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Conserved domains on  [gi|38197552|gb|AAH61752|]
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Wars protein [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nt_trans super family cl00015
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ...
 44-377 0e+00

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.


The actual alignment was detected with superfamily member PLN02486:

Pssm-ID: 469580  Cd Length: 383  Bit Score: 607.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   44 VDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 123
Cdd:PLN02486   3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  124 SSEAMHLGHLVPFIFTKWLQDVFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLEYMGQS 203
Cdd:PLN02486  83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  204 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 283
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  284 PRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGRDTVEEHRQFGGNCEVDVSFMYLT 363
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320

                        330
                 ....*....|....
gi 38197552  364 FFLEDDDSLEQIRK 377
Cdd:PLN02486 321 FFLEDDAELERIKK 334
S15_NS1_EPRS_RNA-bind super family cl00349
S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, ...
 1-20 2.55e-04

S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic aminoacyl tRNA synthetases (aaRSs), where it occurs as a single or a repeated unit. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions in the formation of tRNA-synthetases into multienzyme complexes. While this domain lacks significant sequence similarity between the subgroups in which it is found, they share similar electrostatic surface potentials and thus are likely to bind to RNA via the same mechanism.


The actual alignment was detected with superfamily member cd00936:

Pssm-ID: 469733 [Multi-domain]  Cd Length: 50  Bit Score: 38.37  E-value: 2.55e-04
                        10        20
                ....*....|....*....|
gi 38197552   1 MLLSLKMNYKTAMGEEYKAG 20
Cdd:cd00936  31 KLLALKADYKEATGQDYKPG 50
 
Name Accession Description Interval E-value
PLN02486 PLN02486
aminoacyl-tRNA ligase
 44-377 0e+00

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 607.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   44 VDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 123
Cdd:PLN02486   3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  124 SSEAMHLGHLVPFIFTKWLQDVFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLEYMGQS 203
Cdd:PLN02486  83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  204 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 283
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  284 PRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGRDTVEEHRQFGGNCEVDVSFMYLT 363
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320

                        330
                 ....*....|....
gi 38197552  364 FFLEDDDSLEQIRK 377
Cdd:PLN02486 321 FFLEDDAELERIKK 334
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 116-377 8.52e-108

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS 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 formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 317.60  E-value: 8.52e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 116 YLYTGRGPSSeAMHLGHLVP-FIFTKWLQDVfDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIF 194
Cdd:cd00806   1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 195 SDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTD------SDCIGKISFPAVQAAPSFSNSFpkifrdrtdiqCLIPC 268
Cdd:cd00806  79 FQSDV----PEHYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 269 AIDQDPYFRMTRDVAPRIGH------PKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGR 340
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNKlygeifPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38197552 341 DtvEEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRK 377
Cdd:cd00806 224 T--EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDE 258
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 113-377 2.00e-107

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: 318.51  E-value: 2.00e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   113 KPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQdVFDVPLVIQMSDDEKYLWKDlTLEQAYSYTVEN-AKDIIACGFDVNKT 191
Cdd:TIGR00233   1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   192 FIFSDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTDSD-----CIGKISFPAVQAAPSFSNSFPkifrdrtdiqcLI 266
Cdd:TIGR00233  78 FIFLQSDY----PEHYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   267 PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKSKVNKHAFSGG 339
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNKkfknffPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 38197552   340 RDTVEEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRK 377
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYE 260
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
110-344 4.61e-20

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 89.26  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   110 ENKKPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQDVFDVPLVI----------QMSDDEKylwkdlTLEQAYSYTVENAK 179
Cdd:pfam00579   1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhaiigdPSKSPER------KLLSRETVLENAIK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   180 DIIACGFDVNKTFIF--------SDLEYMGQSPGfykNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAApsfsns 251
Cdd:pfam00579  74 AQLACGLDPEKAEIVnnsdwlehLELAWLLRDLG---KHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   252 fpKIFRDRTDIQcliPCAIDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKS 329
Cdd:pfam00579 145 --DILLLKADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYK 219

