|
Name |
Accession |
Description |
Interval |
E-value |
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
405-988 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 678.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLefQRMNKF----FI-LRDAYGQTQVLLSPKTYGLEEyAETgVPIESIVRVEGTVIPR 479
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWV--HRRRDHggliFIdLRDREGIVQVVFDPDAEAFEV-AES-LRSEYVIQVTGTVRAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 480 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 559
Cdd:PRK00476 80 PEGTVNPNLPTGEIEVLASELEVLNKSK-TLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 560 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 638
Cdd:PRK00476 158 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 639 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSD--EFKEKYD 714
Cdd:PRK00476 238 EMSFVTQEDVMALMEGLIRHVF-KEVLgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGfkVFAGAAN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 715 DLGAY-AIVVRaseafwNGAA---RKHYESLGKefkgtlFVRKFG---------PTKDVQEKLGKLLGEDVATEVADKFD 781
Cdd:PRK00476 317 DGGRVkAIRVP------GGAAqlsRKQIDELTE------FAKIYGakglayikvNEDGLKGPIAKFLSEEELAALLERTG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 782 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 861
Cdd:PRK00476 385 AKDGDLIFFGADKAKVVNDALGALRL----KLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 862 NFATSceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 937
Cdd:PRK00476 461 ELETT--DPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFE-ILGISeeeaEEKFGFLLDALKYGAPPHGGIAFGLD 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 442628131 938 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEE 988
Cdd:PRK00476 538 RLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
405-989 |
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: 671.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLEFQRmNK----FFILRDAYGQTQVLLSPKTYG-LEEYAETgVPIESIVRVEGTVIPR 479
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRR-DHggliFIDLRDRYGITQVVFDPDDSAeAFEKAEK-LRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 480 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 559
Cdd:COG0173 81 PEGTVNPKLPTGEIEVLASELEILNKAK-TPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 560 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 638
Cdd:COG0173 159 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 639 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSdEFK--EKYD 714
Cdd:COG0173 239 EMSFVDQEDVFELMEGLIRHLF-KEVLgvELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDS-GFKvfAGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 715 DLGAY--AIVVRaseafwNGAA--RKHYESLGKefkgtlFVRKFGP--------TKD-VQEKLGKLLGEDVATEVADKFD 781
Cdd:COG0173 317 ENGGRvkAINVP------GGASlsRKQIDELTE------FAKQYGAkglayikvNEDgLKSPIAKFLSEEELAAILERLG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 782 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 861
Cdd:COG0173 385 AKPGDLIFFVADKPKVVNKALGALRL----KLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 862 NFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 937
Cdd:COG0173 461 LLET---DPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFE-LLGISeeeaEEKFGFLLEAFKYGAPPHGGIAFGLD 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 442628131 938 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEEE 989
Cdd:COG0173 537 RLVMLLAGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
405-985 |
5.62e-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: 537.78 E-value: 5.62e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLEFQR----MNkFFILRDAYGQTQVLLSPKTYGLEeyAETGVPIESIVRVEGTVIPRP 480
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRdlggLI-FIDLRDRSGIVQVVCDPDADALK--LAKGLRNEDVVQVKGKVSARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 481 AATINPKMQTGHVEVEADKVVVLNPAKKnLPFEIRKFNrAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLiNYL 560
Cdd:TIGR00459 79 EGNINRNLDTGEIEILAESITLLNKSKT-PPLIIEKTD-AEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL-DQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 561 GFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIE 639
Cdd:TIGR00459 156 GFLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDME 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 640 LSFTSRDDIMQLIEETLRYSWPKDFP-RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIeKSDEFKEKYDDLGA 718
Cdd:TIGR00459 236 MSFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLF-KDSEFKVFSNLIND 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 719 YAIV----VRASEAFWNGAARKHYESLGKEF--KGT--LFVRKfgptKDVQEKLGKLLGEDVATEVADKFDLEENDLLFL 790
Cdd:TIGR00459 315 GGRVkairVPGGWAELSRKSIKELRKFAKEYgaKGLayLKVNE----DGINSPIKKFLDEKKGKILLERTDAQNGDILLF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 791 GIGSKVETRELLGRIRLDyqdfLVENAKIKKPNDFRFLWVIDFPLFERNREtNQLESVHHPFTLPHSDDLENFATsceNL 870
Cdd:TIGR00459 391 GAGSKKIVLDALGALRLK----LGKDLGLVDPDLFSFLWVVDFPMFEKDKE-GRLCAAHHPFTMPKDEDLENLEA---AP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 871 ESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKI----PHDHLSHLLSALESGCPPHGGIALGLDRLIAILCRA 946
Cdd:TIGR00459 463 EEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFE-ILGIdpeeAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGT 541
|
570 580 590
....*....|....*....|....*....|....*....
gi 442628131 947 RSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVV 985
Cdd:TIGR00459 542 DNIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYV 580
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
542-960 |
3.06e-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: 420.44 E-value: 3.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 542 LRLRSAVIMKMREYLINyLGFVEVETPTLFRRTPGGAQEFVVPTRK-AGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCY 620
Cdd:cd00777 1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRLhPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 621 RDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPR-LQTPFRRITYEEAMEKYGndkpdtrfgfllnnv 699
Cdd:cd00777 80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVeLTTPFPRMTYAEAMERYG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 700 seiieksdefkekyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadk 779
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 780 fdleendllflgigskvetrellgrirldyqdflvenakikkpndFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDD 859
Cdd:cd00777 145 ---------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEED 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 860 LENFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGL 936
Cdd:cd00777 180 LDLLEK---DPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEeeaEEKFGFLLEAFKYGAPPHGGIALGL 256
|
410 420
....*....|....*....|....
gi 442628131 937 DRLIAILCRARSIRDVIAFPKSLN 960
Cdd:cd00777 257 DRLVMLLTGSESIRDVIAFPKTQN 280
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
521-957 |
6.83e-115 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 358.03 E-value: 6.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 521 GERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLFR-RTPGGAQEFVVPTRKAGHFYSLVQSPQ 599
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 600 QFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK-----------DFPRLQ 668
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEvegiakeleggTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 669 TPFRRITYEEAMEK----------YGNDKPDTRFGFLLnnvseiieksdefkekyddlgayaivvraseafwngaarkhy 738
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLEL------------------------------------------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 739 eslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadkfdleendllflgigskvetrellgrirldyqdflvenak 818
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 819 IKKPNDFRFLWVIDFPlfernretnqleSVHHPFTLPHSDDLEnfatscenlesIRSQAYDLVLNGQEVGGGSIRIHDRD 898
Cdd:pfam00152 198 VIDKNKFNPLWVTDFP------------AEHHPFTMPKDEDDP-----------ALAEAFDLVLNGVEIGGGSIRIHDPE 254
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442628131 899 MQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPK 957
Cdd:pfam00152 255 LQEERFEEQGLDPeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
234-353 |
7.77e-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: 7.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 234 RDLTCNDLRRDDVGKTVTLVGWIPSTKNN---KFLQLKDGYGQTQLMIEDQSLS--DTFLSTPEQTVIQIVGKVLGRPKA 308
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPefELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 442628131 309 NVNLKYDTGEVEVSVTSVKVLNPDDP----YDGPIKAKE-KKQKFSIDDL 353
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTlpfeIDDDVNVSEeLRLKYRYLDL 130
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
91-246 |
3.60e-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: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 91 CGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVlEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNSC 167
Cdd:cd04317 5 CGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYG-IVQVVF-DPEEAPEFELAEKLRNESVIQVTGKVRARPEGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 168 NQTMPTGEIEVEVQD--ILN----IHFPAggtkragdkrtystmvqqqsnlgitstEYKIAKNENI-LKYfenRDLtcnD 240
Cdd:cd04317 83 NPKLPTGEIEVVASEleVLNkaktLPFEI---------------------------DDDVNVSEELrLKY---RYL---D 129
|
....*.
gi 442628131 241 LRRDDV 246
Cdd:cd04317 130 LRRPKM 135
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
71-185 |
1.76e-09 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 61.73 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 71 SAMASNFNMNSQPPQPMR-QSCGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVLEDKHPRVARRMNN 146
Cdd:PLN02903 42 PVVSAVDSMSSQLTWPSRsHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTG-IVQVVTLPDEFPEAHRTANR 120
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442628131 147 MPENTTLTIVGLVMRRPHNSCNQTMPTGEIEV--EVQDILN 185
Cdd:PLN02903 121 LRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVvaESVDILN 161
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
91-185 |
1.95e-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: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 91 CGELRNHHCGLFVELSGRlikkrVNR--------FAELRDRNGgACQLVVLEDKHP---RVARRMNNmpEnTTLTIVGLV 159
Cdd:COG0173 7 CGELRESDVGQEVTLSGW-----VHRrrdhggliFIDLRDRYG-ITQVVFDPDDSAeafEKAEKLRS--E-YVIAVTGKV 77
|
90 100
....*....|....*....|....*...
gi 442628131 160 MRRPHNSCNQTMPTGEIEVEVQD--ILN 185
Cdd:COG0173 78 RARPEGTVNPKLPTGEIEVLASEleILN 105
|
|
| tRNA_anti-codon |
pfam01336 |
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ... |
250-329 |
1.64e-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: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 250 VTLVGWIPSTKNNK----FLQLKDGYGQTQLMIEDQSLSDTFLSTPEQTVIQIVGKVlgrpkanvnLKYDTGEVEVSVTS 325
Cdd:pfam01336 1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKV---------KKRKGGELELVVEE 71
|
....
gi 442628131 326 VKVL 329
Cdd:pfam01336 72 IELL 75
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
241-343 |
2.92e-04 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 44.71 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 241 LRRDDVGKTVTLVGWIPSTKNNK---FLQLKDGYGQTQLMIEDQSLSDTF---LSTPEQTVIQIVGKVLGRPKANvnlky 314
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDGSCFKQLQVVKDNGEEYFeeiKKLTTGSSVIVTGTVVESPRAG----- 84
|
90 100
....*....|....*....|....*....
