|
Name |
Accession |
Description |
Interval |
E-value |
| CysS |
COG0215 |
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ... |
2-327 |
5.59e-162 |
|
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439985 [Multi-domain] Cd Length: 465 Bit Score: 459.95 E-value: 5.59e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 2 VCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGIR 81
Cdd:COG0215 27 VCGPTVYDYAHIGHARTFVVFDVLRRYLRYLGYKVTYVRNITDVDDKIIKRAAEEGESIWELAERYIAAFHEDMDALGVL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 82 SVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAaDGSVYFSVARFPNYGRLSGQKVEALQPGARLAPDERKAAPEDFVLWKA 161
Cdd:COG0215 107 PPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLSGRNLDDLRAGARVEVDEEKRDPLDFALWKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 162 ARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGaAPLVNYWMHWGLLNLHGE 241
Cdd:COG0215 186 AKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEIAQSEAATG-KPFARYWMHNGFLTVNGE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 242 KMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEFDEAtSLPEANEAYARLARPAGRLQELLDRDGIDRPGLDLTE 321
Cdd:COG0215 265 KMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEE-ALEEAEKALERLYNALRRLEEALGAADSSAEEIEELR 343
|
....*.
gi 531011126 322 ERARAA 327
Cdd:COG0215 344 EEFIAA 349
|
|
| tRNA-synt_1e |
pfam01406 |
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ... |
1-282 |
9.27e-122 |
|
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.
Pssm-ID: 396128 [Multi-domain] Cd Length: 301 Bit Score: 351.67 E-value: 9.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:pfam01406 13 YVCGPTVYDYSHIGHARSAVAFDVLRRYLQALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTKDMDALNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAADGSVYFSVARFPNYGRLSGQKVEALQPGARLAPDERKAAPEDFVLWK 160
Cdd:pfam01406 93 LPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQLEAGARGEVSEGKRDPLDFALWK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 161 AARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGaAPLVNYWMHWGLLNLHG 240
Cdd:pfam01406 173 ASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFD-KQLANYWLHNGHVMIDG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 531011126 241 EKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEFDE 282
Cdd:pfam01406 252 EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSE 293
|
|
| cysS |
TIGR00435 |
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ... |
1-311 |
2.11e-118 |
|
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273076 [Multi-domain] Cd Length: 464 Bit Score: 349.37 E-value: 2.11e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:TIGR00435 25 YVCGPTVYDYCHIGHARTAIVFDVLRRYLRYLGYKVQYVQNITDIDDKIIKRARENGESVYEVSERFIEAYFEDMKALNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAADGSVYFSVARFPNYGRLSGQKVEALQPGARLAPDERKAAPEDFVLWK 160
Cdd:TIGR00435 105 LPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQLEAGARVDVDEAKRNKLDFVLWK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 161 AARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGaAPLVNYWMHWGLLNLHG 240
Cdd:TIGR00435 185 SSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIAQSEAAFG-KQLAKYWMHNGFLMIDN 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 531011126 241 EKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEFDEaTSLPEANEAYARLARPAGRLQELLDRDG 311
Cdd:TIGR00435 264 EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSE-ELLEAAKNALERLYKALRVLDTSLAYSG 333
|
|
| PLN02946 |
PLN02946 |
cysteine-tRNA ligase |
1-280 |
1.85e-104 |
|
cysteine-tRNA ligase
Pssm-ID: 178532 [Multi-domain] Cd Length: 557 Bit Score: 316.49 E-value: 1.85e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:PLN02946 84 YVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLGYEVRYVRNFTDVDDKIIARANELGEDPISLSRRYCEEFLSDMAYLHC 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSVNYYAYSTDHLPDIVAQVQQLLDRGFAYvAADGSVYFSVARFPNYGRLSGQKVEALQPGARLAPDERKAAPEDFVLWK 160
