|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
8-328 |
3.16e-99 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 302.94 E-value: 3.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 8 EEKLHLITRNLQEVLGEEKLKEILKERE-LKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560 2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 87 WELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560 81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 167 PGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 245 LKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316
|
....
gi 4507947 325 REKF 328
Cdd:PRK08560 317 REYL 320
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
36-320 |
4.58e-86 |
|
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it 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 formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173902 [Multi-domain] Cd Length: 269 Bit Score: 266.78 E-value: 4.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 36 LKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMK--------APWELLELRVSYYENVIKAMLE 106
Cdd:cd00805 1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 107 SIgvPLEKLKFIKGTDYQLsKEYTLDVYRLSSVVTQHDSKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:cd00805 81 FI--PPEKAKFVNNSDWLL-SLYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 185 GIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSF 263
Cdd:cd00805 158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947 264 IKHVLFPLksefvilrdekwggnktYTAYVDLEKDFAAEvVHPGDLKNSVEVALNKL 320
Cdd:cd00805 231 LKLFTFLD-----------------YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
31-321 |
1.69e-74 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 237.56 E-value: 1.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 31 LKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL-DNMKAPWELLELRVSYYENVIKAMLeSIG 109
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 110 VPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHD--SKKagaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRmlQFK---DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 185 GIDQRKIFTFAEKYLPALGYS---KRVHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGV 260
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507947 261 LSFIKHVLFPlkseFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLL 321
Cdd:pfam00579 235 DLKLFTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
327-528 |
7.55e-67 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 230.82 E-value: 7.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 327 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 406
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 407 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 486
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4507947 487 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 528
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
363-468 |
7.17e-61 |
|
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.
Pssm-ID: 239198 [Multi-domain] Cd Length: 105 Bit Score: 195.52 E-value: 7.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 363 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 442
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
|
90 100
....*....|....*....|....*.
gi 4507947 443 ASIEGInRQVEPLDPPAGSAPGEHVF 468
Cdd:cd02799 81 ASNADH-EKVELLEPPEGAKPGERVT 105
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
9-328 |
1.23e-49 |
|
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272976 [Multi-domain] Cd Length: 378 Bit Score: 174.89 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 9 EKLHLITRNLQEVLGEEKLKEILK--ERELKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKA 85
Cdd:TIGR00234 3 NILLLLTKRGLEVQTPEEEKDLLKllERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 86 PWELLELR-----VSYYENVIKAMLESIGVplEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPL 160
Cdd:TIGR00234 83 KSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 161 LSGLLYPGLQALDEEYLKVDAQFGGIDQ----RKIFTFAEKYLPALGYSKRVHLMNP---MVPGLTGS-KM--SSSEEES 230
Cdd:TIGR00234 161 LHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVslDEGKYDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 231 KIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLSFIKHVLFP------------------LKSEFV 276
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDEVP 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 4507947 277 ILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKN-SVEVA--LNKLLDPIREKF 328
Cdd:TIGR00234 321 IFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEPIRKEL 375
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
370-465 |
9.50e-37 |
|
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.
Pssm-ID: 396251 [Multi-domain] Cd Length: 96 Bit Score: 131.21 E-value: 9.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 449
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80
|
90
....*....|....*.
gi 4507947 450 rQVEPLDPPAGSAPGE 465
Cdd:pfam01588 81 -SVGLLEPPADVPPGT 95
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
370-464 |
1.68e-22 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 101.47 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 370 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 444
Cdd:COG0073 44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121
|
90 100
....*....|....*....|.
gi 4507947 445 IEGINRQVE-PLDPPAGSAPG 464
Cdd:COG0073 122 ELGLGEDHDgILELPEDAPPG 142
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
367-467 |
9.43e-20 |
|
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273059 [Multi-domain] Cd Length: 137 Bit Score: 85.56 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 367 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 446
Cdd:TIGR00399 39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117
|
90 100
....*....|....*....|.
