|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
90-765 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 837.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 90 PPLGALLA--VEHVKDDVSISLEEGKENILYVSENVVFTDINSILRYLARVATTTGLYGSNLLEHTEIDHWLEFSATkLS 167
Cdd:PLN02907 12 PPLAVIAAakVAGVPLTIDPSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 168 SCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKAPVHVKRWFGFLEAQ------QAFQSVG 241
Cdd:PLN02907 91 SGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEysdilnEVTAAYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 242 TKWNVSTTKAKVTPEKKQDVGKF----------VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIM 311
Cdd:PLN02907 171 GKRGAGKPAAAKSKEKVADAGKAdgakdkgsfeVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 312 RFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKN 391
Cdd:PLN02907 251 RFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 392 SIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHAL 471
Cdd:PLN02907 331 SVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHAL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 472 RTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQF 551
Cdd:PLN02907 411 RSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQF 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 552 IAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPV---NIPEaQEEMKEVAKHPKNPDVGLKPVWYSPKVF 628
Cdd:PLN02907 491 ILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLtltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIW 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 629 IEGADAETLSEGEMVTFINWGNINITKINKNADGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCVTYEHLI 707
Cdd:PLN02907 570 LDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNELVPLS--LVEFDYLI 646
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 585187043 708 TKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVS 765
Cdd:PLN02907 647 TKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS 704
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
274-579 |
7.51e-162 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 477.20 E-value: 7.51e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 274 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFES 352
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 353 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--RIESKHRKNSIEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSnNGCMR 429
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 430 DPTLYRCKIQP---HPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 505
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585187043 506 NNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 579
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
218-763 |
1.98e-151 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 459.67 E-value: 1.98e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 218 NKAPVHVKRWFGFLEAQQAFQSVGTKWNVS----TTKAKVTPEKKQDVGKF-VELPGAEMGKVTVRFPPEASGYLHIGHA 292
Cdd:TIGR00463 32 NNPELRKKAKEVLEAVEAAVEEVNSLSPEEqkelMKRLGLDIKKKEKKRKGlRELPGAKMGEVVMRFAPNPSGPLHIGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 293 KAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESIMKYAEKLIQEGKAYVDDTP 372
Cdd:TIGR00463 112 RAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 373 AEQMKAEREQRIESKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYP 452
Cdd:TIGR00463 192 PEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 453 TYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDP 530
Cdd:TIGR00463 272 TMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 531 RFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLK-KEVIPVNIPEAQEEMKevAK 609
Cdd:TIGR00463 351 RLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER--PL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 610 HPKNPDVGLKPVWYSPKVFIEGADAETLSegEMVTFINWGNINITKINknadgkivSLDAKLNLENKDYKKTTKITWLAE 689
Cdd:TIGR00463 429 HPDHPEIGERVLILRGEIYVPKDDLEEGV--EPVRLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPA 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585187043 690 TAhalPIPAICVTYEHLITKPVLGKDEDFkqyvnknskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEP 763
Cdd:TIGR00463 499 KD---AVKVKVIMPDASIVEGVIEADASE----------------------LEVGDVVQFERFGFARLDSADKD 547
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
274-583 |
4.13e-139 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 415.50 E-value: 4.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 274 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESI 353
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 354 MKYAEKLIQEGKAYVddtpaeqmkaereqrieskhrknsieknlqmweemkkgsqfgqscclrakidmssnngcmrdptl 433
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 434 yrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 513
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 514 KLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 583
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
273-560 |
2.08e-64 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 225.06 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 273 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFE 351
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 352 SIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESK--------HRKNSIEKNLQMWEEmkkgsqfGQSCCLRAKI---- 419
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGkpprydgrCRDLSPEELERMLAA-------GEPPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 420 ----DMSS-----NNGCMRDPTLYRckiqphpRTGnkynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfy 484
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 485 WIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvneGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 560
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
810-859 |
3.27e-25 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 98.85 E-value: 3.27e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 585187043 810 LYNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPG 859
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
810-862 |
1.03e-24 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 97.57 E-value: 1.03e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 585187043 810 LYNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPP 862
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
811-863 |
1.39e-22 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 91.63 E-value: 1.39e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 585187043 811 YNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPPA 863
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPG 53
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
891-974 |
1.97e-15 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 71.40 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 891 EVVRKLKAEKapkIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCV-CGRNaAKYYTL 969
Cdd:pfam09180 3 EFKEALEEKG---FVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIvCGKP-AKKWVL 62
|
....*
gi 585187043 970 FGRSY 974
Cdd:pfam09180 63 FARSY 67
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
903-974 |
2.42e-15 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 71.45 E-value: 2.42e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585187043 903 KIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCVCGRNAAKYYTLFGRSY 974
Cdd:smart00946 12 KFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFARSY 67
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
903-974 |
5.18e-11 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 63.09 E-value: 5.18e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585187043 903 KIAQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCVPFkPLCELQPGARCV-CGRNaAKYYTLFGRSY 974
Cdd:cd00862 145 GIVLAPWCGEEECEEEIKEETA-------------ATILCIPF-DEAKLEEGGKCVvCGRP-AKAYARFAKSY 202
|
|
| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
814-851 |
2.84e-05 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 48.20 E-value: 2.84e-05
10 20 30
....*....|....*....|....*....|....*...