                         250
                  ....*....|....*
gi 38197552   330 KVNKhAFSGGRDTVE 344
Cdd:pfam00579 220 KIQK-AYTDPDREVR 233
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 118-377 5.72e-16

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


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 77.78  E-value: 5.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 118 YTGRGPSSEaMHLGHLVPFIFtKW--LQDvfDVPLVIQMSDDEKylwkdLTL----EQAYSYTVENAKDIIACGFDVNKT 191
Cdd:COG0180   7 LSGIQPTGR-LHLGNYLGALK-NWveLQD--EYECFFFIADLHA-----LTTpqdpEELRENTREVAADYLAAGLDPEKS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 192 FIF--SD-------------------LEYMGQspgfYKNvvKIQKHVTFNQVKGIFGFtdsdcigkisfPAVQAApsfsn 250
Cdd:COG0180  78 TIFvqSDvpehaelawllscltplgeLERMPQ----FKD--KSAKNGKENVNAGLLTY-----------PVLMAA----- 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 251 sfpkifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQG--AQTKMSASDpNS 316
Cdd:COG0180 136 ----------DI--LLykadlvPVGEDQKQHLELTRDIARRFNHrygevfPEPEALIPEEGARIPGldGRKKMSKSY-GN 202

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38197552 317 SIFLTDTAKQIKSKVNKhAFSggrDTVEEHRQFGGNCEVDVSFMYLTFFLeDDDSLEQIRK 377
Cdd:COG0180 203 TINLLDDPKEIRKKIKS-AVT---DSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEA 258
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 1-20 2.55e-04

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 38.37  E-value: 2.55e-04
                        10        20
                ....*....|....*....|
gi 38197552   1 MLLSLKMNYKTAMGEEYKAG 20
Cdd:cd00936  31 KLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
2-23 3.04e-04

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 38.24  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|..
gi 38197552     2 LLSLKMNYKTAMGEEYKAGCPP 23
Cdd:pfam00458  32 LLALKAQYKALTGKDYKPGAAP 53
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 1-26 5.22e-04

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 5.22e-04
                           10        20
                   ....*....|....*....|....*.
gi 38197552      1 MLLSLKMNYKTAMGEEYKAGCPPGNS 26
Cdd:smart00991  30 KLLALKAQLKEATGQDYKPGAPPGDT 55
 
Name Accession Description Interval E-value
PLN02486 PLN02486
aminoacyl-tRNA ligase
 44-377 0e+00

aminoacyl-tRNA ligase


Pssm-ID: 178104  Cd Length: 383  Bit Score: 607.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   44 VDPWTVRTSSAKGIDYDKLIVQFGSSKIDKELINRIERATGQRPHRFLRRGIFFSHRDMNQILDAYENKKPFYLYTGRGP 123
Cdd:PLN02486   3 VTPWEVSAKDGGKIDYDKLVDKFGCQRLDPSLIDRVERLTGRPAHPFLRRGVFFAHRDLEEILDAYEKGEKFYLYTGRGP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  124 SSEAMHLGHLVPFIFTKWLQDVFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLEYMGQS 203
Cdd:PLN02486  83 SSEALHLGHLIPFMFTKYLQDAFKVPLVIQLTDDEKFLWKNLSVEESQRLARENAKDIIACGFDVERTFIFSDFDYVGGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  204 pgFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFSNSFPKIFRDRTDIQCLIPCAIDQDPYFRMTRDVA 283
Cdd:PLN02486 163 --FYKNMVKIAKCVTLNQVRGIFGFSGEDNIGKISFPAVQAAPSFPSSFPHLFGGKDKLRCLIPCAIDQDPYFRMTRDVA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  284 PRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGRDTVEEHRQFGGNCEVDVSFMYLT 363
Cdd:PLN02486 241 PRLGYYKPALIESRFFPALQGESGKMSASDPNSAIYVTDTPKEIKNKINKYAFSGGQDTVEEHRELGANLEVDIPWKYLN 320

