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Conserved domains on  [gi|156058674|ref|XP_001595260|]
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hypothetical protein SS1G_03349 [Sclerotinia sclerotiorum 1980 UF-70]

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 ...
 51-240 1.60e-83

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 cd00808:

Pssm-ID: 469580 [Multi-domain]  Cd Length: 239  Bit Score: 257.52  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  51 IRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG------------------------------------PKVGGPFAPYK 94
Cdd:cd00808    2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGkfilriedtdqersvpeaeeailealkwlgldwdegPDVGGPYGPYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  95 Q--------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRK 166
Cdd:cd00808   82 QserleiyrKYAEKLLEKGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGK 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156058674 167 KLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKH 240
Cdd:cd00808  162 KLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLeRVSKSPAIFDPEKLDWLNGQY 236
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 47-453 1.92e-74

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: 241.62  E-value: 1.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  47 AAGPIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGGPkvggpF---------------------------------APY 93
Cdd:COG0008    1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGK-----FilriedtdpersteeavdailedlrwlgldwdeGPY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  94 KQ------------------------------------------------------------------------------ 95
Cdd:COG0008   76 YQsdrfdiyyeyaekliekgkayvcfctpeelealretqtapgkpprydgrcrdlspeelermlaageppvlrfkipeeg 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 ----------------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGL 159
Cdd:COG0008  156 vvfddlvrgeitfpnpNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 160 LLDKDRKKLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQR 238
Cdd:COG0008  236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLdRVSRSPAVFDPVKLVWLNG 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 239 KHaarykeLRRSnepipPSQDLLELAAkPVLQRMKSLPEYEELIfyncentDAAKEnyilsiicagiqNYNLPDTFYATH 318
Cdd:COG0008  316 PY------IRAL-----DDEELAELLA-PELPEAGIREDLERLV-------PLVRE------------RAKTLSELAELA 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 319 KYFFTAPTPLElesrtpPHKLHDAPQGVihpiPDDFSTSFDGFSSIaaENWNAAELKGftnliidqgtmmstaeftATKV 398
Cdd:COG0008  365 RFFFIEREDEK------AAKKRLAPEEV----RKVLKAALEVLEAV--ETWDPETVKG------------------TIHW 414

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156058674 399 YSEDAQkvIRKswtKLVHSYIRWAIAGGQSGPDGSDIMEILGREESLRRLRVAKE 453
Cdd:COG0008  415 VSAEAG--VKD---GLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAID 464
 
Name Accession Description Interval E-value
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 51-240 1.60e-83

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: 257.52  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  51 IRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG------------------------------------PKVGGPFAPYK 94
Cdd:cd00808    2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGkfilriedtdqersvpeaeeailealkwlgldwdegPDVGGPYGPYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  95 Q--------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRK 166
Cdd:cd00808   82 QserleiyrKYAEKLLEKGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGK 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156058674 167 KLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKH 240
Cdd:cd00808  162 KLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLeRVSKSPAIFDPEKLDWLNGQY 236
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 47-453 1.92e-74

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: 241.62  E-value: 1.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  47 AAGPIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGGPkvggpF---------------------------------APY 93
Cdd:COG0008    1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGK-----FilriedtdpersteeavdailedlrwlgldwdeGPY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  94 KQ------------------------------------------------------------------------------ 95
Cdd:COG0008   76 YQsdrfdiyyeyaekliekgkayvcfctpeelealretqtapgkpprydgrcrdlspeelermlaageppvlrfkipeeg 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 ----------------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGL 159
Cdd:COG0008  156 vvfddlvrgeitfpnpNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 160 LLDKDRKKLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQR 238
Cdd:COG0008  236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLdRVSRSPAVFDPVKLVWLNG 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 239 KHaarykeLRRSnepipPSQDLLELAAkPVLQRMKSLPEYEELIfyncentDAAKEnyilsiicagiqNYNLPDTFYATH 318
Cdd:COG0008  316 PY------IRAL-----DDEELAELLA-PELPEAGIREDLERLV-------PLVRE------------RAKTLSELAELA 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 319 KYFFTAPTPLElesrtpPHKLHDAPQGVihpiPDDFSTSFDGFSSIaaENWNAAELKGftnliidqgtmmstaeftATKV 398
Cdd:COG0008  365 RFFFIEREDEK------AAKKRLAPEEV----RKVLKAALEVLEAV--ETWDPETVKG------------------TIHW 414

