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Conserved domains on  [gi|19922218|ref|NP_610930|]
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Cysteinyl-tRNA synthetase, mitochondrial, isoform A [Drosophila melanogaster]

Protein Classification

cysteine--tRNA ligase( domain architecture ID 11415459)

cysteine--tRNA ligase catalyzes the attachment of cysteine to tRNA(Cys)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
48-543 1.87e-161

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: 468.04  E-value: 1.87e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  48 INIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRD-YFKINLVtaMNITDVDDKIIKRAQ 126
Cdd:COG0215   2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYlGYKVTYV--RNITDVDDKIIKRAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 127 LAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTpDNSVYFDVSKSKNYGKL--QN 204
Cdd:COG0215  80 EEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLsgRN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 205 LglseDKL--------DPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFP 276
Cdd:COG0215 159 L----DDLragarvevDEEKRDPLDFALWKAAKPG-EPSWDSPWG-RGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 277 HHENEEAQCCARYKtDQWVNYWVHTGqlHMVGDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMV 356
Cdd:COG0215 233 HHENEIAQSEAATG-KPFARYWMHNG--FLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 357 TARQTLQRFRNFQADLSAYTQflkpvhllDEGALKAQLTHTVTEFDNCLRDDFDTARAISVLIDQMSSISRCINEQqvDA 436
Cdd:COG0215 310 EAEKALERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEG--ED 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 437 QEEPAYCIDLLLAAGNFinraivtFGLselqDKESLQEKVSFTDHSIDPNlLVNDVINVRGRMRER---ATSgnvknpql 513
Cdd:COG0215 380 KAALAALAALLRALGGV-------LGL----LLLEPEAWQGAAEDELLDA-LIEALIEERAEARKAkdfARA-------- 439
                       490       500       510
                ....*....|....*....|....*....|
gi 19922218 514 laacDELRSLLQQHGIQVRDHKQGSSWVFA 543
Cdd:COG0215 440 ----DRIRDELAALGIVLEDTPDGTTWRRK 465
 
Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
48-543 1.87e-161

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: 468.04  E-value: 1.87e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  48 INIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRD-YFKINLVtaMNITDVDDKIIKRAQ 126
Cdd:COG0215   2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYlGYKVTYV--RNITDVDDKIIKRAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 127 LAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTpDNSVYFDVSKSKNYGKL--QN 204
Cdd:COG0215  80 EEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLsgRN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 205 LglseDKL--------DPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFP 276
Cdd:COG0215 159 L----DDLragarvevDEEKRDPLDFALWKAAKPG-EPSWDSPWG-RGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 277 HHENEEAQCCARYKtDQWVNYWVHTGqlHMVGDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMV 356
Cdd:COG0215 233 HHENEIAQSEAATG-KPFARYWMHNG--FLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 357 TARQTLQRFRNFQADLSAYTQflkpvhllDEGALKAQLTHTVTEFDNCLRDDFDTARAISVLIDQMSSISRCINEQqvDA 436
Cdd:COG0215 310 EAEKALERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEG--ED 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 437 QEEPAYCIDLLLAAGNFinraivtFGLselqDKESLQEKVSFTDHSIDPNlLVNDVINVRGRMRER---ATSgnvknpql 513
Cdd:COG0215 380 KAALAALAALLRALGGV-------LGL----LLLEPEAWQGAAEDELLDA-LIEALIEERAEARKAkdfARA-------- 439
                       490       500       510
                ....*....|....*....|....*....|
gi 19922218 514 laacDELRSLLQQHGIQVRDHKQGSSWVFA 543
Cdd:COG0215 440 ----DRIRDELAALGIVLEDTPDGTTWRRK 465
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
23-552 9.88e-157

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 462.58  E-value: 9.88e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   23 RNISEEAPKQDSPF-KWRKPIGQ---HTGINIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQR 98
Cdd:PTZ00399  11 AGLNGTGQVSKSRLpEWKKPSKEgkyLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   99 ILRDYFKINLVTAMNITDVDDKIIKRAQLAGLD-WQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLID 177
Cdd:PTZ00399  91 ILEDYFGYDVFYVMNITDIDDKIIKRAREEKLSiFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIID 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  178 GKQAYVTpDNSVYFDVSKSK----NYGKL--------QNLGLSEDKLDPI---KRNTADFALWKARKSGsEPTWAAPWgG 242
Cdd:PTZ00399 171 NGFAYES-NGSVYFDVEAFRkaghVYPKLepesvadeDRIAEGEGALGKVsgeKRSPNDFALWKASKPG-EPSWDSPW-G 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  243 EGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTDQWVNYWVHTGQLHMVGDreKMSKSLGNTIS 322
Cdd:PTZ00399 248 KGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL--KMSKSLKNFIT 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  323 VSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQRFRNFQADLSAY--TQFLKPVHLLDEG--ALKAQLTHTV 398
Cdd:PTZ00399 326 IRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKlrESELTSPQKWTQHdfELNELFEETK 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  399 TEFDNCLRDDFDTARAISVLIDQMSSISRCINE-QQVDAqeepayciDLLLAAGNFINRAIVTFGLSELQDKESLQEKVS 477
Cdd:PTZ00399 406 SAVHAALLDNFDTPEALQALQKLISATNTYLNSgEQPSA--------PLLRSVAQYVTKILSIFGLVEGSDGLGSQGQNS 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  478 fTDHSIDPnlLVNDVINVRGRMRERATSGNV------KNPQLLAACDELRS-LLQQHGIQVRDHKQGSSWVfavsceKQD 550
Cdd:PTZ00399 478 -TSENFKP--LLEALLRFRDEVRDAAKAEMKlisldkKKKQLLQLCDKLRDeWLPNLGIRIEDKPDGPSVW------KLD 548