                        330
                 ....*....|....
gi 38197552  364 FFLEDDDSLEQIRK 377
Cdd:PLN02486 321 FFLEDDAELERIKK 334
PRK12285 PRK12285
tryptophanyl-tRNA synthetase; Reviewed
 40-377 1.49e-125

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 237037 [Multi-domain]  Cd Length: 368  Bit Score: 366.11  E-value: 1.49e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   40 SEDF-VDPWTVRTSsakgIDYDKLIVQFGSSKIDKELINrIERatgqrPHRFLRRGIFFSHRDMNQILDAYENKKPFYLY 118
Cdd:PRK12285   1 EDEFmVTPWEVSGI----VDYDKLFEEFGIEPFTEVLPE-LPE-----PHPLMRRGIIFGHRDYDKILEAYRNGKPFAVY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  119 TGRGPSSEaMHLGHLVPFIFTKWLQDvFDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIFSDLE 198
Cdd:PRK12285  71 TGFMPSGP-MHIGHKMVFDELKWHQE-FGANVYIPIADDEAYAARGLSWEETREWAYEYILDLIALGFDPDKTEIYFQSE 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  199 YMgqspGFYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAAPSFsnsFPKIFRDRTdiQCLIPCAIDQDPYFRM 278
Cdd:PRK12285 149 NI----KVYDLAFELAKKVNFSELKAIYGFTGETNIGHIFYPATQAADIL---HPQLEEGPK--PTLVPVGIDQDPHIRL 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  279 TRDVAPRI----GHPKPALLHSTFFPALQGaqTKMSASDPNSSIFLTDTAKQIKSKVnKHAFSGGRDTVEEHRQFGGNCE 354
Cdd:PRK12285 220 TRDIAERLhggyGFIKPSSTYHKFMPGLTG--GKMSSSKPESAIYLTDDPETVKKKI-MKALTGGRATLEEQRKLGGEPD 296

                        330       340
                 ....*....|....*....|....
gi 38197552  355 VDVSFMYLTFFLEDDDS-LEQIRK 377
Cdd:PRK12285 297 ECVVYELLLYHLEEDDKeLKEIYE 320
TrpRS_core cd00806
catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) ...
 116-377 8.52e-108

catalytic core domain of tryptophanyl-tRNA synthetase; Tryptophanyl-tRNA synthetase (TrpRS) catalytic core domain. TrpRS is a homodimer which attaches Tyr to the appropriate tRNA. TrpRS 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 formation of the enzyme bound aminoacyl-adenylate. It contains class I characteristic HIGH and KMSKS motifs, which are involved in ATP binding


Pssm-ID: 173903 [Multi-domain]  Cd Length: 280  Bit Score: 317.60  E-value: 8.52e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 116 YLYTGRGPSSeAMHLGHLVP-FIFTKWLQDVfDVPLVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNKTFIF 194
Cdd:cd00806   1 RVLSGIQPSG-SLHLGHYLGaFRFWVWLQEA-GYELFFFIADLHALTVKQLDPEELRQNTRENAKDYLACGLDPEKSTIF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 195 SDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTD------SDCIGKISFPAVQAAPSFSNSFpkifrdrtdiqCLIPC 268
Cdd:cd00806  79 FQSDV----PEHYELAWLLSCVVTFGELERMTGFKDksaqgeSVNIGLLTYPVLQAADILLYKA-----------CLVPV 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 269 AIDQDPYFRMTRDVAPRIGH------PKPALLHS--TFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNKHAFSGGR 340
Cdd:cd00806 144 GIDQDPHLELTRDIARRFNKlygeifPKPAALLSkgAFLPGLQGPSKKMSKSDPNNAIFLTDSPKEIKKKIMKAATDGGR 223

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 38197552 341 DtvEEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRK 377
Cdd:cd00806 224 T--EHRRDGGGPGVSNLVEIYSAFFNDDDEELEEIDE 258
trpS TIGR00233
tryptophanyl-tRNA synthetase; This model represents tryptophanyl-tRNA synthetase. Some members ...
 113-377 2.00e-107