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156058674 399 YSEDAQkvIRKswtKLVHSYIRWAIAGGQSGPDGSDIMEILGREESLRRLRVAKE 453
Cdd:COG0008  415 VSAEAG--VKD---GLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAID 464
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 50-448 2.23e-66

glutamyl-tRNA synthetase, bacterial 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 bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273092 [Multi-domain]  Cd Length: 470  Bit Score: 220.69  E-value: 2.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   50 PIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGGPKV-------------------------------GGP------FAP 92
Cdd:TIGR00464   1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFIlriedtdlernieeaeeaileglkwlgiswdEGPyyqsqrLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   93 YKQ----------------------------------------------------------------------------- 95
Cdd:TIGR00464  81 YKKyakelleeglayrcycskerlerlreeqkanketprydgrcrnlheeeienklakgippvvrfkipqeavvsfndqv 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   96 ---------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRK 166
Cdd:TIGR00464 161 rgeitfqnsELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  167 KLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKHaarYK 245
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLnRVSKSPAKFDWKKLQWLNAHY---IK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  246 ELrrsnepipPSQDLLELAakpvlqrmksLPEYEELIfynceNTDAAKENYILSIICAGIQNYNLPDTFYATHKYFFTAP 325
Cdd:TIGR00464 318 EL--------PDEELFELL----------DPHLKSLV-----NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDK 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  326 TPLELESRTpPHKLHDAPQGVIHpipddFSTSFDGFssiaaENWNAAELKGFTNliidqgTMMSTAEFTATKVYSEdaqk 405
Cdd:TIGR00464 375 KEVDEDAFK-KHLKKNVKEVLEA-----LKKKLQAL-----EEWTADEVKSAIK------QIAEELGLKGKKVFMP---- 433

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 156058674  406 virkswtklvhsyIRWAIAGGQSGPDGSDIMEILGREESLRRL 448
Cdd:TIGR00464 434 -------------LRLALTGKGHGPDLAQILELIGKTESIKRL 463
PLN02627 PLN02627
glutamyl-tRNA synthetase
 12-240 6.37e-44

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 161.83  E-value: 6.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  12 TSQRIWKQNVCSICRRHASTEANeYPLSVASTKLRAAGPIRTRFAPSPTGNLHLGSLRTALFNFLLAKATG--------- 82
Cdd:PLN02627   8 TPIRLLPELAPPFLRRSRSSRRR-FSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGgkfvlried 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  83 ---------------------------GPKVGGPFAPYKQ---------------------------------------- 95
Cdd:PLN02627  87 tdlarstkeseeavlrdlkwlgldwdeGPDVGGEYGPYRQsernaiykqyaekllesghvypcfctdeeleamkeeaelk 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 ----------------EFQ---------------------------------------DPIMVKSDGFPTYHLANVVDDH 120
Cdd:PLN02627 167 klpprytgkwatasdeEVQaelakgtpytyrfrvpkegsvkiddlirgevswntdtlgDFVLLRSNGQPVYNFCVAVDDA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 121 FMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLSKRDGAIDIATYRDAGYFPETVTNFVALLGWS 200
Cdd:PLN02627 247 TMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN 326

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 156058674 201 HERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKH 240
Cdd:PLN02627 327 DGTENEIFTLEELVEKFSIdRINKSGAVFDSTKLKWMNGQH 367
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 50-213 9.13e-43

