|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
52-683 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 948.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 52 KEESMNSFTNTNFIHQIIEDDLKKKKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRY 131
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 132 INSIQEDVKWLGFNWNEHLYYASDYFDQLYEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPYRNRSIEENLVLF 211
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 212 ENMKLGKYKEGEKVLRAKIDMSSGNINLRDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHR 291
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 292 PLYEWFQDKLNI-FKTRQIEFARLNVSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAK 370
Cdd:PRK05347 241 PLYDWVLDNLPIpPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 371 RENMISYELLELCAREDMNKKAIRLFSILKPLKVIITNFDDNLYNntnyyELTALNHPKNEQMGIRKIKFEKEIYIDHDD 450
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVE-----ELEAPNHPEDPEMGTREVPFSRELYIERED 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 451 FQENPASNFYRLAPNRTVRLRYAFCITCNEVIKDEsTGKIIELRCTYDPDSKSGNlttsnntttiGENIKKVKSTIHWVS 530
Cdd:PRK05347 396 FMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDA-DGNITEIHCTYDPDTLSGN----------PADGRKVKGTIHWVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 531 AKNSHKAEFRMYDKLFLKANPESDyddthvekimKNFTSelgtspnndnnndnnnndgiamsndldktyqdeyyldtenk 610
Cdd:PRK05347 465 AAHAVPAEVRLYDRLFTVPNPAAG----------KDFLD----------------------------------------- 493
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23489563 611 nddqeklktdkdnqvgwrkYINKNSLIVHHGLVENYSKNCNIGDPIQFERVGFFVKDKDSTDNEPIFNLTVEL 683
Cdd:PRK05347 494 -------------------FLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGL 547
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
81-685 |
0e+00 |
|
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: 596.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAKIDMSSGNINLR 240
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 241 DPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIF-KTRQIEFARLNVSYM 319
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 320 VMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIRLFSIL 399
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 400 KPLKVIITNFDDnlynntNYYELTALNHPKNEQMGIRKIKFEKEIYIDHDDFQENPASNFYRLAPNRTVRLRYAFCITCN 479
Cdd:TIGR00440 321 DPVEVVIENLSD------EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 480 EVIKDEStGKIIELRCTYDPDSKSGNlttsnntttiGENIKKVKSTIHWVSAKNSHKAEFRMYDKLFLKANPesdyddTH 559
Cdd:TIGR00440 395 RVEKDAA-GKITTIFCTYDNKTLGKE----------PADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP------GA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 560 VEKIMKNftselgtspnndnnndnnnndgiamsndldktyqdeyyldtenknddqeklktdkdnqvgwrkyINKNSLIVH 639
Cdd:TIGR00440 458 PDDFLSV----------------------------------------------------------------INPESLVIK 473
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 23489563 640 HGLVENYSKNCNIGDPIQFERVGFFVKD-KDSTDNEPIFNLTVELVE 685
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKD 520
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
80-394 |
1.65e-141 |
|
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: 421.66 E-value: 1.65e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 80 YVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNeHLYYASDYFDQ 159
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 160 LYEWALQLIKQGDAYVddqtieeirknrgslkepginspyrnrsieenlvlfenmklgkykegekvlrakidmssgninl 239
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 240 rdpilyrimnkiHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYM 319
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23489563 320 VMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIR 394
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
81-389 |
6.02e-121 |
|
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: 371.27 E-value: 6.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLkePGINSPYRNRSIEENLVLF-ENMKLGKYKEGEKVLRAKIDMSSgNINL 239
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 240 RDPILYRIMN---KIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIF-KTRQIEFARLN 315
Cdd:pfam00749 159 RDPVRGRIKFtpqEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23489563 316 VSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKR-ENMISYELLELCAREDMN 389
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
81-549 |
9.94e-114 |
|
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: 357.95 E-value: 9.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPY----RNRSIEENlvlfENMKlgkyKEGEK-VLRAKI----- 230
Cdd:COG0008 85 YEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGEPpVLRFKIpeegv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 231 ---DMSSG-----NINLRDPILYRiMNKihpktknkwviYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLN 302
Cdd:COG0008 157 vfdDLVRGeitfpNPNLRDPVLYR-ADG-----------YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 303 IFKtrqIEFARLNVSY----MVMSKRKLLTlvnekwvndwddprmpTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYE 378
Cdd:COG0008 225 WEP---PEFAHLPLILgpdgTKLSKRKGAV----------------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 379 LLELCAREDMNKKAiRLFSILKPLKVIITNFDdnLYNNTNYYELTALNHPKNEQMGI-----RKIKFEKE---------- 443
Cdd:COG0008 286 LEELIEAFDLDRVS-RSPAVFDPVKLVWLNGP--YIRALDDEELAELLAPELPEAGIredleRLVPLVREraktlselae 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 444 ----IYIDHDDfqENPASNfyRLAPNrTVRlryafcitcnEVIKDEStgKIIELRCTYDPDSksgnlttsnntttigeni 519
Cdd:COG0008 363 larfFFIERED--EKAAKK--RLAPE-EVR----------KVLKAAL--EVLEAVETWDPET------------------ 407
|
490 500 510
....*....|....*....|....*....|
gi 23489563 520 kkVKSTIHWVSAknshKAEFRmyDKLFLKA 549
Cdd:COG0008 408 --VKGTIHWVSA----EAGVK--DGLLFMP 429
|
|
| PTPLA |
pfam04387 |
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ... |
815-950 |
2.88e-38 |
|
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein tyrosine phosphatase-like protein, PTPLA. A significant variation of PTPLA from other protein tyrosine phosphatases is the presence of proline instead of catalytic arginine at the active site. It is thought that PTPLA proteins have a role in the development, differentiation, and maintenance of a number of tissue types.