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: 318.51  E-value: 2.00e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   113 KPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQdVFDVPLVIQMSDDEKYLWKDlTLEQAYSYTVEN-AKDIIACGFDVNKT 191
Cdd:TIGR00233   1 KKFRVLTGIQPSG-KMHLGHYLGAIQTKWLQ-QFGVELFICIADLHAITVKQ-TDPDALRKAREElAADYLAVGLDPEKT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   192 FIFSDLEYmgqsPGFYKNVVKIQKHVTFNQVKGIFGFTDSD-----CIGKISFPAVQAAPSFSNSFPkifrdrtdiqcLI 266
Cdd:TIGR00233  78 FIFLQSDY----PEHYELAWLLSCQVTFGELKRMTQFKDKSqaenvPIGLLSYPVLQAADILLYQAD-----------LV 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   267 PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQGAQT-KMSASDPNSSIFLTDTAKQIKSKVNKHAFSGG 339
Cdd:TIGR00233 143 PVGIDQDQHLELTRDLAERFNKkfknffPKPESLISKFFPRLMGLSGkKMSKSDPNSAIFLTDTPKQIKKKIRKAATDGG 222

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 38197552   340 RDTVEEHRQFGGNCEVDVSFMYLTFFLEDDDSLEQIRK 377
Cdd:TIGR00233 223 RVTLFEHREKPGVPNLLVIYQYLSFFLIDDDKLKEIYE 260
PRK08560 PRK08560
tyrosyl-tRNA synthetase; Validated
 118-356 1.25e-20

tyrosyl-tRNA synthetase; Validated


Pssm-ID: 236286 [Multi-domain]  Cd Length: 329  Bit Score: 91.47  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  118 YTGRGPSSEaMHLGHLVpfiftkW------LQDV-FDVplVIQMSDDEKYLWKDLTLEQAYSYTVENAKDIIACGFDVNK 190
Cdd:PRK08560  34 YIGFEPSGK-IHLGHLL------TmnkladLQKAgFKV--TVLLADWHAYLNDKGDLEEIRKVAEYNKKVFEALGLDPDK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  191 T-FIF-----SDLEYMGqspgfykNVVKIQKHVTFNQVK---GIFG--FTDSDcIGKISFPAVQAApsfsnsfpKIFRDR 259
Cdd:PRK08560 105 TeFVLgsefqLDKEYWL-------LVLKLAKNTTLARARrsmTIMGrrMEEPD-VSKLVYPLMQVA--------DIFYLD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  260 TDIqclipcA---IDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNK--- 333
Cdd:PRK08560 169 VDI------AvggMDQRKIHMLAREVLPKLGYKKPVCIHTPLLTGLDGGGIKMSKSKPGSAIFVHDSPEEIRRKIKKayc 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 38197552  334 ----------------HAFSG-GRDTVEEHRQFGGNCEVD 356
Cdd:PRK08560 243 ppgevegnpvleiakyHIFPRyDPFVIERPEKYGGDLEYE 282
tRNA-synt_1b pfam00579
tRNA synthetases class I (W and Y);
110-344 4.61e-20

tRNA synthetases class I (W and Y);


Pssm-ID: 395461 [Multi-domain]  Cd Length: 292  Bit Score: 89.26  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   110 ENKKPFYLYTGRGPSSeAMHLGHLVPFIFTKWLQDVFDVPLVI----------QMSDDEKylwkdlTLEQAYSYTVENAK 179
Cdd:pfam00579   1 KKNRPLRVYSGIDPTG-PLHLGYLVPLMKLRQFQQAGHEVFFLigdlhaiigdPSKSPER------KLLSRETVLENAIK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   180 DIIACGFDVNKTFIF--------SDLEYMGQSPGfykNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAVQAApsfsns 251
Cdd:pfam00579  74 AQLACGLDPEKAEIVnnsdwlehLELAWLLRDLG---KHFSLNRMLQFKDVKKRLEQGPGISLGEFTYPLLQAY------ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   252 fpKIFRDRTDIQcliPCAIDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGA--QTKMSASDPNSSIFLTDTAKQIKS 329
Cdd:pfam00579 145 --DILLLKADLQ---PGGSDQWGNIELGRDLARRFNKKIFKKPVGLTNPLLTGLdgGKKMSKSAGNSAIFLDDDPESVYK 219