gi 585187043 814 VAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEK 851
Cdd:PLN02734 16 VTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSAL 53
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
90-765 |
0e+00 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 837.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 90 PPLGALLA--VEHVKDDVSISLEEGKENILYVSENVVFTDINSILRYLARVATTTGLYGSNLLEHTEIDHWLEFSATkLS 167
Cdd:PLN02907 12 PPLAVIAAakVAGVPLTIDPSLKSGSAPTLLFSSGEKLTGTNVLLRYIARSASLPGFYGQDAFESSQVDEWLDYAPT-FS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 168 SCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKAPVHVKRWFGFLEAQ------QAFQSVG 241
Cdd:PLN02907 91 SGSEFENACEYVDGYLASRTFLVGYSLTIADIAIWSGLAGSGQRWESLRKSKKYQNLVRWFNSISAEysdilnEVTAAYV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 242 TKWNVSTTKAKVTPEKKQDVGKF----------VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIM 311
Cdd:PLN02907 171 GKRGAGKPAAAKSKEKVADAGKAdgakdkgsfeVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 312 RFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKN 391
Cdd:PLN02907 251 RFDDTNPSKESDEFVENILKDIETLGIKYDAVTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMDGIESKCRNN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 392 SIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHAL 471
Cdd:PLN02907 331 SVEENLRLWKEMIAGSERGLQCCVRGKLDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHAL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 472 RTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQF 551
Cdd:PLN02907 411 RSSEYHDRNAQYYRILEDMGLRKVHIWEFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQF 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 552 IAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLKKEVIPV---NIPEaQEEMKEVAKHPKNPDVGLKPVWYSPKVF 628
Cdd:PLN02907 491 ILSQGASKNLNLMEWDKLWTINKKIIDPVCPRHTAVLKEGRVLLtltDGPE-TPFVRIIPRHKKYEGAGKKATTFTNRIW 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 629 IEGADAETLSEGEMVTFINWGNINITKINKNADGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCVTYEHLI 707
Cdd:PLN02907 570 LDYADAEAISEGEEVTLMDWGNAIIKEITKDEGGAVTALSGELHLEG-SVKTTKlKLTWLPDTNELVPLS--LVEFDYLI 646
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 585187043 708 TKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEPVS 765
Cdd:PLN02907 647 TKKKLEEDDNFLDVLNPCTKKETAALGDSNMRNLKRGEIIQLERKGYYRCDAPFVRSS 704
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
267-761 |
0e+00 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 581.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 267 LPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYT 346
Cdd:PLN03233 4 LEGAIAGQIVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIKPDSVSFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 347 SDHFESIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNG 426
Cdd:PLN03233 84 SDYFEPIRCYAIILIEEGLAYMDDTPQEEMKKERADRAESKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 427 CMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLN 506
Cdd:PLN03233 164 TLRDPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 507 NTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVA 586
Cdd:PLN03233 244 NTVLSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 587 LLKKEVIPVNIPEAQEE----MKEVAKHPKNPDVGLKPVWYSPKVFIEGADAETLSEGEMVTFINWGNINITKINKNADG 662
Cdd:PLN03233 324 IDKADHTALTVTNADEEadfaFSETDCHPKDPGFGKRAMRICDEVLLEKADTEDIQLGEDIVLLRWGVIEISKIDGDLEG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 663 KIVSldaklnleNKDYKKTT-KITWLAETAHAlpIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDL 741
Cdd:PLN03233 404 HFIP--------DGDFKAAKkKISWIADVSDN--IPVVLSEFDNLIIKEKLEEDDKFEDFINPDTLAETDVIGDAGLKTL 473
|
490 500
....*....|....*....|
gi 585187043 742 KKGDIIQLQRRGFFICDQPY 761
Cdd:PLN03233 474 KEHDIIQLERRGFYRVDRPY 493
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
265-758 |
0e+00 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 551.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 265 VELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQF- 343
Cdd:PTZ00402 43 LQLTNAEEGKVVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGp 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 344 TYTSDHFESIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSS 423
Cdd:PTZ00402 123 TYSSDYMDLMYEKAEELIKKGLAYCDKTPREEMQKCRFDGVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 424 NNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRL 503
Cdd:PTZ00402 203 ENKAMRDPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRL 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 504 NLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 583
Cdd:PTZ00402 283 NMEYSVMSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 584 YVALLKKEVIPVNIpEAQEEMKEVAK--HPKNPDVGLKPVWYSPKVFIEGADAETLSEGEMVTFINWGNINITKINK-NA 660
Cdd:PTZ00402 363 YTVVSNTLKVRCTV-EGQIHLEACEKllHKKVPDMGEKTYYKSDVIFLDAEDVALLKEGDEVTLMDWGNAYIKNIRRsGE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 661 DGKIVSLDAKLNLENkDYKKTT-KITWLAETAHALPIPaiCVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLK 739
Cdd:PTZ00402 442 DALITDADIVLHLEG-DVKKTKfKLTWVPESPKAEVME--LNEYDHLLTKKKPDPEESIDDIIAPVTKYTQEVYGEEALS 518
|
490
....*....|....*....