Pssm-ID: 461286 Cd Length: 163 Bit Score: 140.35 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 815 FIKSDVKIVVTQIFSRFFIVHLIFNYLPN--NNKWILSCLIPWAIIDIIRYLIYSLNLLNIRV-GILTSLRNKLPLILYP 891
Cdd:pfam04387 15 LVRSPVLTTFMQVASRLFVVWGVIYSFPEvqTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYFLTWLRYTLFIVLYP 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 23489563 892 IGIVSEVVCTLTSLKNIQSTPflrSFPYAMPNNLNFQIDIYYFCIFVLFLYIPGSIFVY 950
Cdd:pfam04387 95 LGVLSEALLIYQALPYFEETG---LYSVSLPNPFNFSFSYPYFLILLLLLYIPGFYVLY 150
|
|
| PLN02838 |
PLN02838 |
3-hydroxyacyl-CoA dehydratase subunit of elongase |
816-961 |
2.16e-16 |
|
3-hydroxyacyl-CoA dehydratase subunit of elongase
Pssm-ID: 166479 Cd Length: 221 Bit Score: 79.07 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 816 IKSDVKIVVTQIFSRFFIVHLIFNYLPNNNKWIL--SCLIPWAIIDIIRYLIYSLN-LLNIRVGILTSLRNKLPLILYPI 892
Cdd:PLN02838 70 VRSPVSATLPQIGSRLFLTWGILWSFPEVRSHILvtSLVISWSITEIIRYSFFGMKeAFGFAPSWLLWLRYSTFLLLYPT 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23489563 893 GIVSEVVCTLTSLKNIQSTpflRSFPYAMPNNLNFQIDIYYFCIFVLFLYIPGSIFVYAAAISHFKLAI 961
Cdd:PLN02838 150 GITSEVGLIYIALPYMKAS---EKYCLRMPNKWNFSFDYFYASILVLAIYVPGSPHMYSYMLGQRKKAL 215
|
|
| Ptpl |
COG5198 |
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General ... |
824-950 |
1.06e-11 |
|
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General function prediction only];
Pssm-ID: 227525 Cd Length: 209 Bit Score: 65.31 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 824 VTQIFSRFFIVHLIFnyLPNN---NKWI-LSCLIPWAIIDIIRYLIYSLNLlNIRVGILTSLRNKLPLILYPIGIVSEVV 899
Cdd:COG5198 75 VMQVISRLFIVWGVF--YPYCgiiNSWTyPSITTAWSITEIVRYAFYTFRL-NGIPNTLRVLRYNLFLILYPIGFVSEMY 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 23489563 900 CTLTSLKNIQSTpflrsFPYampnnlnfqidIYYFCIFVLFLYIPGSIFVY 950
Cdd:COG5198 152 CLRALYNAAGKI-----FSL-----------LKVVLPIVMLLYIPGFIFLF 186
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05347 |
PRK05347 |
glutaminyl-tRNA synthetase; Provisional |
52-683 |
0e+00 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 235424 [Multi-domain] Cd Length: 554 Bit Score: 948.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 52 KEESMNSFTNTNFIHQIIEDDLKKKKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRY 131
Cdd:PRK05347 1 MMMSEAEARPSNFIRQIIDEDLASGKHTRVHTRFPPEPNGYLHIGHAKSICLNFGLAQDYGGKCNLRFDDTNPEKEDQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 132 INSIQEDVKWLGFNWNEHLYYASDYFDQLYEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPYRNRSIEENLVLF 211
Cdd:PRK05347 81 VDSIKEDVRWLGFDWSGELRYASDYFDQLYEYAVELIKKGKAYVDDLSAEEIREYRGTLTEPGKNSPYRDRSVEENLDLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 212 ENMKLGKYKEGEKVLRAKIDMSSGNINLRDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHR 291
Cdd:PRK05347 161 ERMRAGEFPEGSAVLRAKIDMASPNINMRDPVLYRIRHAHHHRTGDKWCIYPMYDFAHCISDAIEGITHSLCTLEFEDHR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 292 PLYEWFQDKLNI-FKTRQIEFARLNVSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAK 370
Cdd:PRK05347 241 PLYDWVLDNLPIpPHPRQYEFSRLNLTYTVMSKRKLKQLVEEKHVDGWDDPRMPTISGLRRRGYTPESIREFCERIGVTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 371 RENMISYELLELCAREDMNKKAIRLFSILKPLKVIITNFDDNLYNntnyyELTALNHPKNEQMGIRKIKFEKEIYIDHDD 450
Cdd:PRK05347 321 QDSVIDMSMLESCIREDLNENAPRAMAVLDPLKLVITNYPEGQVE-----ELEAPNHPEDPEMGTREVPFSRELYIERED 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 451 FQENPASNFYRLAPNRTVRLRYAFCITCNEVIKDEsTGKIIELRCTYDPDSKSGNlttsnntttiGENIKKVKSTIHWVS 530
Cdd:PRK05347 396 FMEEPPKKYFRLVPGKEVRLRNAYVIKCEEVVKDA-DGNITEIHCTYDPDTLSGN----------PADGRKVKGTIHWVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 531 AKNSHKAEFRMYDKLFLKANPESDyddthvekimKNFTSelgtspnndnnndnnnndgiamsndldktyqdeyyldtenk 610
Cdd:PRK05347 465 AAHAVPAEVRLYDRLFTVPNPAAG----------KDFLD----------------------------------------- 493
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23489563 611 nddqeklktdkdnqvgwrkYINKNSLIVHHGLVENYSKNCNIGDPIQFERVGFFVKDKDSTDNEPIFNLTVEL 683
Cdd:PRK05347 494 -------------------FLNPDSLVIKQGFVEPSLADAKPEDRFQFEREGYFCADKDSTPGKLVFNRTVGL 547
|
|
| PRK14703 |
PRK14703 |
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional |
63-683 |
0e+00 |
|
glutaminyl-tRNA synthetase/YqeY domain fusion protein; Provisional
Pssm-ID: 237793 [Multi-domain] Cd Length: 771 Bit Score: 713.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 63 NFIHQIIEDDLKKKKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWL 142
