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Conserved domains on  [gi|6323011|ref|NP_013083|]
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aspartate--tRNA ligase DPS1 [Saccharomyces cerevisiae S288C]

Protein Classification

aspartate--tRNA ligase( domain architecture ID 1005012)

aspartate--tRNA ligase attaches aspartate to the 3' OH group of ribose of tRNA(Asp)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02850 super family cl33579
aspartate-tRNA ligase
19-557 0e+00

aspartate-tRNA ligase


The actual alignment was detected with superfamily member PLN02850:

Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 691.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    19 QVILGEDGKPLSKKALKKLQKEQEKQRKKEERalqleaeREAREKKAAAEDTAKDNYGKLPLIQSRdSDRTGQKRVKFVD 98
Cdd:PLN02850   3 QEAVEESGEKISKKAAKKAAAKAEKLRREATA-------KAAAASLEDEDDPLASNYGDVPLEELQ-SKVTGREWTDVSD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    99 LDEAKDsDKEVLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKAnKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEP 178
Cdd:PLN02850  75 LGEELA-GSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFV-SEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   179 IKSATvQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAG-----LPVVNLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:PLN02850 152 VKGTT-QQVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALqtgeqLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQ 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHR 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   334 HMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFK-LPkdgKMVRLTYKEGIEMLRAA 412
Cdd:PLN02850 311 HLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKyLP---KTLRLTFAEGIQMLKEA 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   413 GKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:PLN02850 388 GVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELL 467
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011   493 QERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:PLN02850 468 EKRAEECGIDVKT--ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
 
Name Accession Description Interval E-value
PLN02850 PLN02850
aspartate-tRNA ligase
19-557 0e+00

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 691.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    19 QVILGEDGKPLSKKALKKLQKEQEKQRKKEERalqleaeREAREKKAAAEDTAKDNYGKLPLIQSRdSDRTGQKRVKFVD 98
Cdd:PLN02850   3 QEAVEESGEKISKKAAKKAAAKAEKLRREATA-------KAAAASLEDEDDPLASNYGDVPLEELQ-SKVTGREWTDVSD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    99 LDEAKDsDKEVLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKAnKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEP 178
Cdd:PLN02850  75 LGEELA-GSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFV-SEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   179 IKSATvQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAG-----LPVVNLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:PLN02850 152 VKGTT-QQVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALqtgeqLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQ 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHR 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   334 HMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFK-LPkdgKMVRLTYKEGIEMLRAA 412
Cdd:PLN02850 311 HLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKyLP---KTLRLTFAEGIQMLKEA 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   413 GKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:PLN02850 388 GVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELL 467
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011   493 QERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:PLN02850 468 EKRAEECGIDVKT--ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
aspS_nondisc TIGR00458
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ...
94-557 0e+00

nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273087 [Multi-domain]  Cd Length: 428  Bit Score: 664.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011     94 VKFVDLDEAKDSdKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKegtISKNMVKWAGSLNLESIVLVRGIVK 173
Cdd:TIGR00458   1 VYSADIKPEMDG-QEVTFMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAKK---VSKNLFKWAKKLNLESVVAVRGIVK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    174 kvdepIKSATVQNLEIHITKIYTISETPEALPILLEDasRSEAEaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:TIGR00458  76 -----IKEKAPGGFEIIPTKIEVINEAKEPLPLDPTE--KVPAE----------LDTRLDYRFLDLRRPTVQAIFRIRSG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:TIGR00458 139 VLESVREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHR 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    334 HMTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELPKRFAHeielvrkQYPVEEFKLPK-DGKMVRLTYKEGIEMLRAA 412
Cdd:TIGR00458 219 HLNEATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAH-------QLETLEFKLEKpEGKFVRLTYDEAIEMANAK 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    413 GKEIGDFEDLSTENEKFLGklvrDKYDTDFYILDkFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:TIGR00458 291 GVEIGWGEDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLL 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011    493 QERMKAHGLSPEdpGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:TIGR00458 366 VERIKAKGLNPE--GFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
226-553 3.67e-171

Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238399 [Multi-domain]  Cd Length: 322  Bit Score: 487.07  E-value: 3.67e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  226 VNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFN 305
Cdd:cd00776   2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  306 KQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVrKQYP 385
Cdd:cd00776  82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQLN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  386 VEEFKLPKdgKMVRLTYKEGIEMLRAAGK--EIGDFEDLSTENEKFLGKLVRdkydTDFYILDKFPLEIRPFYTMPDPAN 463
Cdd:cd00776 160 RELLKPLE--PFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDN 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  464 PKYSNSYDFFMRG-EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNI 542
Cdd:cd00776 234 PETVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPES--FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNI 311
                       330
                ....*....|.
gi 6323011  543 RRASLFPRDPK 553
Cdd:cd00776 312 REAILFPRDPK 322
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
92-557 5.63e-151

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


Pssm-ID: 439788 [Multi-domain]  Cd Length: 430  Bit Score: 439.87  E-value: 5.63e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   92 KRVKFVDLDEAKDsDKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGTISKnmvkwAGSLNLESIVLVRGI 171
Cdd:COG0017   1 KRTYIKDLLPEHV-GQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEE-----AKKLTTESSVEVTGT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  172 VKKvdEPIKSatvQNLEIHITKIYTISETPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQ 251
Cdd:COG0017  74 VVE--SPRAP---QGVELQAEEIEVLGEADEPYPLQPKRHS---------------LEFLLDNRHLRLRTNRFGAIFRIR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  252 AGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNT 331
Cdd:COG0017 134 SELARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNT 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  332 HRHMTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELPKRFAHEIELvrkqYPVEEFKLPK--DGKMVRLTYKEGIEML 409
Cdd:COG0017 213 RRHLAEFWMIEPEMAFADL-EDVMDLAEEMLKYIIKYVLENCPEELEF----LGRDVERLEKvpESPFPRITYTEAIEIL 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  410 RAAGKEIGDFEDLSTENEKFLGklvrDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRG-EEILSGAQRIHD 488
Cdd:COG0017 288 KKSGEKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHR 363
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323011  489 HALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:COG0017 364 YDVLVERIKEKGLDPED--YEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
227-552 1.79e-97

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 298.71  E-value: 1.79e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    227 NLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEV------TYFkgkaYLAQ 300
Cdd:pfam00152   1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    301 SPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELpkrfaHEIELV 380
Cdd:pfam00152  77 SPQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEV-----EGIAKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    381 RKQYPVEEFKLPkdgkMVRLTYKEGIEMLRAAGKEIGDFeDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPD 460
Cdd:pfam00152 150 LEGGTLLDLKKP----FPRITYAEAIEKLNGKDVEELGY-GSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    461 PANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKD--YCDGFSYGCPPHAGGGIGLERVVMFYLD 538
Cdd:pfam00152 225 EDDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEKFgfYLDALKYGAPPHGGLGIGLDRLVMLLTG 304
                         330
                  ....*....|....
gi 6323011    539 LKNIRRASLFPRDP 552
Cdd:pfam00152 305 LESIREVIAFPKTR 318
 