gi 4507947 447 GINRQVepLDPPAGSAPGEHV 467
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
|
|
| TyrS |
COG0162 |
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ... |
11-72 |
1.21e-03 |
|
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439932 [Multi-domain] Cd Length: 409 Bit Score: 41.17 E-value: 1.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947 11 LHLITRNLQEVLGEEKLKEILKERELKIYWG---TAttgkP--HVAYFVPMSKIADFLKAGCEVTIL 72
Cdd:COG0162 5 LELIWRGLIEQITDEELREKLAGGPLTIYLGfdpTA----PslHLGHLVPLMKLRRFQDLGHRPIAL 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08560 |
PRK08560 |
tyrosyl-tRNA synthetase; Validated |
8-328 |
3.16e-99 |
|
tyrosyl-tRNA synthetase; Validated
Pssm-ID: 236286 [Multi-domain] Cd Length: 329 Bit Score: 302.94 E-value: 3.16e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 8 EEKLHLITRNLQEVLGEEKLKEILKERE-LKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNmKAP 86
Cdd:PRK08560 2 EERLELITRNTEEVVTEEELRELLESKEePKAYIGFEPSGKIHLGHLLTMNKLADLQKAGFKVTVLLADWHAYLND-KGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 87 WELLELRVSYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLLY 166
Cdd:PRK08560 81 LEEIRKVAEYNKKVFEAL----GLDPDKTEFVLGSEFQLDKEYWLLVLKLAKNTTLARARRSMTIMGRRMEEPDVSKLVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 167 PGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGS--KMSSSEEESKIDLLDRKEDVKKK 244
Cdd:PRK08560 157 PLMQVADIFYLDVDIAVGGMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGgiKMSKSKPGSAIFVHDSPEEIRRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 245 LKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLLDPI 324
Cdd:PRK08560 237 IKKAYCPPGEVEGNPVLEIAKYHIFPRYDPFVIERPEKYGGDLEYESYEELERDYAEGKLHPMDLKNAVAEYLIEILEPV 316
|
....
gi 4507947 325 REKF 328
Cdd:PRK08560 317 REYL 320
|
|
| TyrRS_core |
cd00805 |
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ... |
36-320 |
4.58e-86 |
|
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) catalytic core domain. TyrRS is a homodimer which attaches Tyr to the appropriate tRNA. TyrRS is a class I tRNA synthetases, so it 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 formationof the enzyme bound aminoacyl-adenylate. It contains the class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173902 [Multi-domain] Cd Length: 269 Bit Score: 266.78 E-value: 4.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 36 LKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMK--------APWELLELRVSYYENVIKAMLE 106
Cdd:cd00805 1 LKVYIGFDPTApSLHLGHLVPLMKLRDFQQAGHEVIVLIGDATAMIGDPSgkseerklLDLELIRENAKYYKKQLKAILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 107 SIgvPLEKLKFIKGTDYQLsKEYTLDVYRLSSVVTQHDSKKAGAEVVKQ--VEHPLLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:cd00805 81 FI--PPEKAKFVNNSDWLL-SLYTLDFLRLGKHFTVNRMLRRDAVKVRLeeEEGISFSEFIYPLLQAYDFVYLDVDLQLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 185 GIDQRKIFTFAEKYLPALGYSKRVHLMNPMVPGLTGSKM-SSSEEESKIDLLDRKEDVKKKLKKAFCEPgnvenngVLSF 263
Cdd:cd00805 158 GSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGGKMsKSEGNAIWDPVLDSPYDVYQKIRNAFDPD-------VLEF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947 264 IKHVLFPLksefvilrdekwggnktYTAYVDLEKDFAAEvVHPGDLKNSVEVALNKL 320
Cdd:cd00805 231 LKLFTFLD-----------------YEEIEELEEEHAEG-PLPRDAKKALAEELTKL 269
|
|
| tRNA-synt_1b |
pfam00579 |
tRNA synthetases class I (W and Y); |
31-321 |
1.69e-74 |
|
tRNA synthetases class I (W and Y);
Pssm-ID: 395461 [Multi-domain] Cd Length: 292 Bit Score: 237.56 E-value: 1.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 31 LKERELKIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYL-DNMKAPWELLELRVSYYENVIKAMLeSIG 109
Cdd:pfam00579 1 KKNRPLRVYSGIDPTGPLHLGYLVPLMKLRQFQQAGHEVFFLIGDLHAIIgDPSKSPERKLLSRETVLENAIKAQL-ACG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 110 VPLEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHD--SKKagaEVVKQVEHP---LLSGLLYPGLQALDEEYLKVDAQFG 184