Cdd:PRK14703 14 NFITEIIEEDLEAGRYPRVVTRFPPEPNGYLHIGHAKSILLNFGIARDYGGRCHLRMDDTNPETEDTEYVEAIKDDVRWL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 143 GFNWNEHLYYASDYFDQLYEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPYRNRSIEENLVLFENMKLGKYKEG 222
Cdd:PRK14703 94 GFDWGEHLYYASDYFERMYAYAEQLIKMGLAYVDSVSEEEIRELRGTVTEPGTPSPYRDRSVEENLDLFRRMRAGEFPDG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 223 EKVLRAKIDMSSGNINLRDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLN 302
Cdd:PRK14703 174 AHVLRAKIDMSSPNMKLRDPLLYRIRHAHHYRTGDEWCIYPMYDFAHPLEDAIEGVTHSICTLEFENNRAIYDWVLDHLG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 303 IFKTR--QIEFARLNVSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELL 380
Cdd:PRK14703 254 PWPPRprQYEFARLALGYTVMSKRKLRELVEEGYVSGWDDPRMPTIAGQRRRGVTPEAIRDFADQIGVAKTNSTVDIGVL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 381 ELCAREDMNKKAIRLFSILKPLKVIITNFDDnlynnTNYYELTALNHPKN-EQMGIRKIKFEKEIYIDHDDFQENPASNF 459
Cdd:PRK14703 334 EFAIRDDLNRRAPRVMAVLDPLKVVIENLPA-----GKVEELDLPYWPHDvPKEGSRKVPFTRELYIERDDFSEDPPKGF 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 460 YRLAPNRTVRLRYAFCITCNEVIKDEStGKIIELRCTYDPDSKSGnlttsnntttiGENIKKVKSTIHWVSAKNSHKAEF 539
Cdd:PRK14703 409 KRLTPGREVRLRGAYIIRCDEVVRDAD-GAVTELRCTYDPESAKG-----------EDTGRKAAGVIHWVSAKHALPAEV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 540 RMYDKLFLKANPESdyddthvekimknftselgtspnndnnndnnnndgiamsndldktyQDEYYLdtenknddqeklkt 619
Cdd:PRK14703 477 RLYDRLFKVPQPEA----------------------------------------------ADEDFL-------------- 496
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23489563 620 dkdnqvgwrKYINKNSLIVHHGLVENYSKNCNIGDPIQFERVGFFVKDK-DSTDNEPIFNLTVEL 683
Cdd:PRK14703 497 ---------EFLNPDSLRVAQGRVEPAVRDDPADTRYQFERQGYFWADPvDSRPDALVFNRIITL 552
|
|
| glnS |
TIGR00440 |
glutaminyl-tRNA synthetase; This protein is a relatively rare aminoacyl-tRNA synthetase, found ... |
81-685 |
0e+00 |
|
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: 596.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:TIGR00440 1 VHTRFPPEPNGYLHIGHAKSICLNFGYAKYYNGTCNLRFDDTNPVKEDPEYVESIKRDVEWLGFKWEGKIRYSSDYFDEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAKIDMSSGNINLR 240
Cdd:TIGR00440 81 YRYAEELIKKGLAYVDELTPEEIREYRGTLTDPGKNSPYRDRSIEENLALFEKMRDGKFKEGKAILRAKIDMASPFPVMR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 241 DPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIF-KTRQIEFARLNVSYM 319
Cdd:TIGR00440 161 DPVAYRIKFAPHHQTGTKWCIYPMYDFTHCISDAMENITHSLCTLEFQDNRRLYDWVLDNIHIFpRPAQYEFSRLNLEGT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 320 VMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIRLFSIL 399
Cdd:TIGR00440 241 VLSKRKLAQLVDDKFVRGWDDPRMPTISGLRRRGYTPASIREFCNRIGVTKQDNNIEVVRLESCIREDLNENAPRAMAVI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 400 KPLKVIITNFDDnlynntNYYELTALNHPKNEQMGIRKIKFEKEIYIDHDDFQENPASNFYRLAPNRTVRLRYAFCITCN 479
Cdd:TIGR00440 321 DPVEVVIENLSD------EYELATIPNHPNTPEFGERQVPFTNEFYIDRADFREEANKQYKRLVLGKEVRLRNAYVIKAE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 480 EVIKDEStGKIIELRCTYDPDSKSGNlttsnntttiGENIKKVKSTIHWVSAKNSHKAEFRMYDKLFLKANPesdyddTH 559
Cdd:TIGR00440 395 RVEKDAA-GKITTIFCTYDNKTLGKE----------PADGRKVKGVIHWVSASSKYPTETRLYDRLFKVPNP------GA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 560 VEKIMKNftselgtspnndnnndnnnndgiamsndldktyqdeyyldtenknddqeklktdkdnqvgwrkyINKNSLIVH 639
Cdd:TIGR00440 458 PDDFLSV----------------------------------------------------------------INPESLVIK 473
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 23489563 640 HGLVENYSKNCNIGDPIQFERVGFFVKD-KDSTDNEPIFNLTVELVE 685
Cdd:TIGR00440 474 QGFMEHSLGDAVANKRFQFEREGYFCLDsKESTTEKVVFNRTVSLKD 520
|
|
| PLN02859 |
PLN02859 |
glutamine-tRNA ligase |
81-694 |
2.16e-171 |
|
glutamine-tRNA ligase
Pssm-ID: 178450 [Multi-domain] Cd Length: 788 Bit Score: 519.32 E-value: 2.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGfnWNEH-LYYASDYFDQ 159
Cdd:PLN02859 265 VYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGGCCYLRFDDTNPEAEKKEYIDHIEEIVEWMG--WEPFkITYTSDYFQE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 160 LYEWALQLIKQGDAYVDDQTIEEIRKNRgslkEPGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAKIDMSSGNINL 239
Cdd:PLN02859 343 LYELAVELIRRGHAYVDHQTPEEIKEYR----EKKMNSPWRDRPIEESLKLFEDMRRGLIEEGKATLRMKQDMQNDNFNM 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 240 RDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYM 319
Cdd:PLN02859 419 YDLIAYRIKFTPHPHAGDKWCIYPSYDYAHCIVDSLENITHSLCTLEFETRRASYYWLLDSLGLYQPYVWEYSRLNVTNT 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 320 VMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKREN-MISYELLELCAREDMNKKAIRLFSI 398