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: 153.63  E-value: 9.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   50 PIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG---------------------------------------------- 83
Cdd:pfam00749   1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGkfilrfedtdperetpefeesiledlkwlgikwdygpyyqsdrfdi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   84 -------------------------------PKVGGPFAPYKQE---------------------------------FQD 99
Cdd:pfam00749  81 yykyaeelikkgkayvcfctpeeleeereeqEALGSPSRDRYDEenlhlfeeemkkgsaeggpatvrakipmespyvFRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  100 P---------------IMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKD 164
Cdd:pfam00749 161 PvrgrikftpqeihdrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156058674  165 RKKLSKRDGAI--DIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQEL 213
Cdd:pfam00749 241 GTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGV 291
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 52-174 1.17e-26

glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274810  Cd Length: 271  Bit Score: 108.40  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   52 RTRFAPSPTGNLHLGSLRTALFNFLLAKATGG-----------PKV---------------------------------- 86
Cdd:TIGR03838   2 RGRFAPSPSGPLHFGSLVAALGSYLDARAHGGrwlvriedldpPREvpgaaddilrtleayglhwdgevvyqsqrhalyq 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   87 -------------------------GGPFAPYK-------------------------QEFQD----------------P 100
Cdd:TIGR03838  82 aaldrllaaglaypcqctrkeiaaaRDGGGIYPgtcrnglpgrpgrpaawrlrvpdgvIAFDDrlqgpqqqdlaaavgdF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156058674  101 IMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLSKRDGA 174
Cdd:TIGR03838 162 VLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGA 235
Anticodon_2 pfam19269
Anticodon binding domain; This entry represents the anticodon binding domain found at the ...
 419-451 2.66e-09

Anticodon binding domain; This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.


Pssm-ID: 466020 [Multi-domain]  Cd Length: 148  Bit Score: 55.66  E-value: 2.66e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 156058674  419 IRWAIAGGQSGPDGSDIMEILGREESLRRLRVA 451
Cdd:pfam19269 115 LRVALTGKTVSPGLFEIMEILGKEETLARLRKA 147
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
 96-173 6.46e-03

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


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 38.98  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 EFQDP---IMVKSDGFPTYH---LANVVD----DHFMKITHVVrGSEwipsTHMHV----AMYQAFGWKPPTFAHV---G 158
Cdd:COG0018  296 EFGDDkdrVLVKSDGTYTYFttdIAYHLYkferYGFDRVIYVV-GAD----QHGHFkrlfAALKALGYDPAKDLEHllfG 370

                         90
                 ....*....|....*
gi 156058674 159 LLLDKDRKKLSKRDG 173
Cdd:COG0018  371 MVNLRDGEKMSTRAG 385
 
Name Accession Description Interval E-value
GluRS_core cd00808
catalytic core domain of discriminating glutamyl-tRNA synthetase; Discriminating Glutamyl-tRNA ...
 51-240 1.60e-83

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: 257.52  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  51 IRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG------------------------------------PKVGGPFAPYK 94
Cdd:cd00808    2 VRTRFAPSPTGFLHIGGARTALFNYLFARKHGGkfilriedtdqersvpeaeeailealkwlgldwdegPDVGGPYGPYR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  95 Q--------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRK 166
Cdd:cd00808   82 QserleiyrKYAEKLLEKGDGFPTYHLANVVDDHLMGITHVIRGEEHLSSTPKQILLYEALGWEPPKFAHLPLILNPDGK 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156058674 167 KLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKH 240
Cdd:cd00808  162 KLSKRKGDTSISDYREEGYLPEALLNYLALLGWSPPDGEEFFTLEELIELFDLeRVSKSPAIFDPEKLDWLNGQY 236
GlnS COG0008
Glutamyl- or glutaminyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 47-453 1.92e-74

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: 241.62  E-value: 1.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  47 AAGPIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGGPkvggpF---------------------------------APY 93
Cdd:COG0008    1 HGMKVRTRFAPSPTGYLHIGHARTALFNWLFARKYGGK-----FilriedtdpersteeavdailedlrwlgldwdeGPY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  94 KQ------------------------------------------------------------------------------ 95
Cdd:COG0008   76 YQsdrfdiyyeyaekliekgkayvcfctpeelealretqtapgkpprydgrcrdlspeelermlaageppvlrfkipeeg 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 ----------------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGL 159
Cdd:COG0008  156 vvfddlvrgeitfpnpNLRDPVLYRADGYPTYNFAVVVDDHLMGITHVIRGEEHLSNTPRQIWLYEALGWEPPEFAHLPL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 160 LLDKDRKKLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQR 238
Cdd:COG0008  236 ILGPDGTKLSKRKGAVTVSGLRRRGYLPEAIRNYLALLGWSKSDDQEIFSLEELIEAFDLdRVSRSPAVFDPVKLVWLNG 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 239 KHaarykeLRRSnepipPSQDLLELAAkPVLQRMKSLPEYEELIfyncentDAAKEnyilsiicagiqNYNLPDTFYATH 318
Cdd:COG0008  316 PY------IRAL-----DDEELAELLA-PELPEAGIREDLERLV-------PLVRE------------RAKTLSELAELA 364