                         250
                  ....*....|....*
gi 38197552   330 KVNKhAFSGGRDTVE 344
Cdd:pfam00579 220 KIQK-AYTDPDREVR 233
TrpS COG0180
Tryptophanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 118-377 5.72e-16

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


Pssm-ID: 439950 [Multi-domain]  Cd Length: 330  Bit Score: 77.78  E-value: 5.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 118 YTGRGPSSEaMHLGHLVPFIFtKW--LQDvfDVPLVIQMSDDEKylwkdLTL----EQAYSYTVENAKDIIACGFDVNKT 191
Cdd:COG0180   7 LSGIQPTGR-LHLGNYLGALK-NWveLQD--EYECFFFIADLHA-----LTTpqdpEELRENTREVAADYLAAGLDPEKS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 192 FIF--SD-------------------LEYMGQspgfYKNvvKIQKHVTFNQVKGIFGFtdsdcigkisfPAVQAApsfsn 250
Cdd:COG0180  78 TIFvqSDvpehaelawllscltplgeLERMPQ----FKD--KSAKNGKENVNAGLLTY-----------PVLMAA----- 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 251 sfpkifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGH------PKPALLHSTFFPALQG--AQTKMSASDpNS 316
Cdd:COG0180 136 ----------DI--LLykadlvPVGEDQKQHLELTRDIARRFNHrygevfPEPEALIPEEGARIPGldGRKKMSKSY-GN 202

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 38197552 317 SIFLTDTAKQIKSKVNKhAFSggrDTVEEHRQFGGNCEVDVSFMYLTFFLeDDDSLEQIRK 377
Cdd:COG0180 203 TINLLDDPKEIRKKIKS-AVT---DSERLRYDDPGKPEVCNLFTIYSAFS-GKEEVEELEA 258
PRK12282 PRK12282
tryptophanyl-tRNA synthetase II; Reviewed
 112-375 2.56e-10

tryptophanyl-tRNA synthetase II; Reviewed


Pssm-ID: 183400 [Multi-domain]  Cd Length: 333  Bit Score: 61.02  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  112 KKPFYLyTGRGPSSeAMHLGHLV--------------PFIF---TKWLQDVFDVPlviqmsddekylwkdltlEQAYSYT 174
Cdd:PRK12282   1 TKPIIL-TGDRPTG-KLHLGHYVgslknrvalqneheQFVLiadQQALTDNAKNP------------------EKIRRNI 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  175 VENAKDIIACGFDVNKTFIFSdleymgQS--PG------FYKNVV-------------KIQKHvtfnqvkgifGFTDSDC 233
Cdd:PRK12282  61 LEVALDYLAVGIDPAKSTIFI------QSqiPElaeltmYYMNLVtvarlernptvktEIAQK----------GFGRSIP 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  234 IGKISFPAVQAApsfsnsfpkifrdrtDIQC----LIPCAIDQDPYFRMTRDVAPRIGH---------PKPALLHSTFFP 300
Cdd:PRK12282 125 AGFLTYPVSQAA---------------DITAfkatLVPVGDDQLPMIEQTREIVRRFNSlygtdvlvePEALLPEAGRLP 189

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38197552  301 ALQGaQTKMSASDPNsSIFLTDTAKQIKSKVNKHAFSGGRDTVEEHRQFGGNcevdVSFMYLTFFLEDDDSLEQI 375
Cdd:PRK12282 190 GLDG-KAKMSKSLGN-AIYLSDDADTIKKKVMSMYTDPNHIRVEDPGKVEGN----VVFTYLDAFDPDKAEVAEL 258
PTZ00126 PTZ00126
tyrosyl-tRNA synthetase; Provisional
 183-333 4.40e-09