Cdd:PLN02859 499 VMSKRKLNRLVTEKYVDGWDDPRLLTLAGLRRRGVTPTAINAFCRGIGITRSDNsLIRMDRLEHHIREELNKTAPRTMVV 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 399 LKPLKVIITNFDDnlynnTNYYELTALNHP---KNEQMGIRKIKFEKEIYIDHDDFQENPASNFYRLAPNRTVRLRYAFC 475
Cdd:PLN02859 579 LHPLKVVITNLES-----GEVIELDAKRWPdaqNDDPSAFYKVPFSRVVYIERSDFRLKDSKDYYGLAPGKSVLLRYAFP 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 476 ITCNEVIKDESTGKIIELRCTYDPDSKSgnlttsnntttigenikKVKSTIHWVSA----KNSHKAEFRMYDKLFLKANP 551
Cdd:PLN02859 654 IKCTDVVLADDNETVVEIRAEYDPEKKT-----------------KPKGVLHWVAEpspgVEPLKVEVRLFDKLFLSENP 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 552 esdyddthvekimknftSELgtspnndnnndnnnndgiamsndldktyqdeyyldtenknDDqeklktdkdnqvgWRKYI 631
Cdd:PLN02859 717 -----------------AEL----------------------------------------ED-------------WLEDL 726
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23489563 632 NKNSLIVHHGLVENYS-KNCNIGDPIQFERVGFFVKDKDSTDNEPIFNLTVELVEnaSIKKNKK 694
Cdd:PLN02859 727 NPQSKEVISGAYAVPSlKDAKVGDRFQFERLGYFAVDKDSTPEKLVFNRTVTLKD--SYGKGGK 788
|
|
| PTZ00437 |
PTZ00437 |
glutaminyl-tRNA synthetase; Provisional |
84-688 |
6.71e-152 |
|
glutaminyl-tRNA synthetase; Provisional
Pssm-ID: 240418 [Multi-domain] Cd Length: 574 Bit Score: 461.37 E-value: 6.71e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 84 RFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGF--NWnehLYYASDYFDQLY 161
Cdd:PTZ00437 55 RFPPEPNGFLHIGHAKSMNLNFGSARAHGGKCYLRYDDTNPETEEQVYIDAIMEMVKWMGWkpDW---VTFSSDYFDQLH 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 162 EWALQLIKQGDAYVDDQTIEEIRKNRGSLKEpginSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAKIDMSSGNINLRD 241
Cdd:PTZ00437 132 EFAVQLIKDGKAYVDHSTPDELKQQREQRED----SPWRNRSVEENLLLFEHMRQGRYAEGEATLRVKADMKSDNPNMRD 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 242 PILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYMVM 321
Cdd:PTZ00437 208 FIAYRVKYVEHPHAKDKWCIYPSYDFTHCLIDSLEDIDYSLCTLEFETRRESYFWLLEELNLWRPHVWEFSRLNVTGSLL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 322 SKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIRLFSILKP 401
Cdd:PTZ00437 288 SKRKINVLVRKGIVRGFDDPRLLTLAGMRRRGYTPAAINRFCELVGITRSMNVIQISMLENTLREDLDERCERRLMVIDP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 402 LKVIITNFDDNLynntnyyELTALNHPKNEQMGIRKIKFEKEIYIDHDDFQ-ENPASNFYRLAPN-RTVRLRYAFCITCN 479
Cdd:PTZ00437 368 IKVVVDNWKGER-------EFECPNHPRKPELGSRKVMFTDTFYVDRSDFRtEDNNSKFYGLAPGpRVVGLKYSGNVVCK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 480 EVIKDEStGKIIELRCTYDPDSKSgnlttsnntttigenikKVKSTIHWVSAKNSHKAEFRMYDKLFlkanpesdyddth 559
Cdd:PTZ00437 441 GFEVDAA-GQPSVIHVDIDFERKD-----------------KPKTNISWVSATACTPVEVRLYNALL------------- 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 560 vekimknftselgtspnndnnndnnnndgiamsndldktyqdeyyldtenkNDDQEKLKTDkdnqvgWRKYINKNSLIVH 639
Cdd:PTZ00437 490 ---------------------------------------------------KDDRAAIDPE------FLKFIDEDSEVVS 512
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 23489563 640 HGLVENYSKNCNIGDPIQFERVGFFVKDKDSTDNEPIFNLTVELVENAS 688
Cdd:PTZ00437 513 HGYAEKGIENAKHFESVQAERFGYFVVDPDTRPDHLVMNRVLGLREDKE 561
|
|
| GlnRS_core |
cd00807 |
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ... |
80-394 |
1.65e-141 |
|
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: 421.66 E-value: 1.65e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 80 YVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNeHLYYASDYFDQ 159
Cdd:cd00807 1 KVVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGGRCNLRFDDTNPEKEEEEYVDSIKEDVKWLGIKPY-KVTYASDYFDQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 160 LYEWALQLIKQGDAYVddqtieeirknrgslkepginspyrnrsieenlvlfenmklgkykegekvlrakidmssgninl 239
Cdd:cd00807 80 LYEYAEQLIKKGKAYV---------------------------------------------------------------- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 240 rdpilyrimnkiHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYM 319
Cdd:cd00807 96 ------------HHRTGDKWCIYPTYDFAHPIVDSIEGITHSLCTLEFEDRRPSYYWLCDALRLYRPHQWEFSRLNLTYT 163
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23489563 320 VMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIR 394
Cdd:cd00807 164 VMSKRKLLQLVDEGYVDGWDDPRLPTLRGLRRRGVTPEAIRQFILRQGVSKADSTIDWDKLEACVRKDLNPTAPR 238
|
|
| tRNA-synt_1c |
pfam00749 |
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ... |
81-389 |
6.02e-121 |
|
