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Conserved domains on  [gi|1834199288|ref|NP_001260520|]
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Aspartyl-tRNA synthetase, mitochondrial, isoform D [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
aspS super family cl35101
aspartyl-tRNA synthetase; Validated
 462-1045 0e+00

aspartyl-tRNA synthetase; Validated


The actual alignment was detected with superfamily member PRK00476:

Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 679.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLefQRMNKF----FI-LRDAYGQTQVLLSPKTYGLEEyAETgVPIESIVRVEGTVIPR 536
Cdd:PRK00476     4 RTHYCGELRESHVGQTVTLCGWV--HRRRDHggliFIdLRDREGIVQVVFDPDAEAFEV-AES-LRSEYVIQVTGTVRAR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  537 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 616
Cdd:PRK00476    80 PEGTVNPNLPTGEIEVLASELEVLNKSK-TLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDD- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  617 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 695
Cdd:PRK00476   158 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDI 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  696 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSD--EFKEKYD 771
Cdd:PRK00476   238 EMSFVTQEDVMALMEGLIRHVF-KEVLgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGfkVFAGAAN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  772 DLGAY-AIVVRaseafwNGAA---RKHYESLGKefkgtlFVRKFG---------PTKDVQEKLGKLLGEDVATEVADKFD 838
Cdd:PRK00476   317 DGGRVkAIRVP------GGAAqlsRKQIDELTE------FAKIYGakglayikvNEDGLKGPIAKFLSEEELAALLERTG 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  839 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 918
Cdd:PRK00476   385 AKDGDLIFFGADKAKVVNDALGALRL----KLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLD 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  919 NFATSceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 994
Cdd:PRK00476   461 ELETT--DPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFE-ILGISeeeaEEKFGFLLDALKYGAPPHGGIAFGLD 537

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834199288  995 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEE 1045
Cdd:PRK00476   538 RLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 291-410 7.24e-33

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


:

Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 123.79  E-value: 7.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  291 RDLTCNDLRRDDVGKTVTLVGWIPSTKNN---KFLQLKDGYGQTQLMIEDQSLS--DTFLSTPEQTVIQIVGKVLGRPKA 365
Cdd:cd04317      1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPefELAEKLRNESVIQVTGKVRARPEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1834199288  366 NVNLKYDTGEVEVSVTSVKVLNPDDP----YDGPIKAKE-KKQKFSIDDL 410
Cdd:cd04317     81 TVNPKLPTGEIEVVASELEVLNKAKTlpfeIDDDVNVSEeLRLKYRYLDL 130
RPA_2b-aaRSs_OBF_like super family cl09930
Replication protein A, class 2b aminoacyl-tRNA synthetases, and related proteins with ...
 148-303 3.55e-12

Replication protein A, class 2b aminoacyl-tRNA synthetases, and related proteins with oligonucleotide/oligosaccharide (OB) fold.; This superfamily includes two oligonucleotide/oligosaccharide binding fold (OBF) domain families. One of these contains the OBF domains of the large (RPA1, 70kDa), middle (RPA2, RPA4, 32kDa) and small (RPA3, 14 kDa) subunits of human heterotrimeric Replication protein A (RPA), and similar domains. RPA is a nuclear single-strand (ss) DNA-binding protein involved in most aspects of DNA metabolism. This family includes the four OBF domains of RPA1 [DNA-binding domain (DBD)-A, DBD-B, DBD-C, and RPA1N], the OBF domain of RPA2 (RPA2 DBD-D), RPA3, and the OBF domain of RPA4. The major DNA binding activity of human RPA and Saccharomyces cerevisiae RPA appears to be associated with DBD-A and -B, of RPA1. RPA1 DBD-C shows only weak ssDNA-binding activity and is involved in trimerization. The other OBF domain family in this superfamily is the N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids to their cognate tRNAs during protein biosynthesis. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases.


The actual alignment was detected with superfamily member cd04317:

Pssm-ID: 471953 [Multi-domain]  Cd Length: 135  Bit Score: 64.85  E-value: 3.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  148 CGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVlEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNSC 224
Cdd:cd04317      5 CGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYG-IVQVVF-DPEEAPEFELAEKLRNESVIQVTGKVRARPEGTV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  225 NQTMPTGEIEVEVQD--ILN----IHFPAggtkragdkrtystmvqqqsnlgitstEYKIAKNENI-LKYfenRDLtcnD 297
Cdd:cd04317     83 NPKLPTGEIEVVASEleVLNkaktLPFEI---------------------------DDDVNVSEELrLKY---RYL---D 129


                   ....*.
gi 1834199288  298 LRRDDV 303
Cdd:cd04317    130 LRRPKM 135
 
Name Accession Description Interval E-value
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 462-1045 0e+00

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 679.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLefQRMNKF----FI-LRDAYGQTQVLLSPKTYGLEEyAETgVPIESIVRVEGTVIPR 536
Cdd:PRK00476     4 RTHYCGELRESHVGQTVTLCGWV--HRRRDHggliFIdLRDREGIVQVVFDPDAEAFEV-AES-LRSEYVIQVTGTVRAR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  537 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 616
Cdd:PRK00476    80 PEGTVNPNLPTGEIEVLASELEVLNKSK-TLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDD- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  617 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 695
Cdd:PRK00476   158 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDI 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  696 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSD--EFKEKYD 771
Cdd:PRK00476   238 EMSFVTQEDVMALMEGLIRHVF-KEVLgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGfkVFAGAAN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  772 DLGAY-AIVVRaseafwNGAA---RKHYESLGKefkgtlFVRKFG---------PTKDVQEKLGKLLGEDVATEVADKFD 838
Cdd:PRK00476   317 DGGRVkAIRVP------GGAAqlsRKQIDELTE------FAKIYGakglayikvNEDGLKGPIAKFLSEEELAALLERTG 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  839 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 918
Cdd:PRK00476   385 AKDGDLIFFGADKAKVVNDALGALRL----KLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLD 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  919 NFATSceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 994
Cdd:PRK00476   461 ELETT--DPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFE-ILGISeeeaEEKFGFLLDALKYGAPPHGGIAFGLD 537

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834199288  995 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEE 1045
Cdd:PRK00476   538 RLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 462-1046 0e+00

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 672.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLEFQRmNK----FFILRDAYGQTQVLLSPKTYG-LEEYAETgVPIESIVRVEGTVIPR 536
Cdd:COG0173      3 RTHYCGELRESDVGQEVTLSGWVHRRR-DHggliFIDLRDRYGITQVVFDPDDSAeAFEKAEK-LRSEYVIAVTGKVRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  537 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 616
Cdd:COG0173     81 PEGTVNPKLPTGEIEVLASELEILNKAK-TPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDE- 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  617 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 695
Cdd:COG0173    159 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  696 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSdEFK--EKYD 771
Cdd:COG0173    239 EMSFVDQEDVFELMEGLIRHLF-KEVLgvELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDS-GFKvfAGAA 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  772 DLGAY--AIVVRaseafwNGAA--RKHYESLGKefkgtlFVRKFGP--------TKD-VQEKLGKLLGEDVATEVADKFD 838
Cdd:COG0173    317 ENGGRvkAINVP------GGASlsRKQIDELTE------FAKQYGAkglayikvNEDgLKSPIAKFLSEEELAAILERLG 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  839 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 918
Cdd:COG0173    385 AKPGDLIFFVADKPKVVNKALGALRL----KLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLD 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  919 NFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 994
Cdd:COG0173    461 LLET---DPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFE-LLGISeeeaEEKFGFLLEAFKYGAPPHGGIAFGLD 536

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1834199288  995 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEEE 1046
Cdd:COG0173    537 RLVMLLAGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
aspS_bact TIGR00459
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ...
 462-1042 4.14e-180

aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 211576 [Multi-domain]  Cd Length: 583  Bit Score: 539.71  E-value: 4.14e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLEFQR----MNkFFILRDAYGQTQVLLSPKTYGLEeyAETGVPIESIVRVEGTVIPRP 537
Cdd:TIGR00459    2 RTHYCGQLRTEHLGQTVTLAGWVNRRRdlggLI-FIDLRDRSGIVQVVCDPDADALK--LAKGLRNEDVVQVKGKVSARP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  538 AATINPKMQTGHVEVEADKVVVLNPAKKnLPFEIRKFNrAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLiNYL 617
Cdd:TIGR00459   79 EGNINRNLDTGEIEILAESITLLNKSKT-PPLIIEKTD-AEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL-DQQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  618 GFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIE 696
Cdd:TIGR00459  156 GFLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDME 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  697 LSFTSRDDIMQLIEETLRYSWPKDFP-RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIeKSDEFKEKYDDLGA 775
Cdd:TIGR00459  236 MSFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLF-KDSEFKVFSNLIND 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  776 YAIV----VRASEAFWNGAARKHYESLGKEF--KGT--LFVRKfgptKDVQEKLGKLLGEDVATEVADKFDLEENDLLFL 847
Cdd:TIGR00459  315 GGRVkairVPGGWAELSRKSIKELRKFAKEYgaKGLayLKVNE----DGINSPIKKFLDEKKGKILLERTDAQNGDILLF 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  848 GIGSKVETRELLGRIRLDyqdfLVENAKIKKPNDFRFLWVIDFPLFERNREtNQLESVHHPFTLPHSDDLENFATsceNL 927
Cdd:TIGR00459  391 GAGSKKIVLDALGALRLK----LGKDLGLVDPDLFSFLWVVDFPMFEKDKE-GRLCAAHHPFTMPKDEDLENLEA---AP 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  928 ESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKI----PHDHLSHLLSALESGCPPHGGIALGLDRLIAILCRA 1003
Cdd:TIGR00459  463 EEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFE-ILGIdpeeAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGT 541

                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1834199288 1004 RSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVV 1042
Cdd:TIGR00459  542 DNIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYV 580
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 599-1017 5.23e-139

Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.