Cdd:pfam00579 80 LDPEKAEIVNNSDWLEHLELAWLLRDLGKHFSLNRmlQFK---DVKKRLEQGpgiSLGEFTYPLLQAYDILLLKADLQPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 185 GIDQRKIFTFAEKYLPALGYS---KRVHLMNPMVPGLTG-SKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGnvENNGV 260
Cdd:pfam00579 157 GSDQWGNIELGRDLARRFNKKifkKPVGLTNPLLTGLDGgKKMSKSAGNSAIFLDDDPESVYKKIQKAYTDPD--REVRK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507947 261 LSFIKHVLFPlkseFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSVEVALNKLL 321
Cdd:pfam00579 235 DLKLFTFLSN----EEIEILEAELGKSPYREAEELLAREVTGLVHGGDLKKAAAEAVNKLL 291
|
|
| PLN02610 |
PLN02610 |
probable methionyl-tRNA synthetase |
327-528 |
7.55e-67 |
|
probable methionyl-tRNA synthetase
Pssm-ID: 215329 [Multi-domain] Cd Length: 801 Bit Score: 230.82 E-value: 7.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 327 KFNTPALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGL 406
Cdd:PLN02610 602 KLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGL 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 407 VQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRqVEPLDPPAGSAPGEHVFVKGYEkGQPDEELKPKKK 486
Cdd:PLN02610 682 VKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTK-VELVEPPESAAVGERVTFPGFE-GEPDDVLNPKKK 759
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4507947 487 VFEKLQADFKISEECIAQWKQTNFMTKLGSISCKSLKGGNIS 528
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
|
|
| tRNA_bind_EMAP-II_like |
cd02799 |
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ... |
363-468 |
7.17e-61 |
|
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.
Pssm-ID: 239198 [Multi-domain] Cd Length: 105 Bit Score: 195.52 E-value: 7.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 363 VIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLC 442
Cdd:cd02799 1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80
|
90 100
....*....|....*....|....*.
gi 4507947 443 ASIEGInRQVEPLDPPAGSAPGEHVF 468
Cdd:cd02799 81 ASNADH-EKVELLEPPEGAKPGERVT 105
|
|
| tyrS |
TIGR00234 |
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ... |
9-328 |
1.23e-49 |
|
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up tryptophanyl-tRNA synthetases at scores of 0 and below. The proteins found by this model have a deep split between two groups. One group contains bacterial and organellar eukaryotic examples. The other contains archaeal and cytosolic eukaryotic examples. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272976 [Multi-domain] Cd Length: 378 Bit Score: 174.89 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 9 EKLHLITRNLQEVLGEEKLKEILK--ERELKIYWGTATTG-KPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKA 85
Cdd:TIGR00234 3 NILLLLTKRGLEVQTPEEEKDLLKllERPLKLYLGFDPTApSLHLGHLVPLLKLRDFQQAGHEVIVLLGDFTALIGDPTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 86 PWELLELR-----VSYYENVIKAMLESIGVplEKLKFIKGTDYQLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPL 160
Cdd:TIGR00234 83 KSEVRKILtreevQENAENIKKQIARFLDF--EKAKFVYNSEWLLKLNYTDFIRLLGKIFTVNRMLRRDAFSSRFEENIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 161 LSGLLYPGLQALDEEYLKVDAQFGGIDQ----RKIFTFAEKYLPALGYSKRVHLMNP---MVPGLTGS-KM--SSSEEES 230
Cdd:TIGR00234 161 LHEFIYPLLQAYDFVYLNVDLQLGGSDQwfniRKGRDLARENLPSLQFGLTVPLLTPadgEKMGKSLGgAVslDEGKYDF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 231 KIDLLDRKEDVKKKLKKAFCEPGN----------------VENNGVLSFIKHVLFP------------------LKSEFV 276
Cdd:TIGR00234 241 YQKVINTPDELVKKYLKLFTFLGLeeieqlvelkgpnpreVKENLALEITKYVHGPeaalaaeeiseaifsgglNPDEVP 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 4507947 277 ILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKN-SVEVA--LNKLLDPIREKF 328
Cdd:TIGR00234 321 IFRPEKFGGPITLADLLVLSGLFPSKSEARRDIKNgGVYINgeKVEDLEPIRKEL 375