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: 371.27 E-value: 6.02e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:pfam00749 2 VRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGKFILRFEDTDPERETPEFEESILEDLKWLGIKWDYGPYYQSDRFDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLkePGINSPYRNRSIEENLVLF-ENMKLGKYKEGEKVLRAKIDMSSgNINL 239
Cdd:pfam00749 82 YKYAEELIKKGKAYVCFCTPEELEEEREEQ--EALGSPSRDRYDEENLHLFeEEMKKGSAEGGPATVRAKIPMES-PYVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 240 RDPILYRIMN---KIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIF-KTRQIEFARLN 315
Cdd:pfam00749 159 RDPVRGRIKFtpqEIHDRTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEpPPFIHEYLRLN 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23489563 316 VSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKR-ENMISYELLELCAREDMN 389
Cdd:pfam00749 239 LDGTKLSKRKLSWSVDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGVIKSfDVNRLSKSLEAFDRKKLD 313
|
|
| GlnS |
COG0008 |
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ... |
81-549 |
9.94e-114 |
|
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: 357.95 E-value: 9.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:COG0008 5 VRTRFAPSPTGYLHIGHARTALFNWLFARKYGGKFILRIEDTDPERSTEEAVDAILEDLRWLGLDWDEGPYYQSDRFDIY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEPGINSPY----RNRSIEENlvlfENMKlgkyKEGEK-VLRAKI----- 230
Cdd:COG0008 85 YEYAEKLIEKGKAYVCFCTPEELEALRETQTAPGKPPRYdgrcRDLSPEEL----ERML----AAGEPpVLRFKIpeegv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 231 ---DMSSG-----NINLRDPILYRiMNKihpktknkwviYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLN 302
Cdd:COG0008 157 vfdDLVRGeitfpNPNLRDPVLYR-ADG-----------YPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 303 IFKtrqIEFARLNVSY----MVMSKRKLLTlvnekwvndwddprmpTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYE 378
Cdd:COG0008 225 WEP---PEFAHLPLILgpdgTKLSKRKGAV----------------TVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFS 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 379 LLELCAREDMNKKAiRLFSILKPLKVIITNFDdnLYNNTNYYELTALNHPKNEQMGI-----RKIKFEKE---------- 443
Cdd:COG0008 286 LEELIEAFDLDRVS-RSPAVFDPVKLVWLNGP--YIRALDDEELAELLAPELPEAGIredleRLVPLVREraktlselae 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 444 ----IYIDHDDfqENPASNfyRLAPNrTVRlryafcitcnEVIKDEStgKIIELRCTYDPDSksgnlttsnntttigeni 519
Cdd:COG0008 363 larfFFIERED--EKAAKK--RLAPE-EVR----------KVLKAAL--EVLEAVETWDPET------------------ 407
|
490 500 510
....*....|....*....|....*....|
gi 23489563 520 kkVKSTIHWVSAknshKAEFRmyDKLFLKA 549
Cdd:COG0008 408 --VKGTIHWVSA----EAGVK--DGLLFMP 429
|
|
| gltX_arch |
TIGR00463 |
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ... |
70-565 |
3.03e-94 |
|
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: 309.45 E-value: 3.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 70 EDDLKKKKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEh 149
Cdd:TIGR00463 83 LRELPGAKMGEVVMRFAPNPSGPLHIGHARAAILNHEYAKKYDGKLIIRFDDTDPRRVDPEAYDMILEDLEWLGVKWDE- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 150 LYYASDYFDQLYEWALQLIKQGDAYVDDQTIEEIRKnrgsLKEPGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAK 229
Cdd:TIGR00463 162 VVYQSDRIETYYDYTRKLIEMGKAYVCDCRPEEFRE----LRNRGEACHCRDRSVEENLERWEEMLEGKEEGGSVVVRVK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 230 IDMSSGNINLRDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEF----ETHRPLYEWFQDKLNIFK 305
Cdd:TIGR00463 238 TDLKHKNPAIRDWVIFRIVKTPHPRTGDKYRVYPTMDFSVAIDDHLLGVTHVLRGKDHidnrRKQEYIYRYFGWEPPEFI 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 306 trQIEFARLNVSYMVMSKRKLLTLVNEKWVNdWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAR 385
Cdd:TIGR00463 318 --HWGRLKIDDVRALSTSSARKGILRGEYSG-WDDPRLPTLRAIRRRGIRPEAIRKFMLSIGVKINDVTMSWKNIYALNR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 386 EDMNKKAIRLFSILKPLKVIITNFDDNLynntnyyELTALNHPKNEQMGIRKIKFEKEIYIDHDDFQENPasnfyrlapn 465
Cdd:TIGR00463 395 KIIDEEARRYFFIWNPVKIEIVGLPEPK-------RVERPLHPDHPEIGERVLILRGEIYVPKDDLEEGV---------- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 466 RTVRLRYAFcitcnEVIKDESTGKIIELrctydpdsksgnlttsnnttTIGENIKKVKSTIHWVSAKNSHKAEFRMYDKL 545
Cdd:TIGR00463 458 EPVRLMDAV-----NVIYSKKELRYHSE--------------------GLEGARKLGKSIIHWLPAKDAVKVKVIMPDAS 512
|
490 500
....*....|....*....|
gi 23489563 546 FLKANPESDYDDTHVEKIMK 565
Cdd:TIGR00463 513 IVEGVIEADASELEVGDVVQ 532
|
|
| PLN02907 |
PLN02907 |
glutamate-tRNA ligase |
70-450 |
2.40e-89 |
|
glutamate-tRNA ligase
Pssm-ID: 215492 [Multi-domain] Cd Length: 722 Bit Score: 300.87 E-value: 2.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 70 EDDLKKKKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWnEH 149