Name Accession Description Interval E-value
PLN02850 PLN02850
aspartate-tRNA ligase
19-557 0e+00

aspartate-tRNA ligase


Pssm-ID: 215456 [Multi-domain]  Cd Length: 530  Bit Score: 691.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    19 QVILGEDGKPLSKKALKKLQKEQEKQRKKEERalqleaeREAREKKAAAEDTAKDNYGKLPLIQSRdSDRTGQKRVKFVD 98
Cdd:PLN02850   3 QEAVEESGEKISKKAAKKAAAKAEKLRREATA-------KAAAASLEDEDDPLASNYGDVPLEELQ-SKVTGREWTDVSD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    99 LDEAKDsDKEVLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKAnKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEP 178
Cdd:PLN02850  75 LGEELA-GSEVLIRGRVHTIRGKG-KSAFLVLRQSGFTVQCVVFV-SEVTVSKGMVKYAKQLSRESVVDVEGVVSVPKKP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   179 IKSATvQNLEIHITKIYTISETPEALPILLEDASRSEAEAEAAG-----LPVVNLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:PLN02850 152 VKGTT-QQVEIQVRKIYCVSKALATLPFNVEDAARSESEIEKALqtgeqLVRVGQDTRLNNRVLDLRTPANQAIFRIQSQ 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:PLN02850 231 VCNLFREFLLSKGFVEIHTPKLIAGASEGGSAVFRLDYKGQPACLAQSPQLHKQMAICGDFRRVFEIGPVFRAEDSFTHR 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   334 HMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFK-LPkdgKMVRLTYKEGIEMLRAA 412
Cdd:PLN02850 311 HLCEFTGLDLEMEIKEHYSEVLDVVDELFVAIFDGLNERCKKELEAIREQYPFEPLKyLP---KTLRLTFAEGIQMLKEA 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   413 GKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:PLN02850 388 GVEVDPLGDLNTESERKLGQLVKEKYGTDFYILHRYPLAVRPFYTMPCPDDPKYSNSFDVFIRGEEIISGAQRVHDPELL 467
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011   493 QERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:PLN02850 468 EKRAEECGIDVKT--ISTYIDSFRYGAPPHGGFGVGLERVVMLFCGLNNIRKTSLFPRDPQRLAP 530
aspS_nondisc TIGR00458
nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative ...
94-557 0e+00

nondiscriminating aspartyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, aspS_arch, represents aspartyl-tRNA synthetases from the eukaryotic cytosol and from the Archaea. In some species, this enzyme aminoacylates tRNA for both Asp and Asn; Asp-tRNA(asn) is subsequently transamidated to Asn-tRNA(asn). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273087 [Multi-domain]  Cd Length: 428  Bit Score: 664.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011     94 VKFVDLDEAKDSdKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKegtISKNMVKWAGSLNLESIVLVRGIVK 173
Cdd:TIGR00458   1 VYSADIKPEMDG-QEVTFMGWVHEIRDLGG-LIFVLLRDREGLIQITAPAKK---VSKNLFKWAKKLNLESVVAVRGIVK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    174 kvdepIKSATVQNLEIHITKIYTISETPEALPILLEDasRSEAEaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQAG 253
Cdd:TIGR00458  76 -----IKEKAPGGFEIIPTKIEVINEAKEPLPLDPTE--KVPAE----------LDTRLDYRFLDLRRPTVQAIFRIRSG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    254 VCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:TIGR00458 139 VLESVREFLAEEGFIEVHTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQQLMAAGFERVYEIGPIFRAEEHNTHR 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    334 HMTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELPKRFAHeielvrkQYPVEEFKLPK-DGKMVRLTYKEGIEMLRAA 412
Cdd:TIGR00458 219 HLNEATSIDIEMAFEDH-HDVMDILEELVVRVFEDVPERCAH-------QLETLEFKLEKpEGKFVRLTYDEAIEMANAK 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    413 GKEIGDFEDLSTENEKFLGklvrDKYDTDFYILDkFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHALL 492
Cdd:TIGR00458 291 GVEIGWGEDLSTEAEKALG----EEMDGLYFITD-WPTEIRPFYTMPDEDNPEISKSFDLMYRDLEISSGAQRIHLHDLL 365
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323011    493 QERMKAHGLSPEdpGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:TIGR00458 366 VERIKAKGLNPE--GFKDYLEAFSYGMPPHAGWGLGAERFVMFLLGLKNIREAVLFPRDRKRLTP 428
AsxRS_core cd00776
Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA ...
226-553 3.67e-171

Asx tRNA synthetase (AspRS/AsnRS) class II core domain. Assignment to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs in the core domain. This family includes AsnRS as well as a subgroup of AspRS. AsnRS and AspRS are homodimers, which attach either asparagine or aspartate to the 3'OH group of ribose of the appropriate tRNA. While archaea lack asnRS, they possess a non-discriminating aspRS, which can mischarge Asp-tRNA with Asn. Subsequently, a tRNA-dependent aspartate amidotransferase converts the bound aspartate to asparagine. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238399 [Multi-domain]  Cd Length: 322  Bit Score: 487.07  E-value: 3.67e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  226 VNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFN 305
Cdd:cd00776   2 ANLETLLDNRHLDLRTPKVQAIFRIRSEVLRAFREFLRENGFTEVHTPKITSTDTEGGAELFKVSYFGKPAYLAQSPQLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  306 KQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVrKQYP 385
Cdd:cd00776  82 KEMLIAA-LERVYEIGPVFRAEKSNTRRHLSEFWMLEAEMAFIEDYNEVMDLIEELIKYIFKRVLERCAKELELV-NQLN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  386 VEEFKLPKdgKMVRLTYKEGIEMLRAAGK--EIGDFEDLSTENEKFLGKLVRdkydTDFYILDKFPLEIRPFYTMPDPAN 463
Cdd:cd00776 160 RELLKPLE--PFPRITYDEAIELLREKGVeeEVKWGEDLSTEHERLLGEIVK----GDPVFVTDYPKEIKPFYMKPDDDN 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  464 PKYSNSYDFFMRG-EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNI 542
Cdd:cd00776 234 PETVESFDLLMPGvGEIVGGSQRIHDYDELEERIKEHGLDPES--FEWYLDLRKYGMPPHGGFGLGLERLVMWLLGLDNI 311
                       330
                ....*....|.
gi 6323011  543 RRASLFPRDPK 553
Cdd:cd00776 312 REAILFPRDPK 322
PTZ00401 PTZ00401
aspartyl-tRNA synthetase; Provisional
30-557 2.61e-170

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 173592 [Multi-domain]  Cd Length: 550  Bit Score: 493.74  E-value: 2.61e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    30 SKKALKKLQKEQEKQRKKEERALQLEAEREAR-EKKAAAEDTAKDNYGKLPLIQSrdSDRTGQKRVKFVDLDEAKDSDKE 108
Cdd:PTZ00401   3 SNHADAGAPAVEKKQSDKEARKAARLAEEKARaAEKAALVEKYKDVFGAAPMVQS--TTYKSRTFIPVAVLSKPELVDKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   109 VLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKAnkEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLE 188
Cdd:PTZ00401  81 VLIRARVSTTRKKG-KMAFMVLRDGSDSVQAMAAV--EGDVPKEMIDFIGQIPTESIVDVEATVCKVEQPITSTSHSDIE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   189 IHITKIYTISETPEALPILLEDASRSEAEAEAAglpvVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFT 268
Cdd:PTZ00401 158 LKVKKIHTVTESLRTLPFTLEDASRKESDEGAK----VNFDTRLNSRWMDLRTPASGAIFRLQSRVCQYFRQFLIDSDFC 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   269 EVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFE 348
Cdd:PTZ00401 234 EIHSPKIINAPSEGGANVFKLEYFNRFAYLAQSPQLYKQMVLQGDVPRVFEVGPVFRSENSNTHRHLTEFVGLDVEMRIN 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   349 EHYHEVLDTLSELFVFIFSELPKRFAhEIELVRKQYP--------------------VEEFKLPKD----------GKMV 398
Cdd:PTZ00401 314 EHYYEVLDLAESLFNYIFERLATHTK-ELKAVCQQYPfeplvwkltpermkelgvgvISEGVEPTDkyqarvhnmdSRML 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   399 RLTYKEGIEMLRAAGKE-IGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGE 477
Cdd:PTZ00401 393 RINYMHCIELLNTVLEEkMAPTDDINTTNEKLLGKLVKERYGTDFFISDRFPSSARPFYTMECKDDERFTNSYDMFIRGE 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   478 EILSGAQRIHDHALLQERMKAHG--LSPedpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRL 555
Cdd:PTZ00401 473 EISSGAQRIHDPDLLLARAKMLNvdLTP----IKEYVDSFRLGAWPHGGFGVGLERVVMLYLGLSNVRLASLFPRDPQRT 548