gi 442628131 315 dtGEVEVSVTSVKVLNpDDPYDGPIKAKE 343
Cdd:PRK03932 85 --QGYELQATKIEVIG-EDPEDYPIQKKR 110
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
405-988 |
0e+00 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 678.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLefQRMNKF----FI-LRDAYGQTQVLLSPKTYGLEEyAETgVPIESIVRVEGTVIPR 479
Cdd:PRK00476 4 RTHYCGELRESHVGQTVTLCGWV--HRRRDHggliFIdLRDREGIVQVVFDPDAEAFEV-AES-LRSEYVIQVTGTVRAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 480 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 559
Cdd:PRK00476 80 PEGTVNPNLPTGEIEVLASELEVLNKSK-TLPFPIDDEEDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDD- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 560 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 638
Cdd:PRK00476 158 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQIDI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 639 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSD--EFKEKYD 714
Cdd:PRK00476 238 EMSFVTQEDVMALMEGLIRHVF-KEVLgvDLPTPFPRMTYAEAMRRYGSDKPDLRFGLELVDVTDLFKDSGfkVFAGAAN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 715 DLGAY-AIVVRaseafwNGAA---RKHYESLGKefkgtlFVRKFG---------PTKDVQEKLGKLLGEDVATEVADKFD 781
Cdd:PRK00476 317 DGGRVkAIRVP------GGAAqlsRKQIDELTE------FAKIYGakglayikvNEDGLKGPIAKFLSEEELAALLERTG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 782 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 861
Cdd:PRK00476 385 AKDGDLIFFGADKAKVVNDALGALRL----KLGKELGLIDEDKFAFLWVVDFPMFEYDEEEGRWVAAHHPFTMPKDEDLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 862 NFATSceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 937
Cdd:PRK00476 461 ELETT--DPGKARAYAYDLVLNGYELGGGSIRIHRPEIQEKVFE-ILGISeeeaEEKFGFLLDALKYGAPPHGGIAFGLD 537
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 442628131 938 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEE 988
Cdd:PRK00476 538 RLVMLLAGADSIRDVIAFPKTQSAQDLLTGAPSPVDEKQLRELGIRLRKKE 588
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
405-989 |
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: 671.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLEFQRmNK----FFILRDAYGQTQVLLSPKTYG-LEEYAETgVPIESIVRVEGTVIPR 479
Cdd:COG0173 3 RTHYCGELRESDVGQEVTLSGWVHRRR-DHggliFIDLRDRYGITQVVFDPDDSAeAFEKAEK-LRSEYVIAVTGKVRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 480 PAATINPKMQTGHVEVEADKVVVLNPAKkNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINy 559
Cdd:COG0173 81 PEGTVNPKLPTGEIEVLASELEILNKAK-TPPFQIDDDTDVSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 560 LGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDI 638
Cdd:COG0173 159 NGFLEIETPILTKSTPEGARDYLVPSRvHPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 639 ELSFTSRDDIMQLIEETLRYSWpKDFP--RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEKSdEFK--EKYD 714
Cdd:COG0173 239 EMSFVDQEDVFELMEGLIRHLF-KEVLgvELPTPFPRMTYAEAMERYGSDKPDLRFGLELVDVTDIFKDS-GFKvfAGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 715 DLGAY--AIVVRaseafwNGAA--RKHYESLGKefkgtlFVRKFGP--------TKD-VQEKLGKLLGEDVATEVADKFD 781
Cdd:COG0173 317 ENGGRvkAINVP------GGASlsRKQIDELTE------FAKQYGAkglayikvNEDgLKSPIAKFLSEEELAAILERLG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 782 LEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDDLE 861
Cdd:COG0173 385 AKPGDLIFFVADKPKVVNKALGALRL----KLGKELGLIDEDEFAFLWVVDFPLFEYDEEEGRWVAMHHPFTMPKDEDLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 862 NFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKIP----HDHLSHLLSALESGCPPHGGIALGLD 937
Cdd:COG0173 461 LLET---DPGKVRAKAYDLVLNGYELGGGSIRIHDPELQEKVFE-LLGISeeeaEEKFGFLLEAFKYGAPPHGGIAFGLD 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 442628131 938 RLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVVDEEE 989
Cdd:COG0173 537 RLVMLLAGEDSIRDVIAFPKTQSAQDLMTGAPSEVDEKQLKELHIRLRPPEK 588
|
|
| aspS_bact |
TIGR00459 |
aspartyl-tRNA synthetase, bacterial type; Asparate--tRNA ligases in this family may be ... |
405-985 |
5.62e-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: 537.78 E-value: 5.62e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLEFQR----MNkFFILRDAYGQTQVLLSPKTYGLEeyAETGVPIESIVRVEGTVIPRP 480
Cdd:TIGR00459 2 RTHYCGQLRTEHLGQTVTLAGWVNRRRdlggLI-FIDLRDRSGIVQVVCDPDADALK--LAKGLRNEDVVQVKGKVSARP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 481 AATINPKMQTGHVEVEADKVVVLNPAKKnLPFEIRKFNrAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLiNYL 560
Cdd:TIGR00459 79 EGNINRNLDTGEIEILAESITLLNKSKT-PPLIIEKTD-AEEEVRLKYRYLDLRRPEMQQRLKLRHKVTKAVRNFL-DQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 561 GFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIE 639
Cdd:TIGR00459 156 GFLEIETPMLTKSTPEGARDYLVPSRvHKGEFYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDLRADRQPEFTQIDME 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 640 LSFTSRDDIMQLIEETLRYSWPKDFP-RLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIeKSDEFKEKYDDLGA 718
Cdd:TIGR00459 236 MSFMTQEDVMELIEKLVSHVFLEVKGiDLKKPFPVMTYAEAMERYGSDKPDLRFPLELIDVTDLF-KDSEFKVFSNLIND 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 719 YAIV----VRASEAFWNGAARKHYESLGKEF--KGT--LFVRKfgptKDVQEKLGKLLGEDVATEVADKFDLEENDLLFL 790
Cdd:TIGR00459 315 GGRVkairVPGGWAELSRKSIKELRKFAKEYgaKGLayLKVNE----DGINSPIKKFLDEKKGKILLERTDAQNGDILLF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 791 GIGSKVETRELLGRIRLDyqdfLVENAKIKKPNDFRFLWVIDFPLFERNREtNQLESVHHPFTLPHSDDLENFATsceNL 870
Cdd:TIGR00459 391 GAGSKKIVLDALGALRLK----LGKDLGLVDPDLFSFLWVVDFPMFEKDKE-GRLCAAHHPFTMPKDEDLENLEA---AP 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 871 ESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEqILKI----PHDHLSHLLSALESGCPPHGGIALGLDRLIAILCRA 946
Cdd:TIGR00459 463 EEALAEAYDLVLNGVELGGGSIRIHDPEVQKKVFE-ILGIdpeeAREKFGFLLEAFKYGTPPHAGFALGLDRLMMLLTGT 541
|
570 580 590
....*....|....*....|....*....|....*....
gi 442628131 947 RSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVV 985
Cdd:TIGR00459 542 DNIRDVIAFPKTTAAACLMTEAPSFIDEKQLEELSIKYV 580
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
377-985 |
5.04e-171 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 517.03 E-value: 5.04e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 377 SAEASTTANASLIAEQRAKVADTNKFADRTHNCGELTSNDINEKVVICGWLEFQRMN---KFFILRDAYGQTQVLLSPKT 453
Cdd:PLN02903 31 SSAASSAATVIPVVSAVDSMSSQLTWPSRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTGIVQVVTLPDE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 454 YGLEEYAETGVPIESIVRVEGTVIPRPAATINPKMQTGHVEVEADKVVVLNPAKKNLPFEIRKF----NRAGERLRLTHR 529
Cdd:PLN02903 111 FPEAHRTANRLRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVVAESVDILNVVTKSLPFLVTTAdeqkDSIKEEVRLRYR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 530 YLDLRFNDMQHNLRLRSAVIMKMREYLINYLGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSG 608
Cdd:PLN02903 191 VLDLRRPQMNANLRLRHRVVKLIRRYLEDVHGFVEIETPILSRSTPEGARDYLVPSRvQPGTFYALPQSPQLFKQMLMVS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 609 GIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLR--YSWPKDFpRLQTPFRRITYEEAMEKYGND 686
Cdd:PLN02903 271 GFDRYYQIARCFRDEDLRADRQPEFTQLDMELAFTPLEDMLKLNEDLIRqvFKEIKGV-QLPNPFPRLTYAEAMSKYGSD 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 687 KPDTRFGFLLNNVSEIIEKSdEFKEKYDDLGA----YAIVVRASEAFWNGAARK----HYESLGKEFKGTLFVRKfgpTK 758
Cdd:PLN02903 350 KPDLRYGLELVDVSDVFAES-SFKVFAGALESggvvKAICVPDGKKISNNTALKkgdiYNEAIKSGAKGLAFLKV---LD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 759 DVQEKLGKLLGEDVATEVADKF----DLEENDLLFLGIGSKVETRELLGRIRLdyqdFLVENAKIKKPNDFRFLWVIDFP 834
Cdd:PLN02903 426 DGELEGIKALVESLSPEQAEQLlaacGAGPGDLILFAAGPTSSVNKTLDRLRQ----FIAKTLDLIDPSRHSILWVTDFP 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 835 LFERNRETNQLESVHHPFTLPHSDDLenfatscENLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEQILKIP--- 911
Cdd:PLN02903 502 MFEWNEDEQRLEALHHPFTAPNPEDM-------GDLSSARALAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPeea 574
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442628131 912 HDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMRLYHLSVV 985
Cdd:PLN02903 575 ESKFGYLLEALDMGAPPHGGIAYGLDRLVMLLAGAKSIRDVIAFPKTTTAQCALTRAPSEVDDKQLQDLSIAST 648
|
|
| AspRS_core |
cd00777 |
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ... |
542-960 |
3.06e-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: 420.44 E-value: 3.06e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 542 LRLRSAVIMKMREYLINyLGFVEVETPTLFRRTPGGAQEFVVPTRK-AGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCY 620
Cdd:cd00777 1 LRLRSRVIKAIRNFLDE-QGFVEIETPILTKSTPEGARDFLVPSRLhPGKFYALPQSPQLFKQLLMVSGFDRYFQIARCF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 621 RDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPR-LQTPFRRITYEEAMEKYGndkpdtrfgfllnnv 699
Cdd:cd00777 80 RDEDLRADRQPEFTQIDIEMSFVDQEDIMSLIEGLLKYVFKEVLGVeLTTPFPRMTYAEAMERYG--------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 700 seiieksdefkekyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadk 779
Cdd:cd00777 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 780 fdleendllflgigskvetrellgrirldyqdflvenakikkpndFRFLWVIDFPLFERNRETNQLESVHHPFTLPHSDD 859
Cdd:cd00777 145 ---------------------------------------------FKFLWIVDFPLFEWDEEEGRLVSAHHPFTAPKEED 179
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 860 LENFATsceNLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGL 936
Cdd:cd00777 180 LDLLEK---DPEDARAQAYDLVLNGVELGGGSIRIHDPDIQEKVFEILGLSEeeaEEKFGFLLEAFKYGAPPHGGIALGL 256
|
410 420
....*....|....*....|....