Cdd:PLN02907 203 EVDLPGAEEGKVCTRFPPEPSGYLHIGHAKAALLNQYFARRYKGKLIVRFDDTNPSKESDEFVENILKDIETLGIKY-DA 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 150 LYYASDYFDQLYEWALQLIKQGDAYVDDQTIEEIRKNRGSlkepGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAK 229
Cdd:PLN02907 282 VTYTSDYFPQLMEMAEKLIKEGKAYVDDTPREQMRKERMD----GIESKCRNNSVEENLRLWKEMIAGSERGLQCCVRGK 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 230 IDMSSGNINLRDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQI 309
Cdd:PLN02907 358 LDMQDPNKSLRDPVYYRCNPTPHHRIGSKYKVYPTYDFACPFVDALEGVTHALRSSEYHDRNAQYYRILEDMGLRKVHIW 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 310 EFARLNVSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLelcarEDMN 389
Cdd:PLN02907 438 EFSRLNFVYTLLSKRKLQWFVDNGKVEGWDDPRFPTVQGIVRRGLKIEALKQFILSQGASKNLNLMEWDKL-----WTIN 512
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23489563 390 KKAI-----RLFSILKPLKVIITnfddnLYNNTNYYEL-TALNHPKNEQMGIRKIKFEKEIYIDHDD 450
Cdd:PLN02907 513 KKIIdpvcpRHTAVLKEGRVLLT-----LTDGPETPFVrIIPRHKKYEGAGKKATTFTNRIWLDYAD 574
|
|
| gltX |
PRK04156 |
glutamyl-tRNA synthetase; Provisional |
72-543 |
8.46e-87 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 235229 [Multi-domain] Cd Length: 567 Bit Score: 289.44 E-value: 8.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 72 DLKKKKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTE--DIRYINSIQEDVKWLGFNWNEh 149
Cdd:PRK04156 93 PLPNAEKGKVVMRFAPNPSGPLHLGHARAAILNDEYAKMYGGKFILRFEDTDPRTKrpDPEAYDMILEDLKWLGVKWDE- 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 150 LYYASDYFDQLYEWALQLIKQGDAYVDDQTIEEIRKnrgsLKEPGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAK 229
Cdd:PRK04156 172 VVIQSDRLEIYYEYARKLIEMGGAYVCTCDPEEFKE----LRDAGKPCPHRDKSPEENLELWEKMLDGEYKEGEAVVRVK 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 230 IDMSSGNINLRDPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEF----ETHRPLYEWFQDKLNIFk 305
Cdd:PRK04156 248 TDLEHPNPSVRDWVAFRIVKTPHPRVGDKYRVWPTYNFAVAVDDHLLGVTHVLRGKDHidntEKQRYIYDYFGWEYPET- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 306 trqIEFARLNVSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAR 385
Cdd:PRK04156 327 ---IHYGRLKIEGFVLSTSKIRKGIEEGEYSGWDDPRLPTLRALRRRGILPEAIRELIIEVGVKETDATISWENLYAINR 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 386 EDMNKKAIRLFSILKPLKVIITNFDDnlynntnyYELTALNHPKNEQMGIRKIKFEKEIYIDHDDFQENpasnfyrlapN 465
Cdd:PRK04156 404 KLIDPIANRYFFVRDPVELEIEGAEP--------LEAKIPLHPDRPERGEREIPVGGKVYVSSDDLEAE----------G 465
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23489563 466 RTVRLRYAFCItcneVIKDESTGKIIelrctYDPDSKsgnlttsnntttigENIKKVK-STIHWVSAKNSHKAEFRMYD 543
Cdd:PRK04156 466 KMVRLMDLFNV----EITGVSVDKAR-----YHSDDL--------------EEARKNKaPIIQWVPEDESVPVRVLKPD 521
|
|
| PTZ00402 |
PTZ00402 |
glutamyl-tRNA synthetase; Provisional |
81-450 |
4.49e-81 |
|
glutamyl-tRNA synthetase; Provisional
Pssm-ID: 240404 [Multi-domain] Cd Length: 601 Bit Score: 274.92 E-value: 4.49e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:PTZ00402 53 VVTRFPPEASGFLHIGHAKAALINSMLADKYKGKLVFRFDDTNPSKEKEHFEQAILDDLATLGVSWDVGPTYSSDYMDLM 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSlkepGINSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAKIDMSSGNINLR 240
Cdd:PTZ00402 133 YEKAEELIKKGLAYCDKTPREEMQKCRFD----GVPTKYRDISVEETKRLWNEMKKGSAEGQETCLRAKISVDNENKAMR 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 241 DPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYMV 320
Cdd:PTZ00402 209 DPVIYRVNLTPHARQGTKYKAYPTYDFCCPIIDSVEGVTHALRTNEYHDRNDQYYWFCDALGIRKPIVEDFSRLNMEYSV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 321 MSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIRLFSILK 400
Cdd:PTZ00402 289 MSKRKLTQLVDTHVVDGWDDPRFPTVRALVRRGLKMEALRQFVQEQGMSKTVNFMEWSKLWYFNTQILDPSVPRYTVVSN 368
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 23489563 401 PLKVIITnfddnLYNNTNYYELTALNHPKNEQMGIRKIKFEKEIYIDHDD 450
Cdd:PTZ00402 369 TLKVRCT-----VEGQIHLEACEKLLHKKVPDMGEKTYYKSDVIFLDAED 413
|
|
| PLN03233 |
PLN03233 |
putative glutamate-tRNA ligase; Provisional |
81-450 |
1.10e-80 |
|
putative glutamate-tRNA ligase; Provisional
Pssm-ID: 178772 [Multi-domain] Cd Length: 523 Bit Score: 271.50 E-value: 1.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNwNEHLYYASDYFDQL 160
Cdd:PLN03233 12 IVTRFPPEPSGYLHIGHAKAALLNDYYARRYKGRLILRFDDTNPSKEKAEFEESIIEDLGKIEIK-PDSVSFTSDYFEPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGDAYVDDQTIEEIRKNRGSLKEpginSPYRNRSIEENLVLFENMKLGKYKEGEKVLRAKIDMSSGNINLR 240