|
|
| PTZ00126 |
PTZ00126 |
tyrosyl-tRNA synthetase; Provisional |
5-338 |
1.32e-48 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 240282 [Multi-domain] Cd Length: 383 Bit Score: 172.57 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 5 PSPEEKLHLITRNLQEVLGEEKLKEILKERELKI-YWGTATTGKPHVAYFVPMSKIADFL-KAGCEVTILFADLHAYLDN 82
Cdd:PTZ00126 35 LSLEERVKLCLSIGEECIQPEELRELLKLKERPIcYDGFEPSGRMHIAQGILKAINVNKLtKAGCVFVFWVADWFALLNN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 83 mKAPWELLELRV--SYYENVIKAmlesIGVPLEKLKFIKGTDY--QLSKEYTLDVYRLSSVVTQHDSKKAGAEVVKQV-- 156
Cdd:PTZ00126 115 -KMGGDLEKIRKvgEYFIEVWKA----AGMDMDNVRFLWASEEinKNPNDYWLRVMDIARSFNITRIKRCSQIMGRSEgd 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 157 EHPLlSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYSKR-VHLMNPMVPGLT--GSKMSSSEEESKID 233
Cdd:PTZ00126 190 EQPC-AQILYPCMQCADIFYLKADICQLGMDQRKVNMLAREYCDKKKIKKKpIILSHHMLPGLLegQEKMSKSDPNSAIF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 234 LLDRKEDVKKKLKKAFCEPGNVENNGVLSFIKHVLFPLKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSV 313
Cdd:PTZ00126 269 MEDSEEDVNRKIKKAYCPPGVIEGNPILAYFKSIVFPAFNSFTVLRKEKNGGDVTYTTYEELEKDYLSGALHPGDLKPAL 348
|
330 340
....*....|....*....|....*.
gi 4507947 314 EVALNKLLDPIREKF-NTPALKKLAS 338
Cdd:PTZ00126 349 AKYLNLMLQPVRDHFqNNPEAKSLLS 374
|
|
| tRNA_bindingDomain |
cd02153 |
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ... |
370-467 |
5.28e-39 |
|
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.
Pssm-ID: 239066 [Multi-domain] Cd Length: 99 Bit Score: 137.27 E-value: 5.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGI- 448
Cdd:cd02153 1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEELGLe 80
|
90
....*....|....*....
gi 4507947 449 NRQVEPLDPPAGSAPGEHV 467
Cdd:cd02153 81 EGSVGILELPEDAPVGDRI 99
|
|
| tRNA_bind |
pfam01588 |
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ... |
370-465 |
9.50e-37 |
|
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.
Pssm-ID: 396251 [Multi-domain] Cd Length: 96 Bit Score: 131.21 E-value: 9.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGIN 449
Cdd:pfam01588 1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80
|
90
....*....|....*.
gi 4507947 450 rQVEPLDPPAGSAPGE 465
Cdd:pfam01588 81 -SVGLLEPPADVPPGT 95
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
332-467 |
5.80e-28 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 118.33 E-value: 5.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 332 ALKKLASAAYPDPSKQKPMAKGPAKnsepeEVIP----SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLV 407
Cdd:PRK00133 541 ASKEAAAAKAAAAAAAAPLAEEPIA-----ETISfddfAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIK 614
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 408 QFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVepLDPPAGSAPGEHV 467
Cdd:PRK00133 615 SAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAAGPGGGDLFL--LEPDEGAKPGMRV 672
|
|
| PRK12267 |
PRK12267 |
methionyl-tRNA synthetase; Reviewed |
331-461 |
1.39e-27 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237028 [Multi-domain] Cd Length: 648 Bit Score: 116.82 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 331 PALKKLASAAYPDPSKQKPMAKGPAKNSEPEEVIP------SRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVS 404
Cdd:PRK12267 508 PRIDVEEEIAYIKEQMEGSAPKEPEEKEKKPEKPEitiddfDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVS 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 4507947 405 GLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIEGINRQVEPLDP-PAGS 461
Cdd:PRK12267 588 GIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDDGKLTLLTVDKEvPNGS 645
|
|
| tRNA_bind_EcMetRS_like |
cd02800 |
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ... |
366-467 |
4.27e-26 |
|
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.