                 ..
gi 19922218  551 DK 552
Cdd:PTZ00399 549 DK 550
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
50-540 1.54e-130

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: 389.05  E-value: 1.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218    50 IYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDVDDKIIKRAQLAG 129
Cdd:TIGR00435   3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARENG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   130 LDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE 209
Cdd:TIGR00435  82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   210 ------DKLDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEA 283
Cdd:TIGR00435 162 leagarVDVDEAKRNKLDFVLWKSSKEG-EPKWDSPWG-KGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   284 QCCARYKTdQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQ 363
Cdd:TIGR00435 240 QSEAAFGK-QLAKYWMHNGFLMI--DNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   364 RFRNfqaDLSAYTQFLKPVHLLDEGALKAQLTHTVtEFDNCLRDDFDTARAISVLIDQMSSISRcineqqvdaqeepaYC 443
Cdd:TIGR00435 317 RLYK---ALRVLDTSLAYSGNQSLNKFPDEKEFEA-RFVEAMDDDLNTANALAVLFELAKSINL--------------TF 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   444 IDLLLAAGNFINraivtfgLSELQDKESLQEKVSFTDHSIDPNLLVN---DVINVRGRMRERatsgnvKNpqlLAACDEL 520
Cdd:TIGR00435 379 VSKADAALLIEH-------LIFLESRLGLLLGLPSKPVQAGSNDDLGeieALIEERSIARKE------KD---FAKADEI 442
                         490       500
                  ....*....|....*....|
gi 19922218   521 RSLLQQHGIQVRDHKQGSSW 540
Cdd:TIGR00435 443 RDELAKKGIVLEDTPQGTTW 462
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
66-359 8.99e-121

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 357.83  E-value: 8.99e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218    66 PQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQ 145
Cdd:pfam01406   7 QGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   146 DMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE------DKLDPIKRNT 219
Cdd:pfam01406  86 DMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQleagarGEVSEGKRDP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   220 ADFALWKARKSGsEPTWAAPWgGEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTdQWVNYWV 299
Cdd:pfam01406 166 LDFALWKASKEG-EPSWDSPW-GKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDK-QLANYWL 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   300 HTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTAR 359
Cdd:pfam01406 243 HNGHVMI--DGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
49-351 3.40e-106

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: 317.21  E-value: 3.40e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  49 NIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDYFkINLVTAMNITDVDDKIIKRAQLA 128
Cdd:cd00672   1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 129 GLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVtttmpviiqfiqqlidgkqayvtpdnsvyfdvsksknygklqnlgls 208
Cdd:cd00672  80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 209 edkldpikrntadfalwkarksgseptwaapwggegrpgWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCAR 288
Cdd:cd00672 113 ---------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAA 153
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922218 289 YKTdQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYS 351
Cdd:cd00672 154 TGK-PFARYWLHTGHLTI--DGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
DALR_2 smart00840
This DALR domain is found in cysteinyl-tRNA-synthetases;
400-454 1.41e-03

This DALR domain is found in cysteinyl-tRNA-synthetases;


Pssm-ID: 214848 [Multi-domain]  Cd Length: 56  Bit Score: 37.16  E-value: 1.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922218    400 EFDNCLRDDFDTARAISVLIDqmssISRCINEQQVDAQ--EEPAYCIDLLLAAGNFI 454
Cdd:smart00840   1 RFEEAMDDDFNTPEALAVLFE----LAREINRLALKATdaEELAALAALLRALGGVL 53
 
Name Accession Description Interval E-value
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
48-543 1.87e-161