Cdd:PLN03233 91 RCYAIILIEEGLAYMDDTPQEEMKKERADRAE----SKHRNQSPEEALEMFKEMCSGKEEGGAWCLRAKIDMQSDNGTLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 241 DPILYRIMNKIHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYMV 320
Cdd:PLN03233 167 DPVLFRQNTTPHHRSGTAYKAYPTYDLACPIVDSIEGVTHALRTTEYDDRDAQFFWIQKALGLRRPRIHAFARMNFMNTV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 321 MSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIRLFSILK 400
Cdd:PLN03233 247 LSKRKLTWFVDNGHVTGWDDARFPTIRGISRRGIDIDALKMFMCSQGASRRVVNLDWAKFWAENKKEIDKRAKRFMAIDK 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 23489563 401 P--LKVIITNFD---DNLYNNTNYyeltalnHPKNEQMGIRKIKFEKEIYIDHDD 450
Cdd:PLN03233 327 AdhTALTVTNADeeaDFAFSETDC-------HPKDPGFGKRAMRICDEVLLEKAD 374
|
|
| GlxRS_core |
cd00418 |
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ... |
81-387 |
7.76e-56 |
|
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: 193.07 E-value: 7.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDQL 160
Cdd:cd00418 2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGKFILRIEDTDPERSRPEYVESILEDLKWLGLDWDEGPYRQSDRFDLY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 161 YEWALQLIKQGdayvddqtieeirknrgslkepginspyrnrsieenlvlfenmklgkykegekvlrakidmssgninlr 240
Cdd:cd00418 82 RAYAEELIKKG--------------------------------------------------------------------- 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 241 dpilyrimnkihpktknkwvIYPMYDFAHGQSDSIEKITHSICTLEFETHRPLYEWFQDKLNIFKTRQIEFARLNVSYM- 319
Cdd:cd00418 93 --------------------GYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGt 152
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23489563 320 VMSKRKLltlvnekwvndwddprMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCARED 387
Cdd:cd00418 153 KLSKRKL----------------NTTLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFS 204
|
|
| tRNA-synt_1c_C |
pfam03950 |
tRNA synthetases class I (E and Q), anti-codon binding domain; Other tRNA synthetase ... |
392-667 |
1.10e-44 |
|
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: 158.97 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 392 AIRLFSILKPLKVIITNFDDNlynntNYYELTALNHPKNEQMGIRKIKFEKEIYIDHDDfqenpasnFYRLAPNRTVRLR 471
Cdd:pfam03950 1 APRYMAVLDPVKVVIENYPEG-----QEETAEVPNHPKNPELGTRKVPFSREIYIERED--------FKRLAPGEEVRLM 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 472 YAFCITCNEVIKDEStGKIIELRCTYDPDSKsgnlttsnntttiGENIKKVKSTIHWVSAKNSHKAEFRMYDKLFLKANP 551
Cdd:pfam03950 68 DAYNIKVTEVVKDED-GNVTELHCTYDGDDL-------------GGARKVKGKIIHWVSASDAVPAEVRLYDRLFKDEDD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 552 ESDyddthvekimknftselgtspnndnnndnnnndgiamsndldktyqdeyyldtenknddqeklktdkdnqvgwrkYI 631
Cdd:pfam03950 134 ADF---------------------------------------------------------------------------LL 138
|
250 260 270
....*....|....*....|....*....|....*..
gi 23489563 632 NKNSLIV-HHGLVENYSKNCNIGDPIQFERVGFFVKD 667
Cdd:pfam03950 139 NPDSLKVlTEGLAEPALANLKPGDIVQFERIGYFRVD 175
|
|
| GluRS_non_core |
cd09287 |
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ... |
81-394 |
6.43e-43 |
|
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: 156.36 E-value: 6.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNP--VTEDIRYINSIQEDVKWLGFNWNEhLYYASDYFD 158
Cdd:cd09287 2 VVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGKFILRFDDTDPrtKRPDPEAYDMIPEDLEWLGVKWDE-VVIASDRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 159 QLYEWALQLIKQGDAYVddqtieeirknrgslkepginspyrnrsieenlvlfenmklgkykegekvlrakidmssgnin 238
Cdd:cd09287 81 LYYEYARKLIEMGGAYV--------------------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 239 lrdpilyrimnkiHPKTKNKWVIYPMYDFAHGQSDSIEKITHSICTLEFET----HRPLYEWFQDKLNIFktrqIEFARL 314
Cdd:cd09287 98 -------------HPRTGSKYRVWPTLNFAVAVDDHLLGVTHVLRGKDHIDntekQRYIYEYFGWEYPET----IHWGRL 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 315 NVSYMVMSKRKLLTLVNEKWVNDWDDPRMPTISGMRRRGYSPDAIKDFCNKVGVAKRENMISYELLELCAREDMNKKAIR 394
Cdd:cd09287 161 KIEGGKLSTSKIRKGIESGEYEGWDDPRLPTLRALRRRGIRPEAIRDFIIEVGVKQTDATISWENLYAINRKLIDPRANR 240
|
|
| PTPLA |
pfam04387 |
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein ... |
815-950 |
2.88e-38 |
|
Protein tyrosine phosphatase-like protein, PTPLA; This family includes the mammalian protein tyrosine phosphatase-like protein, PTPLA. A significant variation of PTPLA from other protein tyrosine phosphatases is the presence of proline instead of catalytic arginine at the active site. It is thought that PTPLA proteins have a role in the development, differentiation, and maintenance of a number of tissue types.