gi 442628131 937 DRLIAILCRARSIRDVIAFPKSLN 960
Cdd:cd00777 257 DRLVMLLTGSESIRDVIAFPKTQN 280
|
|
| PRK12820 |
PRK12820 |
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ... |
402-978 |
1.13e-117 |
|
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional
Pssm-ID: 105955 [Multi-domain] Cd Length: 706 Bit Score: 378.95 E-value: 1.13e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 402 FADRTHnCGELTSNDINEKVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTYGLEEYAE-TGVPIESIVRVEGTVI 477
Cdd:PRK12820 3 ENDRSF-CGHLSLDDTGREVCLAGWVDAFRDHGellFIHLRDRNGFIQAVFSPEAAPADVYELaASLRAEFCVALQGEVQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 478 PRPAATINPKMQTGHVEVEADKVVVLNpAKKNLPFEIR-KFNRAG----------ERLRLTHRYLDLRFNDMQHNLRLRS 546
Cdd:PRK12820 82 KRLEETENPHIETGDIEVFVRELSILA-ASEALPFAISdKAMTAGagsagadavnEDLRLQYRYLDIRRPAMQDHLAKRH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 547 AVIMKMREYLiNYLGFVEVETPTLFRRTPGGAQEFVVPTR-KAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEAT 625
Cdd:PRK12820 161 RIIKCARDFL-DSRGFLEIETPILTKSTPEGARDYLVPSRiHPKEFYALPQSPQLFKQLLMIAGFERYFQLARCFRDEDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 626 RPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPRLQTPFRRITYEEAMEKYGNDKPDTRFGFLLNNVSEIIEK 705
Cdd:PRK12820 240 RPNRQPEFTQLDIEASFIDEEFIFELIEELTARMFAIGGIALPRPFPRMPYAEAMDTTGSDRPDLRFDLKFADATDIFEN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 706 SDE--FKEKYDDLGAY-AIVVR------ASEAFWNGAARKHYESLGKefKGTLFVRkfGPTKDVQEKLGKLLGEDVATEV 776
Cdd:PRK12820 320 TRYgiFKQILQRGGRIkGINIKgqseklSKNVLQNEYAKEIAPSFGA--KGMTWMR--AEAGGLDSNIVQFFSADEKEAL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 777 ADKFDLEEND-LLFLGIGSKVETRELLGRIRLDYQDFLvenaKIKKPNDFRFLWVIDFPLFERNRETNqLESVHHPFTLP 855
Cdd:PRK12820 396 KRRFHAEDGDvIIMIADASCAIVLSALGQLRLHLADRL----GLIPEGVFHPLWITDFPLFEATDDGG-VTSSHHPFTAP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 856 HSDDLEnfATSCENLESIRSQAYDLVLNGQEVGGGSIRIHDRDMQHFIL------EQILKiphDHLSHLLSALESGCPPH 929
Cdd:PRK12820 471 DREDFD--PGDIEELLDLRSRAYDLVVNGEELGGGSIRINDKDIQLRIFaalglsEEDIE---DKFGFFLRAFDFAAPPH 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 442628131 930 GGIALGLDRLIAILCRARSIRDVIAFPKSLNGRDPLSNAPVPISDEEMR 978
Cdd:PRK12820 546 GGIALGLDRVVSMILQTPSIREVIAFPKNRSAACPLTGAPSEVAQEQLA 594
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
521-957 |
6.83e-115 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 358.03 E-value: 6.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 521 GERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLFR-RTPGGAQEFVVPTRKAGHFYSLVQSPQ 599
Cdd:pfam00152 1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDE-NGFLEVETPILTKsATPEGARDFLVPSRALGKFYALPQSPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 600 QFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK-----------DFPRLQ 668
Cdd:pfam00152 80 LYKQLLMVAGFDRVFQIARCFRDEDLRTDRQPEFTQLDLEMSFVDYEDVMDLTEELIKEIFKEvegiakeleggTLLDLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 669 TPFRRITYEEAMEK----------YGNDKPDTRFGFLLnnvseiieksdefkekyddlgayaivvraseafwngaarkhy 738
Cdd:pfam00152 160 KPFPRITYAEAIEKlngkdveelgYGSDKPDLRFLLEL------------------------------------------ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 739 eslgkefkgtlfvrkfgptkdvqeklgkllgedvatevadkfdleendllflgigskvetrellgrirldyqdflvenak 818
Cdd:pfam00152 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 819 IKKPNDFRFLWVIDFPlfernretnqleSVHHPFTLPHSDDLEnfatscenlesIRSQAYDLVLNGQEVGGGSIRIHDRD 898
Cdd:pfam00152 198 VIDKNKFNPLWVTDFP------------AEHHPFTMPKDEDDP-----------ALAEAFDLVLNGVEIGGGSIRIHDPE 254
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442628131 899 MQHFILEQILKIP---HDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPK 957
Cdd:pfam00152 255 LQEERFEEQGLDPeeaEEKFGFYLDALKYGAPPHGGLGIGLDRLVMLLTGLESIREVIAFPK 316
|
|
| aspC |
PRK05159 |
aspartyl-tRNA synthetase; Provisional |
405-964 |
3.18e-60 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 235354 [Multi-domain] Cd Length: 437 Bit Score: 213.13 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWL-EFQRMN--KFFILRDAYGQTQVLLS-PKTYGLEEYAEtGVPIESIVRVEGTVIPrp 480
Cdd:PRK05159 3 KRHLTSELTPELDGEEVTLAGWVhEIRDLGgiAFLILRDRSGIIQVVVKkKVDEELFETIK-KLKRESVVSVTGTVKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 481 aatiNPKMQTGhVEVEADKVVVLNPAKKNLPFEIRKFNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyL 560
Cdd:PRK05159 80 ----NPKAPGG-VEVIPEEIEVLNKAEEPLPLDISGKVLAELDTRLDNRFLDLRRPRVRAIFKIRSEVLRAFREFLYE-N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 561 GFVEVETPTLFRR-TPGGAQEFVVP--TRKAghfYsLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQ-PEFTQL 636
Cdd:PRK05159 154 GFTEIFTPKIVASgTEGGAELFPIDyfEKEA---Y-LAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHNTSRHlNEYTSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 637 DIELSFTSRD-DIMQLIEETLRYSWPK--------------DFPRLQTPFRRITYEEAMEkygndkpdtrfgfLLNnvse 701
Cdd:PRK05159 230 DVEMGFIDDHeDVMDLLENLLRYMYEDvaencekelellgiELPVPETPIPRITYDEAIE-------------ILK---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 702 iiEKSDEFKEkyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgkllGEDVATEvadkfd 781
Cdd:PRK05159 293 --SKGNEISW---------------------------------------------------------GDDLDTE------ 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 782 lEEndllflgigskvetrELLGRIrldyqdflvenakIKKPNDFRFLWVIDFPLFERnretnqlesvhhPF-TLPHSDDL 860
Cdd:PRK05159 308 -GE---------------RLLGEY-------------VKEEYGSDFYFITDYPSEKR------------PFyTMPDEDDP 346
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 861 EnfatscenlesiRSQAYDLVLNGQEVGGGSIRIHDRDMQhfiLEQILK--IPHDHLSHLLSALESGCPPHGGIALGLDR 938
Cdd:PRK05159 347 E------------ISKSFDLLFRGLEITSGGQRIHRYDML---VESIKEkgLNPESFEFYLEAFKYGMPPHGGFGLGLER 411
|
570 580
....*....|....*....|....*.
gi 442628131 939 LIAILCRARSIRDVIAFPkslngRDP 964
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 ... |
542-957 |
2.70e-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: 190.38 E-value: 2.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 542 LRLRSAVIMKMREYLINYlGFVEVETPTLFRRTPG-GAQEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCY 620
Cdd:cd00669 1 FKVRSKIIKAIRDFMDDR-GFLEVETPMLQKITGGaGARPFLVKYNALGLDYYLRISPQLFKKRLMVGGLDRVFEINRNF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 621 RDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSW--------------PKDFPRlqtPFRRITYEEAMEKYGNd 686
Cdd:cd00669 80 RNEDLRARHQPEFTMMDLEMAFADYEDVIELTERLVRHLArevlgvtavtygfeLEDFGL---PFPRLTYREALERYGQ- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 687 kpdtrfgfllnnvseiieksdefkekyddlgayaivvraseafwngaarkhyeslgkefkgtlfvrkfgptkdvqeklgk 766
Cdd:cd00669 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 767 llgedvatevadkfdleendllflgigskvetrellgrirldyqdflvenakikkpndfrFLWVIDFPLFernretnqle 846
Cdd:cd00669 156 ------------------------------------------------------------PLFLTDYPAE---------- 165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 847 sVHHPFTLPHSDDLEnfatscenlesiRSQAYDLVLNGQEVGGGSIRIHDRDMQ-HFILEQIL--KIPHDHLSHLLSALE 923
Cdd:cd00669 166 -MHSPLASPHDVNPE------------IADAFDLFINGVEVGNGSSRLHDPDIQaEVFQEQGInkEAGMEYFEFYLKALE 232
|
410 420 430
....*....|....*....|....*....|....