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 319 KYFFTAPTPLElesrtpPHKLHDAPQGVihpiPDDFSTSFDGFSSIaaENWNAAELKGftnliidqgtmmstaeftATKV 398
Cdd:COG0008  365 RFFFIEREDEK------AAKKRLAPEEV----RKVLKAALEVLEAV--ETWDPETVKG------------------TIHW 414

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156058674 399 YSEDAQkvIRKswtKLVHSYIRWAIAGGQSGPDGSDIMEILGREESLRRLRVAKE 453
Cdd:COG0008  415 VSAEAG--VKD---GLLFMPLRVALTGRTVEPSLFDVLELLGKERVFERLGYAID 464
gltX_bact TIGR00464
glutamyl-tRNA synthetase, bacterial family; The glutamyl-tRNA synthetases of the eukaryotic ...
 50-448 2.23e-66

glutamyl-tRNA synthetase, bacterial 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 bacterial and mitochondrial forms of the enzyme. In many species, the charging of tRNA(gln) proceeds first through misacylation with Glu and then transamidation. For this reason, glutamyl-tRNA synthetases may act on both tRNA(gln) and tRNA(glu). This model is highly specific. Proteins with positive scores below the trusted cutoff may be fragments rather than full-length sequences. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273092 [Multi-domain]  Cd Length: 470  Bit Score: 220.69  E-value: 2.23e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   50 PIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGGPKV-------------------------------GGP------FAP 92
Cdd:TIGR00464   1 KVRTRFAPSPTGYLHIGGARTALFNYLFAKHTGGEFIlriedtdlernieeaeeaileglkwlgiswdEGPyyqsqrLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   93 YKQ----------------------------------------------------------------------------- 95
Cdd:TIGR00464  81 YKKyakelleeglayrcycskerlerlreeqkanketprydgrcrnlheeeienklakgippvvrfkipqeavvsfndqv 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   96 ---------EFQDPIMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRK 166
Cdd:TIGR00464 161 rgeitfqnsELDDFVILRSDGSPTYNFAVVVDDYLMKITHVIRGEDHISNTPKQILIYQALGWKIPVFAHLPMILDEDGK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  167 KLSKRDGAIDIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKHaarYK 245
Cdd:TIGR00464 241 KLSKRDGATSIMQFKEQGYLPEALINYLALLGWSPPDDQEFFSLEELIEIFSLnRVSKSPAKFDWKKLQWLNAHY---IK 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  246 ELrrsnepipPSQDLLELAakpvlqrmksLPEYEELIfynceNTDAAKENYILSIICAGIQNYNLPDTFYATHKYFFTAP 325
Cdd:TIGR00464 318 EL--------PDEELFELL----------DPHLKSLV-----NTDTLNREQLAELLLLFKERLKTLKEIAELIRLFFEDK 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  326 TPLELESRTpPHKLHDAPQGVIHpipddFSTSFDGFssiaaENWNAAELKGFTNliidqgTMMSTAEFTATKVYSEdaqk 405
Cdd:TIGR00464 375 KEVDEDAFK-KHLKKNVKEVLEA-----LKKKLQAL-----EEWTADEVKSAIK------QIAEELGLKGKKVFMP---- 433

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 156058674  406 virkswtklvhsyIRWAIAGGQSGPDGSDIMEILGREESLRRL 448
Cdd:TIGR00464 434 -------------LRLALTGKGHGPDLAQILELIGKTESIKRL 463
GlxRS_core cd00418
catalytic core domain of glutamyl-tRNA and glutaminyl-tRNA synthetase; Glutamyl-tRNA ...
 51-240 2.64e-53