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: 468.04  E-value: 1.87e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  48 INIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRD-YFKINLVtaMNITDVDDKIIKRAQ 126
Cdd:COG0215   2 LKLYNTLTRKKEEFVPLEPGKVRMYVCGPTVYDYAHIGHARTFVVFDVLRRYLRYlGYKVTYV--RNITDVDDKIIKRAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 127 LAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTpDNSVYFDVSKSKNYGKL--QN 204
Cdd:COG0215  80 EEGESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAYEA-DGDVYFDVRSFPDYGKLsgRN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 205 LglseDKL--------DPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFP 276
Cdd:COG0215 159 L----DDLragarvevDEEKRDPLDFALWKAAKPG-EPSWDSPWG-RGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFP 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 277 HHENEEAQCCARYKtDQWVNYWVHTGqlHMVGDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMV 356
Cdd:COG0215 233 HHENEIAQSEAATG-KPFARYWMHNG--FLTVNGEKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALE 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 357 TARQTLQRFRNFQADLSAYTQflkpvhllDEGALKAQLTHTVTEFDNCLRDDFDTARAISVLIDQMSSISRCINEQqvDA 436
Cdd:COG0215 310 EAEKALERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKALDEG--ED 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 437 QEEPAYCIDLLLAAGNFinraivtFGLselqDKESLQEKVSFTDHSIDPNlLVNDVINVRGRMRER---ATSgnvknpql 513
Cdd:COG0215 380 KAALAALAALLRALGGV-------LGL----LLLEPEAWQGAAEDELLDA-LIEALIEERAEARKAkdfARA-------- 439
                       490       500       510
                ....*....|....*....|....*....|
gi 19922218 514 laacDELRSLLQQHGIQVRDHKQGSSWVFA 543
Cdd:COG0215 440 ----DRIRDELAALGIVLEDTPDGTTWRRK 465
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
23-552 9.88e-157

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 462.58  E-value: 9.88e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   23 RNISEEAPKQDSPF-KWRKPIGQ---HTGINIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQR 98
Cdd:PTZ00399  11 AGLNGTGQVSKSRLpEWKKPSKEgkyLTGLKVNNSLTGGKVEFVPQNGRQVRWYTCGPTVYDSSHLGHARTYVTFDIIRR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   99 ILRDYFKINLVTAMNITDVDDKIIKRAQLAGLD-WQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLID 177
Cdd:PTZ00399  91 ILEDYFGYDVFYVMNITDIDDKIIKRAREEKLSiFLELARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIID 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  178 GKQAYVTpDNSVYFDVSKSK----NYGKL--------QNLGLSEDKLDPI---KRNTADFALWKARKSGsEPTWAAPWgG 242
Cdd:PTZ00399 171 NGFAYES-NGSVYFDVEAFRkaghVYPKLepesvadeDRIAEGEGALGKVsgeKRSPNDFALWKASKPG-EPSWDSPW-G 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  243 EGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTDQWVNYWVHTGQLHMVGDreKMSKSLGNTIS 322
Cdd:PTZ00399 248 KGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNELAQSEAYFDKHQWVNYFLHSGHLHIKGL--KMSKSLKNFIT 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  323 VSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQRFRNFQADLSAY--TQFLKPVHLLDEG--ALKAQLTHTV 398
Cdd:PTZ00399 326 IRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEKDKVFFNFFANVKIKlrESELTSPQKWTQHdfELNELFEETK 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  399 TEFDNCLRDDFDTARAISVLIDQMSSISRCINE-QQVDAqeepayciDLLLAAGNFINRAIVTFGLSELQDKESLQEKVS 477
Cdd:PTZ00399 406 SAVHAALLDNFDTPEALQALQKLISATNTYLNSgEQPSA--------PLLRSVAQYVTKILSIFGLVEGSDGLGSQGQNS 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  478 fTDHSIDPnlLVNDVINVRGRMRERATSGNV------KNPQLLAACDELRS-LLQQHGIQVRDHKQGSSWVfavsceKQD 550
Cdd:PTZ00399 478 -TSENFKP--LLEALLRFRDEVRDAAKAEMKlisldkKKKQLLQLCDKLRDeWLPNLGIRIEDKPDGPSVW------KLD 548

                 ..
gi 19922218  551 DK 552
Cdd:PTZ00399 549 DK 550
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
50-540 1.54e-130

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: 389.05  E-value: 1.54e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218    50 IYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDVDDKIIKRAQLAG 129
Cdd:TIGR00435   3 LYNTLTRQKEEFEPLVQGKVKMYVCGPTVYDYCHIGHARTAIVFDVLRRYLR-YLGYKVQYVQNITDIDDKIIKRARENG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   130 LDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE 209
Cdd:TIGR00435  82 ESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKFKDYGKLSKQDLDQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   210 ------DKLDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEA 283
Cdd:TIGR00435 162 leagarVDVDEAKRNKLDFVLWKSSKEG-EPKWDSPWG-KGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEIA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   284 QCCARYKTdQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQ 363
Cdd:TIGR00435 240 QSEAAFGK-QLAKYWMHNGFLMI--DNEKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKNALE 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   364 RFRNfqaDLSAYTQFLKPVHLLDEGALKAQLTHTVtEFDNCLRDDFDTARAISVLIDQMSSISRcineqqvdaqeepaYC 443
Cdd:TIGR00435 317 RLYK---ALRVLDTSLAYSGNQSLNKFPDEKEFEA-RFVEAMDDDLNTANALAVLFELAKSINL--------------TF 378
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   444 IDLLLAAGNFINraivtfgLSELQDKESLQEKVSFTDHSIDPNLLVN---DVINVRGRMRERatsgnvKNpqlLAACDEL 520
Cdd:TIGR00435 379 VSKADAALLIEH-------LIFLESRLGLLLGLPSKPVQAGSNDDLGeieALIEERSIARKE------KD---FAKADEI 442
                         490       500
                  ....*....|....*....|
gi 19922218   521 RSLLQQHGIQVRDHKQGSSW 540
Cdd:TIGR00435 443 RDELAKKGIVLEDTPQGTTW 462
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
66-359 8.99e-121