Cdd:PLN02946 164 LPPSVEPRVSDHIPQIIDMIKQILDNGCAY-RVDGDVYFSVDKFPEYGKLSGRKLEDNRAGERVAVDSRKKNPADFALWK 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 161 AARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGAAPlVNYWMHWGLLNLHG 240
Cdd:PLN02946 243 AAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQSCAACCDSN-ISYWIHNGFVTVDS 321
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 531011126 241 EKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEF 280
Cdd:PLN02946 322 EKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINY 361
|
|
| cysS |
PRK14535 |
cysteinyl-tRNA synthetase; Provisional |
1-296 |
6.19e-91 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173001 [Multi-domain] Cd Length: 699 Bit Score: 285.84 E-value: 6.19e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:PRK14535 252 YVCGMTVYDYCHLGHARVMVVFDMIARWLRECGYPLTYVRNITDIDDKIIARAAENGETIGELTARFIQAMHEDADALGV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAADGSVYFSVARFPNYGRLSGQKVEALQPGARLAPDERKAAPEDFVLWK 160
Cdd:PRK14535 332 LRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDDLRAGERVEVDGFKRDPLDFVLWK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 161 AARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATG---------------AAP 225
Cdd:PRK14535 412 AAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSVGATGhtcghhhaqthhgqsIAS 491
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 531011126 226 LVNYWMHWGLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEFDEAtSLPEANEAYARL 296
Cdd:PRK14535 492 HVKYWLHNGFIRVDGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYSDA-HLDDAKGALTRL 561
|
|
| PTZ00399 |
PTZ00399 |
cysteinyl-tRNA-synthetase; Provisional |
1-289 |
4.17e-87 |
|
cysteinyl-tRNA-synthetase; Provisional
Pssm-ID: 240402 [Multi-domain] Cd Length: 651 Bit Score: 274.60 E-value: 4.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRW-GYRVLCVQSVTNIDDKVIARAAETGTDP-LALSDRNFREYRALAERL 78
Cdd:PTZ00399 64 YTCGPTVYDSSHLGHARTYVTFDIIRRILEDYfGYDVFYVMNITDIDDKIIKRAREEKLSIfLELARKWEKEFFEDMKAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 79 GIRSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAaDGSVYFSVARF----PNYGRLSGQKVEALQ-----PGARLAPDER 149
Cdd:PTZ00399 144 NVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYES-NGSVYFDVEAFrkagHVYPKLEPESVADEDriaegEGALGKVSGE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 150 KAAPEDFVLWKAARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGAAPLVNY 229
Cdd:PTZ00399 223 KRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNY 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 230 WMHWGLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEFDEaTSLPEA 289
Cdd:PTZ00399 303 FLHSGHLHIKGLKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSD-ESMDEA 361
|
|
| PRK12418 |
PRK12418 |
cysteinyl-tRNA synthetase; Provisional |
1-327 |
1.23e-76 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 183518 [Multi-domain] Cd Length: 384 Bit Score: 239.83 E-value: 1.23e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:PRK12418 13 YVCGITPYDATHLGHAATYLAFDLVNRVWRDAGHDVHYVQNVTDVDDPLLERAARDGVDWRDLAEREIALFREDMEALRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAADGS---VYFSVARFPNYGRLSGQKVEALQP--GARLAPDER--KAAP 153
Cdd:PRK12418 93 LPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEEypdVYFSVDATPQFGYESGYDRATMLElfAERGGDPDRpgKRDP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 154 EDFVLWKAARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGAAPLVNYWMHW 233
Cdd:PRK12418 173 LDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRFARHYVHA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 234 GLLNLHGEKMSKSVGN---TSSLAGaiDAFGPEVLRFFYLNAHYRSPLEFDEAtSLPEANEAYAR----LARPAG-RLQE 305
Cdd:PRK12418 253 GMIGLDGEKMSKSRGNlvfVSRLRA--AGVDPAAIRLALLAGHYRADREWTDA-VLAEAEARLARwraaAALPAGpDAAD 329
|
330 340
....*....|....*....|....*....