Pssm-ID: 238400 [Multi-domain]  Cd Length: 280  Bit Score: 421.21  E-value: 5.23e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  599 LRLRSAVIMKMREYLINyLGFVEVETPTLFRRTPGGAQEFVVPTRK-AGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCY 677
Cdd:cd00777      1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRLhPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  678 RDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPR-LQTPFRRITYEEAMEKYGndkpdtrfgfllnnv 756
Cdd:cd00777     80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVeLTTPFPRMTYAEAMERYG--------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  757 seiieksdefkekyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadk 836
Cdd:cd00777        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  837 fdleendllflgigskvetrellgrirldyqdflvenakikkpndFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDD 916
Cdd:cd00777    145 ---------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEED 179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  917 LENFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGL 993
Cdd:cd00777    180 LDLLEK---DPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEeeaEEKFGFLLEAFKYGAPPHGGIALGL 256

                          410       420
                   ....*....|....*....|....
gi 1834199288  994 DRLIAILCRARSIRDVIAFPKSLN 1017
Cdd:cd00777    257 DRLVMLLTGSESIRDVIAFPKTQN 280
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
578-1014 9.83e-115

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 358.80  E-value: 9.83e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  578 GERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLFR-RTPGGAQEFVVPTRKAGHFYSLVQSPQ 656
Cdd:pfam00152    1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  657 QFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK-----------DFPRLQ 725
Cdd:pfam00152   80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEvegiakeleggTLLDLK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  726 TPFRRITYEEAMEK----------YGNDKPDTRFGFLLnnvseiieksdefkekyddlgayaivvraseafwngaarkhy 795
Cdd:pfam00152  160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLEL------------------------------------------ 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  796 eslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadkfdleendllflgigskvetrellgrirldyqdflvenak 875
Cdd:pfam00152      --------------------------------------------------------------------------------

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  876 IKKPNDFRFLWVIDFPlfernretnqleSVHHPFTLPHSDDLEnfatscenlesIRSQAYDLVLNGQEVGGGSIRIHDRD 955
Cdd:pfam00152  198 VIDKNKFNPLWVTDFP------------AEHHPFTMPKDEDDP-----------ALAEAFDLVLNGVEIGGGSIRIHDPE 254

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834199288  956 MQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPK 1014
Cdd:pfam00152  255 LQEERFEEQGLDPeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 291-410 7.24e-33

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 123.79  E-value: 7.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  291 RDLTCNDLRRDDVGKTVTLVGWIPSTKNN---KFLQLKDGYGQTQLMIEDQSLS--DTFLSTPEQTVIQIVGKVLGRPKA 365
Cdd:cd04317      1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPefELAEKLRNESVIQVTGKVRARPEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1834199288  366 NVNLKYDTGEVEVSVTSVKVLNPDDP----YDGPIKAKE-KKQKFSIDDL 410
Cdd:cd04317     81 TVNPKLPTGEIEVVASELEVLNKAKTlpfeIDDDVNVSEeLRLKYRYLDL 130
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 148-303 3.55e-12

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 64.85  E-value: 3.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  148 CGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVlEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNSC 224
Cdd:cd04317      5 CGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYG-IVQVVF-DPEEAPEFELAEKLRNESVIQVTGKVRARPEGTV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  225 NQTMPTGEIEVEVQD--ILN----IHFPAggtkragdkrtystmvqqqsnlgitstEYKIAKNENI-LKYfenRDLtcnD 297
Cdd:cd04317     83 NPKLPTGEIEVVASEleVLNkaktLPFEI---------------------------DDDVNVSEELrLKY---RYL---D 129


                   ....*.
gi 1834199288  298 LRRDDV 303
Cdd:cd04317    130 LRRPKM 135
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 148-242 1.86e-09

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 61.55  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  148 CGELRNHHCGLFVELSGRlikkrVNR--------FAELRDRNGgACQLVVLEDKHP---RVARRMNNmpEnTTLTIVGLV 216
Cdd:COG0173      7 CGELRESDVGQEVTLSGW-----VHRrrdhggliFIDLRDRYG-ITQVVFDPDDSAeafEKAEKLRS--E-YVIAVTGKV 77

                           90       100
                   ....*....|....*....|....*...
gi 1834199288  217 MRRPHNSCNQTMPTGEIEVEVQD--ILN 242
Cdd:COG0173     78 RARPEGTVNPKLPTGEIEVLASEleILN 105
PLN02903 PLN02903
aminoacyl-tRNA ligase
 128-242 2.01e-09

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 61.73  E-value: 2.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  128 SAMASNFNMNSQPPQPMR-QSCGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVLEDKHPRVARRMNN 203
Cdd:PLN02903    42 PVVSAVDSMSSQLTWPSRsHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTG-IVQVVTLPDEFPEAHRTANR 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1834199288  204 MPENTTLTIVGLVMRRPHNSCNQTMPTGEIEV--EVQDILN 242
Cdd:PLN02903   121 LRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVvaESVDILN 161
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 307-386 1.73e-08

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 52.24  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  307 VTLVGWIPSTKNNK----FLQLKDGYGQTQLMIEDQSLSDTFLSTPEQTVIQIVGKVlgrpkanvnLKYDTGEVEVSVTS 382
Cdd:pfam01336    1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKV---------KKRKGGELELVVEE 71


                   ....
gi 1834199288  383 VKVL 386
Cdd:pfam01336   72 IELL 75
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 298-400 2.97e-04

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 44.71  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  298 LRRDDVGKTVTLVGWIPSTKNNK---FLQLKDGYGQTQLMIEDQSLSDTF---LSTPEQTVIQIVGKVLGRPKANvnlky 371
Cdd:PRK03932    10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDGSCFKQLQVVKDNGEEYFeeiKKLTTGSSVIVTGTVVESPRAG----- 84

                           90       100
                   ....*....|....*....|....*....
gi 1834199288  372 dtGEVEVSVTSVKVLNpDDPYDGPIKAKE 400
Cdd:PRK03932    85 --QGYELQATKIEVIG-EDPEDYPIQKKR 110
 
Name Accession Description Interval E-value
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 462-1045 0e+00

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 679.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLefQRMNKF----FI-LRDAYGQTQVLLSPKTYGLEEyAETgVPIESIVRVEGTVIPR 536
Cdd:PRK00476     4 RTHYCGELRESHVGQTVTLCGWV--HRRRDHggliFIdLRDREGIVQVVFDPDAEAFEV-AES-LRSEYVIQVTGTVRAR 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  537 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 616
Cdd:PRK00476    80 PEGTVNPNLPTGEIEVLASELEVLNKSK-TLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDD- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  617 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 695
Cdd:PRK00476   158 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDI 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  696 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSD--EFKEKYD 771
Cdd:PRK00476   238 EMSFVTQEDVMALMEGLIRHVF-KEVLgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGfkVFAGAAN 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  772 DLGAY-AIVVRaseafwNGAA---RKHYESLGKefkgtlFVRKFG---------PTKDVQEKLGKLLGEDVATEVADKFD 838
Cdd:PRK00476   317 DGGRVkAIRVP------GGAAqlsRKQIDELTE------FAKIYGakglayikvNEDGLKGPIAKFLSEEELAALLERTG 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  839 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 918
Cdd:PRK00476   385 AKDGDLIFFGADKAKVVNDALGALRL----KLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLD 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  919 NFATSceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 994
Cdd:PRK00476   461 ELETT--DPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFE-ILGISeeeaEEKFGFLLDALKYGAPPHGGIAFGLD 537

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834199288  995 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEE 1045
Cdd:PRK00476   538 RLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 462-1046 0e+00

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 672.48  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLEFQRmNK----FFILRDAYGQTQVLLSPKTYG-LEEYAETgVPIESIVRVEGTVIPR 536
Cdd:COG0173      3 RTHYCGELRESDVGQEVTLSGWVHRRR-DHggliFIDLRDRYGITQVVFDPDDSAeAFEKAEK-LRSEYVIAVTGKVRAR 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  537 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 616
Cdd:COG0173     81 PEGTVNPKLPTGEIEVLASELEILNKAK-TPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDE- 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  617 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 695
Cdd:COG0173    159 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDI 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  696 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSdEFK--EKYD 771
Cdd:COG0173    239 EMSFVDQEDVFELMEGLIRHLF-KEVLgvELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDS-GFKvfAGAA 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  772 DLGAY--AIVVRaseafwNGAA--RKHYESLGKefkgtlFVRKFGP--------TKD-VQEKLGKLLGEDVATEVADKFD 838
Cdd:COG0173    317 ENGGRvkAINVP------GGASlsRKQIDELTE------FAKQYGAkglayikvNEDgLKSPIAKFLSEEELAAILERLG 384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  839 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 918
Cdd:COG0173    385 AKPGDLIFFVADKPKVVNKALGALRL----KLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLD 460

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  919 NFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 994
Cdd:COG0173    461 LLET---DPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFE-LLGISeeeaEEKFGFLLEAFKYGAPPHGGIAFGLD 536

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1834199288  995 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEEE 1046
Cdd:COG0173    537 RLVMLLAGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
aspS_bact TIGR00459
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ...
 462-1042 4.14e-180

aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be discriminating (6.1.1.12) or nondiscriminating (6.1.1.23). In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_bact, represents aspartyl-tRNA synthetases from the Bacteria and from mitochondria. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). This model generates very low scores for the archaeal type of aspS and for asnS; scores between the trusted and noise cutoffs represent fragmentary sequences. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 211576 [Multi-domain]  Cd Length: 583  Bit Score: 539.71  E-value: 4.14e-180
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLEFQR----MNkFFILRDAYGQTQVLLSPKTYGLEeyAETGVPIESIVRVEGTVIPRP 537
Cdd:TIGR00459    2 RTHYCGQLRTEHLGQTVTLAGWVNRRRdlggLI-FIDLRDRSGIVQVVCDPDADALK--LAKGLRNEDVVQVKGKVSARP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  538 AATINPKMQTGHVEVEADKVVVLNPAKKnLPFEIRKFNrAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLiNYL 617
Cdd:TIGR00459   79 EGNINRNLDTGEIEILAESITLLNKSKT-PPLIIEKTD-AEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL-DQQ 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  618 GFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIE 696
Cdd:TIGR00459  156 GFLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDME 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  697 LSFTSRDDIMQLIEETLRYSWPKDFP-RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIeKSDEFKEKYDDLGA 775
Cdd:TIGR00459  236 MSFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLF-KDSEFKVFSNLIND 314