                 ..
gi 6323011   556 RP 557
Cdd:PTZ00401 549 TP 550
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
92-557 5.63e-151

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


Pssm-ID: 439788 [Multi-domain]  Cd Length: 430  Bit Score: 439.87  E-value: 5.63e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   92 KRVKFVDLDEAKDsDKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGTISKnmvkwAGSLNLESIVLVRGI 171
Cdd:COG0017   1 KRTYIKDLLPEHV-GQEVTVAGWVRTKRDSGG-ISFLILRDGSGFIQVVVKKDKLENFEE-----AKKLTTESSVEVTGT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  172 VKKvdEPIKSatvQNLEIHITKIYTISETPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQ 251
Cdd:COG0017  74 VVE--SPRAP---QGVELQAEEIEVLGEADEPYPLQPKRHS---------------LEFLLDNRHLRLRTNRFGAIFRIR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  252 AGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNT 331
Cdd:COG0017 134 SELARAIREFFQERGFVEVHTPIITASATEGGGELFPVDYFGKEAYLTQSGQLYKEALAMA-LEKVYTFGPTFRAEKSNT 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  332 HRHMTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELPKRFAHEIELvrkqYPVEEFKLPK--DGKMVRLTYKEGIEML 409
Cdd:COG0017 213 RRHLAEFWMIEPEMAFADL-EDVMDLAEEMLKYIIKYVLENCPEELEF----LGRDVERLEKvpESPFPRITYTEAIEIL 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  410 RAAGKEIGDFEDLSTENEKFLGklvrDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRG-EEILSGAQRIHD 488
Cdd:COG0017 288 KKSGEKVEWGDDLGTEHERYLG----EEFFKKPVFVTDYPKEIKAFYMKPNPDDPKTVAAFDLLAPGiGEIIGGSQREHR 363
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323011  489 HALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:COG0017 364 YDVLVERIKEKGLDPED--YEWYLDLRRYGSVPHAGFGLGLERLVMWLTGLENIREVIPFPRDPGRLTP 430
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
91-557 7.90e-151

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 439.63  E-value: 7.90e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    91 QKRVKFVDLDEAKDSdKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKegtiSKNMVKWAGSLNLESIVLVRG 170
Cdd:PRK05159   2 MKRHLTSELTPELDG-EEVTLAGWVHEIRDLGG-IAFLILRDRSGIIQVVVKKKV----DEELFETIKKLKRESVVSVTG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   171 IVKKVDepiKSATvqNLEIHITKIYTISETPEALPilLEDASRSEAEaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRI 250
Cdd:PRK05159  76 TVKANP---KAPG--GVEVIPEEIEVLNKAEEPLP--LDISGKVLAE----------LDTRLDNRFLDLRRPRVRAIFKI 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   251 QAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSN 330
Cdd:PRK05159 139 RSEVLRAFREFLYENGFTEIFTPKIVASGTEGGAELFPIDYFEKEAYLAQSPQLYKQMMVGAGFERVFEIGPVFRAEEHN 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   331 THRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEFKLPkdgkmvRLTYKEGIEMLR 410
Cdd:PRK05159 219 TSRHLNEYTSIDVEMGFIDDHEDVMDLLENLLRYMYEDVAENCEKELELLGIELPVPETPIP------RITYDEAIEILK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   411 AAGKEIGDFEDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHA 490
Cdd:PRK05159 293 SKGNEISWGDDLDTEGERLLGEYVKEEYGSDFYFITDYPSEKRPFYTMPDEDDPEISKSFDLLFRGLEITSGGQRIHRYD 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323011   491 LLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKRLRP 557
Cdd:PRK05159 373 MLVESIKEKGLNPES--FEFYLEAFKYGMPPHGGFGLGLERLTMKLLGLENIREAVLFPRDRHRLTP 437
tRNA-synt_2 pfam00152
tRNA synthetases class II (D, K and N);
227-552 1.79e-97

tRNA synthetases class II (D, K and N);


Pssm-ID: 425487 [Multi-domain]  Cd Length: 318  Bit Score: 298.71  E-value: 1.79e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    227 NLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEV------TYFkgkaYLAQ 300
Cdd:pfam00152   1 DEETRLKYRYLDLRRPKMQANLKLRSKIIKAIRNFLDENGFLEVETPILTKSATPEGARDFLVpsralgKFY----ALPQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    301 SPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELpkrfaHEIELV 380
Cdd:pfam00152  77 SPQLYKQLLMVAGFDRVFQIARCFRDEDLRTDRQP-EFTQLDLEMSFVD-YEDVMDLTEELIKEIFKEV-----EGIAKE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    381 RKQYPVEEFKLPkdgkMVRLTYKEGIEMLRAAGKEIGDFeDLSTENEKFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPD 460
Cdd:pfam00152 150 LEGGTLLDLKKP----FPRITYAEAIEKLNGKDVEELGY-GSDKPDLRFLLELVIDKNKFNPLWVTDFPAEHHPFTMPKD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    461 PANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKD--YCDGFSYGCPPHAGGGIGLERVVMFYLD 538
Cdd:pfam00152 225 EDDPALAEAFDLVLNGVEIGGGSIRIHDPELQEERFEEQGLDPEEAEEKFgfYLDALKYGAPPHGGLGIGLDRLVMLLTG 304
                         330
                  ....*....|....
gi 6323011    539 LKNIRRASLFPRDP 552
Cdd:pfam00152 305 LESIREVIAFPKTR 318
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
92-557 2.23e-75

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 245.79  E-value: 2.23e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    92 KRVKFVDLDEAKDSDKEVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGTISKNmvkwAGSLNLESIVLVRGI 171
Cdd:PRK03932   2 MRVSIKDILKGKYVGQEVTVRGWVRTKRDSGK-IAFLQLRDGSCFKQLQVVKDNGEEYFEE----IKKLTTGSSVIVTGT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   172 VKKvdEPIKSatvQNLEIHITKIYTISETPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFRIQ 251
Cdd:PRK03932  77 VVE--SPRAG---QGYELQATKIEVIGEDPEDYPIQKKRHS---------------IEFLREIAHLRPRTNKFGAVMRIR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   252 AGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVT---------YFKGKAYLAQSPQFNKQQLIVAdFERVYEIGP 322
Cdd:PRK03932 137 NTLAQAIHEFFNENGFVWVDTPIITASDCEGAGELFRVTtldldfskdFFGKEAYLTVSGQLYAEAYAMA-LGKVYTFGP 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   323 VFRAENSNTHRHMTEFTGLDMEMAFEEHYhEVLDtLSELFV-FIFSELPKRFAHEIELVRKQYP---VEEFKLPKDGKMV 398
Cdd:PRK03932 216 TFRAENSNTRRHLAEFWMIEPEMAFADLE-DNMD-LAEEMLkYVVKYVLENCPDDLEFLNRRVDkgdIERLENFIESPFP 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   399 RLTYKEGIEMLRAAGKeigDFE-------DLSTENEKFLGKLVrdkYDTDFYILDkFPLEIRPFYTMPDPAN-------- 463
Cdd:PRK03932 294 RITYTEAIEILQKSGK---KFEfpvewgdDLGSEHERYLAEEH---FKKPVFVTN-YPKDIKAFYMRLNPDGktvaamdl 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   464 --PKYsnsydffmrGeEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKN 541
Cdd:PRK03932 367 laPGI---------G-EIIGGSQREERLDVLEARIKELGLNKED--YWWYLDLRRYGSVPHSGFGLGFERLVAYITGLDN 434
                        490
                 ....*....|....*.
gi 6323011   542 IRRASLFPRDPKRLRP 557
Cdd:PRK03932 435 IRDVIPFPRTPGRAEF 450
asnS TIGR00457
asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative ...
93-557 1.99e-66