Pssm-ID: 461286 Cd Length: 163 Bit Score: 140.35 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 815 FIKSDVKIVVTQIFSRFFIVHLIFNYLPN--NNKWILSCLIPWAIIDIIRYLIYSLNLLNIRV-GILTSLRNKLPLILYP 891
Cdd:pfam04387 15 LVRSPVLTTFMQVASRLFVVWGVIYSFPEvqTKPVVFLLLLAWSITEVIRYPYYALNLLGIEVpYFLTWLRYTLFIVLYP 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 23489563 892 IGIVSEVVCTLTSLKNIQSTPflrSFPYAMPNNLNFQIDIYYFCIFVLFLYIPGSIFVY 950
Cdd:pfam04387 95 LGVLSEALLIYQALPYFEETG---LYSVSLPNPFNFSFSYPYFLILLLLLYIPGFYVLY 150
|
|
| PLN02838 |
PLN02838 |
3-hydroxyacyl-CoA dehydratase subunit of elongase |
816-961 |
2.16e-16 |
|
3-hydroxyacyl-CoA dehydratase subunit of elongase
Pssm-ID: 166479 Cd Length: 221 Bit Score: 79.07 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 816 IKSDVKIVVTQIFSRFFIVHLIFNYLPNNNKWIL--SCLIPWAIIDIIRYLIYSLN-LLNIRVGILTSLRNKLPLILYPI 892
Cdd:PLN02838 70 VRSPVSATLPQIGSRLFLTWGILWSFPEVRSHILvtSLVISWSITEIIRYSFFGMKeAFGFAPSWLLWLRYSTFLLLYPT 149
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23489563 893 GIVSEVVCTLTSLKNIQSTpflRSFPYAMPNNLNFQIDIYYFCIFVLFLYIPGSIFVYAAAISHFKLAI 961
Cdd:PLN02838 150 GITSEVGLIYIALPYMKAS---EKYCLRMPNKWNFSFDYFYASILVLAIYVPGSPHMYSYMLGQRKKAL 215
|
|
| GluRS_core |
cd00808 |
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ... |
81-177 |
2.35e-15 |
|
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA synthetase (GluRS) catalytic core domain . The discriminating form of GluRS is only found in bacteria and cellular organelles. GluRS is a monomer that attaches Glu to the appropriate tRNA. Like other class I tRNA synthetases, GluRS aminoacylates 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.
Pssm-ID: 173905 [Multi-domain] Cd Length: 239 Bit Score: 76.47 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 81 VITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNP--VTEDirYINSIQEDVKWLGFNWNEHL-------- 150
Cdd:cd00808 2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGKFILRIEDTDQerSVPE--AEEAILEALKWLGLDWDEGPdvggpygp 79
|
90 100 110
....*....|....*....|....*....|....*
gi 23489563 151 YYASDYFDQLYEWALQLIKQGDAY--------VDD 177
Cdd:cd00808 80 YRQSERLEIYRKYAEKLLEKGDGFptyhlanvVDD 114
|
|
| PRK05710 |
PRK05710 |
tRNA glutamyl-Q(34) synthetase GluQRS; |
82-174 |
2.93e-13 |
|
tRNA glutamyl-Q(34) synthetase GluQRS;
Pssm-ID: 235573 Cd Length: 299 Bit Score: 71.42 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 82 ITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNEHLYYASDYFDqLY 161
Cdd:PRK05710 7 IGRFAPSPSGPLHFGSLVAALGSWLDARAHGGRWLLRIEDIDPPREVPGAADAILADLEWLGLHWDGPVLYQSQRHD-AY 85
|
90
....*....|....
gi 23489563 162 EWAL-QLIKQGDAY 174
Cdd:PRK05710 86 RAALdRLRAQGLVY 99
|
|
| Ptpl |
COG5198 |
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General ... |
824-950 |
1.06e-11 |
|
Protein tyrosine phosphatase-like protein (contains Pro instead of catalytic Arg) [General function prediction only];
Pssm-ID: 227525 Cd Length: 209 Bit Score: 65.31 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 824 VTQIFSRFFIVHLIFnyLPNN---NKWI-LSCLIPWAIIDIIRYLIYSLNLlNIRVGILTSLRNKLPLILYPIGIVSEVV 899
Cdd:COG5198 75 VMQVISRLFIVWGVF--YPYCgiiNSWTyPSITTAWSITEIVRYAFYTFRL-NGIPNTLRVLRYNLFLILYPIGFVSEMY 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 23489563 900 CTLTSLKNIQSTpflrsFPYampnnlnfqidIYYFCIFVLFLYIPGSIFVY 950
Cdd:COG5198 152 CLRALYNAAGKI-----FSL-----------LKVVLPIVMLLYIPGFIFLF 186
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
82-175 |
1.09e-10 |
|
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: 60.57 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 82 ITRFPPEPNGYLHLGHAKSICLNFGLSQ-----KYGGQTHLRFDDTNPVTED-------------IRYINSIQEDVKWLg 143
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQayrklGYKVRCIALIDDAGGLIGDpankkgenakafvERWIERIKEDVEYM- 79
|
90 100 110
....*....|....*....|....*....|..
gi 23489563 144 fnwnehlyyasdyFDQLYEWALQLIKQGDAYV 175
Cdd:cd00802 80 -------------FLQAADFLLLYETECDIHL 98
|
|
| nt_trans |
cd02156 |
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
83-172 |
1.90e-08 |
|
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain.
Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 52.93 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 83 TRFPPEPnGYLHLGHAKSICLNFGLsqkyGGQTHLRFDDTNPVT------EDIRYINSIQEDVKWLGFNWNEHLyyasdy 156
Cdd:cd02156 2 ARFPGEP-GYLHIGHAKLICRAKGI----ADQCVVRIDDNPPVKvwqdphELEERKESIEEDISVCGEDFQQNR------ 70
|
90
....*....|....*.
gi 23489563 157 fdQLYEWALQLIKQGD 172
Cdd:cd02156 71 --ELYRWVKDNITLPV 84
|
|
| PLN02627 |
PLN02627 |
glutamyl-tRNA synthetase |
76-193 |
1.39e-07 |
|
glutamyl-tRNA synthetase
Pssm-ID: 178234 [Multi-domain] Cd Length: 535 Bit Score: 55.13 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23489563 76 KKHSYVITRFPPEPNGYLHLGHAKSICLNFGLSQKYGGQTHLRFDDTNPVTEDIRYINSIQEDVKWLGFNWNE------- 148
Cdd:PLN02627 41 SKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGGKFVLRIEDTDLARSTKESEEAVLRDLKWLGLDWDEgpdvgge 120
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 23489563 149 -HLYYASDYFDQLYEWALQLIKQGDAY---VDDQTIEEIRKNRGSLKEP 193
Cdd:PLN02627 121 yGPYRQSERNAIYKQYAEKLLESGHVYpcfCTDEELEAMKEEAELKKLP 169
|
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