Pssm-ID: 239199 [Multi-domain] Cd Length: 105 Bit Score: 102.19 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 366 SRLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 445
Cdd:cd02800 7 AKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAED 85
|
90 100
....*....|....*....|..
gi 4507947 446 EGinrQVEPLDPPAGSAPGEHV 467
Cdd:cd02800 86 GG---KLKLLTPDEEVEPGSRV 104
|
|
| tRNA_bind_CsaA |
cd02798 |
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ... |
367-464 |
3.74e-23 |
|
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.
Pssm-ID: 239197 [Multi-domain] Cd Length: 107 Bit Score: 94.23 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 367 RLDIRVGKIITVEKHPDA-DSLYVEKIDVGEAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASI 445
Cdd:cd02798 8 KVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGADD 87
|
90
....*....|....*....
gi 4507947 446 EGinRQVEPLDPPAGSAPG 464
Cdd:cd02798 88 EG--GEVVLLVPDREVPNG 104
|
|
| EMAP |
COG0073 |
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis]; |
370-464 |
1.68e-22 |
|
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
Pssm-ID: 439843 [Multi-domain] Cd Length: 773 Bit Score: 101.47 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 370 IRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGL-----VQFVPkEELQDRLVVVLCNLKPQKMRGVESQGMLLCAS 444
Cdd:COG0073 44 LRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGApnvyaGDKVP-EALVGAQVPGVVNLKPRKIRGVESEGMLCSAE 121
|
90 100
....*....|....*....|.
gi 4507947 445 IEGINRQVE-PLDPPAGSAPG 464
Cdd:COG0073 122 ELGLGEDHDgILELPEDAPPG 142
|
|
| metG_C_term |
TIGR00399 |
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ... |
367-467 |
9.43e-20 |
|
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273059 [Multi-domain] Cd Length: 137 Bit Score: 85.56 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 367 RLDIRVGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCASIE 446
Cdd:TIGR00399 39 KVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAEDD 117
|
90 100
....*....|....*....|.
gi 4507947 447 GINRQVepLDPPAGSAPGEHV 467
Cdd:TIGR00399 118 GKVLFL--LSPDQEAIAGERI 136
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
6-328 |
5.11e-16 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 81.10 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 6 SPEEKLHLITRNLQEVLGEEKLKEIL-KERELKIYWGTATTGKPHVAYFVPMS-KIADFLKAGCEVTILFADLHAyLDNM 83
Cdd:PTZ00348 2 NTDERYKLLRSVGEECIQESELRNLIeKKPLIRCYDGFEPSGRMHIAQGIFKAvNVNKCTQAGCEFVFWVADWFA-LMND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 84 KAPWELLELRV--SYYENVIKAMlesiGVPLEKLKFIKGTDYQLSKEYT-----LDVYRLSSVVTqhdSKKAGAEVVKQV 156
Cdd:PTZ00348 81 KVGGELEKIRIvgRYLIEVWKAA----GMDMDKVLFLWSSEEITNHANTywrtvLDIGRQNTIAR---IKKCCTIMGKTE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 157 EHPLLSGLLYPGLQALDEEYLKVDAQFGGIDQRKIFTFAEKYLPALGYS-KRVHLMNPMVPGLT--GSKMSSSEEESKID 233
Cdd:PTZ00348 154 GTLTAAQVLYPLMQCADIFFLKADICQLGLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKqgQAKMSKSDPDSAIF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 234 LLDRKEDVKKKLKKAFC-----------EPG----NVENNGVLSFIKHVLFPLKSEFVILrdekwgGNKTYTAYVDLEKD 298
Cdd:PTZ00348 234 MEDTEEDVARKIRQAYCprvkqsaseitDDGapvaTDDRNPVLDYFQCVVYARPGAVATI------DGTTYATYEDLEQA 307
|
330 340 350
....*....|....*....|....*....|
gi 4507947 299 FAAEVVHPGDLKNSVEVALNKLLDPIREKF 328
Cdd:PTZ00348 308 FVSDEVSEEALKSCLIDEVNALLEPVRQHF 337
|
|
| tRNA_bind_bactPheRS |
cd02796 |
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ... |
370-446 |
1.55e-14 |
|
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.