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: 178.82  E-value: 2.64e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  51 IRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG----------PKVGGPFA------------------PYKQEFQDPI- 101
Cdd:cd00418    2 VVTRFAPSPTGYLHIGHARTALFNFAFARKYGGkfilriedtdPERSRPEYvesiledlkwlgldwdegPYRQSDRFDLy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 102 ------MVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLSKRDGAI 175
Cdd:cd00418   82 rayaeeLIKKGGYPLYNFVHPVDDALMGITHVLRGEDHLDNTPIQDWLYEALGWEPPRFYHFPRLLLEDGTKLSKRKLNT 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156058674 176 DIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKH 240
Cdd:cd00418  162 TLRALRRRGYLPEALRNYLALIGWSKPDGHELFTLEEMIAAFSVeRVNSADATFDWAKLEWLNREY 227
PLN02627 PLN02627
glutamyl-tRNA synthetase
 12-240 6.37e-44

glutamyl-tRNA synthetase


Pssm-ID: 178234 [Multi-domain]  Cd Length: 535  Bit Score: 161.83  E-value: 6.37e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  12 TSQRIWKQNVCSICRRHASTEANeYPLSVASTKLRAAGPIRTRFAPSPTGNLHLGSLRTALFNFLLAKATG--------- 82
Cdd:PLN02627   8 TPIRLLPELAPPFLRRSRSSRRR-FSVRAAAAGESKGGPVRVRFAPSPTGNLHVGGARTALFNYLFARSKGgkfvlried 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  83 ---------------------------GPKVGGPFAPYKQ---------------------------------------- 95
Cdd:PLN02627  87 tdlarstkeseeavlrdlkwlgldwdeGPDVGGEYGPYRQsernaiykqyaekllesghvypcfctdeeleamkeeaelk 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 ----------------EFQ---------------------------------------DPIMVKSDGFPTYHLANVVDDH 120
Cdd:PLN02627 167 klpprytgkwatasdeEVQaelakgtpytyrfrvpkegsvkiddlirgevswntdtlgDFVLLRSNGQPVYNFCVAVDDA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 121 FMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLSKRDGAIDIATYRDAGYFPETVTNFVALLGWS 200
Cdd:PLN02627 247 TMGITHVIRAEEHLPNTLRQALIYKALGFPMPRFAHVSLILAPDRSKLSKRHGATSVGQFREMGYLPDAMVNYLALLGWN 326

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 156058674 201 HERSYDIMSMQELVDNASM-KYTRGDSVVTMAKLNFMQRKH 240
Cdd:PLN02627 327 DGTENEIFTLEELVEKFSIdRINKSGAVFDSTKLKWMNGQH 367
tRNA-synt_1c pfam00749
tRNA synthetases class I (E and Q), catalytic domain; Other tRNA synthetase sub-families are ...
 50-213 9.13e-43

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: 153.63  E-value: 9.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   50 PIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG---------------------------------------------- 83
Cdd:pfam00749   1 KVRTRFAPSPTGYLHIGHAKAALFNYLYAKNHNGkfilrfedtdperetpefeesiledlkwlgikwdygpyyqsdrfdi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   84 -------------------------------PKVGGPFAPYKQE---------------------------------FQD 99
Cdd:pfam00749  81 yykyaeelikkgkayvcfctpeeleeereeqEALGSPSRDRYDEenlhlfeeemkkgsaeggpatvrakipmespyvFRD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  100 P---------------IMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKD 164
Cdd:pfam00749 161 PvrgrikftpqeihdrTGVKWDGYPTYDFAVVIDDHLMGITHVLRTEEFLDNTPKYIWIYDALGWEPPPFIHEYLRLNLD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156058674  165 RKKLSKRDGAI--DIATYRDAGYFPETVTNFVALLGWSHERSYDIMSMQEL 213
Cdd:pfam00749 241 GTKLSKRKLSWsvDISQVKGWGDPREATLNGLRRRGWTPEGIREFFTREGV 291
PRK05710 PRK05710
tRNA glutamyl-Q(34) synthetase GluQRS;
50-179 4.30e-31

tRNA glutamyl-Q(34) synthetase GluQRS;


