG 79
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 785-886 5.45e-20

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: 85.72  E-value: 5.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   785 QAIVVPcgitVNTKDDEraqLLDACKALEKRLVGGGVRCEGDYRdNYSPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAV 864
Cdd:pfam03129   1 QVVVIP----LGEKAEE---LEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVR 72

                          90       100
                  ....*....|....*....|..
gi 24649468   865 RRDTVEKITIPLADVEKKIPAL 886
Cdd:pfam03129  73 RRDTGEQETVSLDELVEKLKEL 94
WHEP-TRS pfam00458
WHEP-TRS domain;
30-81 1.54e-19

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 82.93  E-value: 1.54e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24649468    30 LDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPGQT 81
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAA 52
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 176-225 1.86e-19

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 82.67  E-value: 1.86e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 176 ILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPG 225
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
103-152 5.91e-19

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 81.00  E-value: 5.91e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 24649468   103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGT 152
Cdd:pfam00458   2 TEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGA 51
WHEP-TRS pfam00458
WHEP-TRS domain;
176-227 7.18e-19

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 81.00  E-value: 7.18e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24649468   176 ILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGTT 227
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAA 52
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 102-151 7.94e-19

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 80.74  E-value: 7.94e-19
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 102 VNASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPG 151
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
ProRS-C_1 smart00946
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 912-996 2.19e-18

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 198014  Cd Length: 67  Bit Score: 79.92  E-value: 2.19e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468    912 WTDFCGFLEQKNILLAPFCGEISCEDKIKADSargeeaepgapamGAKSLCIPFDQPAPiaaSDKCINpsCTNKPKFYTL 991
Cdd:smart00946   1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET-------------GATIRCIPFDQDEE---PGKCVV--CGKPAKKWVL 62


                   ....*
gi 24649468    992 FGRSY 996
Cdd:smart00946  63 FARSY 67
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 255-304 3.35e-17

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 76.12  E-value: 3.35e-17
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 255 LLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPG 304
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 330-379 1.39e-16

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 74.19  E-value: 1.39e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 24649468 330 VLSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPD 379
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
255-307 2.09e-16

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 74.07  E-value: 2.09e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24649468   255 LLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPGTVA 307
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
WHEP-TRS pfam00458
WHEP-TRS domain;
332-382 2.80e-16

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 73.68  E-value: 2.80e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24649468   332 SKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPDAKS 382
Cdd:pfam00458   3 EKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 555-757 7.72e-16

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: 77.54  E-value: 7.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 555 GVKECYFPIFVSKAVLEKEKTHIADFAPevawVTKSGDSDLAepiaVRPTSETvmYPAYAkWVQSYRDLPIRLNQWNNVV 634
Cdd:cd00768  17 GFQEVETPIVEREPLLEKAGHEPKDLLP----VGAENEEDLY----LRPTLEP--GLVRL-FVSHIRKLPLRLAEIGPAF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 635 RWEFKqPTPFLRTREFLWQEGHTAFADKEEaAKEVLDILDLYALVYTHL-LAIPVVKGRKTEKEKFAGGdYTTTVEAFI- 712
Cdd:cd00768  86 RNEGG-RRGLRRVREFTQLEGEVFGEDGEE-ASEFEELIELTEELLRALgIKLDIVFVEKTPGEFSPGG-AGPGFEIEVd 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 24649468 713 SASGRAIQGATSHHLGQNFSKMFEIvYEDPETQQKKYVYQNSWGI 757
Cdd:cd00768 163 HPEGRGLEIGSGGYRQDEQARAADL-YFLDEALEYRYPPTIGFGL 206
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 103-153 8.53e-16

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 72.37  E-value: 8.53e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24649468    103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGTV 153
Cdd:smart00991   1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAP 51
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 404-451 1.66e-15

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 71.11  E-value: 1.66e-15
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 24649468 404 LTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFP 451
Cdd:cd00936   1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYK 48
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 32-80 1.77e-15

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 71.22  E-value: 1.77e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24649468     32 SQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPGQ 80
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGA 50
WHEP-TRS pfam00458
WHEP-TRS domain;
404-451 4.97e-15

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 69.83  E-value: 4.97e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 24649468   404 LTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFP 451
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYK 48
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 178-226 8.21e-15