gi 442628131 924 SGCPPHGGIALGLDRLIAILCRARSIRDVIAFPK 957
Cdd:cd00669 233 YGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPK 266
|
|
| EcAspRS_like_N |
cd04317 |
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ... |
405-538 |
3.50e-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: 184.65 E-value: 3.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLEFQRMN---KFFILRDAYGQTQVLLSPKTYGLEEYAETgVPIESIVRVEGTVIPRPA 481
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEFELAEK-LRNESVIQVTGKVRARPE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442628131 482 ATINPKMQTGHVEVEADKVVVLNPAkKNLPFEIRKFNRAGERLRLTHRYLDLRFNDM 538
Cdd:cd04317 80 GTVNPKLPTGEIEVVASELEVLNKA-KTLPFEIDDDVNVSEELRLKYRYLDLRRPKM 135
|
|
| AsnS |
COG0017 |
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
405-964 |
2.02e-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: 181.40 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 405 RTHNCGELTSNDINEKVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTygLEEYAE-TGVPIESIVRVEGTVIPRP 480
Cdd:COG0017 1 KRTYIKDLLPEHVGQEVTVAGWVRTKRDSGgisFLILRDGSGFIQVVVKKDK--LENFEEaKKLTTESSVEVTGTVVESP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 481 AAtinPkmqtGHVEVEADKVVVLNPAKKNLPFEIrkfNRAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyL 560
Cdd:COG0017 79 RA---P----QGVELQAEEIEVLGEADEPYPLQP---KRHSLEFLLDNRHLRLRTNRFGAIFRIRSELARAIREFFQE-R 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 561 GFVEVETPTLfrrTP----GGAQEFVVP--TRKAghfySLVQSPQQFKQMLMsGGIDRYFQVARCYRDEATRPDRQ-PEF 633
Cdd:COG0017 148 GFVEVHTPII---TAsateGGGELFPVDyfGKEA----YLTQSGQLYKEALA-MALEKVYTFGPTFRAEKSNTRRHlAEF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 634 TQLDIELSFTSRDDIMQLIEETLRY--------------SWPKDFPRLQ----TPFRRITYEEAMekygndkpdtrfgfl 695
Cdd:COG0017 220 WMIEPEMAFADLEDVMDLAEEMLKYiikyvlencpeeleFLGRDVERLEkvpeSPFPRITYTEAI--------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 696 lnnvsEIIEKSDEfKEKY-DDLGayaivvraSEAfwngaarkhyEslgkefkgtlfvrkfgptkdvqeklgKLLGEDVat 774
Cdd:COG0017 285 -----EILKKSGE-KVEWgDDLG--------TEH----------E--------------------------RYLGEEF-- 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 775 evadkFDleendllflgigskvetrellgrirldyqdflvenakikkpndfRFLWVIDFPLFERnretnqlesvhhPF-T 853
Cdd:COG0017 313 -----FK--------------------------------------------KPVFVTDYPKEIK------------AFyM 331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 854 LPHSDDLEnfatscenlesiRSQAYDLVLNGQ-EVGGGSIRIHDRDMqhfiLEQILK---IPHDHLSHLLSALESGCPPH 929
Cdd:COG0017 332 KPNPDDPK------------TVAAFDLLAPGIgEIIGGSQREHRYDV----LVERIKekgLDPEDYEWYLDLRRYGSVPH 395
|
570 580 590
....*....|....*....|....*....|....*
gi 442628131 930 GGIALGLDRLIAILCRARSIRDVIAFPkslngRDP 964
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 ... |
234-353 |
7.77e-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: 7.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 234 RDLTCNDLRRDDVGKTVTLVGWIPSTKNN---KFLQLKDGYGQTQLMIEDQSLS--DTFLSTPEQTVIQIVGKVLGRPKA 308
Cdd:cd04317 1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPefELAEKLRNESVIQVTGKVRARPEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 442628131 309 NVNLKYDTGEVEVSVTSVKVLNPDDP----YDGPIKAKE-KKQKFSIDDL 353
Cdd:cd04317 81 TVNPKLPTGEIEVVASELEVLNKAKTlpfeIDDDVNVSEeLRLKYRYLDL 130
|
|
| AsxRS_core |
cd00776 |
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ... |
519-964 |
5.33e-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: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 519 RAGERLRLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLFRR-TPGGAQEFVVP--TRKAghfYsLV 595
Cdd:cd00776 1 DANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRE-NGFTEVHTPKITSTdTEGGAELFKVSyfGKPA---Y-LA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 596 QSPQQFKQMLMsGGIDRYFQVARCYRDEATRPDRQ-PEFTQLDIELSF-TSRDDIMQLIEETLRYSW------------- 660
Cdd:cd00776 76 QSPQLYKEMLI-AALERVYEIGPVFRAEKSNTRRHlSEFWMLEAEMAFiEDYNEVMDLIEELIKYIFkrvlercakelel 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 661 ----PKDFPRLQTPFRRITYEEAMEkygndkpdtrfgfLLNnvseiiEKSDEFKEKY-DDLGAyaivvrASEafwngaar 735
Cdd:cd00776 155 vnqlNRELLKPLEPFPRITYDEAIE-------------LLR------EKGVEEEVKWgEDLST------EHE-------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 736 khyeslgkefkgtlfvrkfgptkdvqeklgKLLGEDVATevadkfdleendllflgigskvetrellgrirldyqdflve 815
Cdd:cd00776 202 ------------------------------RLLGEIVKG----------------------------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 816 nakikkpndfRFLWVIDFPLFERnretnqlesvhhPFTLPHSDDLENfatscenlesiRSQAYDLVLNG-QEVGGGSIRI 894
Cdd:cd00776 211 ----------DPVFVTDYPKEIK------------PFYMKPDDDNPE-----------TVESFDLLMPGvGEIVGGSQRI 257
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442628131 895 HDRDMqhfiLEQILK---IPHDHLSHLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPkslngRDP 964
Cdd:cd00776 258 HDYDE----LEERIKehgLDPESFEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNIREAILFP-----RDP 321
|
|
| PLN02850 |
PLN02850 |
aspartate-tRNA ligase |
410-969 |
1.29e-30 |
|
aspartate-tRNA ligase
Pssm-ID: 215456 [Multi-domain] Cd Length: 530 Bit Score: 127.90 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 410 GELTSNDINEKVVICGWLEFQRM---NKFFILRDAYGQTQVLLSPK----TYGLEEYAeTGVPIESIVRVEGTVIpRPAA 482
Cdd:PLN02850 73 SDLGEELAGSEVLIRGRVHTIRGkgkSAFLVLRQSGFTVQCVVFVSevtvSKGMVKYA-KQLSRESVVDVEGVVS-VPKK 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 483 TInpKMQTGHVEVEADKVVVLNPAKKNLPFEI-----------------RKFNRAGERLRLTHRYLDLRFNDMQHNLRLR 545
Cdd:PLN02850 151 PV--KGTTQQVEIQVRKIYCVSKALATLPFNVedaarseseiekalqtgEQLVRVGQDTRLNNRVLDLRTPANQAIFRIQ 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 546 SAVIMKMREYLINYlGFVEVETPTLFrrtpGGAQE---FVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRD 622
Cdd:PLN02850 229 SQVCNLFREFLLSK-GFVEIHTPKLI----AGASEggsAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 623 EATRPDRQ-PEFTQLDIELSFTSR-DDIMQLIEE-------TLRYSWPKDFPRL--QTPFR---------RITYEEAMEk 682
Cdd:PLN02850 304 EDSFTHRHlCEFTGLDLEMEIKEHySEVLDVVDElfvaifdGLNERCKKELEAIreQYPFEplkylpktlRLTFAEGIQ- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 683 ygndkpdtrfgfLLNNVSEIIeksdefkEKYDDLgayaivvraseafwNGAARKhyeslgkefkgtlfvrkfgptkdvqe 762
Cdd:PLN02850 383 ------------MLKEAGVEV-------DPLGDL--------------NTESER-------------------------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 763 KLGKLLGEDVATevadkfdleendllflgigskvetrellgrirldyqdflvenakikkpnDFRFLWviDFPLFERnret 842
Cdd:PLN02850 404 KLGQLVKEKYGT-------------------------------------------------DFYILH--RYPLAVR---- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 843 nqlesvhhPF-TLPHSDDlenfatscenleSIRSQAYDLVLNGQEVGGGSIRIHDRDmqhfILEQILK---IPHDHLSHL 918
Cdd:PLN02850 429 --------PFyTMPCPDD------------PKYSNSFDVFIRGEEIISGAQRVHDPE----LLEKRAEecgIDVKTISTY 484
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 442628131 919 LSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFPkslngRDPLSNAP 969
Cdd:PLN02850 485 IDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFP-----RDPQRLAP 530