gi 585187043 740 DLKKGDIIQLQRRGFFICD 758
Cdd:PTZ00402 519 VLKKGDIIQLERRGYYIVD 537
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
274-579 |
7.51e-162 |
|
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 395606 [Multi-domain] Cd Length: 314 Bit Score: 477.20 E-value: 7.51e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 274 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFES 352
Cdd:pfam00749 1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDyGPYYQSDRFDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 353 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQ--RIESKHRKNSIEKNLQMW-EEMKKGSQFGQSCCLRAKIDMSSnNGCMR 429
Cdd:pfam00749 81 YYKYAEELIKKGKAYVCFCTPEELEEEREEqeALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 430 DPTLYRCKIQP---HPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR-KPYIWEYSRLNL 505
Cdd:pfam00749 160 DPVRGRIKFTPqeiHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLNL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585187043 506 NNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSV-VNMEWDKIWAFNKKVIDP 579
Cdd:pfam00749 240 DGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSFdVNRLSKSLEAFDRKKLDW 314
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
218-763 |
1.98e-151 |
|
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. This model models just the eukaryotic cytosolic and archaeal forms of the enzyme. In some eukaryotes, the glutamyl-tRNA synthetase is part of a longer, multifunctional aminoacyl-tRNA ligase. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases, including all known archaeal enzymes (as of 2010) may act on both tRNA(gln) and tRNA(glu). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273091 [Multi-domain] Cd Length: 556 Bit Score: 459.67 E-value: 1.98e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 218 NKAPVHVKRWFGFLEAQQAFQSVGTKWNVS----TTKAKVTPEKKQDVGKF-VELPGAEMGKVTVRFPPEASGYLHIGHA 292
Cdd:TIGR00463 32 NNPELRKKAKEVLEAVEAAVEEVNSLSPEEqkelMKRLGLDIKKKEKKRKGlRELPGAKMGEVVMRFAPNPSGPLHIGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 293 KAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESIMKYAEKLIQEGKAYVDDTP 372
Cdd:TIGR00463 112 RAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDEVVYQSDRIETYYDYTRKLIEMGKAYVCDCR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 373 AEQMKAEREQRIESKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYP 452
Cdd:TIGR00463 192 PEEFRELRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVKTDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 453 TYDFACPIVDSIEGVTHALRTTEYHD--RDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVnEGLVDGWDDP 530
Cdd:TIGR00463 272 TMDFSVAIDDHLLGVTHVLRGKDHIDnrRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALSTSSARKGIL-RGEYSGWDDP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 531 RFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLK-KEVIPVNIPEAQEEMKevAK 609
Cdd:TIGR00463 351 RLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNRKIIDEEARRYFFIWNpVKIEIVGLPEPKRVER--PL 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 610 HPKNPDVGLKPVWYSPKVFIEGADAETLSegEMVTFINWGNINITKINknadgkivSLDAKLNLENKDYKKTTKITWLAE 689
Cdd:TIGR00463 429 HPDHPEIGERVLILRGEIYVPKDDLEEGV--EPVRLMDAVNVIYSKKE--------LRYHSEGLEGARKLGKSIIHWLPA 498
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585187043 690 TAhalPIPAICVTYEHLITKPVLGKDEDFkqyvnknskheelmlgdpclkdLKKGDIIQLQRRGFFICDQPYEP 763
Cdd:TIGR00463 499 KD---AVKVKVIMPDASIVEGVIEADASE----------------------LEVGDVVQFERFGFARLDSADKD 547
|
|
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
273-763 |
2.73e-143 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 438.38 E-value: 2.73e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 273 GKVTVRFPPEASGYLHIGHAKAALLN----QHYQvnfkGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKP-DQFTYTS 347
Cdd:PRK05347 28 TRVHTRFPPEPNGYLHIGHAKSICLNfglaQDYG----GKCNLRFDDTNPEKEDQEYVDSIKEDVRWLGFDWsGELRYAS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 348 DHFESIMKYAEKLIQEGKAYVDDTPAEQMkaeREQR-------IESKHRKNSIEKNLQMWEEMKKGsQF--GqSCCLRAK 418
Cdd:PRK05347 104 DYFDQLYEYAVELIKKGKAYVDDLSAEEI---REYRgtltepgKNSPYRDRSVEENLDLFERMRAG-EFpeG-SAVLRAK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 419 IDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHD-RdeQFY-WIIEALGIR-KP 495
Cdd:PRK05347 179 IDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDhR--PLYdWVLDNLPIPpHP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 496 YIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSR--SVVNM---Ewdkiw 570
Cdd:PRK05347 257 RQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTKqdSVIDMsmlE----- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 571 AFNKKVIDPVAPRYVALLK--KEVIpVNIPEAQEEMKEVAKHPKNPDVGLKPVWYSPKVFIEGAD-AET-------LSEG 640
Cdd:PRK05347 332 SCIREDLNENAPRAMAVLDplKLVI-TNYPEGQVEELEAPNHPEDPEMGTREVPFSRELYIEREDfMEEppkkyfrLVPG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 641 EMVTFINWGNINITKINKNADGKIVSL------DAKLNLENKDYK-KTTkITWLaETAHAlpIPAICVTYEHLITKPVLG 713
Cdd:PRK05347 411 KEVRLRNAYVIKCEEVVKDADGNITEIhctydpDTLSGNPADGRKvKGT-IHWV-SAAHA--VPAEVRLYDRLFTVPNPA 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 585187043 714 KDEDFKQYVNKNSKHEELMLGDPCLKDLKKGDIIQLQRRGFFICDQPYEP 763
Cdd:PRK05347 487 AGKDFLDFLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTP 536
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
274-583 |
4.13e-139 |
|
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Gln to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. GlnRS contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185676 [Multi-domain] Cd Length: 238 Bit Score: 415.50 E-value: 4.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 274 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESI 353
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPYKVTYASDYFDQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 354 MKYAEKLIQEGKAYVddtpaeqmkaereqrieskhrknsieknlqmweemkkgsqfgqscclrakidmssnngcmrdptl 433
Cdd:cd00807 81 YEYAEQLIKKGKAYV----------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 434 yrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKR 513
Cdd:cd00807 96 -------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYTVMSKR 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 514 KLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 583
Cdd:cd00807 169 KLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
275-758 |
6.67e-112 |
|
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found in the cytosolic compartment of eukaryotes, in E. coli and a number of other Gram-negative Bacteria, and in Deinococcus radiodurans. In contrast, the pathway to Gln-tRNA in mitochondria, Archaea, Gram-positive Bacteria, and a number of other lineages is by misacylation with Glu followed by transamidation to correct the aminoacylation to Gln. This enzyme is a class I tRNA synthetase (hit by the pfam model tRNA-synt_1c) and is quite closely related to glutamyl-tRNA synthetases. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273079 [Multi-domain] Cd Length: 522 Bit Score: 355.38 E-value: 6.67e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 275 VTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPD-QFTYTSDHFESI 353
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEgKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 354 MKYAEKLIQEGKAYVDDTPAEQMKAEREQRIE----SKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMR 429
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDpgknSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 430 DPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGI-RKPYIWEYSRLNLNNT 508
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIfPRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 509 VLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALL 588
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 589 KKEVIPVNIPEAQEEMKEVAKHPKNPDVGLKPVWYSPKVFIEGADAET--------LSEGEMVTFINWGNINITKINKNA 660
Cdd:TIGR00440 321 DPVEVVIENLSDEYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREeankqykrLVLGKEVRLRNAYVIKAERVEKDA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 661 DGKIVSL----DAK-LNLENKDYKKT-TKITWLAeTAHALPIPAicVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLG 734
Cdd:TIGR00440 401 AGKITTIfctyDNKtLGKEPADGRKVkGVIHWVS-ASSKYPTET--RLYDRLFKVPNPGAPDDFLSVINPESLVIKQGFM 477
|
490 500
....*....|....*....|....