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  776 YAIV----VRASEAFWNGAARKHYESLGKEF--KGT--LFVRKfgptKDVQEKLGKLLGEDVATEVADKFDLEENDLLFL 847
Cdd:TIGR00459  315 GGRVkairVPGGWAELSRKSIKELRKFAKEYgaKGLayLKVNE----DGINSPIKKFLDEKKGKILLERTDAQNGDILLF 390

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  848 GIGSKVETRELLGRIRLDyqdfLVENAKIKKPNDFRFLWVIDFPLFERNREtNQLESVHHPFTLPHSDDLENFATsceNL 927
Cdd:TIGR00459  391 GAGSKKIVLDALGALRLK----LGKDLGLVDPDLFSFLWVVDFPMFEKDKE-GRLCAAHHPFTMPKDEDLENLEA---AP 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  928 ESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKI----PHDHLSHLLSALESGCPPHGGIALGLDRLIAILCRA 1003
Cdd:TIGR00459  463 EEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFE-ILGIdpeeAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGT 541

                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1834199288 1004 RSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVV 1042
Cdd:TIGR00459  542 DNIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYV 580
PLN02903 PLN02903
aminoacyl-tRNA ligase
 434-1042 2.87e-170

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 517.03  E-value: 2.87e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  434 SAEASTTANASLIAEQRAKVADTNKFADRTHNCGELTSNDINEKVVICGWLEFQRMN---KFFILRDAYGQTQVLLSPKT 510
Cdd:PLN02903    31 SSAASSAATVIPVVSAVDSMSSQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTGIVQVVTLPDE 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  511 YGLEEYAETGVPIESIVRVEGTVIPRPAATINPKMQTGHVEVEADKVVVLNPAKKNLPFEIRKF----NRAGERLRLTHR 586
Cdd:PLN02903   111 FPEAHRTANRLRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVVAESVDILNVVTKSLPFLVTTAdeqkDSIKEEVRLRYR 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  587 YLDLRFNDMQHNLRLRSAVIMKMREYLINYLGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSG 665
Cdd:PLN02903   191 VLDLRRPQMNANLRLRHRVVKLIRRYLEDVHGFVEIETPILSRSTPEGARDYLVPSRvQPGTFYALPQSPQLFKQMLMVS 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  666 GIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLR--YSWPKDFpRLQTPFRRITYEEAMEKYGND 743
Cdd:PLN02903   271 GFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRqvFKEIKGV-QLPNPFPRLTYAEAMSKYGSD 349

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  744 KPDTRFGFLLNNVSEIIEKSdEFKEKYDDLGA----YAIVVRASEAFWNGAARK----HYESLGKEFKGTLFVRKfgpTK 815
Cdd:PLN02903   350 KPDLRYGLELVDVSDVFAES-SFKVFAGALESggvvKAICVPDGKKISNNTALKkgdiYNEAIKSGAKGLAFLKV---LD 425

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  816 DVQEKLGKLLGEDVATEVADKF----DLEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFP 891
Cdd:PLN02903   426 DGELEGIKALVESLSPEQAEQLlaacGAGPGDLILFAAGPTSSVNKTLDRLRQ----FIAKTLDLIDPSRHSILWVTDFP 501

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  892 LFERNRETNQLESVHHPFTLPHSDDLenfatscENLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEQILKIP--- 968
Cdd:PLN02903   502 MFEWNEDEQRLEALHHPFTAPNPEDM-------GDLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPeea 574

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834199288  969 HDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVV 1042
Cdd:PLN02903   575 ESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIAST 648
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
 599-1017 5.23e-139

Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.


Pssm-ID: 238400 [Multi-domain]  Cd Length: 280  Bit Score: 421.21  E-value: 5.23e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  599 LRLRSAVIMKMREYLINyLGFVEVETPTLFRRTPGGAQEFVVPTRK-AGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCY 677
Cdd:cd00777      1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRLhPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  678 RDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPR-LQTPFRRITYEEAMEKYGndkpdtrfgfllnnv 756
Cdd:cd00777     80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVeLTTPFPRMTYAEAMERYG--------------- 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  757 seiieksdefkekyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadk 836
Cdd:cd00777        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  837 fdleendllflgigskvetrellgrirldyqdflvenakikkpndFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDD 916
Cdd:cd00777    145 ---------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEED 179

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  917 LENFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGL 993
Cdd:cd00777    180 LDLLEK---DPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEeeaEEKFGFLLEAFKYGAPPHGGIALGL 256

                          410       420
                   ....*....|....*....|....
gi 1834199288  994 DRLIAILCRARSIRDVIAFPKSLN 1017
Cdd:cd00777    257 DRLVMLLTGSESIRDVIAFPKTQN 280
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 459-1035 1.84e-117

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 379.72  E-value: 1.84e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  459 FADRTHnCGELTSNDINEKVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTYGLEEYAE-TGVPIESIVRVEGTVI 534
Cdd:PRK12820     3 ENDRSF-CGHLSLDDTGREVCLAGWVDAFRDHGellFIHLRDRNGFIQAVFSPEAAPADVYELaASLRAEFCVALQGEVQ 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  535 PRPAATINPKMQTGHVEVEADKVVVLNpAKKNLPFEIR-KFNRAG----------ERLRLTHRYLDLRFNDMQHNLRLRS 603
Cdd:PRK12820    82 KRLEETENPHIETGDIEVFVRELSILA-ASEALPFAISdKAMTAGagsagadavnEDLRLQYRYLDIRRPAMQDHLAKRH 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  604 AVIMKMREYLiNYLGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEAT 682
Cdd:PRK12820   161 RIIKCARDFL-DSRGFLEIETPILTKSTPEGARDYLVPSRiHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  683 RPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPRLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEK 762
Cdd:PRK12820   240 RPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFEN 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  763 SDE--FKEKYDDLGAY-AIVVR------ASEAFWNGAARKHYESLGKefKGTLFVRkfGPTKDVQEKLGKLLGEDVATEV 833
Cdd:PRK12820   320 TRYgiFKQILQRGGRIkGINIKgqseklSKNVLQNEYAKEIAPSFGA--KGMTWMR--AEAGGLDSNIVQFFSADEKEAL 395

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  834 ADKFDLEEND-LLFLGIGSKVETRELLGRIRLDYQDFLvenaKIKKPNDFRFLWVIDFPLFERNRETNqLESVHHPFTLP 912
Cdd:PRK12820   396 KRRFHAEDGDvIIMIADASCAIVLSALGQLRLHLADRL----GLIPEGVFHPLWITDFPLFEATDDGG-VTSSHHPFTAP 470

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  913 HSDDLEnfATSCENLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFIL------EQILKiphDHLSHLLSALESGCPPH 986
Cdd:PRK12820   471 DREDFD--PGDIEELLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFaalglsEEDIE---DKFGFFLRAFDFAAPPH 545

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*....
gi 1834199288  987 GGIALGLDRLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMR 1035
Cdd:PRK12820   546 GGIALGLDRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLA 594
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
578-1014 9.83e-115

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 358.80  E-value: 9.83e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  578 GERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLFR-RTPGGAQEFVVPTRKAGHFYSLVQSPQ 656
Cdd:pfam00152    1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  657 QFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK-----------DFPRLQ 725
Cdd:pfam00152   80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEvegiakeleggTLLDLK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  726 TPFRRITYEEAMEK----------YGNDKPDTRFGFLLnnvseiieksdefkekyddlgayaivvraseafwngaarkhy 795
Cdd:pfam00152  160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLEL------------------------------------------ 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  796 eslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadkfdleendllflgigskvetrellgrirldyqdflvenak 875
Cdd:pfam00152      --------------------------------------------------------------------------------

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  876 IKKPNDFRFLWVIDFPlfernretnqleSVHHPFTLPHSDDLEnfatscenlesIRSQAYDLVLNGQEVGGGSIRIHDRD 955
Cdd:pfam00152  198 VIDKNKFNPLWVTDFP------------AEHHPFTMPKDEDDP-----------ALAEAFDLVLNGVEIGGGSIRIHDPE 254

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834199288  956 MQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPK 1014
Cdd:pfam00152  255 LQEERFEEQGLDPeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 462-1021 2.28e-60

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 213.51  E-value: 2.28e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWL-EFQRMN--KFFILRDAYGQTQVLLS-PKTYGLEEYAEtGVPIESIVRVEGTVIPrp 537
Cdd:PRK05159     3 KRHLTSELTPELDGEEVTLAGWVhEIRDLGgiAFLILRDRSGIIQVVVKkKVDEELFETIK-KLKRESVVSVTGTVKA-- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  538 aatiNPKMQTGhVEVEADKVVVLNPAKKNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyL 617
Cdd:PRK05159    80 ----NPKAPGG-VEVIPEEIEVLNKAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE-N 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  618 GFVEVETPTLFRR-TPGGAQEFVVP--TRKAghfYsLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQ-PEFTQL 693
Cdd:PRK05159   154 GFTEIFTPKIVASgTEGGAELFPIDyfEKEA---Y-LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSI 229

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  694 DIELSFTSRD-DIMQLIEETLRYSWPK--------------DFPRLQTPFRRITYEEAMEkygndkpdtrfgfLLNnvse 758
Cdd:PRK05159   230 DVEMGFIDDHeDVMDLLENLLRYMYEDvaencekelellgiELPVPETPIPRITYDEAIE-------------ILK---- 292