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 69.68  E-value: 8.21e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 24649468    178 SQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGT 226
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGA 50
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 592-769 4.70e-14

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: 71.29  E-value: 4.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   592 DSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPT-PFLRTREFLWQEGHTaFADKEEAAKEVL 670
Cdd:pfam00587   4 EDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTrGLIRVRQFHQDDAHI-FHAPGQSPDELE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468   671 DILDLYALVYThLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISASGRAIQGATSHHLGQNFSKMFEIVYEDPETQQKKYV 750
Cdd:pfam00587  83 DYIKLIDRVYS-RLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPY 161

                         170       180
                  ....*....|....*....|
gi 24649468   751 YQNSWGI-TTRTIGVMIMVH 769
Cdd:pfam00587 162 MIHRAGLgVERFLAAILENN 181
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 257-310 1.27e-13

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 66.21  E-value: 1.27e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 24649468    257 NKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPGTVAPAP 310
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPGDT 55
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 332-382 2.60e-13

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 65.44  E-value: 2.60e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 24649468    332 SKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPDAKS 382
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPP 52
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 33-72 2.88e-13

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 64.87  E-value: 2.88e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24649468  33 QISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSAT 72
Cdd:cd01200   3 KIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 727-883 3.29e-13

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 73.58  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  727 LGQNFSKMFEIVYEDpETQQKKYVYQNSWGI-TTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPcgitVNTKDDEraqL 805
Cdd:PRK09194 412 LGTKYSEAMNATVLD-ENGKAQPLIMGCYGIgVSRLVAAAIEQNHDEKGIIWPKAIAPFDVHIVP----VNMKDEE---V 483

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24649468  806 LDACKALEKRLVGGGVRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKI 883
Cdd:PRK09194 484 KELAEKLYAELQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFL 560
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 177-218 1.10e-12

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 62.94  E-value: 1.10e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24649468 177 LSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAAT 218
Cdd:cd01200   1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 103-144 1.94e-12

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 62.17  E-value: 1.94e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24649468 103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLT 144
Cdd:cd01200   1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
 800-884 6.06e-12

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: 62.80  E-value: 6.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 800 DERAQLLDACKALEKRLVGGGVRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADV 879
Cdd:cd00738  11 DPRVEAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDEL 89


                ....*
gi 24649468 880 EKKIP 884
Cdd:cd00738  90 PEFLV 94
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 331-372 1.35e-11

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 59.86  E-value: 1.35e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24649468 331 LSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLS 372
Cdd:cd01200   1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 406-450 1.67e-11

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 60.05  E-value: 1.67e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 24649468    406 QEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDF 450
Cdd:smart00991   2 EAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDY 46
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 406-446 1.96e-11

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 59.48  E-value: 1.96e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24649468 406 QEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVT 446
Cdd:cd01200   2 EKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
PLN02837 PLN02837
threonine-tRNA ligase
 565-889 2.07e-10

threonine-tRNA ligase


Pssm-ID: 215450 [Multi-domain]  Cd Length: 614  Bit Score: 64.53  E-value: 2.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  565 VSKAVLEKEKTHIaDFAPEVAWVTKSGDSDLAEpiaVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPF 644
Cdd:PLN02837 274 VAKADLWKTSGHL-DFYKENMYDQMDIEDELYQ---LRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGSLHG 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  645 L-RTREFLWQEGHTaFADKEEAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGD-------------------- 703
Cdd:PLN02837 350 LfRVRGFTQDDAHI-FCLEDQIKDEIRGVLDLTEEILKQFGFSKYEINLSTRPEKSVGSDdiwekattalrdalddkgwe 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  704 ----------YTTTVEAFIS-ASGRAIQGATSHhLGQNFSKMFEIVYEDPETQQKK--YVYQNSWGITTRTIGVMIMVHA 770
Cdd:PLN02837 429 ykvdegggafYGPKIDLKIEdALGRKWQCSTIQ-VDFNLPERFDITYVDSNSEKKRpiMIHRAILGSLERFFGVLIEHYA 507

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  771 DNQGLVLPPhvacIQAIVVPcgitvnTKDDEraqlLDACKALEKRLVGGGVRCEGDYRDNYspGWKFNHWELKGVPLRLE 850
Cdd:PLN02837 508 GDFPLWLAP----VQARVLP------VTDNE----LEYCKEVVAKLKAKGIRAEVCHGERL--PKLIRNAETQKIPLMAV 571