gi 585187043 735 DPCLKDLKKGDIIQLQRRGFFICD 758
Cdd:TIGR00440 478 EHSLGDAVANKRFQFEREGYFCLD 501
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
273-803 |
2.86e-103 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 340.16 E-value: 2.86e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 273 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIK-PDQFTYTSDHFE 351
Cdd:PRK14703 30 PRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWLGFDwGEHLYYASDYFE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 352 SIMKYAEKLIQEGKAYVDDTPAEQMkaeREQR-------IESKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSN 424
Cdd:PRK14703 110 RMYAYAEQLIKMGLAYVDSVSEEEI---RELRgtvtepgTPSPYRDRSVEENLDLFRRMRAGEFPDGAHVLRAKIDMSSP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 425 NGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR--KPYIWEYSR 502
Cdd:PRK14703 187 NMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLGPWppRPRQYEFAR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 503 LNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAP 582
Cdd:PRK14703 267 LALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVLEFAIRDDLNRRAP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 583 RYVALLKK-EVIPVNIPEAQEEMKEVAKHPKN-PDVGLKPVWYSPKVFIEGAD-AET-------LSEGEMVTFINWGNIN 652
Cdd:PRK14703 347 RVMAVLDPlKVVIENLPAGKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDfSEDppkgfkrLTPGREVRLRGAYIIR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 653 ITKINKNADGKIVSLDAKLNLENKDYKKTTK-----ITWLAeTAHALPIPAicVTYEHLITKPVL-GKDEDFKQYVNKNS 726
Cdd:PRK14703 427 CDEVVRDADGAVTELRCTYDPESAKGEDTGRkaagvIHWVS-AKHALPAEV--RLYDRLFKVPQPeAADEDFLEFLNPDS 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 727 KHEELMLGDPCLKDLKKGDIIQLQRRGFFICD----QPYEPV---------SASERRGSERRARIGTARmwPTTPFKERP 793
Cdd:PRK14703 504 LRVAQGRVEPAVRDDPADTRYQFERQGYFWADpvdsRPDALVfnriitlkdTWGARAREAAREKRAAAP--KKTAKPRRS 581
|
570
....*....|
gi 585187043 794 GPSLDNTCAP 803
Cdd:PRK14703 582 KAEARAEAAA 591
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
273-763 |
5.29e-103 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 333.49 E-value: 5.29e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 273 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFES 352
Cdd:PTZ00437 50 GKPYFRFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWKPDWVTFSSDYFDQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 353 IMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKNSIEKNLQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPT 432
Cdd:PTZ00437 130 LHEFAVQLIKDGKAYVDHSTPDELKQQREQREDSPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRDFI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 433 LYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSK 512
Cdd:PTZ00437 210 AYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLLSK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 513 RKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPRYVALLkkEV 592
Cdd:PTZ00437 290 RKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVI--DP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 593 IPVNIPEAQEEMK-EVAKHPKNPDVGLKPVWYSPKVFIEGADAET---------LSEGEMVTFINW-GNINITKINKNAD 661
Cdd:PTZ00437 368 IKVVVDNWKGEREfECPNHPRKPELGSRKVMFTDTFYVDRSDFRTednnskfygLAPGPRVVGLKYsGNVVCKGFEVDAA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 662 GKIVSLDAKLNLENKDyKKTTKITWLAETAhalPIPAICVTYEHLITKPVLGKDEDFKQYVNKNSKHEELMLGDPCLKDL 741
Cdd:PTZ00437 448 GQPSVIHVDIDFERKD-KPKTNISWVSATA---CTPVEVRLYNALLKDDRAAIDPEFLKFIDEDSEVVSHGYAEKGIENA 523
|
490 500
....*....|....*....|..