asparaginyl-tRNA synthetase; In a multiple sequence alignment of representative asparaginyl-tRNA synthetases (asnS), archaeal/eukaryotic type aspartyl-tRNA synthetases (aspS_arch), and bacterial type aspartyl-tRNA synthetases (aspS_bact), there is a striking similarity between asnS and aspS_arch in gap pattern and in sequence, and a striking divergence of aspS_bact. Consequently, a separate model was built for each of the three groups. This model, asnS, represents asparaginyl-tRNA synthetases from the three domains of life. Some species lack this enzyme and charge tRNA(asn) by misacylation with Asp, followed by transamidation of Asp to Asn. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273086 [Multi-domain]  Cd Length: 453  Bit Score: 222.64  E-value: 1.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011     93 RVKFVDLDEAKDSDKEVLFRARVHNTRQQgATLAFLTLRQQASL--IQGLVKankeGTISKNMVKWAGSLNLESIVLVRG 170
Cdd:TIGR00457   3 AIKDLLQQVYKFVGDEVTVSGWVRTKRSS-KKIIFLELNDGSSLgpIQAVIN----GEDNPYLFQLLKSLTTGSSVSVTG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    171 IVKKvdEPIKSatvQNLEIHITKIYTISE-TPEALPILLEDASrseaeaeaaglpvvnLDTRLDYRVIDLRTVTNQAIFR 249
Cdd:TIGR00457  78 KVVE--SPGKG---QPVELQVKKIEVVGEaEPDDYPLQKKEHS---------------LEFLRDIAHLRLRTNTLGAVMR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    250 IQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVT---------YFKGKAYLAQSPQFNKQQLIVAdFERVYEI 320
Cdd:TIGR00457 138 VRNALSQAIHRYFQENGFTWVSPPILTSNDCEGAGELFRVStgnidfsqdFFGKEAYLTVSGQLYLETYALA-LSKVYTF 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    321 GPVFRAENSNTHRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPVEEF-KLPKD--GKM 397
Cdd:TIGR00457 217 GPTFRAEKSNTSRHLSEFWMIEPEMAFAN-LNDLLQLAETLIKYIIKAVLENCSQELKFLEKNFDKDLIkRLENIinNKF 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    398 VRLTYKEGIEMLRAAGK--EIGDF--EDLSTENEKFLGklvrDKYDTDFYILDKFPLEIRPFYtMPDPANPKYSNSYDFF 473
Cdd:TIGR00457 296 ARITYTDAIEILKESDKnfEYEDFwgDDLQTEHERFLA----EEYFKPPVFVTNYPKDIKAFY-MKLNDDGKTVAAMDLL 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    474 MRG-EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDP 552
Cdd:TIGR00457 371 APGiGEIIGGSEREDDLDKLENRMKEMGLDTDA--LNWYLDLRKYGSVPHSGFGLGFERLLAYITGLENIRDAIPFPRTP 448

                  ....*
gi 6323011    553 KRLRP 557
Cdd:TIGR00457 449 GNINF 453
Asp_Lys_Asn_RS_core cd00669
Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of ...
248-551 3.97e-60

Asp_Lys_Asn_tRNA synthetase class II core domain. This domain is the core catalytic domain of class II aminoacyl-tRNA synthetases of the subgroup containing aspartyl, lysyl, and asparaginyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. Nearly all class II tRNA synthetases are dimers and enzymes in this subgroup are homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.


Pssm-ID: 238358 [Multi-domain]  Cd Length: 269  Bit Score: 200.01  E-value: 3.97e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  248 FRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYF-KGK-AYLAQSPQFNKQQLIVADFERVYEIGPVFR 325
Cdd:cd00669   1 FKVRSKIIKAIRDFMDDRGFLEVETPMLQKITGGAGARPFLVKYNaLGLdYYLRISPQLFKKRLMVGGLDRVFEINRNFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  326 AEnSNTHRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELPKRFAHEIELVrkqypVEEFKLPkdgkMVRLTYKEG 405
Cdd:cd00669  81 NE-DLRARHQPEFTMMDLEMAFAD-YEDVIELTERLVRHLAREVLGVTAVTYGFE-----LEDFGLP----FPRLTYREA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  406 IEMLRAagkeigdfedlstenekflgklvrdkydtdFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQR 485
Cdd:cd00669 150 LERYGQ------------------------------PLFLTDYPAEMHSPLASPHDVNPEIADAFDLFINGVEVGNGSSR 199
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323011  486 IHDHALLQERMKAHGLSPEDPGLK--DYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRD 551
Cdd:cd00669 200 LHDPDIQAEVFQEQGINKEAGMEYfeFYLKALEYGLPPHGGLGIGIDRLIMLMTNSPTIREVIAFPKM 267
AspRS_cyto_N cd04320
AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
108-210 3.38e-48

AspRS_cyto_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae and human cytoplasmic aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis.


Pssm-ID: 239815 [Multi-domain]  Cd Length: 102  Bit Score: 162.73  E-value: 3.38e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  108 EVLFRARVHNTRQQGATLAFLTLRQQASLIQGLVKANKEGtISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL 187
Cdd:cd04320   1 EVLIRARVHTSRAQGAKLAFLVLRQQGYTIQGVLAASAEG-VSKQMVKWAGSLSKESIVDVEGTVKKPEEPIKSCTQQDV 79
                        90       100
                ....*....|....*....|...
gi 6323011  188 EIHITKIYTISETPEALPILLED 210
Cdd:cd04320  80 ELHIEKIYVVSEAAEPLPFQLED 102
PRK06462 PRK06462
asparagine synthetase A; Reviewed
247-552 5.22e-47

asparagine synthetase A; Reviewed


Pssm-ID: 235808 [Multi-domain]  Cd Length: 335  Bit Score: 167.50  E-value: 5.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   247 IFRIQAGVCELFREYLATKKFTEVHTP-------KLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQqLIVADFERVYE 319
Cdd:PRK06462  29 VLKVQSSILRYTREFLDGRGFVEVLPPiispstdPLMGLGSDLPVKQISIDFYGVEYYLADSMILHKQ-LALRMLGKIFY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   320 IGPVFRAEN--SNTHRHMTEFTGLDMEMAfEEHYHEVLDTLSELFVFIFSELPKRFAHEIELVRKQYPveEFKLPKDgkm 397
Cdd:PRK06462 108 LSPNFRLEPvdKDTGRHLYEFTQLDIEIE-GADLDEVMDLIEDLIKYLVKELLEEHEDELEFFGRDLP--HLKRPFK--- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   398 vRLTYKEGIEMLRAAGKEIGDFEDLSTENEKFLGKlvrdKYDTDFYILDkFPLEIRPFYTMPDPANPKYSNSYDFFMRG- 476
Cdd:PRK06462 182 -RITHKEAVEILNEEGCRGIDLEELGSEGEKSLSE----HFEEPFWIID-IPKGSREFYDREDPERPGVLRNYDLLLPEg 255
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323011   477 -EEILSGAQRIHDHALLQERMKAHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDP 552
Cdd:PRK06462 256 yGEAVSGGEREYEYEEIVERIREHGVDPEK--YKWYLEMAKEGPLPSAGFGIGVERLTRYICGLRHIREVQPFPRVP 330
AspRS_core cd00777
Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its ...
257-549 5.50e-34

Asp tRNA synthetase (aspRS) class II core domain. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. AspRS is a homodimer, which attaches a specific amino acid to the 3' OH group of ribose of the appropriate tRNA. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. AspRS in this family differ from those found in the AsxRS family by a GAD insert in the core domain.