gi 531011126 306 LLDR------DGIDRPG-LDLTEERARAA 327
Cdd:PRK12418 330 VVARvraalaDDLDTPGaLAAVDGWATDA 358
|
|
| mycothiol_MshC |
TIGR03447 |
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ... |
1-298 |
3.36e-74 |
|
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]
Pssm-ID: 132488 [Multi-domain] Cd Length: 411 Bit Score: 234.23 E-value: 3.36e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:TIGR03447 40 YVCGITPYDATHLGHAATYLTFDLVNRVWRDAGHRVHYVQNVTDVDDPLFERAERDGVDWRELGTSQIDLFREDMEALRV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSVNYYAYSTDHLPDIVAQVQQLLDRGFAYV---AADGSVYFSVARFPNYGRLSG-QKVEALQPGARLAPD-ER--KAAP 153
Cdd:TIGR03447 120 LPPRDYIGAVESIDEVVEMVEKLLASGAAYIvegPEYPDVYFSIDATEQFGYESGyDRATMLELFAERGGDpDRpgKRDP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 154 EDFVLWKAARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGAAPLVNYWMHW 233
Cdd:TIGR03447 200 LDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATGVRRMARHYVHA 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 531011126 234 GLLNLHGEKMSKSVGN---TSSLAGAidAFGPEVLRFFYLNAHYRSPLEFDEAtslpEANEAYARLAR 298
Cdd:TIGR03447 280 GMIGLDGEKMSKSLGNlvfVSKLRAA--GVDPAAIRLGLLAGHYRQDRDWTDA----VLAEAEARLAR 341
|
|
| CysRS_core |
cd00672 |
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ... |
1-280 |
7.59e-73 |
|
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) 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. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173899 [Multi-domain] Cd Length: 213 Bit Score: 224.00 E-value: 7.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGI 80
Cdd:cd00672 24 YVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLGYKVRYVQNITDIDDKIIKRAREEGLSWKEVADYYTKEFFEDMKALNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 81 RSvnyyaystdhlPDIVAQVqqlldrgfayvaadgsvyfsvarfpnygrlsgqkvealqpgarlapderkaapedfvlwk 160
Cdd:cd00672 104 LP-----------PDVVPRV------------------------------------------------------------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 161 aarpgepswespwgpgrpgWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGaAPLVNYWMHWGLLNLHG 240
Cdd:cd00672 113 -------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAATG-KPFARYWLHTGHLTIDG 172
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 531011126 241 EKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEF 280
Cdd:cd00672 173 EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDF 212
|
|
| cysS |
PRK14536 |
cysteinyl-tRNA synthetase; Provisional |
1-317 |
1.93e-70 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 184731 [Multi-domain] Cd Length: 490 Bit Score: 226.73 E-value: 1.93e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNI----------DDKVIARAAETGTDPLALSDRNFRE 70
Cdd:PRK14536 27 YGCGPTVYNYAHIGNLRTYVFQDTLRRTLHFLGYRVTHVMNITDVghltddadsgEDKMVKSAQEHGKSVLEIAAHYTAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 71 YRALAERLGIRSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAAdGSVYFSVARFPNYGRLSGQKVEALQPGARLAPDERK 150
Cdd:PRK14536 107 FFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAG-GNVYFDIRTFPSYGSLASAAVEDLQAGARIEHDTNK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 151 AAPEDFVLWKAARPGEP---SWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGaAPLV 227
Cdd:PRK14536 186 RNPHDFVLWFTRSKFENhalTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCEAATG-KPWV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 228 NYWMHWGLLNLHGEKMSKSVGNTSSLAGAID-AFGPEVLRFFYLNAHYRSPLEFdEATSLPEANEAYARL-ARPAGRLQE 305
Cdd:PRK14536 265 RYWLHHEFLLMNKGKMSKSAGQFLTLSSLQEkGFQPLDYRFFLLGGHYRSQLAF-SWEALKTAKAARRSLvRRVARVVDA 343
|
330
....*....|..