Pssm-ID: 235573  Cd Length: 299  Bit Score: 121.50  E-value: 4.30e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  50 PIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG---------------------------------------------- 83
Cdd:PRK05710   5 PYIGRFAPSPSGPLHFGSLVAALGSWLDARAHGGrwllriedidpprevpgaadailadlewlglhwdgpvlyqsqrhda 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  84 ------------------------------PKVGGPFAP----------------------YKQEFQDPIMVK------- 104
Cdd:PRK05710  85 yraaldrlraqglvypcfcsrkeiaaaapaPPDGGGIYPgtcrdllhgprnppawrlrvpdAVIAFDDRLQGRqhqdlal 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 105 ---------SDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLSKRDGAI 175
Cdd:PRK05710 165 avgdfvlrrADGLFAYQLAVVVDDALQGVTHVVRGADLLDSTPRQIYLQQLLGLPTPRYLHLPLVLNADGQKLSKQNGAP 244


                 ....
gi 156058674 176 DIAT 179
Cdd:PRK05710 245 ALDA 248
queuosine_YadB TIGR03838
glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ...
 52-174 1.17e-26

glutamyl-queuosine tRNA(Asp) synthetase; This protein resembles a shortened glutamyl-tRNA ligase, but its purpose is to modify tRNA(Asp) at a queuosine position in the anticodon rather than to charge a tRNA with its cognate amino acid. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274810  Cd Length: 271  Bit Score: 108.40  E-value: 1.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   52 RTRFAPSPTGNLHLGSLRTALFNFLLAKATGG-----------PKV---------------------------------- 86
Cdd:TIGR03838   2 RGRFAPSPSGPLHFGSLVAALGSYLDARAHGGrwlvriedldpPREvpgaaddilrtleayglhwdgevvyqsqrhalyq 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674   87 -------------------------GGPFAPYK-------------------------QEFQD----------------P 100
Cdd:TIGR03838  82 aaldrllaaglaypcqctrkeiaaaRDGGGIYPgtcrnglpgrpgrpaawrlrvpdgvIAFDDrlqgpqqqdlaaavgdF 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156058674  101 IMVKSDGFPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLSKRDGA 174
Cdd:TIGR03838 162 VLRRADGLFAYQLAVVVDDAAQGITHVVRGADLLDSTPRQIYLQRLLGLPPPRYLHLPLVVNADGEKLSKQNGA 235
GluRS_non_core cd09287
catalytic core domain of non-discriminating glutamyl-tRNA synthetase; Non-discriminating ...
 50-198 2.32e-17

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: 81.24  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  50 PIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG----------PKVGGP----FAPYKQEFQ------DPIMVKSDGF- 108
Cdd:cd09287    1 KVVMRFAPNPNGPLHLGHARAAILNGEYAKMYGGkfilrfddtdPRTKRPdpeaYDMIPEDLEwlgvkwDEVVIASDRIe 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 109 ----------------------------PTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLL 160
Cdd:cd09287   81 lyyeyarkliemggayvhprtgskyrvwPTLNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYEYFGWEYPETIHWGRL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156058674 161 -LDKDRKKLSKRDGAID--------------IATYRDAGYFPETVTNFVALLG 198
Cdd:cd09287  161 kIEGGKLSTSKIRKGIEsgeyegwddprlptLRALRRRGIRPEAIRDFIIEVG 213
gltX PRK04156
glutamyl-tRNA synthetase; Provisional
 108-160 2.58e-09

glutamyl-tRNA synthetase; Provisional


Pssm-ID: 235229 [Multi-domain]  Cd Length: 567  Bit Score: 59.48  E-value: 2.58e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 156058674 108 FPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLL 160
Cdd:PRK04156 280 WPTYNFAVAVDDHLLGVTHVLRGKDHIDNTEKQRYIYDYFGWEYPETIHYGRL 332
Anticodon_2 pfam19269
Anticodon binding domain; This entry represents the anticodon binding domain found at the ...
 419-451 2.66e-09

Anticodon binding domain; This entry represents the anticodon binding domain found at the C-terminus of the class-I glutamyl tRNA synthetase enzyme.