|
|
| PTZ00401 |
PTZ00401 |
aspartyl-tRNA synthetase; Provisional |
365-969 |
2.55e-29 |
|
aspartyl-tRNA synthetase; Provisional
Pssm-ID: 173592 [Multi-domain] Cd Length: 550 Bit Score: 124.33 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 365 NLTSNNGESTEDSAEASTTANASLIAEQRAKVAD----TNKFAD---------------RTH-NCGELTSNDINEKVV-I 423
Cdd:PTZ00401 4 NHADAGAPAVEKKQSDKEARKAARLAEEKARAAEkaalVEKYKDvfgaapmvqsttyksRTFiPVAVLSKPELVDKTVlI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 424 CGWLEFQRMN---KFFILRDAYGQTQVLLSPKTYGLEEYAE--TGVPIESIVRVEGTViprpAATINPKMQTGH--VEVE 496
Cdd:PTZ00401 84 RARVSTTRKKgkmAFMVLRDGSDSVQAMAAVEGDVPKEMIDfiGQIPTESIVDVEATV----CKVEQPITSTSHsdIELK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 497 ADKVVVLNPAKKNLPFEI----RKFNRAGERL----RLTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINYlGFVEVETP 568
Cdd:PTZ00401 160 VKKIHTVTESLRTLPFTLedasRKESDEGAKVnfdtRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDS-DFCEIHSP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 569 TLFRR-TPGGAQEFvvptrKAGHFYS---LVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQ-PEFTQLDIELSFT 643
Cdd:PTZ00401 239 KIINApSEGGANVF-----KLEYFNRfayLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHlTEFVGLDVEMRIN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 644 SR-DDIMQLIEETLRYSwpkdFPRL------------QTPFRRITYE---EAMEKYGndkpdtrfgflLNNVSEIIEKSD 707
Cdd:PTZ00401 314 EHyYEVLDLAESLFNYI----FERLathtkelkavcqQYPFEPLVWKltpERMKELG-----------VGVISEGVEPTD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 708 EFKEKYDDLGAYAIvvraseafwngaaRKHYESLgKEFKGTLFVRKFGPTKDVQEKLGKLLGEDVatevadkfdleendl 787
Cdd:PTZ00401 379 KYQARVHNMDSRML-------------RINYMHC-IELLNTVLEEKMAPTDDINTTNEKLLGKLV--------------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 788 lflgigskvetRELLGrirldyQDFLVENAkikkpndfrflwvidFPlfernretnqleSVHHPF-TLPHSDDlENFATS 866
Cdd:PTZ00401 430 -----------KERYG------TDFFISDR---------------FP------------SSARPFyTMECKDD-ERFTNS 464
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 867 cenlesirsqaYDLVLNGQEVGGGSIRIHDRDMqhfILE--QILKIPHDHLSHLLSALESGCPPHGGIALGLDRLIAILC 944
Cdd:PTZ00401 465 -----------YDMFIRGEEISSGAQRIHDPDL---LLAraKMLNVDLTPIKEYVDSFRLGAWPHGGFGVGLERVVMLYL 530
|
650 660
....*....|....*....|....*
gi 442628131 945 RARSIRDVIAFPkslngRDPLSNAP 969
Cdd:PTZ00401 531 GLSNVRLASLFP-----RDPQRTTP 550
|
|
| LysU |
COG1190 |
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
400-956 |
1.26e-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: 102.81 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 400 NKFaDRTHNCGELTSN--------DINEKVVICGWLEFQR-MNK--FFILRDAYGQTQVLLSPKTYGLEEYAE-TGVPIE 467
Cdd:COG1190 31 NKF-PRTHTAAEIREKydeleaeeETGDEVSVAGRIMAKRdMGKasFADLQDGSGRIQLYLRRDELGEEAYELfKLLDLG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 468 SIVRVEGTVIprpaatinpKMQTGHVEVEADKVVVLNPAKKNLPFEIRKFNRAGERLRltHRYLDLRFN-DMQHNLRLRS 546
Cdd:COG1190 110 DIVGVEGTVF---------RTKTGELSVKVEELTLLSKSLRPLPEKFHGLTDPETRYR--QRYVDLIVNpEVRETFRKRS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 547 AVIMKMREYLINyLGFVEVETPTLfRRTPGGA--QEFVvpTrkagHFYSLVQ------SPQQFKQMLMSGGIDRYFQVAR 618
Cdd:COG1190 179 KIIRAIRRFLDE-RGFLEVETPML-QPIAGGAaaRPFI--T----HHNALDMdlylriAPELYLKRLIVGGFERVFEIGR 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 619 CYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK--------------DFprlQTPFRRITYEEAMEKYG 684
Cdd:COG1190 251 NFRNEGIDTTHNPEFTMLELYQAYADYNDMMDLTEELIREAAEAvlgttkvtyqgqeiDL---SPPWRRITMVEAIKEAT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 685 NDKPDTrfgfllnnvseiiEKSDEfkekyddlgayaivvraseafwngAARKHYESLGKEFKGTlfvrkfgptkdvqEKL 764
Cdd:COG1190 328 GIDVTP-------------LTDDE------------------------ELRALAKELGIEVDPG-------------WGR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 765 GKLLgedvatevadkfdleenDLLFlgigskvetrellgrirldyqDFLVEnAKIKKPndfrfLWVIDFPLfernrETnq 844
Cdd:COG1190 358 GKLI-----------------DELF---------------------EELVE-PKLIQP-----TFVTDYPV-----EV-- 386
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 845 leSvhhPFTLPHSDDlENFAtscenlesirsQAYDLVLNGQEVGGG-S-----IRIHDRdmqhFiLEQILK--------- 909
Cdd:COG1190 387 --S---PLAKRHRDD-PGLT-----------ERFELFIAGREIANAfSelndpIDQRER----F-EEQLELkaagddeam 444
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 442628131 910 -IPHDhlshLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 956
Cdd:COG1190 445 pMDED----FLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
|
|
| lysS |
PRK00484 |
lysyl-tRNA synthetase; Reviewed |
388-956 |
2.01e-22 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 234778 [Multi-domain] Cd Length: 491 Bit Score: 102.09 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 388 LIAEQRAKVAD---------TNKFaDRTHNCGELTSN----------DINEKVVICGWLEFQR-MNK--FFILRDAYGQT 445
Cdd:PRK00484 6 QIAVRREKLAElreqgidpyPNKF-ERTHTAAELRAKyddkekeeleELEIEVSVAGRVMLKRvMGKasFATLQDGSGRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 446 QVLLSPKTYGLEEYAE-TGVPIESIVRVEGTVIprpaatinpKMQTGHVEVEADKVVVLNPAKKNLPfeiRKFnrAGER- 523
Cdd:PRK00484 85 QLYVSKDDVGEEALEAfKKLDLGDIIGVEGTLF---------KTKTGELSVKATELTLLTKSLRPLP---DKF--HGLTd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 524 --LRLTHRYLDLRFN-DMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLfRRTPGG--AQEFVvpTrkagHFYSLVQ-- 596
Cdd:PRK00484 151 veTRYRQRYVDLIVNpESRETFRKRSKIISAIRRFLDN-RGFLEVETPML-QPIAGGaaARPFI--T----HHNALDIdl 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 597 ----SPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWPK---------- 662
Cdd:PRK00484 223 ylriAPELYLKRLIVGGFERVYEIGRNFRNEGIDTRHNPEFTMLEFYQAYADYNDMMDLTEELIRHLAQAvlgttkvtyq 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 663 ----DFprlQTPFRRITYEEAMEKYgndkpdTRFGFLLNNVSEIIEKSDEFKEKYDDlgayaivvraseafwngaarkhy 738
Cdd:PRK00484 303 gteiDF---GPPFKRLTMVDAIKEY------TGVDFDDMTDEEARALAKELGIEVEK----------------------- 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 739 eslgkefkgtlfvrkfgptkdvQEKLGKLLgedvatevadkfdleenDLLFlgigskvetrellgrirldyqDFLVEnAK 818
Cdd:PRK00484 351 ----------------------SWGLGKLI-----------------NELF---------------------EEFVE-PK 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 819 IKKPNdFrflwVIDFPLfernrETNqlesvhhPFTLPHSDDlENFAtscenlesirsQAYDLVLNGQEVGGG------SI 892
Cdd:PRK00484 370 LIQPT-F----ITDYPV-----EIS-------PLAKRHRED-PGLT-----------ERFELFIGGREIANAfselndPI 420
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442628131 893 RIHDRdmqhFiLEQILK----------IPHDhlshLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 956
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 ... |
420-505 |
1.20e-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: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 420 KVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTYGLEEYAETGVPIESIVRVEGTVIPRPAatinPKMQTGHVEVE 496
Cdd:cd04100 1 EVTLAGWVHSRRDHGgliFIDLRDGSGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPE----GNLATGEIELQ 76
|
....*....