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 357.83  E-value: 8.99e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218    66 PQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQ 145
Cdd:pfam01406   7 QGKVTMYVCGPTVYDYSHIGHARSAVAFDVLRRYLQ-ALGYDVQFVQNFTDIDDKIIKRARQEGESFRQLAARFIEAYTK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   146 DMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE------DKLDPIKRNT 219
Cdd:pfam01406  86 DMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSSFPDYGKLSGQNLEQleagarGEVSEGKRDP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   220 ADFALWKARKSGsEPTWAAPWgGEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTdQWVNYWV 299
Cdd:pfam01406 166 LDFALWKASKEG-EPSWDSPW-GKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAFDK-QLANYWL 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   300 HTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTAR 359
Cdd:pfam01406 243 HNGHVMI--DGEKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
49-351 3.40e-106

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: 317.21  E-value: 3.40e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  49 NIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDYFkINLVTAMNITDVDDKIIKRAQLA 128
Cdd:cd00672   1 RLYNTLTRQKEEFVPLNPGLVTMYVCGPTVYDYAHIGHARTYVVFDVLRRYLEDLG-YKVRYVQNITDIDDKIIKRAREE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 129 GLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVtttmpviiqfiqqlidgkqayvtpdnsvyfdvsksknygklqnlgls 208
Cdd:cd00672  80 GLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV----------------------------------------------- 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 209 edkldpikrntadfalwkarksgseptwaapwggegrpgWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCAR 288
Cdd:cd00672 113 ---------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSEAA 153
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922218 289 YKTdQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYS 351
Cdd:cd00672 154 TGK-PFARYWLHTGHLTI--DGEKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
PLN02946 PLN02946
cysteine-tRNA ligase
41-555 6.06e-93

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 295.30  E-value: 6.06e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   41 PIGQHTGINIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVTamNITDVDD 119
Cdd:PLN02946  53 PASRGRELHLYNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLYRYLKHLgYEVRYVR--NFTDVDD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  120 KIIKRAQLAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTpDNSVYFDVSKSKNY 199
Cdd:PLN02946 131 KIIARANELGEDPISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRV-DGDVYFSVDKFPEY 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  200 GKLQNLGLSEDK------LDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDL 273
Cdd:PLN02946 210 GKLSGRKLEDNRagervaVDSRKKNPADFALWKAAKEG-EPFWDSPWG-PGRPGWHIECSAMSAAYLGHSFDIHGGGMDL 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  274 RFPHHENEEAQCCARYKtDQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQ 353
Cdd:PLN02946 288 VFPHHENEIAQSCAACC-DSNISYWIHNGFVTV--DSEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDV 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  354 LMVTAR-------QTLQRFRN-FQADLSAYTQFLKPVHLLDEgalkaqLTHTVTEFDNCLRDDFDTARAISVLIDQMSSI 425
Cdd:PLN02946 365 QLESASerifyiyQTLHDCEEsLQQHDSTFEKDSVPPDTLNC------INKFHDEFVTSMSDDLHTPVALAALSEPLKTI 438
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  426 SRCINEQQVDAQEEPaycIDLLLAAGNFINRAIVTFGLSELQDKESLQEkvsFTDHSIDPNLLVNDviNVRGRMRERATS 505
Cdd:PLN02946 439 NDLLHTRKGKKQEKR---LESLAALEKKIRDVLSVLGLMPTSYSEALQQ---LREKALRRAKLTEE--QVLQKIEERTVA 510
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 19922218  506 GNVKNPQllaACDELRSLLQQHGIQVRDHKQGSSWVFAVSCEKQDDKSKS 555
Cdd:PLN02946 511 RKNKEYE---KSDAIRKDLAAVGIALMDSPDGTTWRPAIPLALQEQVAAT 557
PRK12418 PRK12418
cysteinyl-tRNA synthetase; Provisional
69-418 6.15e-79