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  759 iiEKSDEFKEkyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgkllGEDVATEvadkfd 838
Cdd:PRK05159   293 --SKGNEISW---------------------------------------------------------GDDLDTE------ 307

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  839 lEEndllflgigskvetrELLGRIrldyqdflvenakIKKPNDFRFLWVIDFPLFERnretnqlesvhhPF-TLPHSDDL 917
Cdd:PRK05159   308 -GE---------------RLLGEY-------------VKEEYGSDFYFITDYPSEKR------------PFyTMPDEDDP 346

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  918 EnfatscenlesiRSQAYDLVLNGQEVGGGSIRIHDRDMQhfiLEQILK--IPHDHLSHLLSALESGCPPHGGIALGLDR 995
Cdd:PRK05159   347 E------------ISKSFDLLFRGLEITSGGQRIHRYDML---VESIKEkgLNPESFEFYLEAFKYGMPPHGGFGLGLER 411

                          570       580
                   ....*....|....*....|....*.
gi 1834199288  996 LIAILCRARSIRDVIAFPkslngRDP 1021
Cdd:PRK05159   412 LTMKLLGLENIREAVLFP-----RDR 432
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
 599-1014 1.72e-54

Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It 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. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238358 [Multi-domain]  Cd Length: 269  Bit Score: 191.15  E-value: 1.72e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  599 LRLRSAVIMKMREYLINYlGFVEVETPTLFRRTPG-GAQEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCY 677
Cdd:cd00669      1 FKVRSKIIKAIRDFMDDR-GFLEVETPMLQKITGGaGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  678 RDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSW--------------PKDFPRlqtPFRRITYEEAMEKYGNd 743
Cdd:cd00669     80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLArevlgvtavtygfeLEDFGL---PFPRLTYREALERYGQ- 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  744 kpdtrfgfllnnvseiieksdefkekyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgk 823
Cdd:cd00669        --------------------------------------------------------------------------------

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  824 llgedvatevadkfdleendllflgigskvetrellgrirldyqdflvenakikkpndfrFLWVIDFPLFernretnqle 903
Cdd:cd00669    156 ------------------------------------------------------------PLFLTDYPAE---------- 165

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  904 sVHHPFTLPHSDDLEnfatscenlesiRSQAYDLVLNGQEVGGGSIRIHDRDMQ-HFILEQIL--KIPHDHLSHLLSALE 980
Cdd:cd00669    166 -MHSPLASPHDVNPE------------IADAFDLFINGVEVGNGSSRLHDPDIQaEVFQEQGInkEAGMEYFEFYLKALE 232

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1834199288  981 SGCPPHGGIALGLDRLIAILCRARSIRDVIAFPK 1014
Cdd:cd00669    233 YGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 462-595 3.22e-54

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 185.03  E-value: 3.22e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLEFQRMN---KFFILRDAYGQTQVLLSPKTYGLEEYAETgVPIESIVRVEGTVIPRPA 538
Cdd:cd04317      1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEFELAEK-LRNESVIQVTGKVRARPE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199288  539 ATINPKMQTGHVEVEADKVVVLNPAkKNLPFEIRKFNRAGERLRLTHRYLDLRFNDM 595
Cdd:cd04317     80 GTVNPKLPTGEIEVVASELEVLNKA-KTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 462-1021 1.92e-49

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


Pssm-ID: 439788 [Multi-domain]  Cd Length: 430  Bit Score: 181.79  E-value: 1.92e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  462 RTHNCGELTSNDINEKVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTygLEEYAE-TGVPIESIVRVEGTVIPRP 537
Cdd:COG0017      1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGgisFLILRDGSGFIQVVVKKDK--LENFEEaKKLTTESSVEVTGTVVESP 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  538 AAtinPkmqtGHVEVEADKVVVLNPAKKNLPFEIrkfNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyL 617
Cdd:COG0017     79 RA---P----QGVELQAEEIEVLGEADEPYPLQP---KRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQE-R 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  618 GFVEVETPTLfrrTP----GGAQEFVVP--TRKAghfySLVQSPQQFKQMLMsGGIDRYFQVARCYRDEATRPDRQ-PEF 690
Cdd:COG0017    148 GFVEVHTPII---TAsateGGGELFPVDyfGKEA----YLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRRHlAEF 219

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  691 TQLDIELSFTSRDDIMQLIEETLRY--------------SWPKDFPRLQ----TPFRRITYEEAMekygndkpdtrfgfl 752
Cdd:COG0017    220 WMIEPEMAFADLEDVMDLAEEMLKYiikyvlencpeeleFLGRDVERLEkvpeSPFPRITYTEAI--------------- 284

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  753 lnnvsEIIEKSDEfKEKY-DDLGayaivvraSEAfwngaarkhyEslgkefkgtlfvrkfgptkdvqeklgKLLGEDVat 831
Cdd:COG0017    285 -----EILKKSGE-KVEWgDDLG--------TEH----------E--------------------------RYLGEEF-- 312

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  832 evadkFDleendllflgigskvetrellgrirldyqdflvenakikkpndfRFLWVIDFPLFERnretnqlesvhhPF-T 910
Cdd:COG0017    313 -----FK--------------------------------------------KPVFVTDYPKEIK------------AFyM 331

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  911 LPHSDDLEnfatscenlesiRSQAYDLVLNGQ-EVGGGSIRIHDRDMqhfiLEQILK---IPHDHLSHLLSALESGCPPH 986
Cdd:COG0017    332 KPNPDDPK------------TVAAFDLLAPGIgEIIGGSQREHRYDV----LVERIKekgLDPEDYEWYLDLRRYGSVPH 395

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1834199288  987 GGIALGLDRLIAILCRARSIRDVIAFPkslngRDP 1021
Cdd:COG0017    396 AGFGLGLERLVMWLTGLENIREVIPFP-----RDP 425
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 291-410 7.24e-33

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 123.79  E-value: 7.24e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  291 RDLTCNDLRRDDVGKTVTLVGWIPSTKNN---KFLQLKDGYGQTQLMIEDQSLS--DTFLSTPEQTVIQIVGKVLGRPKA 365
Cdd:cd04317      1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPefELAEKLRNESVIQVTGKVRARPEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1834199288  366 NVNLKYDTGEVEVSVTSVKVLNPDDP----YDGPIKAKE-KKQKFSIDDL 410
Cdd:cd04317     81 TVNPKLPTGEIEVVASELEVLNKAKTlpfeIDDDVNVSEeLRLKYRYLDL 130
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
 576-1021 4.84e-32

Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238399 [Multi-domain]  Cd Length: 322  Bit Score: 127.68  E-value: 4.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  576 RAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLFRR-TPGGAQEFVVP--TRKAghfYsLV 652
Cdd:cd00776      1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRE-NGFTEVHTPKITSTdTEGGAELFKVSyfGKPA---Y-LA 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  653 QSPQQFKQMLMsGGIDRYFQVARCYRDEATRPDRQ-PEFTQLDIELSF-TSRDDIMQLIEETLRYSW------------- 717
Cdd:cd00776     76 QSPQLYKEMLI-AALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFiEDYNEVMDLIEELIKYIFkrvlercakelel 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  718 ----PKDFPRLQTPFRRITYEEAMEkygndkpdtrfgfLLNnvseiiEKSDEFKEKY-DDLGAyaivvrASEafwngaar 792
Cdd:cd00776    155 vnqlNRELLKPLEPFPRITYDEAIE-------------LLR------EKGVEEEVKWgEDLST------EHE-------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  793 khyeslgkefkgtlfvrkfgptkdvqeklgKLLGEDVATevadkfdleendllflgigskvetrellgrirldyqdflve 872
Cdd:cd00776    202 ------------------------------RLLGEIVKG----------------------------------------- 210

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  873 nakikkpndfRFLWVIDFPLFERnretnqlesvhhPFTLPHSDDLENfatscenlesiRSQAYDLVLNG-QEVGGGSIRI 951
Cdd:cd00776    211 ----------DPVFVTDYPKEIK------------PFYMKPDDDNPE-----------TVESFDLLMPGvGEIVGGSQRI 257

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834199288  952 HDRDMqhfiLEQILK---IPHDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPkslngRDP 1021
Cdd:cd00776    258 HDYDE----LEERIKehgLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP-----RDP 321
PLN02850 PLN02850
aspartate-tRNA ligase
 467-1026 1.04e-30

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 128.29  E-value: 1.04e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  467 GELTSNDINEKVVICGWLEFQRM---NKFFILRDAYGQTQVLLSPK----TYGLEEYAeTGVPIESIVRVEGTVIpRPAA 539
Cdd:PLN02850    73 SDLGEELAGSEVLIRGRVHTIRGkgkSAFLVLRQSGFTVQCVVFVSevtvSKGMVKYA-KQLSRESVVDVEGVVS-VPKK 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  540 TInpKMQTGHVEVEADKVVVLNPAKKNLPFEI-----------------RKFNRAGERLRLTHRYLDLRFNDMQHNLRLR 602
Cdd:PLN02850   151 PV--KGTTQQVEIQVRKIYCVSKALATLPFNVedaarseseiekalqtgEQLVRVGQDTRLNNRVLDLRTPANQAIFRIQ 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  603 SAVIMKMREYLINYlGFVEVETPTLFrrtpGGAQE---FVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRD 679
Cdd:PLN02850   229 SQVCNLFREFLLSK-GFVEIHTPKLI----AGASEggsAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRA 303

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  680 EATRPDRQ-PEFTQLDIELSFTSR-DDIMQLIEE-------TLRYSWPKDFPRL--QTPFR---------RITYEEAMEk 739
Cdd:PLN02850   304 EDSFTHRHlCEFTGLDLEMEIKEHySEVLDVVDElfvaifdGLNERCKKELEAIreQYPFEplkylpktlRLTFAEGIQ- 382