gi 531011126 306 LLDRDGIDRPGL 317
Cdd:PRK14536 344 ARATTGSVRGTL 355
|
|
| cysS |
PRK14534 |
cysteinyl-tRNA synthetase; Provisional |
1-280 |
1.49e-39 |
|
cysteinyl-tRNA synthetase; Provisional
Pssm-ID: 173000 [Multi-domain] Cd Length: 481 Bit Score: 144.99 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 1 FVCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNI----------DDKVIARAAETGTDPLALSDRNFRE 70
Cdd:PRK14534 25 YACGPTVYNYAHIGNFRTYIFEDLLIKSLRLLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTVYEISRFFTEA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 71 YRALAERLGIRSVNYYAYSTDHLPDIVAQVQQLLDRGFAYVAaDGSVYFSVARFPNYGRLSGQKVEALQPGA--RLAPDE 148
Cdd:PRK14534 105 FFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFV-NGNVYFDTSCFKSYGQMAGINLNDFKDMSvsRVEIDK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 149 RKAAPEDFVLW---KAARPGEPSWESPWGPGRPGWHIEDTAITTRIFGPRYDLHGGGLDLIFPHHEAEIAQAESATGAAp 225
Cdd:PRK14534 184 SKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEIAIAECYLNKK- 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 531011126 226 LVNYWMHWGLLNLHGEKMSKSVGNTSSLAG-AIDAFGPEVLRFFYLNAHYRSPLEF 280
Cdd:PRK14534 263 WCDMFVHGEFLIMEYEKMSKSNNNFITIKDlEDQGFSPLDFRYFCLTAHYRTQLKF 318
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
2-99 |
3.42e-12 |
|
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.
Pssm-ID: 173901 [Multi-domain] Cd Length: 143 Bit Score: 63.27 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 2 VCGLTPYAEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALaerlgir 81
Cdd:cd00802 3 FSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKKGENAKAFVERWIERIKED------- 75
|
90
....*....|....*...
gi 531011126 82 svnyYAYSTDHLPDIVAQ 99
Cdd:cd00802 76 ----VEYMFLQAADFLLL 89
|
|
| MetRS_core |
cd00814 |
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ... |
7-281 |
1.74e-08 |
|
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. 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. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.
Pssm-ID: 173907 [Multi-domain] Cd Length: 319 Bit Score: 54.85 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 7 PYA--EAHVGHGRGFVVFDMVVRAFRRWGYRVLcvqSVTNIDD---KVIARAAETGTDPLALSDRNFREYRALAERLGIr 81
Cdd:cd00814 9 PYVngVPHLGHLYGTVLADVFARYQRLRGYDVL---FVTGTDEhgtKIEQKAEEEGVTPQELCDKYHEIFKDLFKWLNI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 82 SVNYYAYSTDhlPDIVAQVQ----QLLDRGF--------AYVAADGSVYFSVARFPNYG-RLSGQKvEALQ-----PGAR 143
Cdd:cd00814 85 SFDYFIRTTS--PRHKEIVQeffkKLYENGYiyegeyegLYCVSCERFLPEWREEEHYFfRLSKFQ-DRLLewlekNPDF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 144 LAPDERKAAPEDFVlwkaaRPGEPSWE-----SPWG---PGRPG-----W------HIEDTA-ITTRIFGPRY------- 196
Cdd:cd00814 162 IWPENARNEVLSWL-----KEGLKDLSitrdlFDWGipvPLDPGkviyvWfdaligYISATGyYNEEWGNSWWwkdgwpe 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 197 DLHGGGLDlIFPHHeAEIAQA-ESATGAaPLVNYWMHWGLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLnahYR 275
Cdd:cd00814 237 LVHFIGKD-IIRFH-AIYWPAmLLGAGL-PLPTRIVAHGYLTVEGKKMSKSRGNVVDPDDLLERYGADALRYYLL---RE 310
|
....*.