gi 442628131 497 ADKVVVLNP 505
Cdd:cd04100 77 AEELEVLSK 85
|
|
| PLN02502 |
PLN02502 |
lysyl-tRNA synthetase |
368-956 |
9.91e-20 |
|
lysyl-tRNA synthetase
Pssm-ID: 215278 [Multi-domain] Cd Length: 553 Bit Score: 94.29 E-value: 9.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 368 SNNGESTEDSAEASTTAN-ASLIAEQRAKvaDTNKFA---DRTHNCGEL------TSN---DINEKVVICGWLEFQR-MN 433
Cdd:PLN02502 47 KSAAADDETMDPTQYRANrLKKVEALRAK--GVEPYPykfDVTHTAPELqekygsLENgeeLEDVSVSVAGRIMAKRaFG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 434 K--FFILRDAYGQTQVLLSPKTYGLEEYA----ETGVPIESIVRVEGTViprpaatinPKMQTGHVEVEADKVVVLNPAK 507
Cdd:PLN02502 125 KlaFYDLRDDGGKIQLYADKKRLDLDEEEfeklHSLVDRGDIVGVTGTP---------GKTKKGELSIFPTSFEVLTKCL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 508 KNLPFEIRKFNRAGERLRltHRYLDLRFN-DMQHNLRLRSAVIMKMREYLINyLGFVEVETPTLfRRTPGG--AQEFVVp 584
Cdd:PLN02502 196 LMLPDKYHGLTDQETRYR--QRYLDLIANpEVRDIFRTRAKIISYIRRFLDD-RGFLEVETPML-NMIAGGaaARPFVT- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 585 trkagHFYSLVQ------SPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRY 658
Cdd:PLN02502 271 -----HHNDLNMdlylriATELHLKRLVVGGFERVYEIGRQFRNEGISTRHNPEFTTCEFYQAYADYNDMMELTEEMVSG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 659 SwpkdfprlqtpfrrityeeAMEKYGNdkpdtrfgfllnnvseiieksdeFKEKYddlGAYAIvvraseafwngaarkhy 738
Cdd:PLN02502 346 M-------------------VKELTGS-----------------------YKIKY---HGIEI----------------- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 739 eSLGKEFkgtlfvRKFGPTKDVQEKLGKLLGEDVATEVADKF--DLEENDllflgiGSKVETRELLGRIrLD--YQDFLV 814
Cdd:PLN02502 364 -DFTPPF------RRISMISLVEEATGIDFPADLKSDEANAYliAACEKF------DVKCPPPQTTGRL-LNelFEEFLE 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 815 EnaKIKKPNdfrflWVIDFPlfernretnQLESvhhPFTLPHsddlenfatscenlesiRSQA-----YDLVLNGQEVGG 889
Cdd:PLN02502 430 E--TLVQPT-----FVLDHP---------VEMS---PLAKPH-----------------RSKPglterFELFINGRELAN 473
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442628131 890 GSIRIHDRDMQHFILEQILKiphDHLS----------HLLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 956
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 ... |
540-956 |
6.67e-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: 89.18 E-value: 6.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 540 HNLRLRSAVIMKMREYLINyLGFVEVETPTLfRRTPGGA--QEFVVPTRKAG-HFYsLVQSPQQFKQMLMSGGIDRYFQV 616
Cdd:cd00775 6 QTFIVRSKIISYIRKFLDD-RGFLEVETPML-QPIAGGAaaRPFITHHNALDmDLY-LRIAPELYLKRLIVGGFERVYEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 617 ARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRY-------SWPKDFPRLQT----PFRRITYEEAMEKY-G 684
Cdd:cd00775 83 GRNFRNEGIDLTHNPEFTMIEFYEAYADYNDMMDLTEDLFSGlvkkingKTKIEYGGKELdftpPFKRVTMVDALKEKtG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 685 NDKPDTRfgfllnnvseiIEKSDEFKEKYDDLGAyaivvraseafwngaarKHYEslgkefkgtlfvrkfgptkdVQEKL 764
Cdd:cd00775 163 IDFPELD-----------LEQPEELAKLLAKLIK-----------------EKIE--------------------KPRTL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 765 GKLLgedvatevadkfdleenDLLFlgiGSKVEtrellgrirldyqdflvenAKIKKPNdfrflWVIDF-----PLFERN 839
Cdd:cd00775 195 GKLL-----------------DKLF---EEFVE-------------------PTLIQPT-----FIIDHpveisPLAKRH 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 840 RETNQLesvhhpftlphsddlenfatsCENLEsirsqaydLVLNGQEVGGGSIRIHDRDMQHFILEQILKIPH--DHLSH 917
Cdd:cd00775 231 RSNPGL---------------------TERFE--------LFICGKEIANAYTELNDPFDQRERFEEQAKQKEagDDEAM 281
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 442628131 918 L-----LSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 956
Cdd:cd00775 282 MmdedfVTALEYGMPPTGGLGIGIDRLVMLLTDSNSIRDVILFP 325
|
|
| PRK12445 |
PRK12445 |
lysyl-tRNA synthetase; Reviewed |
388-956 |
5.63e-18 |
|
lysyl-tRNA synthetase; Reviewed
Pssm-ID: 171504 [Multi-domain] Cd Length: 505 Bit Score: 88.58 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 388 LIAEQRAKVADTNKF-----ADRTHNCGELTSND----INEKVVICGWLEFQR-MNK--FFILRDAYGQTQVLLS----P 451
Cdd:PRK12445 26 LAALRQQGVAFPNDFrrdhtSDQLHEEFDAKDNQelesLNIEVSVAGRMMTRRiMGKasFVTLQDVGGRIQLYVArdslP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 452 KTYGLEEYAETGvpIESIVRVEGTVIprpaatinpKMQTGHVEVEADKVVVLNPAKKNLPFEIRKFNraGERLRLTHRYL 531
Cdd:PRK12445 106 EGVYNDQFKKWD--LGDIIGARGTLF---------KTQTGELSIHCTELRLLTKALRPLPDKFHGLQ--DQEVRYRQRYL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 532 DLRFND-MQHNLRLRSAVIMKMREYLINYlGFVEVETPtLFRRTPGG--AQEFVVPTRKAGHFYSLVQSPQQFKQMLMSG 608
Cdd:PRK12445 173 DLIANDkSRQTFVVRSKILAAIRQFMVAR-GFMEVETP-MMQVIPGGasARPFITHHNALDLDMYLRIAPELYLKRLVVG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 609 GIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLR-----------YSWPKDFPRLQTPFRRITYE 677
Cdd:PRK12445 251 GFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYHDLIELTESLFRtlaqevlgttkVTYGEHVFDFGKPFEKLTMR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 678 EAMEKYgndKPDTRFGFLlnnvseiieksDEFKekyddlgayaivvraseafwngAARKHYESLGKEFKgtlfvRKFGpt 757
Cdd:PRK12445 331 EAIKKY---RPETDMADL-----------DNFD----------------------AAKALAESIGITVE-----KSWG-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 758 kdvqekLGKLLGEdVATEVADKFDLEENDLlflgigskvetrellgrirldyQDFLVENAKIKKPNDFRFLWVIDFPLFE 837
Cdd:PRK12445 368 ------LGRIVTE-IFDEVAEAHLIQPTFI----------------------TEYPAEVSPLARRNDVNPEITDRFEFFI 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 838 RNRETNQlesvhhpfTLPHSDDLENfatscenlesiRSQAYDLVLNGQEVGGGSIRIHDRDMqhfileqilkiphdhlsh 917
Cdd:PRK12445 419 GGREIGN--------GFSELNDAED-----------QAERFQEQVNAKAAGDDEAMFYDEDY------------------ 461
|
570 580 590
....*....|....*....|....*....|....*....
gi 442628131 918 lLSALESGCPPHGGIALGLDRLIAILCRARSIRDVIAFP 956
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 ... |
249-331 |
1.34e-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: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 249 TVTLVGWIPSTKNNK---FLQLKDGYGQTQLMIEDQSLSDTFL---STPEQTVIQIVGKVLGRPKANvnlkYDTGEVEVS 322
Cdd:cd04100 1 EVTLAGWVHSRRDHGgliFIDLRDGSGIVQVVVNKEELGEFFEeaeKLRTESVVGVTGTVVKRPEGN----LATGEIELQ 76
|
....*....
gi 442628131 323 VTSVKVLNP 331
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 ... |
544-671 |
3.54e-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: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 544 LRSAVIMKMREYLiNYLGFVEVETP-----TLFRRTPGGAQEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGI----DRYF 614
Cdd:cd00768 1 IRSKIEQKLRRFM-AELGFQEVETPiverePLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIrklpLRLA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442628131 615 QVARCYRDEATR--PDRQPEFTQLDIELSFTSRDDI------MQLIEETLRYSWPKD--FPRLQTPF 671
Cdd:cd00768 80 EIGPAFRNEGGRrgLRRVREFTQLEGEVFGEDGEEAsefeelIELTEELLRALGIKLdiVFVEKTPG 146
|
|
| PTZ00417 |
PTZ00417 |
lysine-tRNA ligase; Provisional |
487-705 |
5.09e-14 |
|
lysine-tRNA ligase; Provisional
Pssm-ID: 173607 [Multi-domain] Cd Length: 585 Bit Score: 76.20 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 487 KMQTGHVEVEADKVVVLNPAKKNLPFeirKFNRAGERLRLTHRYLDLRFND-MQHNLRLRSAVIMKMREYLiNYLGFVEV 565
Cdd:PTZ00417 200 KSKKGELSIFPKETIILSPCLHMLPM---KYGLKDTEIRYRQRYLDLMINEsTRSTFITRTKIINYLRNFL-NDRGFIEV 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 566 ETPTLfRRTPGGA--QEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQLDIELSFT 643
Cdd:PTZ00417 276 ETPTM-NLVAGGAnaRPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYA 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 644 SRDDIMQLIEE-----------TLRYSWPKDFPRLQ-------TPFRRITYEEAMEKYGNDKPDTRFgfllnNVSEIIEK 705
Cdd:PTZ00417 355 DFYDLIKWSEDffsqlvmhlfgTYKILYNKDGPEKDpieidftPPYPKVSIVEELEKLTNTKLEQPF-----DSPETINK 429
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
412-718 |
1.13e-13 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 74.76 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 412 LTSNDINEKVVICGWLEFQRMNK---FFILRD--AYGQTQVLLSPktyGLEEYAE-TGVPIESIVRVEGTVIPRPAATin 485
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDgsCFKQLQVVKDN---GEEYFEEiKKLTTGSSVIVTGTVVESPRAG-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 486 pkmqtGHVEVEADKVVVLNPAKKNLPfeIRKfNRAG-ERLRlTHRYLDLRFNDMQHNLRLRSAVIMKMREYLINYlGFVE 564
Cdd:PRK03932 85 -----QGYELQATKIEVIGEDPEDYP--IQK-KRHSiEFLR-EIAHLRPRTNKFGAVMRIRNTLAQAIHEFFNEN-GFVW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 565 VETPTLfrrTP----GGAQEFVVPT-----------RKAghfySLVQSPQ-QFKQMLMSGGidRYFQVARCYRDEATRPD 628
Cdd:PRK03932 155 VDTPII---TAsdceGAGELFRVTTldldfskdffgKEA----YLTVSGQlYAEAYAMALG--KVYTFGPTFRAENSNTR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 629 RQ-PEFTQLDIELSFTSRDDIMQLIEETLRY-------------------SWPKDFPRLQ----TPFRRITYEEAMekyg 684
Cdd:PRK03932 226 RHlAEFWMIEPEMAFADLEDNMDLAEEMLKYvvkyvlencpddleflnrrVDKGDIERLEnfieSPFPRITYTEAI---- 301
|
330 340 350
....*....|....*....|....*....|....*...