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 183518 [Multi-domain]  Cd Length: 384  Bit Score: 253.31  E-value: 6.15e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   69 VTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVtaMNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQDM 147
Cdd:PRK12418  10 ATMYVCGITPYDATHLGHAATYLAFDLVNRVWRDAgHDVHYV--QNVTDVDDPLLERAARDGVDWRDLAEREIALFREDM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  148 LRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNS---VYFDVSKSKNYGKLQNLGLSE----------DKLDP 214
Cdd:PRK12418  88 EALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYVVDDEEypdVYFSVDATPQFGYESGYDRATmlelfaerggDPDRP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  215 IKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEAQCCARYKTDQW 294
Cdd:PRK12418 168 GKRDPLDALLWRAARPG-EPSWPSPFG-PGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATGERRF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  295 VNYWVHTGqlhMVG-DREKMSKSLGNTISVSELlkkyTADEF-----RMACLLSNYRNAMPYSDQLMVTARQTLQRFRNF 368
Cdd:PRK12418 246 ARHYVHAG---MIGlDGEKMSKSRGNLVFVSRL----RAAGVdpaaiRLALLAGHYRADREWTDAVLAEAEARLARWRAA 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 19922218  369 QAdlsaytqflkpvhlLDEGALKAQLTHTVTEFdncLRDDFDTARAISVL 418
Cdd:PRK12418 319 AA--------------LPAGPDAADVVARVRAA---LADDLDTPGALAAV 351
mycothiol_MshC TIGR03447
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ...
43-418 8.37e-78

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: 251.18  E-value: 8.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218    43 GQHTGINIYNHGLRQKVPLilRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVtaMNITDVDDKI 121
Cdd:TIGR03447  13 GTGPPLRLFDTADGQVRPV--EPGPEAGMYVCGITPYDATHLGHAATYLTFDLVNRVWRDAgHRVHYV--QNVTDVDDPL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   122 IKRAQLAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNS---VYFDVSKSKN 198
Cdd:TIGR03447  89 FERAERDGVDWRELGTSQIDLFREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYIVEGPEypdVYFSIDATEQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   199 YGKLQNLGLSE----------DKLDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHA 268
Cdd:TIGR03447 169 FGYESGYDRATmlelfaerggDPDRPGKRDPLDALLWRAAREG-EPSWDSPFG-RGRPGWHIECSAIALNRLGAGFDIQG 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   269 GGLDLRFPHHENEEAQCCARYKTDQWVNYWVHTGqlhMVG-DREKMSKSLGNTISVSELLKK-YTADEFRMACLLSNYRN 346
Cdd:TIGR03447 247 GGSDLIFPHHEFSAAHAEAATGVRRMARHYVHAG---MIGlDGEKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQ 323
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922218   347 AMPYSDQLMVTARQTLQRFRNFQADLSAytqflkpvhlldegalkAQLTHTVTEFDNCLRDDFDTARAISVL 418
Cdd:TIGR03447 324 DRDWTDAVLAEAEARLARWRAALALPDA-----------------PDATDLIARLRQHLANDLDTPAALAAV 378
cysS PRK14535
cysteinyl-tRNA synthetase; Provisional
50-540 2.18e-73

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173001 [Multi-domain]  Cd Length: 699  Bit Score: 247.32  E-value: 2.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   50 IYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRDyFKINLVTAMNITDVDDKIIKRAQLAG 129
Cdd:PRK14535 230 IYNTLTRQKEPFAPIDPENVRMYVCGMTVYDYCHLGHARVMVVFDMIARWLRE-CGYPLTYVRNITDIDDKIIARAAENG 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  130 LDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNSVYFDVSKSKNYGKLQNLGLSE 209
Cdd:PRK14535 309 ETIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYAVREFAAYGQLSGKSLDD 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  210 DK------LDPIKRNTADFALWKARKSGsEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEEA 283
Cdd:PRK14535 389 LRagerveVDGFKRDPLDFVLWKAAKAG-EPAWESPWG-NGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIA 466
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  284 Q-------CCARYKTD--------QWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAM 348
Cdd:PRK14535 467 QsvgatghTCGHHHAQthhgqsiaSHVKYWLHNGFIRV--DGEKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPL 544
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  349 PYSDQLMVTARQTLQRFrnfqadlsaYTQfLKPVHLLDEGALKAQLTHTvTEFDNCLRDDFDTARAISVLIDQMSSISRc 428
Cdd:PRK14535 545 NYSDAHLDDAKGALTRL---------YTT-LKNTPAAEFMLSENVNDYT-RRFYAAMNDDFGTVEAVAVLFELAGEVNK- 612
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  429 INEQQVDAQeepaycidlLLAAGNFInraivtfGLSELQDKESLQEKVSFTDHSidpNLLVNDVINVRGRMRERatsgnv 508
Cdd:PRK14535 613 TNDAQLAGC---------LKALGGII-------GLLQRDPTEFLQGGAASDGLS---NEEIEDLIARRKQARAD------ 667
                        490       500       510
                 ....*....|....*....|....*....|..
gi 19922218  509 KNpqlLAACDELRSLLQQHGIQVRDHKQGSSW 540
Cdd:PRK14535 668 KN---WAESDRIRDLLNEHKIILEDNAGGTTW 696
cysS PRK14536
cysteinyl-tRNA synthetase; Provisional
48-540 9.68e-72