gi 531011126 276 SPLEFD 281
Cdd:cd00814 311 RPEGKD 316
|
|
| PRK11893 |
PRK11893 |
methionyl-tRNA synthetase; Reviewed |
12-270 |
1.55e-07 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 237012 [Multi-domain] Cd Length: 511 Bit Score: 52.58 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 12 HVGHGRGFVVFDMVVRAFRRWGYRVLCVqsvTNIDD---KVIARAAETGTDPLALSDRNFREYRALAERLGIrSVNYYAY 88
Cdd:PRK11893 17 HIGHAYTTLAADVLARFKRLRGYDVFFL---TGTDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALNI-SYDDFIR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 89 STD--HLpDIVAQV-QQLLDRGFAYvAADGSVYFSVA--RF-------------------------PNYG-RLS--GQKV 135
Cdd:PRK11893 93 TTDprHK-EAVQEIfQRLLANGDIY-LGKYEGWYCVRceEFyteseliedgyrcpptgapvewveeESYFfRLSkyQDKL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 136 EAL---QPGaRLAPDERKAAPEDFVlwkaaRPGEPSW---ESP--WG---PGRP----------------GWHIEDTAIT 188
Cdd:PRK11893 171 LELyeaNPD-FIQPASRRNEVISFV-----KSGLKDLsisRTNfdWGipvPGDPkhviyvwfdaltnyltALGYPDDEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 189 TRIFGPRY---DLHGGGLDLIFPHHEAEIAQAESATGAAP---LVNYWmhwglLNLHGEKMSKSVGNTSSLAGAIDAFGP 262
Cdd:PRK11893 245 LAELFNKYwpaDVHLIGKDILRFHAVYWPAFLMAAGLPLPkrvFAHGF-----LTLDGEKMSKSLGNVIDPFDLVDEYGV 319
|
....*...
gi 531011126 263 EVLRFFYL 270
Cdd:PRK11893 320 DAVRYFLL 327
|
|
| LeuRS_core |
cd00812 |
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ... |
7-272 |
9.39e-06 |
|
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) 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. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173906 [Multi-domain] Cd Length: 314 Bit Score: 46.47 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 7 PY--AEAHVGHGRGFVVFDMVVRAFRRWGYRVLCVQSVTNIDDKVIARAAETGTDPLALSDRNFREYRALAERLGIrSVN 84
Cdd:cd00812 9 PYpsGALHVGHVRTYTIGDIIARYKRMQGYNVLFPMGFDAFGLPAENAAIKIGRDPEDWTEYNIKKMKEQLKRMGF-SYD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 85 YYAYSTDHLPDIVAQVQ----QLLDRGFAYVAADGSVYFSVAR--FPNYGRLS-GQKVEALQPGARLAPDERKAAPEDFV 157
Cdd:cd00812 88 WRREFTTCDPEYYKFTQwlflKLYEKGLAYKKEAPVNWCKLLDqwFLKYSETEwKEKLLKDLEKLDGWPEEVRAMQENWI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 158 lwKAARP---GEP--------SW-ESPWGPGR--PGWHIEDTAITTRIFGPRY-------DLHGGGLDLIFPH------H 210
Cdd:cd00812 168 --GCSRQrywGTPipwtdtmeSLsDSTWYYARytDAHNLEQPYEGDLEFDREEfeywypvDIYIGGKEHAPNHllysrfN 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 531011126 211 EAEIAQAESATGAAP---LVNywmhwGLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNA 272
Cdd:cd00812 246 HKALFDEGLVTDEPPkglIVQ-----GMVLLEGEKMSKSKGNVVTPDEAIKKYGADAARLYILFA 305
|
|
| MetG |
COG0143 |
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ... |
234-270 |
1.73e-05 |
|
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439913 [Multi-domain] Cd Length: 544 Bit Score: 46.26 E-value: 1.73e-05
10 20 30
....*....|....*....|....*....|....*..