Pssm-ID: 238400 [Multi-domain]  Cd Length: 280  Bit Score: 130.00  E-value: 5.50e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  257 LFREYLATKKFTEVHTPkLLGAPSEGGSSVFEVTY--FKGKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHR 333
Cdd:cd00777  10 AIRNFLDEQGFVEIETP-ILTKSTPEGARDFLVPSrlHPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  334 HmTEFTGLDMEMAFEEHyHEVLDTLSELFVFIFSELpkrFAHEIELvrkqypveefKLPkdgkmvRLTYKEGIEMLRAAG 413
Cdd:cd00777  89 Q-PEFTQIDIEMSFVDQ-EDIMSLIEGLLKYVFKEV---LGVELTT----------PFP------RMTYAEAMERYGFKF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  414 KEIGDFEDLSTENEKflGKLV---------RDKYDTDfyiLDKFPLEIRpfytmpdpanpkySNSYDFFMRGEEILSGAQ 484
Cdd:cd00777 148 LWIVDFPLFEWDEEE--GRLVsahhpftapKEEDLDL---LEKDPEDAR-------------AQAYDLVLNGVELGGGSI 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323011  485 RIHDhALLQERM-KAHGLSPEDPGLKDYC--DGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:cd00777 210 RIHD-PDIQEKVfEILGLSEEEAEEKFGFllEAFKYGAPPHGGIALGLDRLVMLLTGSESIRDVIAFP 276
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
115-549 1.22e-32

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 132.04  E-value: 1.22e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  115 VHNTRQQGAtLAFLTLRQQASLIQglVKANKEgtISKNMVKWAGSLNLESIVLVRGIVKKVDE----P-IKSATVqnlEI 189
Cdd:COG0173  25 VHRRRDHGG-LIFIDLRDRYGITQ--VVFDPD--DSAEAFEKAEKLRSEYVIAVTGKVRARPEgtvnPkLPTGEI---EV 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  190 HITKIYTISETpEALPILLEDASRseaeaeaaglpvVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTE 269
Cdd:COG0173  97 LASELEILNKA-KTPPFQIDDDTD------------VSEELRLKYRYLDLRRPEMQKNLILRHKVTKAIRNYLDENGFLE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  270 VHTPkLLGAPS-EGG------SSVfevtyFKGKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGL 341
Cdd:COG0173 164 IETP-ILTKSTpEGArdylvpSRV-----HPGKFYaLPQSPQLFKQLLMVSGFDRYFQIARCFRDEDLRADRQP-EFTQL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  342 DMEMAF--EEhyhEVLDTLSELFVFIFSE-----LPK---------------------RFAHEI----ELVRKqypvEEF 389
Cdd:COG0173 237 DIEMSFvdQE---DVFELMEGLIRHLFKEvlgveLPTpfprmtyaeamerygsdkpdlRFGLELvdvtDIFKD----SGF 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  390 KL----PKDGKMVR-LTYKEGIEMLRaagKEIGDFEDLS-------------TENE------KFLGKLVR---------- 435
Cdd:COG0173 310 KVfagaAENGGRVKaINVPGGASLSR---KQIDELTEFAkqygakglayikvNEDGlkspiaKFLSEEELaailerlgak 386
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  436 ---------DKYDT--------------DFYILDK----------FPL------EIR------PFyTMPDP-------AN 463
Cdd:COG0173 387 pgdliffvaDKPKVvnkalgalrlklgkELGLIDEdefaflwvvdFPLfeydeeEGRwvamhhPF-TMPKDedldlleTD 465
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  464 PK--YSNSYDFFMRGEEILSGAQRIHDHAlLQERM-KAHGLSPED-----PGLkdyCDGFSYGCPPHAGGGIGLERVVMF 535
Cdd:COG0173 466 PGkvRAKAYDLVLNGYELGGGSIRIHDPE-LQEKVfELLGISEEEaeekfGFL---LEAFKYGAPPHGGIAFGLDRLVML 541
                       570
                ....*....|....
gi 6323011  536 YLDLKNIRRASLFP 549
Cdd:COG0173 542 LAGEDSIRDVIAFP 555
aspS PRK00476
aspartyl-tRNA synthetase; Validated
115-549 1.43e-32

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 131.73  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   115 VHNTRQQGAtLAFLTLRQQASLIQGLVKANKEgtisknMVKWAGSLNLESIVLVRGIVKKVDEP-----IKSATVqnlEI 189
Cdd:PRK00476  26 VHRRRDHGG-LIFIDLRDREGIVQVVFDPDAE------AFEVAESLRSEYVIQVTGTVRARPEGtvnpnLPTGEI---EV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   190 HITKIYTISEtPEALPILLEDAsrseaeaeaaglPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREYLATKKFTE 269
Cdd:PRK00476  96 LASELEVLNK-SKTLPFPIDDE------------EDVSEELRLKYRYLDLRRPEMQKNLKLRSKVTSAIRNFLDDNGFLE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   270 VHTPkLLGAPS-EGG------SSVfevtyFKGKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHMtEFTGL 341
Cdd:PRK00476 163 IETP-ILTKSTpEGArdylvpSRV-----HPGKFYaLPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQP-EFTQI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   342 DMEMAF--EEhyhEVLDTLSELFVFIFSE-----LPK---------------------RFAHEI----ELVRKqypvEEF 389
Cdd:PRK00476 236 DIEMSFvtQE---DVMALMEGLIRHVFKEvlgvdLPTpfprmtyaeamrrygsdkpdlRFGLELvdvtDLFKD----SGF 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   390 KL----PKDGKMVRltykeGIEMLRAAG----KEIGDFEDLSTENE-------------------KFLGK---------- 432
Cdd:PRK00476 309 KVfagaANDGGRVK-----AIRVPGGAAqlsrKQIDELTEFAKIYGakglayikvnedglkgpiaKFLSEeelaallert 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   433 ---------LVRDKYDT--------------DFYILDK----------FPL------EIR------PFyTMPDP------ 461
Cdd:PRK00476 384 gakdgdlifFGADKAKVvndalgalrlklgkELGLIDEdkfaflwvvdFPMfeydeeEGRwvaahhPF-TMPKDedldel 462
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   462 --ANPK--YSNSYDFFMRGEEILSGAQRIHDHAlLQERM-KAHGLSPEDP-----GLkdyCDGFSYGCPPHAGGGIGLER 531
Cdd:PRK00476 463 etTDPGkaRAYAYDLVLNGYELGGGSIRIHRPE-IQEKVfEILGISEEEAeekfgFL---LDALKYGAPPHGGIAFGLDR 538
                        570
                 ....*....|....*...
gi 6323011   532 VVMFYLDLKNIRRASLFP 549
Cdd:PRK00476 539 LVMLLAGADSIRDVIAFP 556
PLN02603 PLN02603
asparaginyl-tRNA synthetase
47-552 1.27e-30