gi 585187043 742 KKGDIIQLQRRGFFICDQPYEP 763
Cdd:PTZ00437 524 KHFESVQAERFGYFVVDPDTRP 545
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
237-763 |
1.98e-102 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 338.27 E-value: 1.98e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 237 FQSVGTKWNVSTTKAKVTPEKKqdvgkfvelpgAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDT 316
Cdd:PLN02859 238 FFSDGSVLRPSNTKEILEKHLK-----------ATGGKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 317 NPEKEKEDFEKVILEDVAMLHIKPDQFTYTSDHFESIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKNSIEKN 396
Cdd:PLN02859 307 NPEAEKKEYIDHIEEIVEWMGWEPFKITYTSDYFQELYELAVELIRRGHAYVDHQTPEEIKEYREKKMNSPWRDRPIEES 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 397 LQMWEEMKKGSQFGQSCCLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEY 476
Cdd:PLN02859 387 LKLFEDMRRGLIEEGKATLRMKQDMQNDNFNMYDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEF 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 477 HDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQG 556
Cdd:PLN02859 467 ETRRASYYWLLDSLGLYQPYVWEYSRLNVTNTVMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 557 SSRS---VVNMewDKIWAFNKKVIDPVAPRYVALLKK-EVIPVNIPEAQEEMKEVAKHPKNPDVGLKP---VWYSPKVFI 629
Cdd:PLN02859 547 ITRSdnsLIRM--DRLEHHIREELNKTAPRTMVVLHPlKVVITNLESGEVIELDAKRWPDAQNDDPSAfykVPFSRVVYI 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 630 EGADAET--------LSEGEMVTFINWGNINITK-INKNADGKIVSLDAKLnlenkDYKKTTK----ITWLAETAHAL-P 695
Cdd:PLN02859 625 ERSDFRLkdskdyygLAPGKSVLLRYAFPIKCTDvVLADDNETVVEIRAEY-----DPEKKTKpkgvLHWVAEPSPGVeP 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585187043 696 IPAICVTYEHLITKPVLGKDEDFKQYVNKNSKheELMLGD---PCLKDLKKGDIIQLQRRGFFICDQPYEP 763
Cdd:PLN02859 700 LKVEVRLFDKLFLSENPAELEDWLEDLNPQSK--EVISGAyavPSLKDAKVGDRFQFERLGYFAVDKDSTP 768
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
256-754 |
1.49e-100 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 326.42 E-value: 1.49e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 256 EKKQDVGKFVELPGAEMGKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDV 333
Cdd:PRK04156 83 EKKEEKKGLPPLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKRPDPEayDMILEDL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 334 AMLHIKPDQFTYTSDHFESIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESKHRKNSIEKNLQMWEEMKKGSQFGQSC 413
Cdd:PRK04156 163 KWLGVKWDEVVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKELRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 414 CLRAKIDMSSNNGCMRDPTLYRCKIQPHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIR 493
Cdd:PRK04156 243 VVRVKTDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 494 KPYIWEYSRLNLNNTVLSKRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFN 573
Cdd:PRK04156 323 YPETIHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAIN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 574 KKVIDPVAPRYVALlkKEVIPVNIPEAQEEMKEVAKHPKNPDVGLKPVWYSPKVFIEGADAETLseGEMVTFINWGNINI 653
Cdd:PRK04156 403 RKLIDPIANRYFFV--RDPVELEIEGAEPLEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAE--GKMVRLMDLFNVEI 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 654 TKINKNAdGKIVSLDaklnLENKDYKKTTKITWLAETaHALPIPAIcvtyehlitKPVLGKDEDFkqyvnknskheelml 733
Cdd:PRK04156 479 TGVSVDK-ARYHSDD----LEEARKNKAPIIQWVPED-ESVPVRVL---------KPDGGDIEGL--------------- 528
|
490 500
....*....|....*....|.
gi 585187043 734 GDPCLKDLKKGDIIQLQRRGF 754
Cdd:PRK04156 529 AEPDVADLEVDDIVQFERFGF 549
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
273-560 |
2.08e-64 |
|
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Glutamyl- or glutaminyl-tRNA synthetase is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 439779 [Multi-domain] Cd Length: 467 Bit Score: 225.06 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 273 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFE 351
Cdd:COG0008 3 MKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEgPYYQSDRFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 352 SIMKYAEKLIQEGKAYVDDTPAEQMKAEREQRIESK--------HRKNSIEKNLQMWEEmkkgsqfGQSCCLRAKI---- 419
Cdd:COG0008 83 IYYEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGkpprydgrCRDLSPEELERMLAA-------GEPPVLRFKIpeeg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 420 ----DMSS-----NNGCMRDPTLYRckiqphpRTGnkynvYPTYDFACPIVDSIEGVTHALRT------TEYHDrdeqfy 484
Cdd:COG0008 156 vvfdDLVRgeitfPNPNLRDPVLYR-------ADG-----YPTYNFAVVVDDHLMGITHVIRGeehlsnTPRQI------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 485 WIIEALGIRKPyiwEYSRLNL----NNTVLSKRKltwfvneGLVdgwddprfpTVRGVLRRGMTVEGLKQFIAAQGSSRS 560
Cdd:COG0008 218 WLYEALGWEPP---EFAHLPLilgpDGTKLSKRK-------GAV---------TVSGLRRRGYLPEAIRNYLALLGWSKS 278
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
274-583 |
1.16e-62 |
|
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating Glutamyl-tRNA synthetase (GluRS) cataytic core domain. These enzymes attach Glu to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea and most bacteria lack GlnRS. In these organisms, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme.