gi 531011126 234 GLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYL 270
Cdd:COG0143 319 GFLTVEGEKMSKSRGNVIDPDDLLDRYGPDALRYYLL 355
|
|
| IleS |
COG0060 |
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ... |
239-296 |
2.01e-05 |
|
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439830 [Multi-domain] Cd Length: 931 Bit Score: 46.23 E-value: 2.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 531011126 239 HGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYRSPLEFDEATsLPEANEAYARL 296
Cdd:COG0060 600 DGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEI-LKEVRDVYRRL 656
|
|
| leuS |
PRK12300 |
leucyl-tRNA synthetase; Reviewed |
233-298 |
2.39e-05 |
|
leucyl-tRNA synthetase; Reviewed
Pssm-ID: 237049 [Multi-domain] Cd Length: 897 Bit Score: 46.01 E-value: 2.39e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 531011126 233 WGLLNlhGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYL-NAHYRSPLEFDEAtslpEANEAYARLAR 298
Cdd:PRK12300 570 FVLLE--GKKMSKSKGNVIPLRKAIEEYGADVVRLYLTsSAELLQDADWREK----EVESVRRQLER 630
|
|
| tRNA-synt_1g |
pfam09334 |
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases. |
3-270 |
3.14e-05 |
|
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
Pssm-ID: 401322 [Multi-domain] Cd Length: 387 Bit Score: 45.36 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 3 CGLtPYAEA--HVGHGRGFVVFDMVVRAFRRWGYRVLcvqSVTNIDD---KVIARAAETGTDPLALSDRNFREYRALAER 77
Cdd:pfam09334 5 TAL-PYANGppHLGHLYSYIPADIFARYLRLRGYDVL---FVCGTDEhgtPIELKAEKEGITPEELVDRYHEIHREDFKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 78 LGIRSVNYYAYSTDHLPDIVAQ-VQQLLDRGFAYVAADgSVYFSVA--RF----------PNYGRLSGQKVEALQPGARL 144
Cdd:pfam09334 81 FNISFDDYGRTTSERHHELVQEfFLKLYENGYIYEKEI-EQFYCPSdeRFlpdryvegtcPHCGSEDARGDQCENCGRHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 145 APDE--------RKAAPE---------------DFVL-WkaARPGEPSWES-----------------------PWG--- 174
Cdd:pfam09334 160 EPTElinpkcviCGTTPEvketehyffdlskfqDKLReW--IEENNPEWPEnvknmvlewlkeglkdraisrdlDWGipv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 175 PGRPG-----WH---IEDTAITTRIFG------------PRYDL-HGGGLDLIfPHHeAEIAQAESATGAAPLVNYWMHW 233
Cdd:pfam09334 238 PGAEGkvfyvWLdapIGYISATKELSGneekwkewwpndPDTELvHFIGKDII-YFH-TIFWPAMLLGAGYRLPTTVFAH 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 531011126 234 GLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYL 270
Cdd:pfam09334 316 GYLTYEGGKMSKSRGNVVWPSEALDRFPPDALRYYLA 352
|
|
| tRNA-synt_1 |
pfam00133 |
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ... |
188-281 |
1.16e-04 |
|
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.
Pssm-ID: 459685 [Multi-domain] Cd Length: 602 Bit Score: 43.55 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 188 TTRIFGPRY--DLHGGGLDLIFPHHEAEIAQAESATGAAPLVNYWMHWGLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVL 265
Cdd:pfam00133 507 NTEEFKKFFpaDMLLEGSDQTRGWFYRMIMLSTALTGSVPFKNVLVHGLVRDEQGRKMSKSLGNVIDPLDVIDKYGADAL 586
|
90
....*....|....*.