asparaginyl-tRNA synthetase


Pssm-ID: 178213 [Multi-domain]  Cd Length: 565  Bit Score: 125.86  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    47 KEERALQLEAEREAREKKAAAEDTAKDNYG-KLPLIQSRDSDRTGQ--KRVKFVDLDEAKDSD-----KEVLFRARVHNT 118
Cdd:PLN02603  40 TFHHLAALSGLPRRRRFCAAASASLQSPESaKVEAAKGAFGEAVGEfrKKLRIADVKGGEDEGlarvgKTLNVMGWVRTL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   119 RQQgATLAFLTLRQQASL--IQGLVKANKEGTiskNMVKwAGSLNLESIVLVRGIVKKvdepiKSATVQNLEIHITKIYT 196
Cdd:PLN02603 120 RAQ-SSVTFIEVNDGSCLsnMQCVMTPDAEGY---DQVE-SGLITTGASVLVQGTVVS-----SQGGKQKVELKVSKIVV 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   197 ISETPEALPILLEDASRSEAEAEAAGLPvvnldtrldyrvidlRTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLL 276
Cdd:PLN02603 190 VGKSDPSYPIQKKRVSREFLRTKAHLRP---------------RTNTFGAVARVRNALAYATHKFFQENGFVWVSSPIIT 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   277 GAPSEGGSSVFEVT------------------------------YFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRA 326
Cdd:PLN02603 255 ASDCEGAGEQFCVTtlipnsaenggslvddipktkdglidwsqdFFGKPAFLTVSGQLNGETYATA-LSDVYTFGPTFRA 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   327 ENSNTHRHMTEFTGLDMEMAFEEHYHE--------------VLDTLSELFVFIFSELPKRFAHEI-ELVRKQYpveefkl 391
Cdd:PLN02603 334 ENSNTSRHLAEFWMIEPELAFADLNDDmacataylqyvvkyILENCKEDMEFFNTWIEKGIIDRLsDVVEKNF------- 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   392 pkdgkmVRLTYKEGIEMLRAAGKEigdFE-------DLSTENEKFLGKLVrdkYDTDFYILDKFPLEIRPFYtMPDPANP 464
Cdd:PLN02603 407 ------VQLSYTDAIELLLKAKKK---FEfpvkwglDLQSEHERYITEEA---FGGRPVIIRDYPKEIKAFY-MRENDDG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   465 KYSNSYDFFM-RGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLkdYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIR 543
Cdd:PLN02603 474 KTVAAMDMLVpRVGELIGGSQREERLEYLEARLDELKLNKESYWW--YLDLRRYGSVPHAGFGLGFERLVQFATGIDNIR 551

                 ....*....
gi 6323011   544 RASLFPRDP 552
Cdd:PLN02603 552 DAIPFPRVP 560
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
104-551 9.27e-29

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 121.25  E-value: 9.27e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   104 DSDKEVLFRARVHNTRQQGATLaFLTLRQQASLIQGLVkaNKEGTiSKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSAT 183
Cdd:PRK12820  16 DTGREVCLAGWVDAFRDHGELL-FIHLRDRNGFIQAVF--SPEAA-PADVYELAASLRAEFCVALQGEVQKRLEETENPH 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   184 VQ--NLEIHITKIYTISETpEALPILLEDASRSeAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFREY 261
Cdd:PRK12820  92 IEtgDIEVFVRELSILAAS-EALPFAISDKAMT-AGAGSAGADAVNEDLRLQYRYLDIRRPAMQDHLAKRHRIIKCARDF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   262 LATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAY--LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHmTEFT 339
Cdd:PRK12820 170 LDSRGFLEIETPILTKSTPEGARDYLVPSRIHPKEFyaLPQSPQLFKQLLMIAGFERYFQLARCFRDEDLRPNRQ-PEFT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   340 GLDMEMAF--EEHYHEVLDtlsELFVFIFS----ELPKRF-----AHEIE---------------------LVRKQYPVE 387
Cdd:PRK12820 249 QLDIEASFidEEFIFELIE---ELTARMFAiggiALPRPFprmpyAEAMDttgsdrpdlrfdlkfadatdiFENTRYGIF 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   388 EFKLPKDGKMVRLTYK-------------------------EGIEMLRA-AGKEIGDFEDLSTENEKFLGKLVRDKYDTD 441
Cdd:PRK12820 326 KQILQRGGRIKGINIKgqseklsknvlqneyakeiapsfgaKGMTWMRAeAGGLDSNIVQFFSADEKEALKRRFHAEDGD 405
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   442 FYIL---------------------DK---------FPLEIRPF-----------------YTMP-----DPANPK---- 465
Cdd:PRK12820 406 VIIMiadascaivlsalgqlrlhlaDRlglipegvfHPLWITDFplfeatddggvtsshhpFTAPdredfDPGDIEelld 485
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   466 -YSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDpgLKD----YCDGFSYGCPPHAGGGIGLERVVMFYLDLK 540
Cdd:PRK12820 486 lRSRAYDLVVNGEELGGGSIRINDKDIQLRIFAALGLSEED--IEDkfgfFLRAFDFAAPPHGGIALGLDRVVSMILQTP 563
                        570
                 ....*....|.
gi 6323011   541 NIRRASLFPRD 551
Cdd:PRK12820 564 SIREVIAFPKN 574
PLN02221 PLN02221
asparaginyl-tRNA synthetase
197-554 3.67e-27

asparaginyl-tRNA synthetase


Pssm-ID: 177867 [Multi-domain]  Cd Length: 572  Bit Score: 115.48  E-value: 3.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   197 ISETPEALPILLEDASRSEAEAEAAGLPVVNLDtrldyRVIDLRTVTNQAIFRIQAGVCELfreYLATKKFTEVHTPKLL 276
Cdd:PLN02221 216 INYTERLEQDLIDNPPPTEADVEAARLIVKERG-----EVVAQLKAAKASKEEITAAVAEL---KIAKESLAHIEERSKL 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   277 --GAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEhYHEV 354
Cdd:PLN02221 288 kpGLPKKDGKIDYSKDFFGRQAFLTVSGQLQVETYACA-LSSVYTFGPTFRAENSHTSRHLAEFWMVEPEIAFAD-LEDD 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   355 LDTLSELFVFIFSELPKRFAHEIELVRKQYP---VEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFE-------DLST 424
Cdd:PLN02221 366 MNCAEAYVKYMCKWLLDKCFDDMELMAKNFDsgcIDRLRMVASTPFGRITYTEAIELLEEAVAKGKEFDnnvewgiDLAS 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   425 ENEKFLGKLVRDKYdtdfYILDKFPLEIRPFYtMPDPANPKYSNSYDFFM-RGEEILSGAQRIHDHALLQERMKAHGLsP 503
Cdd:PLN02221 446 EHERYLTEVLFQKP----LIVYNYPKGIKAFY-MRLNDDEKTVAAMDVLVpKVGELIGGSQREERYDVIKQRIEEMGL-P 519
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6323011   504 EDPgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDPKR 554
Cdd:PLN02221 520 IEP-YEWYLDLRRYGTVKHCGFGLGFERMILFATGIDNIRDVIPFPRYPGK 569
PLN02903 PLN02903
aminoacyl-tRNA ligase
103-550 5.82e-27