Pssm-ID: 185682 [Multi-domain] Cd Length: 240 Bit Score: 212.21 E-value: 1.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 274 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFE--KVILEDVAMLHIKPDQFTYTSDHFE 351
Cdd:cd09287 1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPRTKRPDPEayDMIPEDLEWLGVKWDEVVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 352 SIMKYAEKLIQEGKAYVddtpaeqmkaereqrieskhrknsieknlqmweemkkgsqfgqscclrakidmssnngcmrdp 431
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 432 tlyrckiqpHPRTGNKYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNLNNTVLS 511
Cdd:cd09287 98 ---------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRLKIEGGKLS 168
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585187043 512 KRKLTWFVNEGLVDGWDDPRFPTVRGVLRRGMTVEGLKQFIAAQGSSRSVVNMEWDKIWAFNKKVIDPVAPR 583
Cdd:cd09287 169 TSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
581-758 |
5.14e-48 |
|
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only glutamyl and glutaminyl tRNA synthetases. In some organizms, a single glutamyl-tRNA synthetase aminoacylates both tRNA(Glu) and tRNA(Gln).
Pssm-ID: 427609 [Multi-domain] Cd Length: 175 Bit Score: 168.60 E-value: 5.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 581 APRYVALLKKEVIPV-NIPEAQEEMKEVAKHPKNPDVGLKPVWYSPKVFIEGADAETLSEGEMVTFINWGNINITKINKN 659
Cdd:pfam03950 1 APRYMAVLDPVKVVIeNYPEGQEETAEVPNHPKNPELGTRKVPFSREIYIEREDFKRLAPGEEVRLMDAYNIKVTEVVKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 660 ADGKIVSLDAKLNLENKDY---KKTTKITWLAETAhalPIPAICVTYEHLITkpvlgKDEDFKQYVNKNSKHE-ELMLGD 735
Cdd:pfam03950 81 EDGNVTELHCTYDGDDLGGarkVKGKIIHWVSASD---AVPAEVRLYDRLFK-----DEDDADFLLNPDSLKVlTEGLAE 152
|
170 180
....*....|....*....|...
gi 585187043 736 PCLKDLKKGDIIQLQRRGFFICD 758
Cdd:pfam03950 153 PALANLKPGDIVQFERIGYFRVD 175
|
|
| GST_C_GluProRS_N |
cd10309 |
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ... |
151-234 |
2.31e-38 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198342 [Multi-domain] Cd Length: 81 Bit Score: 137.45 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 151 EHTEIDHWLEFSATKLSSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEqlkQNKAPVHVKRWFGF 230
Cdd:cd10309 1 EQTEVDHWISFSAGRLSCDQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGEWLA---SKEKYVNVTRWFKF 77
|
....
gi 585187043 231 LEAQ 234
Cdd:cd10309 78 ISSQ 81
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
274-559 |
1.22e-37 |
|
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA synthetase(GluRS)/Glutaminyl-tRNA synthetase (GlnRS) cataytic core domain. These enzymes attach Glu or Gln, respectively, to the appropriate tRNA. Like other class I tRNA synthetases, they aminoacylate the 2'-OH of the nucleotide at the 3' end of the tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. These enzymes function as monomers. Archaea, cellular organelles, and some bacteria lack GlnRS. In these cases, the "non-discriminating" form of GluRS aminoacylates both tRNA(Glu) and tRNA(Gln) with Glu, which is converted to Gln when appropriate by a transamidation enzyme. The discriminating form of GluRS differs from GlnRS and the non-discriminating form of GluRS in their C-terminal anti-codon binding domains.
Pssm-ID: 185672 [Multi-domain] Cd Length: 230 Bit Score: 141.07 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 274 KVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ-FTYTSDHFES 352
Cdd:cd00418 1 TVVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEgPYRQSDRFDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 353 IMKYAEKLIQEGkayvddtpaeqmkaereqrieskhrknsieknlqmweemkkgsqfgqscclrakidmssnngcmrdpt 432
Cdd:cd00418 81 YRAYAEELIKKG-------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 433 lyrckiqphprtgnkynVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEALGIRKPYIWEYSRLNL-NNTVLS 511
Cdd:cd00418 93 -----------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLeDGTKLS 155
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 585187043 512 KRKLtwfvneglvdgwddprFPTVRGVLRRGMTVEGLKQFIAAQGSSR 559
Cdd:cd00418 156 KRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSK 187
|
|
| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
810-859 |
3.27e-25 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 98.85 E-value: 3.27e-25
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 585187043 810 LYNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPG 859
Cdd:cd00936 1 LYKKIAAQGDLVRELKAKKAPKEEIDAAVKKLLALKADYKEATGQDYKPG 50
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
810-862 |
1.03e-24 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 97.57 E-value: 1.03e-24
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 585187043 810 LYNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPP 862
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKALTGKDYKPGAAP 53
|
|
| GST_C_AaRS_like |
cd10289 |
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ... |
151-234 |
3.23e-23 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198322 [Multi-domain] Cd Length: 82 Bit Score: 94.30 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 151 EHTEIDHWLEFsATKLSSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKaPVHVKRWFGF 230
Cdd:cd10289 1 EAAQVDQWLDL-AGSLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSDKEKKK-FPHVTRWFNH 78
|
....
gi 585187043 231 LEAQ 234
Cdd:cd10289 79 IQNL 82
|
|
| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
811-863 |
1.39e-22 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 91.63 E-value: 1.39e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 585187043 811 YNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTGQEYKPGNPPA 863
Cdd:smart00991 1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQDYKPGAPPG 53
|
|
| GST_C_GluRS_N |
cd10306 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ... |
151-233 |
1.69e-17 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.