gi 442628131 685 ndkpdtrfgfllnnvsEIIEKSD---EFKEKY-DDLGA 718
Cdd:PRK03932 302 ----------------EILQKSGkkfEFPVEWgDDLGS 323
|
|
| PTZ00385 |
PTZ00385 |
lysyl-tRNA synthetase; Provisional |
487-688 |
1.54e-13 |
|
lysyl-tRNA synthetase; Provisional
Pssm-ID: 185588 [Multi-domain] Cd Length: 659 Bit Score: 75.07 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 487 KMQTGHVEVEADKVVVLNP---AKKNLPFEIRKFNRAGERlRLTHRYldlRFNDMQHN------LRLRSAVIMKMREYLi 557
Cdd:PTZ00385 173 RMQRGELSVAASRMLILSPyvcTDQVVCPNLRGFTVLQDN-DVKYRY---RFTDMMTNpcvietIKKRHVMLQALRDYF- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 558 NYLGFVEVETPTLFRRTPGG-AQEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQPEFTQL 636
Cdd:PTZ00385 248 NERNFVEVETPVLHTVASGAnAKSFVTHHNANAMDLFLRVAPELHLKQCIVGGMERIYEIGKVFRNEDADRSHNPEFTSC 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442628131 637 DIELSFTSRDDIMQLIEETLRY------------SWPKD---FPR---LQTPFRRIT-YEEAMEKYGNDKP 688
Cdd:PTZ00385 328 EFYAAYHTYEDLMPMTEDIFRQlamrvngttvvqIYPENahgNPVtvdLGKPFRRVSvYDEIQRMSGVEFP 398
|
|
| PRK06462 |
PRK06462 |
asparagine synthetase A; Reviewed |
537-681 |
7.98e-13 |
|
asparagine synthetase A; Reviewed
Pssm-ID: 235808 [Multi-domain] Cd Length: 335 Bit Score: 70.82 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 537 DMQHNLRLRSAVIMKMREYLINYlGFVEVETPTLFRRT----PGGAQEFVVPTRKA--GHFYSLVQSPQQFKQML--MSG 608
Cdd:PRK06462 25 KYRKVLKVQSSILRYTREFLDGR-GFVEVLPPIISPSTdplmGLGSDLPVKQISIDfyGVEYYLADSMILHKQLAlrMLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 609 GIdryFQVARCYRDEATRPDRQP---EFTQLDIELSFTSRDDIMQLIEETLRY--------------SWPKDFPRLQTPF 671
Cdd:PRK06462 104 KI---FYLSPNFRLEPVDKDTGRhlyEFTQLDIEIEGADLDEVMDLIEDLIKYlvkelleehedeleFFGRDLPHLKRPF 180
|
170
....*....|
gi 442628131 672 RRITYEEAME 681
Cdd:PRK06462 181 KRITHKEAVE 190
|
|
| lysS |
PRK02983 |
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX; |
404-956 |
3.12e-12 |
|
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
Pssm-ID: 235095 [Multi-domain] Cd Length: 1094 Bit Score: 71.15 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 404 DRTHNCGELTSNDINEKVVICGWLEFQRMNK---FFILRDAYGQTQVLLSPKTYGLEEYAE--TGVPIESIVRVEGTVIp 478
Cdd:PRK02983 637 PPTHTVAEALDAPTGEEVSVSGRVLRIRDYGgvlFADLRDWSGELQVLLDASRLEQGSLADfrAAVDLGDLVEVTGTMG- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 479 rpaatinpKMQTGHVEVEADKVVV----LNPakknLPFEIRKFNRAGERLRLthRYLDLRFN-DMQHNLRLRSAVIMKMR 553
Cdd:PRK02983 716 --------TSRNGTLSLLVTSWRLagkcLRP----LPDKWKGLTDPEARVRQ--RYLDLAVNpEARDLLRARSAVVRAVR 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 554 EYLINyLGFVEVETPTLfRRTPGGA--QEFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQP 631
Cdd:PRK02983 782 ETLVA-RGFLEVETPIL-QQVHGGAnaRPFVTHINAYDMDLYLRIAPELYLKRLCVGGVERVFELGRNFRNEGVDATHNP 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 632 EFTQLDIELSFTSRDDIMQLIEETLRyswpkdfprlqtpfrrityEEAMEKYGndKPdtrfgfllnnvseiieksdefke 711
Cdd:PRK02983 860 EFTLLEAYQAHADYDTMRDLTRELIQ-------------------NAAQAAHG--AP----------------------- 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 712 kyddlgayaIVVRASeafwnGAARKHYESLGKEFkgtlfvrkfgPTKDVQEKLGKLLGE--DVATEVADKFDLEENdllf 789
Cdd:PRK02983 896 ---------VVMRPD-----GDGVLEPVDISGPW----------PVVTVHDAVSEALGEeiDPDTPLAELRKLCDA---- 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 790 LGIgsKVETRELLGRIRLDYQDFLVENAkIKKPNdfrflWVIDFPLfernrETNqlesvhhPFTLPHSDD--Lenfatsc 867
Cdd:PRK02983 948 AGI--PYRTDWDAGAVVLELYEHLVEDR-TTFPT-----FYTDFPT-----SVS-------PLTRPHRSDpgL------- 1000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 868 enlesirSQAYDLVLNGQEVGGGSIRIHDRDMQHFIL-EQILK----------IPHDhlshLLSALESGCPPHGGIALGL 936
Cdd:PRK02983 1001 -------AERWDLVAWGVELGTAYSELTDPVEQRRRLtEQSLLaaggdpeameLDED----FLQALEYAMPPTGGLGMGV 1069
|
570 580
....*....|....*....|
gi 442628131 937 DRLIaILCRARSIRDVIAFP 956
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 ... |
91-246 |
3.60e-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: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 91 CGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVlEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNSC 167
Cdd:cd04317 5 CGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYG-IVQVVF-DPEEAPEFELAEKLRNESVIQVTGKVRARPEGTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 168 NQTMPTGEIEVEVQD--ILN----IHFPAggtkragdkrtystmvqqqsnlgitstEYKIAKNENI-LKYfenRDLtcnD 240
Cdd:cd04317 83 NPKLPTGEIEVVASEleVLNkaktLPFEI---------------------------DDDVNVSEELrLKY---RYL---D 129
|
....*.
gi 442628131 241 LRRDDV 246
Cdd:cd04317 130 LRRPKM 135
|
|
| genX |
TIGR00462 |
EF-P lysine aminoacylase GenX; Many Gram-negative bacteria have a protein closely homologous ... |
561-954 |
3.36e-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: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 561 GFVEVETPTLfrrTPGGAQE---------FVVPTRKAGHFYsLVQSPQQFKQMLMSGGIDRYFQVARCYRDEATRPDRQP 631
Cdd:TIGR00462 6 GVLEVETPLL---SPAPVTDphldafateFVGPDGQGRPLY-LQTSPEYAMKRLLAAGSGPIFQICKVFRNGERGRRHNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 632 EFTQLDIELSFTSRDDIMQLIEETLRYSWPKDFPrlqtPFRRITYEEAMEKYGNDKPDTrfgfllnnvseiiEKSDEFKE 711
Cdd:TIGR00462 82 EFTMLEWYRPGFDYHDLMDEVEALLQELLGDPFA----PAERLSYQEAFLRYAGIDPLT-------------ASLAELQA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 712 KYDDLGayaiVVRASEAFWNgaarkhyeslgkefkgTLFvrkfgptkdvqeklgkllgedvatevadkfdleenDLLFLg 791
Cdd:TIGR00462 145 AAAAHG----IRASEEDDRD----------------DLL-----------------------------------DLLFS- 168
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 792 igSKVETRelLGRIRLdyqdflvenakikkpndfrfLWVIDFP-----LFErnretnqlesvhhpftlPHSDDlENFAts 866
Cdd:TIGR00462 169 --EKVEPH--LGFGRP--------------------TFLYDYPasqaaLAR-----------------ISPDD-PRVA-- 204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 867 cENLEsirsqaydLVLNGQEVGGGSIRIHDRDMQ--HFILEQILK-------IPHDhlSHLLSALESGCPPHGGIALGLD 937
Cdd:TIGR00462 205 -ERFE--------LYIKGLELANGFHELTDAAEQrrRFEADNALRkalglprYPLD--ERFLAALEAGLPECSGVALGVD 273
|
410
....*....|....*..
gi 442628131 938 RLIAILCRARSIRDVIA 954
Cdd:TIGR00462 274 RLLMLALGADSIDDVLA 290
|
|
| PLN02903 |
PLN02903 |
aminoacyl-tRNA ligase |
71-185 |
1.76e-09 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215490 [Multi-domain] Cd Length: 652 Bit Score: 61.73 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 71 SAMASNFNMNSQPPQPMR-QSCGELRNHHCGLFVELSGRLIKKRVN---RFAELRDRNGgACQLVVLEDKHPRVARRMNN 146
Cdd:PLN02903 42 PVVSAVDSMSSQLTWPSRsHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVRDHTG-IVQVVTLPDEFPEAHRTANR 120
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 442628131 147 MPENTTLTIVGLVMRRPHNSCNQTMPTGEIEV--EVQDILN 185
Cdd:PLN02903 121 LRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVvaESVDILN 161
|
|
| AspS |
COG0173 |
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ... |
91-185 |
1.95e-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: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 91 CGELRNHHCGLFVELSGRlikkrVNR--------FAELRDRNGgACQLVVLEDKHP---RVARRMNNmpEnTTLTIVGLV 159
Cdd:COG0173 7 CGELRESDVGQEVTLSGW-----VHRrrdhggliFIDLRDRYG-ITQVVFDPDDSAeafEKAEKLRS--E-YVIAVTGKV 77
|
90 100
....*....|....*....|....*...