Pssm-ID: 466020 [Multi-domain]  Cd Length: 148  Bit Score: 55.66  E-value: 2.66e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 156058674  419 IRWAIAGGQSGPDGSDIMEILGREESLRRLRVA 451
Cdd:pfam19269 115 LRVALTGKTVSPGLFEIMEILGKEETLARLRKA 147
gltX_arch TIGR00463
glutamyl-tRNA synthetase, archaeal and eukaryotic family; The glutamyl-tRNA synthetases of the ...
 108-198 2.28e-08

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: 56.37  E-value: 2.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  108 FPTYHLANVVDDHFMKITHVVRGSEWIPSTHMHVAMYQAFGWKPPTFAHVGLLLDKDRKKLS---KRDGAID-------- 176
Cdd:TIGR00463 270 YPTMDFSVAIDDHLLGVTHVLRGKDHIDNRRKQEYIYRYFGWEPPEFIHWGRLKIDDVRALStssARKGILRgeysgwdd 349

                          90       100
                  ....*....|....*....|....*..
gi 156058674  177 -----IATYRDAGYFPETVTNFVALLG 198
Cdd:TIGR00463 350 prlptLRAIRRRGIRPEAIRKFMLSIG 376
GlnRS_core cd00807
catalytic core domain of glutaminyl-tRNA synthetase; Glutaminyl-tRNA synthetase (GlnRS) ...
 51-83 6.98e-05

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: 44.16  E-value: 6.98e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 156058674  51 IRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG 83
Cdd:cd00807    2 VVTRFPPEPNGYLHIGHAKAILLNFGYAKKYGG 34
argS PRK01611
arginyl-tRNA synthetase; Reviewed
 101-173 1.71e-03

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 40.91  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674 101 IMVKSDGFPTYH---LANVVD--DHFMKITHVVrGSEwipsTHMHV----AMYQAFGWKPPTFAH-----VGLLLDKDRK 166
Cdd:PRK01611 247 VLIKSDGTYTYFtrdIAYHLYkfERFDRVIYVV-GAD----HHGHFkrlkAALKALGYDPDALEVllhqmVGLVRGGEGV 321


                 ....*..
gi 156058674 167 KLSKRDG 173
Cdd:PRK01611 322 KMSTRAG 328
PLN02859 PLN02859
glutamine-tRNA ligase
 23-83 3.19e-03

glutamine-tRNA ligase


Pssm-ID: 178450 [Multi-domain]  Cd Length: 788  Bit Score: 40.13  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156058674  23 SICRRHASTEANEYPLSVAStklraaGPIRTRFAPSPTGNLHLGSLRTALFNFLLAKATGG 83
Cdd:PLN02859 243 SVLRPSNTKEILEKHLKATG------GKVYTRFPPEPNGYLHIGHAKAMFVDFGLAKERGG 297
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
 96-173 6.46e-03

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


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 38.98  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 EFQDP---IMVKSDGFPTYH---LANVVD----DHFMKITHVVrGSEwipsTHMHV----AMYQAFGWKPPTFAHV---G 158
Cdd:COG0018  296 EFGDDkdrVLVKSDGTYTYFttdIAYHLYkferYGFDRVIYVV-GAD----QHGHFkrlfAALKALGYDPAKDLEHllfG 370

                         90
                 ....*....|....*
gi 156058674 159 LLLDKDRKKLSKRDG 173
Cdd:COG0018  371 MVNLRDGEKMSTRAG 385
ArgRS_core cd00671
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ...
 96-173 7.42e-03

catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates 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. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.


Pssm-ID: 185675 [Multi-domain]  Cd Length: 212  Bit Score: 37.93  E-value: 7.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156058674  96 EFQDP---IMVKSDGFPTY---HLANVVD---DHFMKITHVVrGSEwipsTHMHV----AMYQAFGWKPPTFAHV---GL 159
Cdd:cd00671  124 EFGDDkdrVLVRSDGTYTYftrDIAYHLDkfeRGADKIIYVV-GAD----HHGHFkrlfAALELLGYDEAKKLEHllyGM 198

                         90
                 ....*....|....
gi 156058674 160 LLDKDRKKLSKRDG 173
Cdd:cd00671  199 VNLPKEGKMSTRAG 212
 
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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