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  740 ygndkpdtrfgfLLNNVSEIIeksdefkEKYDDLgayaivvraseafwNGAARKhyeslgkefkgtlfvrkfgptkdvqe 819
Cdd:PLN02850   383 ------------MLKEAGVEV-------DPLGDL--------------NTESER-------------------------- 403

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  820 KLGKLLGEDVATevadkfdleendllflgigskvetrellgrirldyqdflvenakikkpnDFRFLWviDFPLFERnret 899
Cdd:PLN02850   404 KLGQLVKEKYGT-------------------------------------------------DFYILH--RYPLAVR---- 428

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  900 nqlesvhhPF-TLPHSDDlenfatscenleSIRSQAYDLVLNGQEVGGGSIRIHDRDmqhfILEQILK---IPHDHLSHL 975
Cdd:PLN02850   429 --------PFyTMPCPDD------------PKYSNSFDVFIRGEEIISGAQRVHDPE----LLEKRAEecgIDVKTISTY 484

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834199288  976 LSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPkslngRDPLSNAP 1026
Cdd:PLN02850   485 IDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP-----RDPQRLAP 530
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
 422-1026 2.13e-29

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 124.72  E-value: 2.13e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  422 NLTSNNGESTEDSAEASTTANASLIAEQRAKVAD----TNKFAD---------------RTH-NCGELTSNDINEKVV-I 480
Cdd:PTZ00401     4 NHADAGAPAVEKKQSDKEARKAARLAEEKARAAEkaalVEKYKDvfgaapmvqsttyksRTFiPVAVLSKPELVDKTVlI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  481 CGWLEFQRMN---KFFILRDAYGQTQVLLSPKTYGLEEYAE--TGVPIESIVRVEGTViprpAATINPKMQTGH--VEVE 553
Cdd:PTZ00401    84 RARVSTTRKKgkmAFMVLRDGSDSVQAMAAVEGDVPKEMIDfiGQIPTESIVDVEATV----CKVEQPITSTSHsdIELK 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  554 ADKVVVLNPAKKNLPFEI----RKFNRAGERL----RLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINYlGFVEVETP 625
Cdd:PTZ00401   160 VKKIHTVTESLRTLPFTLedasRKESDEGAKVnfdtRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDS-DFCEIHSP 238

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  626 TLFRR-TPGGAQEFvvptrKAGHFYS---LVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQ-PEFTQLDIELSFT 700
Cdd:PTZ00401   239 KIINApSEGGANVF-----KLEYFNRfayLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRIN 313

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  701 SR-DDIMQLIEETLRYSwpkdFPRL------------QTPFRRITYE---EAMEKYGndkpdtrfgflLNNVSEIIEKSD 764
Cdd:PTZ00401   314 EHyYEVLDLAESLFNYI----FERLathtkelkavcqQYPFEPLVWKltpERMKELG-----------VGVISEGVEPTD 378

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  765 EFKEKYDDLGAYAIvvraseafwngaaRKHYESLgKEFKGTLFVRKFGPTKDVQEKLGKLLGEDVatevadkfdleendl 844
Cdd:PTZ00401   379 KYQARVHNMDSRML-------------RINYMHC-IELLNTVLEEKMAPTDDINTTNEKLLGKLV--------------- 429

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  845 lflgigskvetRELLGrirldyQDFLVENAkikkpndfrflwvidFPlfernretnqleSVHHPF-TLPHSDDlENFATS 923
Cdd:PTZ00401   430 -----------KERYG------TDFFISDR---------------FP------------SSARPFyTMECKDD-ERFTNS 464

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  924 cenlesirsqaYDLVLNGQEVGGGSIRIHDRDMqhfILE--QILKIPHDHLSHLLSALESGCPPHGGIALGLDRLIAILC 1001
Cdd:PTZ00401   465 -----------YDMFIRGEEISSGAQRIHDPDL---LLAraKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYL 530

                          650       660
                   ....*....|....*....|....*
gi 1834199288 1002 RARSIRDVIAFPkslngRDPLSNAP 1026
Cdd:PTZ00401   531 GLSNVRLASLFP-----RDPQRTTP 550
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
 457-1013 1.06e-22

Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440803 [Multi-domain]  Cd Length: 495  Bit Score: 103.19  E-value: 1.06e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  457 NKFaDRTHNCGELTSN--------DINEKVVICGWLEFQR-MNK--FFILRDAYGQTQVLLSPKTYGLEEYAE-TGVPIE 524
Cdd:COG1190     31 NKF-PRTHTAAEIREKydeleaeeETGDEVSVAGRIMAKRdMGKasFADLQDGSGRIQLYLRRDELGEEAYELfKLLDLG 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  525 SIVRVEGTVIprpaatinpKMQTGHVEVEADKVVVLNPAKKNLPFEIRKFNRAGERLRltHRYLDLRFN-DMQHNLRLRS 603
Cdd:COG1190    110 DIVGVEGTVF---------RTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYR--QRYVDLIVNpEVRETFRKRS 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  604 AVIMKMREYLINyLGFVEVETPTLfRRTPGGA--QEFVvpTrkagHFYSLVQ------SPQQFKQMLMSGGIDRYFQVAR 675
Cdd:COG1190    179 KIIRAIRRFLDE-RGFLEVETPML-QPIAGGAaaRPFI--T----HHNALDMdlylriAPELYLKRLIVGGFERVFEIGR 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  676 CYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK--------------DFprlQTPFRRITYEEAMEKYG 741
Cdd:COG1190    251 NFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAvlgttkvtyqgqeiDL---SPPWRRITMVEAIKEAT 327

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  742 NDKPDTrfgfllnnvseiiEKSDEfkekyddlgayaivvraseafwngAARKHYESLGKEFKGTlfvrkfgptkdvqEKL 821
Cdd:COG1190    328 GIDVTP-------------LTDDE------------------------ELRALAKELGIEVDPG-------------WGR 357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  822 GKLLgedvatevadkfdleenDLLFlgigskvetrellgrirldyqDFLVEnAKIKKPndfrfLWVIDFPLfernrETnq 901
Cdd:COG1190    358 GKLI-----------------DELF---------------------EELVE-PKLIQP-----TFVTDYPV-----EV-- 386

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  902 leSvhhPFTLPHSDDlENFAtscenlesirsQAYDLVLNGQEVGGG-S-----IRIHDRdmqhFiLEQILK--------- 966
Cdd:COG1190    387 --S---PLAKRHRDD-PGLT-----------ERFELFIAGREIANAfSelndpIDQRER----F-EEQLELkaagddeam 444

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1834199288  967 -IPHDhlshLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 1013
Cdd:COG1190    445 pMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
 445-1013 1.51e-22

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 102.86  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  445 LIAEQRAKVAD---------TNKFaDRTHNCGELTSN----------DINEKVVICGWLEFQR-MNK--FFILRDAYGQT 502
Cdd:PRK00484     6 QIAVRREKLAElreqgidpyPNKF-ERTHTAAELRAKyddkekeeleELEIEVSVAGRVMLKRvMGKasFATLQDGSGRI 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  503 QVLLSPKTYGLEEYAE-TGVPIESIVRVEGTVIprpaatinpKMQTGHVEVEADKVVVLNPAKKNLPfeiRKFnrAGER- 580
Cdd:PRK00484    85 QLYVSKDDVGEEALEAfKKLDLGDIIGVEGTLF---------KTKTGELSVKATELTLLTKSLRPLP---DKF--HGLTd 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  581 --LRLTHRYLDLRFN-DMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLfRRTPGG--AQEFVvpTrkagHFYSLVQ-- 653
Cdd:PRK00484   151 veTRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDN-RGFLEVETPML-QPIAGGaaARPFI--T----HHNALDIdl 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  654 ----SPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK---------- 719
Cdd:PRK00484   223 ylriAPELYLKRLIVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAvlgttkvtyq 302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  720 ----DFprlQTPFRRITYEEAMEKYgndkpdTRFGFLLNNVSEIIEKSDEFKEKYDDlgayaivvraseafwngaarkhy 795
Cdd:PRK00484   303 gteiDF---GPPFKRLTMVDAIKEY------TGVDFDDMTDEEARALAKELGIEVEK----------------------- 350

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  796 eslgkefkgtlfvrkfgptkdvQEKLGKLLgedvatevadkfdleenDLLFlgigskvetrellgrirldyqDFLVEnAK 875
Cdd:PRK00484   351 ----------------------SWGLGKLI-----------------NELF---------------------EEFVE-PK 369

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  876 IKKPNdFrflwVIDFPLfernrETNqlesvhhPFTLPHSDDlENFAtscenlesirsQAYDLVLNGQEVGGG------SI 949
Cdd:PRK00484   370 LIQPT-F----ITDYPV-----EIS-------PLAKRHRED-PGLT-----------ERFELFIGGREIANAfselndPI 420

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834199288  950 RIHDRdmqhFiLEQILK----------IPHDhlshLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 1013
Cdd:PRK00484   421 DQRER----F-EAQVEAkeagddeamfMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
Asp_Lys_Asn_RS_N cd04100
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ...
 477-562 1.27e-20

Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239766 [Multi-domain]  Cd Length: 85  Bit Score: 87.24  E-value: 1.27e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  477 KVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTYGLEEYAETGVPIESIVRVEGTVIPRPAatinPKMQTGHVEVE 553
Cdd:cd04100      1 EVTLAGWVHSRRDHGgliFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQ 76


                   ....*....
gi 1834199288  554 ADKVVVLNP 562
Cdd:cd04100     77 AEELEVLSK 85
PLN02502 PLN02502
lysyl-tRNA synthetase
 425-1013 6.89e-20