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 24649468  851 VGPKDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLET 889
Cdd:PLN02837 572 VGPKEVETRTLTVRSRHGGELGTMPVDDFINRIQLAVEN 610
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 256-297 2.94e-10

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 56.01  E-value: 2.94e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24649468 256 LNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLT 297
Cdd:cd01200   1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 333-374 1.60e-08

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 51.32  E-value: 1.60e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24649468 333 KIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGK 374
Cdd:cd00939   4 EVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
PRK12325 PRK12325
prolyl-tRNA synthetase; Provisional
 726-883 3.64e-08

prolyl-tRNA synthetase; Provisional


Pssm-ID: 237059 [Multi-domain]  Cd Length: 439  Bit Score: 56.79  E-value: 3.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  726 HLGQNFSKMFEIVYEDPEtQQKKYVYQNSWGI-TTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPcgitVNTKDDEraq 804
Cdd:PRK12325 288 YFGTKYSEPMNAKVQGPD-GKEVPVHMGSYGIgVSRLVAAIIEASHDDKGIIWPESVAPFKVGIIN----LKQGDEA--- 359

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24649468  805 LLDACKALEKRLVGGGVRCEGDYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKI 883
Cdd:PRK12325 360 CDAACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDLIGLPWQIIVGPKGLAEGKVELKDRKTGEREELSVEAAINRL 437
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 404-448 9.08e-08

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 49.39  E-value: 9.08e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24649468 404 LTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGT 448
Cdd:cd00939   1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 255-298 3.09e-07

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 47.85  E-value: 3.09e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24649468 255 LLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTG 298
Cdd:cd00939   1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 180-219 6.20e-07

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 46.70  E-value: 6.20e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24649468 180 ITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATG 219
Cdd:cd00939   5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 28-66 1.53e-06

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 45.92  E-value: 1.53e-06
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24649468  28 SELDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKA 66
Cdd:cd00938   1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKA 39
PLN02734 PLN02734
glycyl-tRNA synthetase
 171-220 6.28e-06

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 50.13  E-value: 6.28e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24649468  171 DSVAQILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLK-------ADYKAATGS 220
Cdd:PLN02734   7 DALAEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKleksaleKELQAAVGA 63
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 403-440 8.37e-06

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 43.61  E-value: 8.37e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24649468 403 ELTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKA 440
Cdd:cd00938   2 KLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKA 39
PLN02734 PLN02734
glycyl-tRNA synthetase
 103-137 2.00e-05

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 48.59  E-value: 2.00e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 24649468  103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELK 137
Cdd:PLN02734  13 QAAVTAQGNAVRALKASKADKAEIDAAIEKLKALK 47
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 103-139 3.28e-05

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 42.07  E-value: 3.28e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 24649468 103 NASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQ 139
Cdd:cd00938   4 EEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
 619-889 3.39e-05

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 47.82  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  619 SYRDLPIRLNQWNNVVRWEFKQP-TPFLRTREFLWQEGHTaFADKEEAAKEVLDILDLYALVY----------------- 680
Cdd:PRK12444 350 SYRELPIRMCEFGQVHRHEFSGAlNGLLRVRTFCQDDAHL-FVTPDQIEDEIKSVMAQIDYVYktfgfeyevelstrped 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  681 ----THL-----LAIPVVKGRKTEKEKFAGGD---YTTTVEAFIS-ASGRAIQGATShHLGQNFSKMFEIVY--EDPETQ 745
Cdd:PRK12444 429 smgdDELweqaeASLENVLQSLNYKYRLNEGDgafYGPKIDFHIKdALNRSHQCGTI-QLDFQMPEKFDLNYidEKNEKR 507

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  746 QKKYVYQNSWGITTRTIGVMImvhaDNQGLVLPPHVACIQAIVVPCGITVNtkdderaqlLDACKALEKRLVGGGVRCEG 825
Cdd:PRK12444 508 RPVVIHRAVLGSLDRFLAILI----EHFGGAFPAWLAPVQVKVIPVSNAVH---------VQYADEVADKLAQAGIRVER 574