gi 442628131 160 MRRPHNSCNQTMPTGEIEVEVQD--ILN 185
Cdd:COG0173 78 RARPEGTVNPKLPTGEIEVLASEleILN 105
|
|
| ND_PkAspRS_like_N |
cd04316 |
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ... |
407-514 |
9.87e-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: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 407 HNCGELTSNDINEKVVICGWLEFQR---MNKFFILRDAYGQTQVLLSPKTYGLEEYAET-GVPIESIVRVEGTVIPrpaa 482
Cdd:cd04316 1 HYSAEITPELDGEEVTVAGWVHEIRdlgGIKFVILRDREGIVQVTAPKKKVDKELFKTVrKLSRESVISVTGTVKA---- 76
|
90 100 110
....*....|....*....|....*....|..
gi 442628131 483 tiNPKMQTGhVEVEADKVVVLNPAKKNLPFEI 514
Cdd:cd04316 77 --EPKAPNG-VEIIPEEIEVLSEAKTPLPLDP 105
|
|
| aspS |
PRK00476 |
aspartyl-tRNA synthetase; Validated |
87-185 |
1.21e-08 |
|
aspartyl-tRNA synthetase; Validated
Pssm-ID: 234775 [Multi-domain] Cd Length: 588 Bit Score: 58.93 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 87 MR-QSCGELRNHHCGLFVELSGRlikkrVNR--------FAELRDRNGgACQLVVLEDKHP-RVARRMNNmpEnTTLTIV 156
Cdd:PRK00476 3 MRtHYCGELRESHVGQTVTLCGW-----VHRrrdhggliFIDLRDREG-IVQVVFDPDAEAfEVAESLRS--E-YVIQVT 73
|
90 100 110
....*....|....*....|....*....|.
gi 442628131 157 GLVMRRPHNSCNQTMPTGEIEVEVQD--ILN 185
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 ... |
250-329 |
1.64e-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: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 250 VTLVGWIPSTKNNK----FLQLKDGYGQTQLMIEDQSLSDTFLSTPEQTVIQIVGKVlgrpkanvnLKYDTGEVEVSVTS 325
Cdd:pfam01336 1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVFKEEAEKLAKKLKEGDVVRVTGKV---------KKRKGGELELVVEE 71
|
....
gi 442628131 326 VKVL 329
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 ... |
103-183 |
2.79e-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: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 103 VELSGRLIKKRVN---RFAELRDRnGGACQLVVLEDKHPRVARRMNNMPENTTLTIVGLVMRRPHNscnqTMPTGEIEVE 179
Cdd:cd04100 2 VTLAGWVHSRRDHgglIFIDLRDG-SGIVQVVVNKEELGEFFEEAEKLRTESVVGVTGTVVKRPEG----NLATGEIELQ 76
|
....
gi 442628131 180 VQDI 183
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 ... |
421-503 |
1.62e-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: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 421 VVICGWLEFQRMNK----FFILRDAYGQTQVLLSPKTYglEEYAETgVPIESIVRVEGTVIPRPaatinpkmqTGHVEVE 496
Cdd:pfam01336 1 VTVAGRVTSIRRSGgkllFLTLRDGTGSIQVVVFKEEA--EKLAKK-LKEGDVVRVTGKVKKRK---------GGELELV 68
|
....*..
gi 442628131 497 ADKVVVL 503
Cdd:pfam01336 69 VEEIELL 75
|
|
| PRK09350 |
PRK09350 |
elongation factor P--(R)-beta-lysine ligase; |
541-952 |
2.55e-07 |
|
elongation factor P--(R)-beta-lysine ligase;
Pssm-ID: 236474 [Multi-domain] Cd Length: 306 Bit Score: 53.78 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 541 NLRLRSAVIMKMREYLINyLGFVEVETPTLFRRTPGGAQ------EFVVPTRKAGHFYSLVQSPQQFKQMLMSGGIDRYF 614
Cdd:PRK09350 4 NLLKRAKIIAEIRRFFAD-RGVLEVETPILSQATVTDIHlvpfetRFVGPGASQGKTLWLMTSPEYHMKRLLAAGSGPIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 615 QVARCYRDEATRPDRQPEFTQLDIELSFTSRDDIMQLIEETLRYSWpkdfprLQTPFRRITYEEAMEKYGNDKPdtrfgf 694
Cdd:PRK09350 83 QICKSFRNEEAGRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVL------DCEPAESLSYQQAFLRYLGIDP------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 695 LLNNVSEIIEKSDEFK--------EKYDDL--GAYAIVVRAseafwngaarkhyeSLGKEfKGTlFVRKFGPTkdvQEKL 764
Cdd:PRK09350 151 LSADKTQLREVAAKLGlsniadeeEDRDTLlqLLFTFGVEP--------------NIGKE-KPT-FVYHFPAS---QAAL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 765 GKLLGEDvaTEVADKFdleenDLLFLGIgskvetrELLgrirldyqdflvenakikkpNDFRFLwvidfplfernreTNQ 844
Cdd:PRK09350 212 AKISTED--HRVAERF-----EVYFKGI-------ELA--------------------NGFHEL-------------TDA 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 845 LEsvhhpftlphsddlenfatscenlesirsqaydlvlngqevgggSIRIHDRDMQHFILEQILKIPHDHlsHLLSALES 924
Cdd:PRK09350 245 RE--------------------------------------------QRQRFEQDNRKRAARGLPQQPIDE--NLIAALEA 278
|
410 420
....*....|....*....|....*...
gi 442628131 925 GCPPHGGIALGLDRLIAILCRARSIRDV 952
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 ... |
239-334 |
2.88e-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: 46.92 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 239 NDLRRDDVGKTVTLVGWIPSTKN---NKFLQLKDGYGQTQLMIEDQSLSD----TFLSTPEQTVIQIVGKVLGRPKAnvn 311
Cdd:cd04316 4 AEITPELDGEEVTVAGWVHEIRDlggIKFVILRDREGIVQVTAPKKKVDKelfkTVRKLSRESVISVTGTVKAEPKA--- 80
|
90 100
....*....|....*....|....*....
gi 442628131 312 lkydTGEVEVSVTSVKVLN------PDDP 334
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 ... |
420-504 |
5.53e-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: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 420 KVVICGWLEFQ-RMNK---FFILRDAYGQT-QVLLSPKTYGLEeyAETGVPIESIVRVEGTVIPRPAATinpKMQTGHVE 494
Cdd:cd04321 1 KVTLNGWIDRKpRIVKklsFADLRDPNGDIiQLVSTAKKDAFS--LLKSITAESPVQVRGKLQLKEAKS---SEKNDEWE 75
|
90
....*....|
gi 442628131 495 VEADKVVVLN 504
Cdd:cd04321 76 LVVDDIQTLN 85
|
|
| AspRS_cyto_N |
cd04320 |
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ... |
420-514 |
7.30e-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: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 420 KVVICGWLEFQRM--NK--FFILRDAYGQTQVLLSPKTYGLEE----YAEtGVPIESIVRVEGTVIpRPAATINPKMQTG 491
Cdd:cd04320 1 EVLIRARVHTSRAqgAKlaFLVLRQQGYTIQGVLAASAEGVSKqmvkWAG-SLSKESIVDVEGTVK-KPEEPIKSCTQQD 78
|
90 100
....*....|....*....|...
gi 442628131 492 hVEVEADKVVVLNPAKKNLPFEI 514
Cdd:cd04320 79 -VELHIEKIYVVSEAAEPLPFQL 100
|
|
| asnC |
PRK03932 |
asparaginyl-tRNA synthetase; Validated |
241-343 |
2.92e-04 |
|
asparaginyl-tRNA synthetase; Validated
Pssm-ID: 235176 [Multi-domain] Cd Length: 450 Bit Score: 44.71 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 241 LRRDDVGKTVTLVGWIPSTKNNK---FLQLKDGYGQTQLMIEDQSLSDTF---LSTPEQTVIQIVGKVLGRPKANvnlky 314
Cdd:PRK03932 10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDGSCFKQLQVVKDNGEEYFeeiKKLTTGSSVIVTGTVVESPRAG----- 84
|
90 100
....*....|....*....|....*....
gi 442628131 315 dtGEVEVSVTSVKVLNpDDPYDGPIKAKE 343
Cdd:PRK03932 85 --QGYELQATKIEVIG-EDPEDYPIQKKR 110
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
542-640 |
3.61e-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: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 542 LRLRSAVIMKMREYLINYlGFVEVETPT-----LFRRTPGG--AQEFVVPTRKAGHFYSL------------VQSPQQFK 602
Cdd:cd00773 2 AALRRYIEDTLREVFERY-GYEEIDTPVfeyteLFLRKSGDevSKEMYRFKDKGGRDLALrpdltapvaravAENLLSLP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 442628131 603 QMLmsggidRYFQVARCYRDEATRPDRQPEFTQLDIEL 640
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 ... |
250-330 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 250 VTLVGWIPST----KNNKFLQLKDGYGQT-QLMIEDQSLSDTFL-STPEQTVIQIVGKVLGRPKANvnlKYDTGEVEVSV 323
Cdd:cd04321 2 VTLNGWIDRKprivKKLSFADLRDPNGDIiQLVSTAKKDAFSLLkSITAESPVQVRGKLQLKEAKS---SEKNDEWELVV 78
|
....*..
gi 442628131 324 TSVKVLN 330
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 ... |
249-329 |
8.22e-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: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442628131 249 TVTLVGW---IPSTKNNKFLQLKDGYGQTQLMIEDQSLSDTFLS---TPEQTVIqIVGKVLGRPKAnvnlKYDTGEVEVS 322
Cdd:cd04323 1 RVKVFGWvhrLRSQKKLMFLVLRDGTGFLQCVLSKKLVTEFYDAkslTQESSVE-VTGEVKEDPRA----KQAPGGYELQ 75
|
....*..
gi 442628131 323 VTSVKVL 329
Cdd:cd04323 76 VDYLEII 82
|
|
| |