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 95.06  E-value: 6.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  425 SNNGESTEDSAEASTTAN-ASLIAEQRAKvaDTNKFA---DRTHNCGEL------TSN---DINEKVVICGWLEFQR-MN 490
Cdd:PLN02502    47 KSAAADDETMDPTQYRANrLKKVEALRAK--GVEPYPykfDVTHTAPELqekygsLENgeeLEDVSVSVAGRIMAKRaFG 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  491 K--FFILRDAYGQTQVLLSPKTYGLEEYA----ETGVPIESIVRVEGTViprpaatinPKMQTGHVEVEADKVVVLNPAK 564
Cdd:PLN02502   125 KlaFYDLRDDGGKIQLYADKKRLDLDEEEfeklHSLVDRGDIVGVTGTP---------GKTKKGELSIFPTSFEVLTKCL 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  565 KNLPFEIRKFNRAGERLRltHRYLDLRFN-DMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLfRRTPGG--AQEFVVp 641
Cdd:PLN02502   196 LMLPDKYHGLTDQETRYR--QRYLDLIANpEVRDIFRTRAKIISYIRRFLDD-RGFLEVETPML-NMIAGGaaARPFVT- 270

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  642 trkagHFYSLVQ------SPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRY 715
Cdd:PLN02502   271 -----HHNDLNMdlylriATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSG 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  716 SwpkdfprlqtpfrrityeeAMEKYGNdkpdtrfgfllnnvseiieksdeFKEKYddlGAYAIvvraseafwngaarkhy 795
Cdd:PLN02502   346 M-------------------VKELTGS-----------------------YKIKY---HGIEI----------------- 363

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  796 eSLGKEFkgtlfvRKFGPTKDVQEKLGKLLGEDVATEVADKF--DLEENDllflgiGSKVETRELLGRIrLD--YQDFLV 871
Cdd:PLN02502   364 -DFTPPF------RRISMISLVEEATGIDFPADLKSDEANAYliAACEKF------DVKCPPPQTTGRL-LNelFEEFLE 429

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  872 EnaKIKKPNdfrflWVIDFPlfernretnQLESvhhPFTLPHsddlenfatscenlesiRSQA-----YDLVLNGQEVGG 946
Cdd:PLN02502   430 E--TLVQPT-----FVLDHP---------VEMS---PLAKPH-----------------RSKPglterFELFINGRELAN 473

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199288  947 GSIRIHDRDMQHFILEQILKiphDHLS----------HLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 1013
Cdd:PLN02502   474 AFSELTDPVDQRERFEEQVK---QHNAgddeamaldeDFCTALEYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
 597-1013 4.08e-19

Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238398 [Multi-domain]  Cd Length: 329  Bit Score: 89.95  E-value: 4.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  597 HNLRLRSAVIMKMREYLINyLGFVEVETPTLfRRTPGGA--QEFVVPTRKAG-HFYsLVQSPQQFKQMLMSGGIDRYFQV 673
Cdd:cd00775      6 QTFIVRSKIISYIRKFLDD-RGFLEVETPML-QPIAGGAaaRPFITHHNALDmDLY-LRIAPELYLKRLIVGGFERVYEI 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  674 ARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRY-------SWPKDFPRLQT----PFRRITYEEAMEKY-G 741
Cdd:cd00775     83 GRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGlvkkingKTKIEYGGKELdftpPFKRVTMVDALKEKtG 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  742 NDKPDTRfgfllnnvseiIEKSDEFKEKYDDLGAyaivvraseafwngaarKHYEslgkefkgtlfvrkfgptkdVQEKL 821
Cdd:cd00775    163 IDFPELD-----------LEQPEELAKLLAKLIK-----------------EKIE--------------------KPRTL 194

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  822 GKLLgedvatevadkfdleenDLLFlgiGSKVEtrellgrirldyqdflvenAKIKKPNdfrflWVIDF-----PLFERN 896
Cdd:cd00775    195 GKLL-----------------DKLF---EEFVE-------------------PTLIQPT-----FIIDHpveisPLAKRH 230

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  897 RETNQLesvhhpftlphsddlenfatsCENLEsirsqaydLVLNGQEVGGGSIRIHDRDMQHFILEQILKIPH--DHLSH 974
Cdd:cd00775    231 RSNPGL---------------------TERFE--------LFICGKEIANAYTELNDPFDQRERFEEQAKQKEagDDEAM 281

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....
gi 1834199288  975 L-----LSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 1013
Cdd:cd00775    282 MmdedfVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
 445-1013 5.12e-18

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 88.97  E-value: 5.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  445 LIAEQRAKVADTNKF-----ADRTHNCGELTSND----INEKVVICGWLEFQR-MNK--FFILRDAYGQTQVLLS----P 508
Cdd:PRK12445    26 LAALRQQGVAFPNDFrrdhtSDQLHEEFDAKDNQelesLNIEVSVAGRMMTRRiMGKasFVTLQDVGGRIQLYVArdslP 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  509 KTYGLEEYAETGvpIESIVRVEGTVIprpaatinpKMQTGHVEVEADKVVVLNPAKKNLPFEIRKFNraGERLRLTHRYL 588
Cdd:PRK12445   106 EGVYNDQFKKWD--LGDIIGARGTLF---------KTQTGELSIHCTELRLLTKALRPLPDKFHGLQ--DQEVRYRQRYL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  589 DLRFND-MQHNLRLRSAVIMKMREYLINYlGFVEVETPtLFRRTPGG--AQEFVVPTRKAGHFYSLVQSPQQFKQMLMSG 665
Cdd:PRK12445   173 DLIANDkSRQTFVVRSKILAAIRQFMVAR-GFMEVETP-MMQVIPGGasARPFITHHNALDLDMYLRIAPELYLKRLVVG 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  666 GIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLR-----------YSWPKDFPRLQTPFRRITYE 734
Cdd:PRK12445   251 GFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRtlaqevlgttkVTYGEHVFDFGKPFEKLTMR 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  735 EAMEKYgndKPDTRFGFLlnnvseiieksDEFKekyddlgayaivvraseafwngAARKHYESLGKEFKgtlfvRKFGpt 814
Cdd:PRK12445   331 EAIKKY---RPETDMADL-----------DNFD----------------------AAKALAESIGITVE-----KSWG-- 367

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  815 kdvqekLGKLLGEdVATEVADKFDLEENDLlflgigskvetrellgrirldyQDFLVENAKIKKPNDFRFLWVIDFPLFE 894
Cdd:PRK12445   368 ------LGRIVTE-IFDEVAEAHLIQPTFI----------------------TEYPAEVSPLARRNDVNPEITDRFEFFI 418

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  895 RNRETNQlesvhhpfTLPHSDDLENfatscenlesiRSQAYDLVLNGQEVGGGSIRIHDRDMqhfileqilkiphdhlsh 974
Cdd:PRK12445   419 GGREIGN--------GFSELNDAED-----------QAERFQEQVNAKAAGDDEAMFYDEDY------------------ 461

                          570       580       590
                   ....*....|....*....|....*....|....*....
gi 1834199288  975 lLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 1013
Cdd:PRK12445   462 -VTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
Asp_Lys_Asn_RS_N cd04100
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ...
 306-388 1.41e-14

Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239766 [Multi-domain]  Cd Length: 85  Bit Score: 69.90  E-value: 1.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  306 TVTLVGWIPSTKNNK---FLQLKDGYGQTQLMIEDQSLSDTFL---STPEQTVIQIVGKVLGRPKANvnlkYDTGEVEVS 379
Cdd:cd04100      1 EVTLAGWVHSRRDHGgliFIDLRDGSGIVQVVVNKEELGEFFEeaeKLRTESVVGVTGTVVKRPEGN----LATGEIELQ 76


                   ....*....
gi 1834199288  380 VTSVKVLNP 388
Cdd:cd04100     77 AEELEVLSK 85
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 601-728 3.86e-14

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: 72.54  E-value: 3.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  601 LRSAVIMKMREYLiNYLGFVEVETP-----TLFRRTPGGAQEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGI----DRYF 671
Cdd:cd00768      1 IRSKIEQKLRRFM-AELGFQEVETPiverePLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834199288  672 QVARCYRDEATR--PDRQPEFTQLDIELSFTSRDDI------MQLIEETLRYSWPKD--FPRLQTPF 728
Cdd:cd00768     80 EIGPAFRNEGGRrgLRRVREFTQLEGEVFGEDGEEAsefeelIELTEELLRALGIKLdiVFVEKTPG 146
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
 544-762 4.18e-14

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 76.59  E-value: 4.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  544 KMQTGHVEVEADKVVVLNPAKKNLPFeirKFNRAGERLRLTHRYLDLRFND-MQHNLRLRSAVIMKMREYLiNYLGFVEV 622
Cdd:PTZ00417   200 KSKKGELSIFPKETIILSPCLHMLPM---KYGLKDTEIRYRQRYLDLMINEsTRSTFITRTKIINYLRNFL-NDRGFIEV 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  623 ETPTLfRRTPGGA--QEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFT 700
Cdd:PTZ00417   276 ETPTM-NLVAGGAnaRPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYA 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  701 SRDDIMQLIEE-----------TLRYSWPKDFPRLQ-------TPFRRITYEEAMEKYGNDKPDTRFgfllnNVSEIIEK 762
Cdd:PTZ00417   355 DFYDLIKWSEDffsqlvmhlfgTYKILYNKDGPEKDpieidftPPYPKVSIVEELEKLTNTKLEQPF-----DSPETINK 429
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 469-775 1.11e-13

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 74.76  E-value: 1.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  469 LTSNDINEKVVICGWLEFQRMNK---FFILRD--AYGQTQVLLSPktyGLEEYAE-TGVPIESIVRVEGTVIPRPAATin 542
Cdd:PRK03932    10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDgsCFKQLQVVKDN---GEEYFEEiKKLTTGSSVIVTGTVVESPRAG-- 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  543 pkmqtGHVEVEADKVVVLNPAKKNLPfeIRKfNRAG-ERLRlTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINYlGFVE 621
Cdd:PRK03932    85 -----QGYELQATKIEVIGEDPEDYP--IQK-KRHSiEFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNEN-GFVW 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  622 VETPTLfrrTP----GGAQEFVVPT-----------RKAghfySLVQSPQ-QFKQMLMSGGidRYFQVARCYRDEATRPD 685
Cdd:PRK03932   155 VDTPII---TAsdceGAGELFRVTTldldfskdffgKEA----YLTVSGQlYAEAYAMALG--KVYTFGPTFRAENSNTR 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  686 RQ-PEFTQLDIELSFTSRDDIMQLIEETLRY-------------------SWPKDFPRLQ----TPFRRITYEEAMekyg 741
Cdd:PRK03932   226 RHlAEFWMIEPEMAFADLEDNMDLAEEMLKYvvkyvlencpddleflnrrVDKGDIERLEnfieSPFPRITYTEAI---- 301