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 240282 [Multi-domain]  Cd Length: 383  Bit Score: 57.39  E-value: 4.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  183 ACGFDV-NKTFIFSDLEYMGQSPGFYKNVVKIQKHVTFNQVK---GIFGFTDSD--CIGKISFPAVQAApsfsnsfpKIF 256
Cdd:PTZ00126 136 AAGMDMdNVRFLWASEEINKNPNDYWLRVMDIARSFNITRIKrcsQIMGRSEGDeqPCAQILYPCMQCA--------DIF 207

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38197552  257 RDRTDIQCLipcAIDQDPYFRMTRDVA--PRIGHpKPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVNK 333
Cdd:PTZ00126 208 YLKADICQL---GMDQRKVNMLAREYCdkKKIKK-KPIILSHHMLPGLLEGQEKMSKSDPNSAIFMEDSEEDVNRKIKK 282
PRK00927 PRK00927
tryptophanyl-tRNA synthetase; Reviewed
 173-333 4.49e-08

tryptophanyl-tRNA synthetase; Reviewed


Pssm-ID: 234866 [Multi-domain]  Cd Length: 333  Bit Score: 54.32  E-value: 4.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  173 YTVENAKDIIACGFDVNKTFIF--SD-------------------LEYMGQspgfYKNvvKIQKHvtfnqvkgifgfTDS 231
Cdd:PRK00927  57 NTRELAADYLACGIDPEKSTIFvqSHvpehaelawilncitplgeLERMTQ----FKD--KSAKQ------------KEN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  232 DCIGKISFPAVQAApsfsnsfpkifrdrtDIqcLI------PCAIDQDPYFRMTRDVAPRIGHpkpalLHSTFFPA---- 301
Cdd:PRK00927 119 VSAGLFTYPVLMAA---------------DI--LLykadlvPVGEDQKQHLELTRDIARRFNN-----LYGEVFPVpepl 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 38197552  302 ----------LQGAQTKMSASDPN--SSIFLTDTAKQIKSKVNK 333
Cdd:PRK00927 177 ipkvgarvmgLDGPTKKMSKSDPNdnNTINLLDDPKTIAKKIKK 220
PTZ00348 PTZ00348
tyrosyl-tRNA synthetase; Provisional
 183-336 2.16e-07

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 173541 [Multi-domain]  Cd Length: 682  Bit Score: 52.98  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  183 ACGFDVNKT-FIFSDLEYMGQSPGFYKNVVKIQKHVTFNQVKG---IFGFTDSDCIG-KISFPAVQAApsfsnsfpKIFR 257
Cdd:PTZ00348 102 AAGMDMDKVlFLWSSEEITNHANTYWRTVLDIGRQNTIARIKKcctIMGKTEGTLTAaQVLYPLMQCA--------DIFF 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552  258 DRTDIQCLipcAIDQDPYFRMTRDVAPRIGHP-KPALLHSTFFPALQGAQTKMSASDPNSSIFLTDTAKQIKSKVnKHAF 336
Cdd:PTZ00348 174 LKADICQL---GLDQRKVNMLAREYCDLIGRKlKPVILSHHMLAGLKQGQAKMSKSDPDSAIFMEDTEEDVARKI-RQAY 249
TyrRS_core cd00805
catalytic core domain of tyrosinyl-tRNA synthetase; Tyrosinyl-tRNA synthetase (TyrRS) ...
 117-333 5.90e-06