Pssm-ID: 239196 [Multi-domain] Cd Length: 103 Bit Score: 69.46 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 370 IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------LKPQKMRGVESQGMlL 441
Cdd:cd02796 1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG----APNVRAGDKVVVALPGavlpgglkIKKRKLRGVESEGM-L 75
|
....*
gi 4507947 442 CASIE 446
Cdd:cd02796 76 CSAKE 80
|
|
| PRK10089 |
PRK10089 |
chaperone CsaA; |
367-443 |
3.59e-14 |
|
chaperone CsaA;
Pssm-ID: 182232 [Multi-domain] Cd Length: 112 Bit Score: 68.70 E-value: 3.59e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4507947 367 RLDIRVGKIITVEKHPDADSL-YVEKIDVG-EAEPRTVVSGLVQFVPKEELQDRLVVVLCNLKPQKMRGVESQGMLLCA 443
Cdd:PRK10089 11 KVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGF 89
|
|
| pheT_bact |
TIGR00472 |
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ... |
358-446 |
1.20e-12 |
|
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273097 [Multi-domain] Cd Length: 797 Bit Score: 70.40 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 358 SEPEEVIPSRLD---IRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGlvqfVPKEELQDRLVVVLCN--------L 426
Cdd:TIGR00472 31 LEVEAVIPFSKPlkgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCG----APNVEAGKKVAVALPGaklpnglkI 106
|
90 100
....*....|....*....|
gi 4507947 427 KPQKMRGVESQGMlLCASIE 446
Cdd:TIGR00472 107 KKSKLRGVESEGM-LCSESE 125
|
|
| pheT |
PRK00629 |
phenylalanyl-tRNA synthetase subunit beta; Reviewed |
361-446 |
3.45e-11 |
|
phenylalanyl-tRNA synthetase subunit beta; Reviewed
Pssm-ID: 234804 [Multi-domain] Cd Length: 791 Bit Score: 65.96 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 361 EEVIPSRLDIR---VGKIITVEKHPDADSLYVEKIDVGEaEPRTVVSG-----LVQFVPkeelqdrlvVVLCN------- 425
Cdd:PRK00629 33 EGVEDVAAGLSgvvVGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGapnvrAGDKVP---------VALPGavlpggf 102
|
90 100
....*....|....*....|..
gi 4507947 426 -LKPQKMRGVESQGMlLCASIE 446
Cdd:PRK00629 103 kIKKAKLRGVESEGM-LCSASE 123
|
|
| trpS |
TIGR00233 |
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ... |
38-351 |
4.70e-08 |
|
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members of the family have a pfam00458 domain amino-terminal to the region described by this model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 272975 [Multi-domain] Cd Length: 327 Bit Score: 55.03 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 38 IYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLdnmkAPWELLELRVSYYENVIKAMLeSIGVPLEKLKF 117
Cdd:TIGR00233 5 VLTGIQPSGKMHLGHYLGAIQTKWLQQFGVELFICIADLHAIT----VKQTDPDALRKAREELAADYL-AVGLDPEKTFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 118 IKGTDYQlskEYTLDVYRLSSVVTQHDSKKAGAEVVKQVEHPLLSGLL-YPGLQALDEEYLKVDAQFGGIDQRKIF---- 192
Cdd:TIGR00233 80 FLQSDYP---EHYELAWLLSCQVTFGELKRMTQFKDKSQAENVPIGLLsYPVLQAADILLYQADLVPVGIDQDQHLeltr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 193 ----TFAEKY-----LPALGYSKRVhlmnPMVPGLTGSKMSSSEEESKIDLLDRKEDVKKKLKKAFCEPGNV------EN 257
Cdd:TIGR00233 157 dlaeRFNKKFknffpKPESLISKFF----PRLMGLSGKKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGGRVtlfehrEK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 258 NGVLSFIkhVLFPLKSEFVILRDEKWGgnktytayvDLEKDFAAEVVHpGDLKNSVEVALNKLLDPIREKFNTPALKKLA 337
Cdd:TIGR00233 233 PGVPNLL--VIYQYLSFFLIDDDKLKE---------IYEAYKSGKLGY-GECKKALIEVLQEFLKEIQERRAEIAEEILD 300
|
330
....*....|....