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 115.27  E-value: 5.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   103 KDSDKEVLFRARVHNTRQQGAtLAFLTLRQQAsliqGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKK--VDEPIK 180
Cdd:PLN02903  69 NDVGSRVTLCGWVDLHRDMGG-LTFLDVRDHT----GIVQVVTLPDEFPEAHRTANRLRNEYVVAVEGTVRSrpQESPNK 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   181 SATVQNLEIHITKIYTISETPEALPILLEDASRSEaeaeaaglPVVNLDTRLDYRVIDLRTVTNQAIFRIQAGVCELFRE 260
Cdd:PLN02903 144 KMKTGSVEVVAESVDILNVVTKSLPFLVTTADEQK--------DSIKEEVRLRYRVLDLRRPQMNANLRLRHRVVKLIRR 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   261 YLA-TKKFTEVHTPKLLGAPSEGGSSVFEVTYFK-GKAY-LAQSPQFNKQQLIVADFERVYEIGPVFRAENSNTHRHmTE 337
Cdd:PLN02903 216 YLEdVHGFVEIETPILSRSTPEGARDYLVPSRVQpGTFYaLPQSPQLFKQMLMVSGFDRYYQIARCFRDEDLRADRQ-PE 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   338 FTGLDMEMAFEEhYHEVLDTLSELFVFIFSE-----LPK---------------------RFAHEIELVRKQYPVEEFKL 391
Cdd:PLN02903 295 FTQLDMELAFTP-LEDMLKLNEDLIRQVFKEikgvqLPNpfprltyaeamskygsdkpdlRYGLELVDVSDVFAESSFKV 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   392 ----------------PKDGKMVRLTYK----------------------------EGI-------------EMLRAAGK 414
Cdd:PLN02903 374 fagalesggvvkaicvPDGKKISNNTALkkgdiyneaiksgakglaflkvlddgelEGIkalveslspeqaeQLLAACGA 453
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   415 EIGDFEDLSTENEKFLGK-------LVRDKYD------------TDFYILDKFPLEIR------PFyTMPDPANPK-YSN 468
Cdd:PLN02903 454 GPGDLILFAAGPTSSVNKtldrlrqFIAKTLDlidpsrhsilwvTDFPMFEWNEDEQRlealhhPF-TAPNPEDMGdLSS 532
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   469 ----SYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLK-DYC-DGFSYGCPPHAGGGIGLERVVMFYLDLKNI 542
Cdd:PLN02903 533 aralAYDMVYNGVEIGGGSLRIYRRDVQQKVLEAIGLSPEEAESKfGYLlEALDMGAPPHGGIAYGLDRLVMLLAGAKSI 612

                 ....*...
gi 6323011   543 RRASLFPR 550
Cdd:PLN02903 613 RDVIAFPK 620
PRK12445 PRK12445
lysyl-tRNA synthetase; Reviewed
42-549 8.89e-27

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 171504 [Multi-domain]  Cd Length: 505  Bit Score: 114.00  E-value: 8.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    42 EKQRKKEERALQLEAEREAREKKAAAedtAKDNYGKLPLIQSRDSDrTGQKRVKF--VDLDEAKDSDKEVLFRARVHNTR 119
Cdd:PRK12445   3 EQETRGANEAIDFNDELRNRREKLAA---LRQQGVAFPNDFRRDHT-SDQLHEEFdaKDNQELESLNIEVSVAGRMMTRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   120 QQGATlAFLTLRQQASLIQGLVKANK--EGTISKNMVKWagslNLESIVLVRGIVKKVDepiksatVQNLEIHITKIYTI 197
Cdd:PRK12445  79 IMGKA-SFVTLQDVGGRIQLYVARDSlpEGVYNDQFKKW----DLGDIIGARGTLFKTQ-------TGELSIHCTELRLL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   198 SETPEALPILLEDASRSEaeaeaaglpvvnldTRLDYRVIDL-RTVTNQAIFRIQAGVCELFREYLATKKFTEVHTPKLL 276
Cdd:PRK12445 147 TKALRPLPDKFHGLQDQE--------------VRYRQRYLDLiANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQ 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   277 GAPSEGGSSVFeVTYFKG---KAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNThRHMTEFTGLDMEMAFEEhYHE 353
Cdd:PRK12445 213 VIPGGASARPF-ITHHNAldlDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGISV-RHNPEFTMMELYMAYAD-YHD 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   354 VLDTLSELFvfifselpKRFAHEIeLVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRA-----------AGKEIGDFEDL 422
Cdd:PRK12445 290 LIELTESLF--------RTLAQEV-LGTTKVTYGEHVFDFGKPFEKLTMREAIKKYRPetdmadldnfdAAKALAESIGI 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   423 STENEKFLGKLVRDKYD-------TDFYILDKFPLEIRPFYTMPDpANPKYSNSYDFFMRGEEILSGAQRIHDH----AL 491
Cdd:PRK12445 361 TVEKSWGLGRIVTEIFDevaeahlIQPTFITEYPAEVSPLARRND-VNPEITDRFEFFIGGREIGNGFSELNDAedqaER 439
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   492 LQERMKAHGLSPEDPGL--KDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PRK12445 440 FQEQVNAKAAGDDEAMFydEDYVTALEYGLPPTAGLGIGIDRMIMLFTNSHTIRDVILFP 499
PLN02502 PLN02502
lysyl-tRNA synthetase
22-549 2.59e-25

lysyl-tRNA synthetase


Pssm-ID: 215278 [Multi-domain]  Cd Length: 553  Bit Score: 109.70  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    22 LGEDGKPLSKKALKKLQK----EQEKQRKKEERALQLEAEREAREKKAAAEDTA-------KDNygKLPLIQSRDS---- 86
Cdd:PLN02502   1 AESNGEPLSKNALKKRLKakqaEEEKAAKEEAKAAAAAAAAKGRSRKSAAADDEtmdptqyRAN--RLKKVEALRAkgve 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    87 ------DRT---GQKRVKFVDL-DEAKDSDKEVLFRARVHNTRQQGaTLAFLTLRQQASLIQGLVKANKEGTISKNMVKW 156
Cdd:PLN02502  79 pypykfDVThtaPELQEKYGSLeNGEELEDVSVSVAGRIMAKRAFG-KLAFYDLRDDGGKIQLYADKKRLDLDEEEFEKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   157 AGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIHitkiytiseTPEALPilLEDAsrseaeaeAAGLPvvNLDTRLDYRV 236
Cdd:PLN02502 158 HSLVDRGDIVGVTGTPGKTKKGELSIFPTSFEVL---------TKCLLM--LPDK--------YHGLT--DQETRYRQRY 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   237 IDL---RTVTNqaIFRIQAGVCELFREYLATKKFTEVHTPKLLGAPseGGSSV--FeVTYFKG---KAYLAQSPQFNKQQ 308
Cdd:PLN02502 217 LDLianPEVRD--IFRTRAKIISYIRRFLDDRGFLEVETPMLNMIA--GGAAArpF-VTHHNDlnmDLYLRIATELHLKR 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   309 LIVADFERVYEIGPVFRAENSNThRHMTEFTGLDMEMAFEEhYHEVLDTLSELF-----------------VFIFSELPK 371
Cdd:PLN02502 292 LVVGGFERVYEIGRQFRNEGIST-RHNPEFTTCEFYQAYAD-YNDMMELTEEMVsgmvkeltgsykikyhgIEIDFTPPF 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   372 RFAHEIELVRKQYPVeefKLPKDGKMvrltykegiEMLRAAGKEIGDFEDLSTENEKFLGKLVrDKYDTDF--------- 442
Cdd:PLN02502 370 RRISMISLVEEATGI---DFPADLKS---------DEANAYLIAACEKFDVKCPPPQTTGRLL-NELFEEFleetlvqpt 436
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   443 YILDkFPLEIRPFyTMPDPANPKYSNSYDFFMRGEEILSGAQRIHD----HALLQERMKAHGlSPEDPGL---KDYCDGF 515
Cdd:PLN02502 437 FVLD-HPVEMSPL-AKPHRSKPGLTERFELFINGRELANAFSELTDpvdqRERFEEQVKQHN-AGDDEAMaldEDFCTAL 513
                        570       580       590
                 ....*....|....*....|....*....|....
gi 6323011   516 SYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PLN02502 514 EYGLPPTGGWGLGIDRLVMLLTDSASIRDVIAFP 547
LysRS_core cd00775
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ...
248-549 5.24e-24

Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a lysine to the 3' OH group of ribose of the appropriate tRNA. Its assignment to class II aaRS is based upon its structure and the presence of three characteristic sequence motifs in the core domain. It is found in eukaryotes as well as some prokaryotes and archaea. However, LysRS belongs to class I aaRS's in some prokaryotes and archaea. The catalytic core domain is primarily responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate.