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: 47.22  E-value: 5.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 117 LYTGRGPSSEAMHLGHLVPFIFTKWLQDV-FDVPLVI----QMSDD---EKYLWKDLTLEQ------AYSYTVENAKDII 182
Cdd:cd00805   3 VYIGFDPTAPSLHLGHLVPLMKLRDFQQAgHEVIVLIgdatAMIGDpsgKSEERKLLDLELirenakYYKKQLKAILDFI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 183 acgfDVNKTFIFSDLEYmgQSPGFYKNVVKIQKHVTFNQ------VKGIFGFTDSDCIGKISFPAVQAapsfsnsfpkif 256
Cdd:cd00805  83 ----PPEKAKFVNNSDW--LLSLYTLDFLRLGKHFTVNRmlrrdaVKVRLEEEEGISFSEFIYPLLQA------------ 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552 257 rdrTDIQCLIPCA----IDQDPYFRMTRDVAPRIGHPKPALLHSTFFPALQGAqtKMSASDPNSS-IFLTDTAKQIKSKV 331
Cdd:cd00805 145 ---YDFVYLDVDLqlggSDQRGNITLGRDLIRKLGYKKVVGLTTPLLTGLDGG--KMSKSEGNAIwDPVLDSPYDVYQKI 219


                ..
gi 38197552 332 NK 333
Cdd:cd00805 220 RN 221
tyrS TIGR00234
tyrosyl-tRNA synthetase; This tyrosyl-tRNA synthetase model starts picking up ...
 112-333 4.87e-05

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: 45.08  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   112 KKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQDV-FDVPLVI-----------QMSDDEKYLWKDLTLEQAYSYtvenaK 179
Cdd:TIGR00234  29 ERPLKLYLGFDPTAPSLHLGHLVPLLKLRDFQQAgHEVIVLLgdftaligdptGKSEVRKILTREEVQENAENI-----K 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   180 DIIACGFDVNKTFIFSDLEYMGqSPGFYKNVVKIQKHVTFNQ-----------VKGIFgftdsdcIGKISFPAVQAapsf 248
Cdd:TIGR00234 104 KQIARFLDFEKAKFVYNSEWLL-KLNYTDFIRLLGKIFTVNRmlrrdafssrfEENIS-------LHEFIYPLLQA---- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38197552   249 snsfpkifrdrTDIQCL-IPCAI---DQDPYFRMTRDVAPRIGhpkPALLHSTFFPALQGA-QTKMSAS-------DPNS 316
Cdd:TIGR00234 172 -----------YDFVYLnVDLQLggsDQWFNIRKGRDLARENL---PSLQFGLTVPLLTPAdGEKMGKSlggavslDEGK 237

                         250       260
                  ....*....|....*....|
gi 38197552   317 S---IFLTDTAKQIKSKVNK 333
Cdd:TIGR00234 238 YdfyQKVINTPDELVKKYLK 257
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 1-20 2.55e-04

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 38.37  E-value: 2.55e-04
                        10        20
                ....*....|....*....|
gi 38197552   1 MLLSLKMNYKTAMGEEYKAG 20
Cdd:cd00936  31 KLLALKADYKEATGQDYKPG 50
WHEP-TRS pfam00458
WHEP-TRS domain;
2-23 3.04e-04

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 38.24  E-value: 3.04e-04
                          10        20
                  ....*....|....*....|..
gi 38197552     2 LLSLKMNYKTAMGEEYKAGCPP 23
Cdd:pfam00458  32 LLALKAQYKALTGKDYKPGAAP 53
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 1-26 5.22e-04

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 5.22e-04
                           10        20
                   ....*....|....*....|....*.
gi 38197552      1 MLLSLKMNYKTAMGEEYKAGCPPGNS 26
Cdd:smart00991  30 KLLALKAQLKEATGQDYKPGAPPGDT 55
PRK13354 PRK13354
tyrosyl-tRNA synthetase; Provisional
 93-144 1.17e-03

tyrosyl-tRNA synthetase; Provisional


Pssm-ID: 237360 [Multi-domain]  Cd Length: 410  Bit Score: 40.65  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 38197552   93 RGIFFSHRDMNQILDAYENKKPFYLYTGRGPSSEAMHLGHLVPFIFTKWLQD 144
Cdd:PRK13354  12 RGAINQETDEEKLRKSLKEGKPLTLYLGFDPTAPSLHIGHLVPLMKLKRFQD 63
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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