Pssm-ID: 198339 [Multi-domain] Cd Length: 87 Bit Score: 78.16 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 151 EHTEIDHWLEFSATKLSSCNL--FTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKAPvHVKRWF 228
Cdd:cd10306 3 DKEQVAEWIDFATTLLVLKDFkaLSQALEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAGSLIKNKVYV-NLSRWF 81
|
....*
gi 585187043 229 GFLEA 233
Cdd:cd10306 82 SFLES 86
|
|
| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
811-852 |
2.26e-17 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 76.42 E-value: 2.26e-17
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 585187043 811 YNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKT 852
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
|
|
| ProRS-C_1 |
pfam09180 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
891-974 |
1.97e-15 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 462709 Cd Length: 67 Bit Score: 71.40 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 891 EVVRKLKAEKapkIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCV-CGRNaAKYYTL 969
Cdd:pfam09180 3 EFKEALEEKG---FVLAPWCGDEECEDKIKEET-------------GATSRCIPFD---QEEEGGKCIvCGKP-AKKWVL 62
|
....*
gi 585187043 970 FGRSY 974
Cdd:pfam09180 63 FARSY 67
|
|
| ProRS-C_1 |
smart00946 |
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ... |
903-974 |
2.42e-15 |
|
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.
Pssm-ID: 198014 Cd Length: 67 Bit Score: 71.45 E-value: 2.42e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585187043 903 KIAQIPFCGEIDCEDWIKKTTardqdlepgapsmGAKSLCVPFKplcELQPGARCVCGRNAAKYYTLFGRSY 974
Cdd:smart00946 12 KFVLAPWCGDEECEEKIKEET-------------GATIRCIPFD---QDEEPGKCVVCGKPAKKWVLFARSY 67
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
273-529 |
8.64e-14 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 75.16 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 273 GKVTVRFPPEASGYLHIGHAKAALLNQHYQVNFKGKLIMRFDDTNPEKEKEDFEKVILEDVAMLHIKPDQ--------FT 344
Cdd:PLN02627 44 GPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvggeyGP 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 345 YTSDHFESIMK-YAEKLIQEGKAY---VDDTPAEQMKAEREQ-----RIESKHRKNSIEknlQMWEEMKKGSQFgqscCL 415
Cdd:PLN02627 124 YRQSERNAIYKqYAEKLLESGHVYpcfCTDEELEAMKEEAELkklppRYTGKWATASDE---EVQAELAKGTPY----TY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 416 RAKIdmsSNNGCMRDPTLYRCKIQPHPRT-GN----KYNVYPTYDFACPIVDSIEGVTHALRTTEYHDRDEQFYWIIEAL 490
Cdd:PLN02627 197 RFRV---PKEGSVKIDDLIRGEVSWNTDTlGDfvllRSNGQPVYNFCVAVDDATMGITHVIRAEEHLPNTLRQALIYKAL 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 585187043 491 GIRKPyiwEYSRLNL----NNTVLSKR---------KLTWFVNEGLVD-----GWDD 529
Cdd:PLN02627 274 GFPMP---RFAHVSLilapDRSKLSKRhgatsvgqfREMGYLPDAMVNylallGWND 327
|
|
| ProRS_anticodon_zinc |
cd00862 |
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ... |
903-974 |
5.18e-11 |
|
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.
Pssm-ID: 238439 [Multi-domain] Cd Length: 202 Bit Score: 63.09 E-value: 5.18e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585187043 903 KIAQIPFCGEIDCEDWIKKTTArdqdlepgapsmgAKSLCVPFkPLCELQPGARCV-CGRNaAKYYTLFGRSY 974
Cdd:cd00862 145 GIVLAPWCGEEECEEEIKEETA-------------ATILCIPF-DEAKLEEGGKCVvCGRP-AKAYARFAKSY 202
|
|
| GST_C_AIMP3 |
cd10305 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
150-228 |
1.20e-10 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.
Pssm-ID: 198338 [Multi-domain] Cd Length: 101 Bit Score: 59.23 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 150 LEHTEIDHWLEFSATKLSSC---NLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLKG-----SAAWQEQLKqnkap 221
Cdd:cd10305 2 EERAQVDQWLEYRVTQVAPAsdkADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGLHPimkdlSPQEKEQYL----- 76
|
....*..
gi 585187043 222 vHVKRWF 228
Cdd:cd10305 77 -NVSRWF 82
|
|
| GstA |
COG0625 |
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
121-244 |
5.07e-08 |
|
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 54.13 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 121 ENVVFTDINSILRYLARVATTTGLYGSNLLEHTEIDHWLEFSATKLSSC--NLFTS-------------------AINEL 179
Cdd:COG0625 59 DGLVLTESLAILEYLAERYPEPPLLPADPAARARVRQWLAWADGDLHPAlrNLLERlapekdpaaiararaelarLLAVL 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585187043 180 NHCLSLRTYLVGNSLSLADLCVWATLKGSAAWQEQLKQNKapvHVKRWFGFLEAQQAFQSVGTKW 244
Cdd:COG0625 139 EARLAGGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYP---NLAAWLARLAARPAFQRALAAA 200
|
|
| GST_C_Arc1p_N_like |
cd10304 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ... |
151-246 |
5.46e-08 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.
Pssm-ID: 198337 [Multi-domain] Cd Length: 100 Bit Score: 51.60 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 151 EHTEIDHWLEFSATKLSSCNLFTSaINELNHCLSLRTYLVGNS-LSLADLCVWATLKGSAA-WQEQLKQNKAPV-HVKRW 227
Cdd:cd10304 3 QSAEVAQWLSVAKSGPVSKDVQET-LGQLNLHLRTRTFLLGTGkPSVADVAVFEAVLPVVKeWSDEVKTGYAKYrHILRW 81
|
90
....*....|....*....
gi 585187043 228 FGFLEAQQAFQSVGTKWNV 246
Cdd:cd10304 82 VDYVQNLLLFIPEADKIEV 100
|
|
| GST_C_AIMP2 |
cd03200 |
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ... |
132-234 |
2.46e-07 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease.