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 184731 [Multi-domain]  Cd Length: 490  Bit Score: 237.90  E-value: 9.68e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   48 INIYNHGLRQKVPLILRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDV---------- 117
Cdd:PRK14536   3 LRLYNTLGRQQEEFQPIEHGHVRLYGCGPTVYNYAHIGNLRTYVFQDTLRRTLH-FLGYRVTHVMNITDVghltddadsg 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  118 DDKIIKRAQLAGLDWQKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNsVYFDVSKSK 197
Cdd:PRK14536  82 EDKMVKSAQEHGKSVLEIAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTYCAGGN-VYFDIRTFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  198 NYGKLQNLGLSEDK------LDPIKRNTADFALW--KARKSGSEPTWAAPWGgEGRPGWHIECSAIAGLFFGRQLDIHAG 269
Cdd:PRK14536 161 SYGSLASAAVEDLQagarieHDTNKRNPHDFVLWftRSKFENHALTWDSPWG-RGYPGWHIECSAMSMKYLGEQCDIHIG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  270 GLDLRFPHHENEEAQCCArYKTDQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKK-YTADEFRMACLLSNYRNAM 348
Cdd:PRK14536 240 GVDHIRVHHTNEIAQCEA-ATGKPWVRYWLHHEFLLM--NKGKMSKSAGQFLTLSSLQEKgFQPLDYRFFLLGGHYRSQL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  349 PYSDQLMVTARQTLQRFRNFQA---DLSAYTQFLKPVHLLDEGALKAQLTHT------VTEFDNCLRDDFDTARAISVLi 419
Cdd:PRK14536 317 AFSWEALKTAKAARRSLVRRVArvvDAARATTGSVRGTLAECAAERVAESRAsesellLTDFRAALEDDFSTPKALSEL- 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  420 dqmssiSRCINEQQVdaqeEPAYCIDLLLAAGNFINRAIVTFGLSELQDKESLQEKVSFTDHSIdpnllvndvinvrgrm 499
Cdd:PRK14536 396 ------QKLVKDTSV----PPSLCLSVLQAMDTVLGLGLIQEATASLSAQVPAGPSEEEIGQLI---------------- 449
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 19922218  500 RERATSGNVKNPQLlaaCDELRSLLQQHGIQVRDHKQGSSW 540
Cdd:PRK14536 450 EARAHARQTKDFPL---ADEIRDKLKAEGIELEDTHLGTIW 487
cysS PRK14534
cysteinyl-tRNA synthetase; Provisional
63-351 2.13e-51

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173000 [Multi-domain]  Cd Length: 481  Bit Score: 183.13  E-value: 2.13e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   63 LRNPQMVTWYTCGPTVYDSAHLGHASTYVKVDILQRILRdYFKINLVTAMNITDV----------DDKIIKRAQLAGLDW 132
Cdd:PRK14534  16 LKNFSDVKVYACGPTVYNYAHIGNFRTYIFEDLLIKSLR-LLKYNVNYAMNITDIghltgdfddgEDKVVKAARERGLTV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  133 QKMARAYEAEFRQDMLRLNVQAPDVRSHVTTTMPVIIQFIQQLIDGKQAYVTPDNsVYFDVSKSKNYGKLQNLGLSEDK- 211
Cdd:PRK14534  95 YEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTYFVNGN-VYFDTSCFKSYGQMAGINLNDFKd 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  212 -------LDPIKRNTADFALW--KARKSGSEPTWAAPWGGeGRPGWHIECSAIAGLFFGRQLDIHAGGLDLRFPHHENEE 282
Cdd:PRK14534 174 msvsrveIDKSKRNKSDFVLWftNSKFKDQEMKWDSPWGF-GYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHINEI 252
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922218  283 A--QCcarYKTDQWVNYWVHTGQLHMvgDREKMSKSLGNTISVSELLKK-YTADEFRMACLLSNYRNAMPYS 351
Cdd:PRK14534 253 AiaEC---YLNKKWCDMFVHGEFLIM--EYEKMSKSNNNFITIKDLEDQgFSPLDFRYFCLTAHYRTQLKFT 319
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
308-427 2.02e-11