gi 4507947 338 SAAYPDPSKQKPMA 351
Cdd:TIGR00233 301 KILEPGAKKARETA 314
|
|
| PRK12285 |
PRK12285 |
tryptophanyl-tRNA synthetase; Reviewed |
38-241 |
1.14e-03 |
|
tryptophanyl-tRNA synthetase; Reviewed
Pssm-ID: 237037 [Multi-domain] Cd Length: 368 Bit Score: 41.39 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 38 IYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWELLELRVSYYENVIkamleSIGVPLEKLKF 117
Cdd:PRK12285 69 VYTGFMPSGPMHIGHKMVFDELKWHQEFGANVYIPIADDEAYAARGLSWEETREWAYEYILDLI-----ALGFDPDKTEI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 118 IKGTDYQlskeytlDVYRLSSVVtqhdSKKAGAEVVKQV----EHPLLSGLLYPGLQALDEEYLKVDAQFG------GID 187
Cdd:PRK12285 144 YFQSENI-------KVYDLAFEL----AKKVNFSELKAIygftGETNIGHIFYPATQAADILHPQLEEGPKptlvpvGID 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4507947 188 Q-------RKIftfAEKYLPALGYSKRVHLMNPMVPGLTGSKMSSSEEESKIDLLDRKEDV 241
Cdd:PRK12285 213 QdphirltRDI---AERLHGGYGFIKPSSTYHKFMPGLTGGKMSSSKPESAIYLTDDPETV 270
|
|
| TyrS |
COG0162 |
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA ... |
11-72 |
1.21e-03 |
|
Tyrosyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Tyrosyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439932 [Multi-domain] Cd Length: 409 Bit Score: 41.17 E-value: 1.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4507947 11 LHLITRNLQEVLGEEKLKEILKERELKIYWG---TAttgkP--HVAYFVPMSKIADFLKAGCEVTIL 72
Cdd:COG0162 5 LELIWRGLIEQITDEELREKLAGGPLTIYLGfdpTA----PslHLGHLVPLMKLRRFQDLGHRPIAL 67
|
|
| PheT |
COG0072 |
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ... |
358-448 |
2.85e-03 |
|
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase beta subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439842 [Multi-domain] Cd Length: 793 Bit Score: 40.53 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507947 358 SEPEEVIPSRLDIRVGKIITVEKHPDADSLYVEKIDVGEAEPRTVVSGLVQFVPKeelqdrLVVVLC----------NLK 427
Cdd:COG0072 33 EEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVG------VVVVAApggavlpggfKIK 106
|
90 100
....*....|....*....|.
gi 4507947 428 PQKMRGVESQGMLLCASIEGI 448
Cdd:COG0072 107 KAKIRGVESSGMLCSEEELGL 127
|
|
| PTZ00348 |
PTZ00348 |
tyrosyl-tRNA synthetase; Provisional |
236-313 |
6.12e-03 |
|
tyrosyl-tRNA synthetase; Provisional
Pssm-ID: 173541 [Multi-domain] Cd Length: 682 Bit Score: 39.50 E-value: 6.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4507947 236 DRKEDVKKKLKKAFCEPgNVENNGVLSFIKHVLFPlKSEFVILRDEKWGGNKTYTAYVDLEKDFAAEVVHPGDLKNSV 313
Cdd:PTZ00348 570 DNDMDIRRKIKKAYSAP-NEEANPVISVAQHLLAQ-QGALSIERGEANGGNVAYNTPEALVADCGSGALHPADLKAAV 645
|
|
| |