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1834199288  742 ndkpdtrfgfllnnvsEIIEKSD---EFKEKY-DDLGA 775
Cdd:PRK03932   302 ----------------EILQKSGkkfEFPVEWgDDLGS 323
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
 544-745 1.65e-13

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 75.07  E-value: 1.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  544 KMQTGHVEVEADKVVVLNP---AKKNLPFEIRKFNRAGERlRLTHRYldlRFNDMQHN------LRLRSAVIMKMREYLi 614
Cdd:PTZ00385   173 RMQRGELSVAASRMLILSPyvcTDQVVCPNLRGFTVLQDN-DVKYRY---RFTDMMTNpcvietIKKRHVMLQALRDYF- 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  615 NYLGFVEVETPTLFRRTPGG-AQEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQL 693
Cdd:PTZ00385   248 NERNFVEVETPVLHTVASGAnAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSC 327

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834199288  694 DIELSFTSRDDIMQLIEETLRY------------SWPKD---FPR---LQTPFRRIT-YEEAMEKYGNDKP 745
Cdd:PTZ00385   328 EFYAAYHTYEDLMPMTEDIFRQlamrvngttvvqIYPENahgNPVtvdLGKPFRRVSvYDEIQRMSGVEFP 398
PRK06462 PRK06462
asparagine synthetase A; Reviewed
 594-738 8.06e-13

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 71.20  E-value: 8.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  594 DMQHNLRLRSAVIMKMREYLINYlGFVEVETPTLFRRT----PGGAQEFVVPTRKA--GHFYSLVQSPQQFKQML--MSG 665
Cdd:PRK06462    25 KYRKVLKVQSSILRYTREFLDGR-GFVEVLPPIISPSTdplmGLGSDLPVKQISIDfyGVEYYLADSMILHKQLAlrMLG 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  666 GIdryFQVARCYRDEATRPDRQP---EFTQLDIELSFTSRDDIMQLIEETLRY--------------SWPKDFPRLQTPF 728
Cdd:PRK06462   104 KI---FYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYlvkelleehedeleFFGRDLPHLKRPF 180

                          170
                   ....*....|
gi 1834199288  729 RRITYEEAME 738
Cdd:PRK06462   181 KRITHKEAVE 190
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
461-1013 3.35e-12

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 71.15  E-value: 3.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  461 DRTHNCGELTSNDINEKVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTYGLEEYAE--TGVPIESIVRVEGTVIp 535
Cdd:PRK02983   637 PPTHTVAEALDAPTGEEVSVSGRVLRIRDYGgvlFADLRDWSGELQVLLDASRLEQGSLADfrAAVDLGDLVEVTGTMG- 715

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  536 rpaatinpKMQTGHVEVEADKVVV----LNPakknLPFEIRKFNRAGERLRLthRYLDLRFN-DMQHNLRLRSAVIMKMR 610
Cdd:PRK02983   716 --------TSRNGTLSLLVTSWRLagkcLRP----LPDKWKGLTDPEARVRQ--RYLDLAVNpEARDLLRARSAVVRAVR 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  611 EYLINyLGFVEVETPTLfRRTPGGA--QEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQP 688
Cdd:PRK02983   782 ETLVA-RGFLEVETPIL-QQVHGGAnaRPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNP 859

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  689 EFTQLDIELSFTSRDDIMQLIEETLRyswpkdfprlqtpfrrityEEAMEKYGndKPdtrfgfllnnvseiieksdefke 768
Cdd:PRK02983   860 EFTLLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHG--AP----------------------- 895

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  769 kyddlgayaIVVRASeafwnGAARKHYESLGKEFkgtlfvrkfgPTKDVQEKLGKLLGE--DVATEVADKFDLEENdllf 846
Cdd:PRK02983   896 ---------VVMRPD-----GDGVLEPVDISGPW----------PVVTVHDAVSEALGEeiDPDTPLAELRKLCDA---- 947

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  847 LGIgsKVETRELLGRIRLDYQDFLVENAkIKKPNdfrflWVIDFPLfernrETNqlesvhhPFTLPHSDD--Lenfatsc 924
Cdd:PRK02983   948 AGI--PYRTDWDAGAVVLELYEHLVEDR-TTFPT-----FYTDFPT-----SVS-------PLTRPHRSDpgL------- 1000

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  925 enlesirSQAYDLVLNGQEVGGGSIRIHDRDMQHFIL-EQILK----------IPHDhlshLLSALESGCPPHGGIALGL 993
Cdd:PRK02983  1001 -------AERWDLVAWGVELGTAYSELTDPVEQRRRLtEQSLLaaggdpeameLDED----FLQALEYAMPPTGGLGMGV 1069

                          570       580
                   ....*....|....*....|
gi 1834199288  994 DRLIaILCRARSIRDVIAFP 1013
Cdd:PRK02983  1070 DRLV-MLLTGRSIRETLPFP 1088
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 148-303 3.55e-12

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 64.85  E-value: 3.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  148 CGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVlEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNSC 224
Cdd:cd04317      5 CGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYG-IVQVVF-DPEEAPEFELAEKLRNESVIQVTGKVRARPEGTV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  225 NQTMPTGEIEVEVQD--ILN----IHFPAggtkragdkrtystmvqqqsnlgitstEYKIAKNENI-LKYfenRDLtcnD 297
Cdd:cd04317     83 NPKLPTGEIEVVASEleVLNkaktLPFEI---------------------------DDDVNVSEELrLKY---RYL---D 129


                   ....*.
gi 1834199288  298 LRRDDV 303
Cdd:cd04317    130 LRRPKM 135
genX TIGR00462
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ...
 618-1011 3.85e-10

EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous to the C-terminal region of lysyl-tRNA synthetase (LysS). Multiple sequence alignment of these proteins with the homologous regions of collected LysS proteins shows that these proteins form a distinct set rather than just similar truncations of LysS. The protein is termed GenX after its designation in E. coli. Interestingly, genX often is located near a homolog of lysine-2,3-aminomutase. Its function is unknown. [Unknown function, General]


Pssm-ID: 273090 [Multi-domain]  Cd Length: 290  Bit Score: 62.18  E-value: 3.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  618 GFVEVETPTLfrrTPGGAQE---------FVVPTRKAGHFYsLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQP 688
Cdd:TIGR00462    6 GVLEVETPLL---SPAPVTDphldafateFVGPDGQGRPLY-LQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHNP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  689 EFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPrlqtPFRRITYEEAMEKYGNDKPDTrfgfllnnvseiiEKSDEFKE 768
Cdd:TIGR00462   82 EFTMLEWYRPGFDYHDLMDEVEALLQELLGDPFA----PAERLSYQEAFLRYAGIDPLT-------------ASLAELQA 144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  769 KYDDLGayaiVVRASEAFWNgaarkhyeslgkefkgTLFvrkfgptkdvqeklgkllgedvatevadkfdleenDLLFLg 848
Cdd:TIGR00462  145 AAAAHG----IRASEEDDRD----------------DLL-----------------------------------DLLFS- 168

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  849 igSKVETRelLGRIRLdyqdflvenakikkpndfrfLWVIDFP-----LFErnretnqlesvhhpftlPHSDDlENFAts 923
Cdd:TIGR00462  169 --EKVEPH--LGFGRP--------------------TFLYDYPasqaaLAR-----------------ISPDD-PRVA-- 204

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  924 cENLEsirsqaydLVLNGQEVGGGSIRIHDRDMQ--HFILEQILK-------IPHDhlSHLLSALESGCPPHGGIALGLD 994
Cdd:TIGR00462  205 -ERFE--------LYIKGLELANGFHELTDAAEQrrRFEADNALRkalglprYPLD--ERFLAALEAGLPECSGVALGVD 273

                          410
                   ....*....|....*..
gi 1834199288  995 RLIAILCRARSIRDVIA 1011
Cdd:TIGR00462  274 RLLMLALGADSIDDVLA 290
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 148-242 1.86e-09

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 61.55  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  148 CGELRNHHCGLFVELSGRlikkrVNR--------FAELRDRNGgACQLVVLEDKHP---RVARRMNNmpEnTTLTIVGLV 216
Cdd:COG0173      7 CGELRESDVGQEVTLSGW-----VHRrrdhggliFIDLRDRYG-ITQVVFDPDDSAeafEKAEKLRS--E-YVIAVTGKV 77

                           90       100
                   ....*....|....*....|....*...
gi 1834199288  217 MRRPHNSCNQTMPTGEIEVEVQD--ILN 242
Cdd:COG0173     78 RARPEGTVNPKLPTGEIEVLASEleILN 105
PLN02903 PLN02903
aminoacyl-tRNA ligase
 128-242 2.01e-09

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 61.73  E-value: 2.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  128 SAMASNFNMNSQPPQPMR-QSCGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVLEDKHPRVARRMNN 203
Cdd:PLN02903    42 PVVSAVDSMSSQLTWPSRsHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTG-IVQVVTLPDEFPEAHRTANR 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1834199288  204 MPENTTLTIVGLVMRRPHNSCNQTMPTGEIEV--EVQDILN 242
Cdd:PLN02903   121 LRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVvaESVDILN 161
ND_PkAspRS_like_N cd04316
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ...
 464-571 8.41e-09

ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.