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: 67.03  E-value: 2.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 308 GDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYSDQLMVTARQTLQRFRN----FQADLSAY--TQFLKP 381
Cdd:COG0060 599 EDGRKMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEVRDVYRRLRNtyrfLLANLDDFdpAEDAVP 678
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922218 382 V---HLLDEGALkAQLTHTVTEFDNCLrDDFDTARAISVL----IDQMSS----ISR 427
Cdd:COG0060 679 YedlPELDRWIL-SRLNELIKEVTEAY-DNYDFHRAYRALhnfcVEDLSNwyldISK 733
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
72-146 6.83e-10

catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173901 [Multi-domain]  Cd Length: 143  Bit Score: 57.49  E-value: 6.83e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922218  72 YTCGPTVYDSAHLGHASTYVKVDILQRILRDY-FKINLVTamNITDVDDKIIKRAQLAGLDWQKMARAYEAEFRQD 146
Cdd:cd00802   2 TFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLgYKVRCIA--LIDDAGGLIGDPANKKGENAKAFVERWIERIKED 75
Ile_Leu_Val_MetRS_core cd00668
catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic ...
73-336 1.06e-08

catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases; Catalytic core domain of isoleucyl, leucyl, valyl and methioninyl tRNA synthetases. These class I enzymes are all monomers. However, in some species, MetRS functions as a homodimer, as a result of an additional C-terminal domain. These enzymes 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. Enzymes in this subfamily share 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. MetRS has a significantly shorter insertion, which lacks the editing function.


Pssm-ID: 185674 [Multi-domain]  Cd Length: 312  Bit Score: 57.04  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  73 TCG-PTVYDSAHLGHASTYVKVDILQRILR-DYFKINLVTAMNIT------------DVDDKIIKRAQLAGLDWQkMARA 138
Cdd:cd00668   5 TTPpPYANGSLHLGHALTHIIADFIARYKRmRGYEVPFLPGWDTHglpielkaerkgGRKKKTIWIEEFREDPKE-FVEE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 139 YEAEFRQDMLRLNVQAPDVRSHVTTTmPVIIQFIQ----QLIDGKQAY-----VTPDNSVYFDVSKsknygklqnlgLSE 209
Cdd:cd00668  84 MSGEHKEDFRRLGISYDWSDEYITTE-PEYSKAVElifsRLYEKGLIYrgthpVRITEQWFFDMPK-----------FKE 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 210 DKLDPIKRNTADFALWKAR-----KSGSEptWA----APWGGEgRPGWHIECSAIAGLFfgrqldiHAGGLDLRFPHHEN 280
Cdd:cd00668 152 KLLKALRRGKIVPEHVKNRmeawlESLLD--WAisrqRYWGTP-LPEDVFDVWFDSGIG-------PLGSLGYPEEKEWF 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19922218 281 EEAQCCARYKT--DQ---WVNYW----VHTGQLH-----------MVGDREKMSKSLGNTISVSELLKKYTADEFR 336
Cdd:cd00668 222 KDSYPADWHLIgkDIlrgWANFWitmlVALFGEIppknllvhgfvLDEGGQKMSKSKGNVIDPSDVVEKYGADALR 297
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
264-338 1.62e-08

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: 56.49  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 264 LDIHAGGLDL--------RFPHHeneeaqccARYKTDQWVNYWVH--TGQLHMVGDREKMSKSLGNTISVSELLKKYTAD 333
Cdd:cd00812 225 VDIYIGGKEHapnhllysRFNHK--------ALFDEGLVTDEPPKglIVQGMVLLEGEKMSKSKGNVVTPDEAIKKYGAD 296

                ....*
gi 19922218 334 EFRMA 338
Cdd:cd00812 297 AARLY 301
valS PRK13208
valyl-tRNA synthetase; Reviewed
309-418 2.94e-08

valyl-tRNA synthetase; Reviewed


Pssm-ID: 237306 [Multi-domain]  Cd Length: 800  Bit Score: 56.74  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  309 DREKMSKSLGNTISVSELLKKYTADEFRM----ACLLSNYrnamPYSDQLMVTARQTLQRFRN---FQADLSAYTQFLKP 381
Cdd:PRK13208 530 DGKKMSKSKGNVVTPEELLEKYGADAVRYwaasARLGSDT----PFDEKQVKIGRRLLTKLWNasrFVLHFSADPEPDKA 605
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19922218  382 V--HLLDEgALKAQLTHTVTEFDNCLrDDFDTARAISVL 418
Cdd:PRK13208 606 EvlEPLDR-WILAKLAKVVEKATEAL-ENYDFAKALEEI 642
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
311-415 3.09e-07

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 53.33  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  311 EKMSKSLGNTISVSELLKKYTADEFRMAcLLSnyrNAMPYSD-----QLMVTARQTLQRFRNFQADLSAYTqflKPVHLL 385
Cdd:PRK12300 576 KKMSKSKGNVIPLRKAIEEYGADVVRLY-LTS---SAELLQDadwreKEVESVRRQLERFYELAKELIEIG---GEEELR 648
                         90       100       110
                 ....*....|....*....|....*....|.
gi 19922218  386 DEGA-LKAQLTHTVTEFDNCLrDDFDTARAI 415
Cdd:PRK12300 649 FIDKwLLSRLNRIIKETTEAM-ESFQTRDAV 678
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
73-336 1.46e-05