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24649468  826 DYRDNySPGWKFNHWELKGVPLRLEVGPKDLKAQQlVAVRRDTVEKI-TIPLADVEKKIPALLET 889
Cdd:PRK12444 575 DERDE-KLGYKIREAQMQKIPYVLVIGDKEMENGA-VNVRKYGEEKSeVIELDMFVESIKEEIKN 637
PLN02734 PLN02734
glycyl-tRNA synthetase
 28-75 3.77e-05

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 47.82  E-value: 3.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 24649468   28 SELDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADyKSATGKD 75
Cdd:PLN02734  10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLE-KSALEKE 56
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 30-74 3.94e-05

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 41.69  E-value: 3.94e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24649468  30 LDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGK 74
Cdd:cd00939   1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 106-145 9.18e-05

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 40.92  E-value: 9.18e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24649468 106 IVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTG 145
Cdd:cd00939   5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 174-212 2.14e-04

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 39.76  E-value: 2.14e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 24649468 174 AQILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKA 212
Cdd:cd00938   1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKA 39
ProRS_core_prok cd00779
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 603-766 2.44e-04

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: 44.10  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 603 PTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKEEAAKEVLDILDLYALVYTH 682
Cdd:cd00779  92 PTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEIRPRFGLMRGREFLMKDAYSFDIDEESLEETYEKMYQAYSRIFKR 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 683 LLaIPVVKgrktekekfaggdytttVEAfisASGrAIQGATSH--------------------HLGQNFSKMFEIVYEDp 742
Cdd:cd00779 172 LG-LPFVK-----------------VEA---DSG-AIGGSLSHefhvlsplkitkgievghifQLGTKYSKALGATFLD- 228

                       170       180
                ....*....|....*....|....*
gi 24649468 743 ETQQKKYVYQNSWGI-TTRTIGVMI 766
Cdd:cd00779 229 ENGKPKPLEMGCYGIgVSRLLAAII 253
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 760-883 2.62e-04

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: 45.02  E-value: 2.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468 760 RTIGVMIMVHADNqglvLPPHVACIQAIVVPcgITvntkddERAqlLDACKALEKRLVGGGVRCEGDYRDNySPGWKFNH 839
Cdd:COG0441 520 RFIGILIEHYAGA----FPLWLAPVQVVVLP--IS------DKH--ADYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIRE 584

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 24649468 840 WELKGVPLRLEVGPKDLKAQQlVAVR-RDTVEKITIPLADVEKKI 883
Cdd:COG0441 585 AQLQKVPYMLVVGDKEVENGT-VSVRrRGGGDLGTMSLDEFIARL 628
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 331-365 4.31e-04

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 38.99  E-value: 4.31e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 24649468 331 LSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALK 365
Cdd:cd00938   4 EEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELK 38
PLN02734 PLN02734
glycyl-tRNA synthetase
 402-439 6.45e-04

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 43.58  E-value: 6.45e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 24649468  402 DELTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALK 439
Cdd:PLN02734  10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALK 47
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 254-290 1.21e-03

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 37.45  E-value: 1.21e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 24649468 254 TLLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALK 290
Cdd:cd00938   2 KLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELK 38
GlyRS_RNA cd00935
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ...
 104-143 1.39e-03

GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238472 [Multi-domain]  Cd Length: 51  Bit Score: 37.47  E-value: 1.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24649468 104 ASIVKQGDLVRDLKGKKASKPEIDAAVktlLELKAQYKTL 143
Cdd:cd00935   6 AAVKEQGDLVRKLKEEGAPDVDIKKAV---AELKARKKLL 42
PRK13808 PRK13808
adenylate kinase; Provisional
 402-503 2.12e-03

adenylate kinase; Provisional


Pssm-ID: 172341 [Multi-domain]  Cd Length: 333  Bit Score: 41.41  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24649468  402 DELTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTgtdfpVAGRGGGGGGGSAKKAPKEAQpKPAKPVKK 481
Cdd:PRK13808 181 DEVTREIGRVLAAVGAANAKKAAKTPAAKSGAKKASAKAKSAAKK-----VSKKKAAKTAVSAKKAAKTAA-KAAKKAKK 254

                         90       100
                 ....*....|....*....|..
gi 24649468  482 EPAADASGAVKKQTRLGLEATK 503
Cdd:PRK13808 255 TAKKALKKAAKAVKKAAKKAAK 276
 
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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