Pssm-ID: 198309 [Multi-domain] Cd Length: 96 Bit Score: 49.44 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 132 LRYLARVattTGLYGSNLLEHTEIDHWLEFSATKL--SSCNLFTSAINELNHCLSLRTYLVGNSLSLADLCVWATLkgsa 209
Cdd:cd03200 1 ARFLFRL---LGDESDDPVNATLIDSWVDTAIFQLleGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAV---- 73
|
90 100
....*....|....*....|....*
gi 585187043 210 awQEQLKQNKAPVHVKRWFGFLEAQ 234
Cdd:cd03200 74 --LQTGLASGAPANVQRWMKSCENL 96
|
|
| GST_C_EF1Bgamma_like |
cd03181 |
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ... |
151-240 |
3.53e-06 |
|
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.
Pssm-ID: 198290 [Multi-domain] Cd Length: 123 Bit Score: 47.17 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 151 EHTEIDHWLEFSATKL--SSCNLF--------------TSAINELNHC-------LSLRTYLVGNSLSLADLCVWATLKG 207
Cdd:cd03181 1 EAAQVLQWISFANSELlpAAATWVlpllgiapynkkavDKAKEDLKRAlgvleehLLTRTYLVGERITLADIFVASALLR 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 585187043 208 ------SAAWQEQLkqnkapVHVKRWFGFLEAQQAFQSV 240
Cdd:cd03181 81 gfetvlDPEFRKKY------PNVTRWFNTVVNQPKFKAV 113
|
|
| WHEP-TRS |
pfam00458 |
WHEP-TRS domain; |
882-935 |
3.97e-06 |
|
WHEP-TRS domain;
Pssm-ID: 459819 [Multi-domain] Cd Length: 53 Bit Score: 44.79 E-value: 3.97e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585187043 882 LYDEVAAQGEVVRKLKAEKAPKIaqipfcgEIDCEdwIKK--------TTARDQDLEPGAPS 935
Cdd:pfam00458 1 LTEKIKAQGDLVRKLKAEKAPKE-------EIDAA--VKKllalkaqyKALTGKDYKPGAAP 53
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| WEPRS_RNA |
cd00936 |
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ... |
882-903 |
6.99e-06 |
|
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238473 [Multi-domain] Cd Length: 50 Bit Score: 44.15 E-value: 6.99e-06
|
| HisRS_RNA |
cd00938 |
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ... |
813-847 |
1.32e-05 |
|
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238474 [Multi-domain] Cd Length: 45 Bit Score: 43.23 E-value: 1.32e-05
10 20 30
....*....|....*....|....*....|....*
gi 585187043 813 RVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAE 847
Cdd:cd00938 6 AVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQ 40
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| MetRS_RNA |
cd00939 |
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ... |
814-853 |
1.72e-05 |
|
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238475 [Multi-domain] Cd Length: 45 Bit Score: 42.84 E-value: 1.72e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 585187043 814 VAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEKTG 853
Cdd:cd00939 5 VAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEG 44
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| WHEP-TRS |
smart00991 |
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ... |
883-905 |
2.10e-05 |
|
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.
Pssm-ID: 214960 [Multi-domain] Cd Length: 56 Bit Score: 42.71 E-value: 2.10e-05
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| WHEPGMRS_RNA |
cd01200 |
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ... |
883-905 |
2.10e-05 |
|
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238605 [Multi-domain] Cd Length: 42 Bit Score: 42.53 E-value: 2.10e-05
10 20
....*....|....*....|...
gi 585187043 883 YDEVAAQGEVVRKLKAEKAPKIA 905
Cdd:cd01200 1 YEKIAEQGDLVRKLKAEKAPKEE 23
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| PLN02734 |
PLN02734 |
glycyl-tRNA synthetase |
814-851 |
2.84e-05 |
|
glycyl-tRNA synthetase
Pssm-ID: 178335 [Multi-domain] Cd Length: 684 Bit Score: 48.20 E-value: 2.84e-05
10 20 30
....*....|....*....|....*....|....*...
gi 585187043 814 VAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEK 851
Cdd:PLN02734 16 VTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSAL 53
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|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
276-359 |
3.77e-04 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 41.70 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585187043 276 TVRFPPEASGYLHIGHAKAALLN---QHY--QVNFKGKLIMRFDDTNPEKEK------EDFEKVILEDVAMLHikpDQFT 344
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFdflAQAyrKLGYKVRCIALIDDAGGLIGDpankkgENAKAFVERWIERIK---EDVE 77
|
90
....*....|....*
gi 585187043 345 YTSDHFESIMKYAEK 359
Cdd:cd00802 78 YMFLQAADFLLLYET 92
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| GST_C_Delta_Epsilon |
cd03177 |
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ... |
179-228 |
5.59e-04 |
|
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.
Pssm-ID: 198287 [Multi-domain] Cd Length: 117 Bit Score: 40.59 E-value: 5.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 585187043 179 LNHCLSLRTYLVGNSLSLADLCVWATLkGSAAWQEqLKQNKAPvHVKRWF 228
Cdd:cd03177 50 LETFLEGSDYVAGDQLTIADLSLVATV-STLEVVG-FDLSKYP-NVAAWY 96
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| GlyRS_RNA |
cd00935 |
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ... |
810-851 |
1.09e-03 |
|
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.
Pssm-ID: 238472 [Multi-domain] Cd Length: 51 Bit Score: 37.85 E-value: 1.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 585187043 810 LYNRVAAQGDVVRELKSKKAAKEDIDAAVKQLLALKAEYKEK 851
Cdd:cd00935 4 LRAAVKEQGDLVRKLKEEGAPDVDIKKAVAELKARKKLLEDK 45
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