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: 47.14  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218  73 TCG-PTVYDSAHLGHASTYVKVDILQRILR-DYFKINLVTAMnitdvdD----KIIKRAQLAGLDWQKMARAYEAEFRQD 146
Cdd:cd00814   5 TTAlPYVNGVPHLGHLYGTVLADVFARYQRlRGYDVLFVTGT------DehgtKIEQKAEEEGVTPQELCDKYHEIFKDL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 147 MLRLNVQ--------APDvrsHVTTTMpviiQFIQQLID-G-------KQAYVTPDNSVYFDVSKSKNY----GKLQ--- 203
Cdd:cd00814  79 FKWLNISfdyfirttSPR---HKEIVQ----EFFKKLYEnGyiyegeyEGLYCVSCERFLPEWREEEHYffrlSKFQdrl 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 204 -----------------NLGLS--EDKLDP--IKRNTADF-----------------AL---------WkARKSGSEPTW 236
Cdd:cd00814 152 lewleknpdfiwpenarNEVLSwlKEGLKDlsITRDLFDWgipvpldpgkviyvwfdALigyisatgyY-NEEWGNSWWW 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218 237 AAPWGgegrPGWHiecsaiaglFFGRqlDI---HA-------GGLDLRFPHHeneeaqccaryktdqwvnywVH-TGQLH 305
Cdd:cd00814 231 KDGWP----ELVH---------FIGK--DIirfHAiywpamlLGAGLPLPTR--------------------IVaHGYLT 275
                       330       340       350
                ....*....|....*....|....*....|.
gi 19922218 306 MVGdrEKMSKSLGNTISVSELLKKYTADEFR 336
Cdd:cd00814 276 VEG--KKMSKSRGNVVDPDDLLERYGADALR 304
LeuS COG0495
Leucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Leucyl-tRNA ...
307-337 5.77e-05

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


Pssm-ID: 440261 [Multi-domain]  Cd Length: 826  Bit Score: 46.20  E-value: 5.77e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 19922218 307 VGDREKMSKSLGNTISVSELLKKYTADEFRM 337
Cdd:COG0495 584 IGGIEKMSKSKGNVVDPDEIIEKYGADTLRL 614
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
76-153 6.29e-05

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 45.64  E-value: 6.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922218   76 PTVYDSAHLGHASTYVKVDILQRILR-DYFKINLVTAmnitdVDD---KIIKRAQLAGLDWQKMARAYEAEFRQDMLRLN 151
Cdd:PRK11893  10 YYPNGKPHIGHAYTTLAADVLARFKRlRGYDVFFLTG-----TDEhgqKIQRKAEEAGISPQELADRNSAAFKRLWEALN 84

                 ..
gi 19922218  152 VQ 153
Cdd:PRK11893  85 IS 86
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
309-337 1.91e-04

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: 43.76  E-value: 1.91e-04
                        10        20
                ....*....|....*....|....*....
gi 19922218 309 DREKMSKSLGNTISVSELLKKYTADEFRM 337
Cdd:cd00818 296 DGRKMSKSLGNYVDPQEVVDKYGADALRL 324
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
311-343 2.24e-04

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: 43.95  E-value: 2.24e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 19922218 311 EKMSKSLGNTISVSELLKKYTADEFRMAcLLSN 343
Cdd:COG0143 326 EKMSKSRGNVIDPDDLLDRYGPDALRYY-LLRE 357
ValRS_core cd00817
catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) ...
294-346 3.18e-04

catalytic core domain of valyl-tRNA synthetases; Valine amino-acyl tRNA synthetase (ValRS) catalytic core domain. This 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. ValRS 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: 185677 [Multi-domain]  Cd Length: 382  Bit Score: 43.39  E-value: 3.18e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922218 294 WVNYWV-----HTGQ-------LH-MV--GDREKMSKSLGNTISVSELLKKYTADEFRMAclLSNYRN 346
Cdd:cd00817 310 WVARMImrglkLTGKlpfkevyLHgLVrdEDGRKMSKSLGNVIDPLDVIDGYGADALRFT--LASAAT 375
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
308-351 9.24e-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: 42.01  E-value: 9.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 19922218   308 GDREKMSKSLGNTISVSELLKKYTADEFRMACLLSNYRNAMPYS 351
Cdd:pfam00133 559 EQGRKMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
DALR_2 smart00840
This DALR domain is found in cysteinyl-tRNA-synthetases;
400-454 1.41e-03

This DALR domain is found in cysteinyl-tRNA-synthetases;


Pssm-ID: 214848 [Multi-domain]  Cd Length: 56  Bit Score: 37.16  E-value: 1.41e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 19922218    400 EFDNCLRDDFDTARAISVLIDqmssISRCINEQQVDAQ--EEPAYCIDLLLAAGNFI 454
Cdd:smart00840   1 RFEEAMDDDFNTPEALAVLFE----LAREINRLALKATdaEELAALAALLRALGGVL 53
 
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.
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