Pssm-ID: 239811 [Multi-domain]  Cd Length: 108  Bit Score: 54.24  E-value: 8.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  464 HNCGELTSNDINEKVVICGWLEFQR---MNKFFILRDAYGQTQVLLSPKTYGLEEYAET-GVPIESIVRVEGTVIPrpaa 539
Cdd:cd04316      1 HYSAEITPELDGEEVTVAGWVHEIRdlgGIKFVILRDREGIVQVTAPKKKVDKELFKTVrKLSRESVISVTGTVKA---- 76

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1834199288  540 tiNPKMQTGhVEVEADKVVVLNPAKKNLPFEI 571
Cdd:cd04316     77 --EPKAPNG-VEIIPEEIEVLSEAKTPLPLDP 105
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 144-242 1.10e-08

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 59.31  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  144 MR-QSCGELRNHHCGLFVELSGRlikkrVNR--------FAELRDRNGgACQLVVLEDKHP-RVARRMNNmpEnTTLTIV 213
Cdd:PRK00476     3 MRtHYCGELRESHVGQTVTLCGW-----VHRrrdhggliFIDLRDREG-IVQVVFDPDAEAfEVAESLRS--E-YVIQVT 73

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1834199288  214 GLVMRRPHNSCNQTMPTGEIEVEVQD--ILN 242
Cdd:PRK00476    74 GTVRARPEGTVNPNLPTGEIEVLASEleVLN 104
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 307-386 1.73e-08

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 52.24  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  307 VTLVGWIPSTKNNK----FLQLKDGYGQTQLMIEDQSLSDTFLSTPEQTVIQIVGKVlgrpkanvnLKYDTGEVEVSVTS 382
Cdd:pfam01336    1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKV---------KKRKGGELELVVEE 71


                   ....
gi 1834199288  383 VKVL 386
Cdd:pfam01336   72 IELL 75
Asp_Lys_Asn_RS_N cd04100
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ...
 160-240 2.94e-08

Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239766 [Multi-domain]  Cd Length: 85  Bit Score: 52.18  E-value: 2.94e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  160 VELSGRLIKKRVN---RFAELRDRnGGACQLVVLEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNscnqTMPTGEIEVE 236
Cdd:cd04100      2 VTLAGWVHSRRDHgglIFIDLRDG-SGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPEG----NLATGEIELQ 76


                   ....
gi 1834199288  237 VQDI 240
Cdd:cd04100     77 AEEL 80
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 478-560 1.71e-07

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 49.54  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  478 VVICGWLEFQRMNK----FFILRDAYGQTQVLLSPKTYglEEYAETgVPIESIVRVEGTVIPRPaatinpkmqTGHVEVE 553
Cdd:pfam01336    1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVFKEEA--EKLAKK-LKEGDVVRVTGKVKKRK---------GGELELV 68


                   ....*..
gi 1834199288  554 ADKVVVL 560
Cdd:pfam01336   69 VEEIELL 75
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
598-1009 2.11e-07

elongation factor P--(R)-beta-lysine ligase;


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 54.16  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  598 NLRLRSAVIMKMREYLINyLGFVEVETPTLFRRTPGGAQ------EFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYF 671
Cdd:PRK09350     4 NLLKRAKIIAEIRRFFAD-RGVLEVETPILSQATVTDIHlvpfetRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGPIF 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  672 QVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWpkdfprLQTPFRRITYEEAMEKYGNDKPdtrfgf 751
Cdd:PRK09350    83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL------DCEPAESLSYQQAFLRYLGIDP------ 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  752 LLNNVSEIIEKSDEFK--------EKYDDL--GAYAIVVRAseafwngaarkhyeSLGKEfKGTlFVRKFGPTkdvQEKL 821
Cdd:PRK09350   151 LSADKTQLREVAAKLGlsniadeeEDRDTLlqLLFTFGVEP--------------NIGKE-KPT-FVYHFPAS---QAAL 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  822 GKLLGEDvaTEVADKFdleenDLLFLGIgskvetrELlgrirldyqdflvenakikkPNDFRFLwvidfplfernreTNQ 901
Cdd:PRK09350   212 AKISTED--HRVAERF-----EVYFKGI-------EL--------------------ANGFHEL-------------TDA 244

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  902 LEsvhhpftlphsddlenfatscenlesirsqaydlvlngqevgggSIRIHDRDMQHFILEQILKIPHDHlsHLLSALES 981
Cdd:PRK09350   245 RE--------------------------------------------QRQRFEQDNRKRAARGLPQQPIDE--NLIAALEA 278

                          410       420
                   ....*....|....*....|....*...
gi 1834199288  982 GCPPHGGIALGLDRLIAILCRARSIRDV 1009
Cdd:PRK09350   279 GLPDCSGVALGVDRLIMLALGAESISEV 306
ND_PkAspRS_like_N cd04316
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ...
 296-391 2.43e-06

ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.


Pssm-ID: 239811 [Multi-domain]  Cd Length: 108  Bit Score: 47.31  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  296 NDLRRDDVGKTVTLVGWIPSTKN---NKFLQLKDGYGQTQLMIEDQSLSD----TFLSTPEQTVIQIVGKVLGRPKAnvn 368
Cdd:cd04316      4 AEITPELDGEEVTVAGWVHEIRDlggIKFVILRDREGIVQVTAPKKKVDKelfkTVRKLSRESVISVTGTVKAEPKA--- 80

                           90       100
                   ....*....|....*....|....*....
gi 1834199288  369 lkydTGEVEVSVTSVKVLN------PDDP 391
Cdd:cd04316     81 ----PNGVEIIPEEIEVLSeaktplPLDP 105
ScAspRS_mt_like_N cd04321
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
 477-561 5.45e-05

ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.


Pssm-ID: 239816 [Multi-domain]  Cd Length: 86  Bit Score: 42.69  E-value: 5.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  477 KVVICGWLEFQ-RMNK---FFILRDAYGQT-QVLLSPKTYGLEeyAETGVPIESIVRVEGTVIPRPAATinpKMQTGHVE 551
Cdd:cd04321      1 KVTLNGWIDRKpRIVKklsFADLRDPNGDIiQLVSTAKKDAFS--LLKSITAESPVQVRGKLQLKEAKS---SEKNDEWE 75

                           90
                   ....*....|
gi 1834199288  552 VEADKVVVLN 561
Cdd:cd04321     76 LVVDDIQTLN 85
AspRS_cyto_N cd04320
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
 477-571 7.48e-05

AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.


Pssm-ID: 239815 [Multi-domain]  Cd Length: 102  Bit Score: 42.94  E-value: 7.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  477 KVVICGWLEFQRM--NK--FFILRDAYGQTQVLLSPKTYGLEE----YAEtGVPIESIVRVEGTVIpRPAATINPKMQTG 548
Cdd:cd04320      1 EVLIRARVHTSRAqgAKlaFLVLRQQGYTIQGVLAASAEGVSKqmvkWAG-SLSKESIVDVEGTVK-KPEEPIKSCTQQD 78

                           90       100
                   ....*....|....*....|...
gi 1834199288  549 hVEVEADKVVVLNPAKKNLPFEI 571
Cdd:cd04320     79 -VELHIEKIYVVSEAAEPLPFQL 100
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 298-400 2.97e-04

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 44.71  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  298 LRRDDVGKTVTLVGWIPSTKNNK---FLQLKDGYGQTQLMIEDQSLSDTF---LSTPEQTVIQIVGKVLGRPKANvnlky 371
Cdd:PRK03932    10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDGSCFKQLQVVKDNGEEYFeeiKKLTTGSSVIVTGTVVESPRAG----- 84

                           90       100
                   ....*....|....*....|....*....
gi 1834199288  372 dtGEVEVSVTSVKVLNpDDPYDGPIKAKE 400
Cdd:PRK03932    85 --QGYELQATKIEVIG-EDPEDYPIQKKR 110
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 599-697 3.63e-04

Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine 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. 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. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.


Pssm-ID: 238396 [Multi-domain]  Cd Length: 261  Bit Score: 43.75  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  599 LRLRSAVIMKMREYLINYlGFVEVETPT-----LFRRTPGG--AQEFVVPTRKAGHFYSL------------VQSPQQFK 659
Cdd:cd00773      2 AALRRYIEDTLREVFERY-GYEEIDTPVfeyteLFLRKSGDevSKEMYRFKDKGGRDLALrpdltapvaravAENLLSLP 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1834199288  660 QMLmsggidRYFQVARCYRDEATRPDRQPEFTQLDIEL 697
Cdd:cd00773     81 LPL------KLYYIGPVFRYERPQKGRYREFYQVGVEI 112
ScAspRS_mt_like_N cd04321
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
 307-387 1.04e-03

ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.


Pssm-ID: 239816 [Multi-domain]  Cd Length: 86  Bit Score: 39.22  E-value: 1.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  307 VTLVGWIPST----KNNKFLQLKDGYGQT-QLMIEDQSLSDTFL-STPEQTVIQIVGKVLGRPKANvnlKYDTGEVEVSV 380
Cdd:cd04321      2 VTLNGWIDRKprivKKLSFADLRDPNGDIiQLVSTAKKDAFSLLkSITAESPVQVRGKLQLKEAKS---SEKNDEWELVV 78


                   ....*..
gi 1834199288  381 TSVKVLN 387
Cdd:cd04321     79 DDIQTLN 85
AsnRS_cyto_like_N cd04323
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ...
 306-386 8.67e-03

AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239818 [Multi-domain]  Cd Length: 84  Bit Score: 36.44  E-value: 8.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834199288  306 TVTLVGW---IPSTKNNKFLQLKDGYGQTQLMIEDQSLSDTFLS---TPEQTVIqIVGKVLGRPKAnvnlKYDTGEVEVS 379
Cdd:cd04323      1 RVKVFGWvhrLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAkslTQESSVE-VTGEVKEDPRA----KQAPGGYELQ 75


                   ....*..
gi 1834199288  380 VTSVKVL 386
Cdd:cd04323     76 VDYLEII 82
 
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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