gi 531011126 266 RFFYLNAHYRSPLEFD 281
Cdd:pfam00133 587 RLWLANSDYGRDINLS 602
|
|
| PLN02959 |
PLN02959 |
aminoacyl-tRNA ligase |
232-320 |
9.32e-04 |
|
aminoacyl-tRNA ligase
Pssm-ID: 215518 [Multi-domain] Cd Length: 1084 Bit Score: 41.21 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 232 HW-------GLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNAHYrsplEFDEATSLPE-ANEAYARLARPAGRL 303
Cdd:PLN02959 701 HWprgfrcnGHLMLNSEKMSKSTGNFLTLRQAIEEFSADATRFALADAGD----GVDDANFVFEtANAAILRLTKEIAWM 776
|
90
....*....|....*..
gi 531011126 304 QELLDRDGIDRPGLDLT 320
Cdd:PLN02959 777 EEVLAAESSLRTGPPST 793
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
12-119 |
1.65e-03 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 40.14 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531011126 12 HVGHGRGFVVFDMVVRAFRRWGYRVLcvqsVTN-IDDkviaraaeTGT--DPLALS---------DRNFREYRALAERLG 79
Cdd:PRK01611 127 HVGHLRSAVIGDALARILEFAGYDVT----REYyVND--------AGTqiGMLIASlellwrkavDISLDEIKEDLDRLG 194
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 531011126 80 IRSVNYYAYSTDHLPDIVAQ-VQQLLDRGFAYVAADGSVYF 119
Cdd:PRK01611 195 VHFDVWFSESELYYNGKVDEvVEDLKEKGLLYVESDGALWV 235
|
|
| IleRS_core |
cd00818 |
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ... |
222-272 |
2.57e-03 |
|
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) 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. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.
Pssm-ID: 173909 [Multi-domain] Cd Length: 338 Bit Score: 39.14 E-value: 2.57e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 531011126 222 GAAPLVNYWMHWGLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYLNA 272
Cdd:cd00818 279 GKAPYKNVIVHGFVLDEDGRKMSKSLGNYVDPQEVVDKYGADALRLWVASS 329
|
|
| LysRS_core_class_I |
cd00674 |
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) ... |
240-298 |
5.40e-03 |
|
catalytic core domain of class I lysyl tRNA synthetase; Class I lysyl tRNA synthetase (LysRS) 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. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The class I LysRS is found only in archaea and some bacteria and has evolved separately from class II LysRS, as the two do not share structural or sequence similarity.
Pssm-ID: 173900 [Multi-domain] Cd Length: 353 Bit Score: 38.07 E-value: 5.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 531011126 240 GEKMSKSVGNTSSLAGAIDAFGPEVLRFFYlnahYRSP-----LEFDEatSLPEANEAYARLAR 298
Cdd:cd00674 273 GGKMSSSKGNVITPSDWLEVAPPEVLRYLY----ARRKnpekhIGFDL--DILRLYDEYDRLER 330
|
|
| LysS |
COG1384 |
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ... |
239-309 |
6.76e-03 |
|
Lysyl-tRNA synthetase, class I [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase, class I is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440994 [Multi-domain] Cd Length: 525 Bit Score: 38.25 E-value: 6.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 531011126 239 HGEKMSKSVGNTSSLAGAIDAFGPEVLRFFYlnahYRSP-----LEFDEatsLPEANEAYARLAR--PAGRLQELLDR 309
Cdd:COG1384 284 NGEKISKSKGNGLTVEEWLEYAEPESLRYFM----FRKPkkakdLDFDV---IPKLVDEYDRFERkyFGEEDQEEEER 354
|
|
| metG |
PRK00133 |
methionyl-tRNA synthetase; Reviewed |
234-269 |
7.66e-03 |
|
methionyl-tRNA synthetase; Reviewed
Pssm-ID: 234655 [Multi-domain] Cd Length: 673 Bit Score: 37.82 E-value: 7.66e-03
10 20 30
....*....|....*....|....*....|....*.
gi 531011126 234 GLLNLHGEKMSKSVGNTSSLAGAIDAFGPEVLRFFY 269
Cdd:PRK00133 321 GFLTVEGAKMSKSRGTFIWARTYLDHLDPDYLRYYL 356
|
|
| |