Pssm-ID: 238398 [Multi-domain]  Cd Length: 329  Bit Score: 103.05  E-value: 5.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  248 FRIQAGVCELFREYLATKKFTEVHTPKLLGAPseGGSSV--FeVTY---FKGKAYLAQSPQFNKQQLIVADFERVYEIGP 322
Cdd:cd00775   8 FIVRSKIISYIRKFLDDRGFLEVETPMLQPIA--GGAAArpF-ITHhnaLDMDLYLRIAPELYLKRLIVGGFERVYEIGR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  323 VFRAENSNThRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVF----IFSELPKRF-AHEIELVRKqypveeFKlpkdgkm 397
Cdd:cd00775  85 NFRNEGIDL-THNPEFTMIEFYEAYAD-YNDMMDLTEDLFSGlvkkINGKTKIEYgGKELDFTPP------FK------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  398 vRLTYKEGIEmlRAAGKEIGDFEDLSTEN-EKFLGKLVRDKYD---TDFYILDK------------------FPLEIRPF 455
Cdd:cd00775 150 -RVTMVDALK--EKTGIDFPELDLEQPEElAKLLAKLIKEKIEkprTLGKLLDKlfeefveptliqptfiidHPVEISPL 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  456 yTMPDPANPKYSNSYDFFMRGEEILSG----------AQRIhdhaLLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGG 525
Cdd:cd00775 227 -AKRHRSNPGLTERFELFICGKEIANAytelndpfdqRERF----EEQAKQKEAGDDEAMMMDEDFVTALEYGMPPTGGL 301
                       330       340
                ....*....|....*....|....
gi 6323011  526 GIGLERVVMFYLDLKNIRRASLFP 549
Cdd:cd00775 302 GIGIDRLVMLLTDSNSIRDVILFP 325
PTZ00385 PTZ00385
lysyl-tRNA synthetase; Provisional
229-549 2.86e-22

lysyl-tRNA synthetase; Provisional


Pssm-ID: 185588 [Multi-domain]  Cd Length: 659  Bit Score: 100.88  E-value: 2.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   229 DTRLDYRVIDLrtVTNQAIF---RIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFeVTYFKGKA---YLAQSP 302
Cdd:PTZ00385 213 DVKYRYRFTDM--MTNPCVIetiKKRHVMLQALRDYFNERNFVEVETPVLHTVASGANAKSF-VTHHNANAmdlFLRVAP 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   303 QFNKQQLIVADFERVYEIGPVFRAENSNtHRHMTEFTGLDMEMAFeeHYHEVLDTLSElfvFIFSELPKRFAHEIELvrK 382
Cdd:PTZ00385 290 ELHLKQCIVGGMERIYEIGKVFRNEDAD-RSHNPEFTSCEFYAAY--HTYEDLMPMTE---DIFRQLAMRVNGTTVV--Q 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   383 QYPVEEFKLPKD---GKMVRL--TYKegiEMLRAAGKEIGDFEDLSTENEKFLGKLVRDKYD----------------TD 441
Cdd:PTZ00385 362 IYPENAHGNPVTvdlGKPFRRvsVYD---EIQRMSGVEFPPPNELNTPKGIAYMSVVMLRYNiplppvrtaakmfeklID 438
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   442 FYILDKFpleIRPFYTMPDP-----------ANPKYSNSYDFFMRGEEILSGAQRIHD-----HALLQERMKAHGLSPED 505
Cdd:PTZ00385 439 FFITDRV---VEPTFVMDHPlfmsplakeqvSRPGLAERFELFVNGIEYCNAYSELNDpheqyHRFQQQLVDRQGGDEEA 515
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 6323011   506 PGLKD-YCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PTZ00385 516 MPLDEtFLKSLQVGLPPTAGWGMGIDRALMLLTNSSNIRDGIIFP 560
PTZ00425 PTZ00425
asparagine-tRNA ligase; Provisional
291-552 3.70e-20

asparagine-tRNA ligase; Provisional


Pssm-ID: 240414 [Multi-domain]  Cd Length: 586  Bit Score: 93.93  E-value: 3.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   291 YFKGKAYLAQSPQFNKQQLiVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVldTLSELFV-FIFSEL 369
Cdd:PTZ00425 321 FFSKQAFLTVSGQLSLENL-CSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNM--ELAESYIkYCIGYV 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   370 PKRFAHEIELVRKQYP---VEEFKLPKDGKMVRLTYKEGIEMLRAAGKEigdFE-------DLSTENEKFLGKLVRDKYd 439
Cdd:PTZ00425 398 LNNNFDDIYYFEENVEtglISRLKNILDEDFAKITYTNVIDLLQPYSDS---FEvpvkwgmDLQSEHERFVAEQIFKKP- 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   440 tdfYILDKFPLEIRPFYtMPDPANPKYSNSYDFFM-RGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLkdYCDGFSYG 518
Cdd:PTZ00425 474 ---VIVYNYPKDLKAFY-MKLNEDQKTVAAMDVLVpKIGEVIGGSQREDNLERLDKMIKEKKLNMESYWW--YRQLRKFG 547
                        250       260       270
                 ....*....|....*....|....*....|....
gi 6323011   519 CPPHAGGGIGLERVVMFYLDLKNIRRASLFPRDP 552
Cdd:PTZ00425 548 SHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYP 581
lysS PRK00484
lysyl-tRNA synthetase; Reviewed
53-549 2.21e-17

lysyl-tRNA synthetase; Reviewed


Pssm-ID: 234778 [Multi-domain]  Cd Length: 491  Bit Score: 85.14  E-value: 2.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    53 QLEAEReaREKKAAAEDTAKDNYGKlpliqsrDSDRT---GQKRVKFVDLDEAKDSDKEVLFR--ARVHNTRQQGAtLAF 127
Cdd:PRK00484   5 EQIAVR--REKLAELREQGIDPYPN-------KFERThtaAELRAKYDDKEKEELEELEIEVSvaGRVMLKRVMGK-ASF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   128 LTLRQQASLIQGLVKANKEGTISKNMVKwagSLNLESIVLVRGIVkkvdepIKSATVQnLEIHITKIytisetpealpIL 207
Cdd:PRK00484  75 ATLQDGSGRIQLYVSKDDVGEEALEAFK---KLDLGDIIGVEGTL------FKTKTGE-LSVKATEL-----------TL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   208 LEDASRSeaeaeaagLPVV-----NLDTRLDYRVIDLrtVTNQA---IFRIQAGVCELFREYLATKKFTEVHTPKLLGAP 279
Cdd:PRK00484 134 LTKSLRP--------LPDKfhgltDVETRYRQRYVDL--IVNPEsreTFRKRSKIISAIRRFLDNRGFLEVETPMLQPIA 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   280 seGGSSV--FeVTY---FKGKAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSNThRHMTEFTGLDMEMAFEEhYHEV 354
Cdd:PRK00484 204 --GGAAArpF-ITHhnaLDIDLYLRIAPELYLKRLIVGGFERVYEIGRNFRNEGIDT-RHNPEFTMLEFYQAYAD-YNDM 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   355 LDTLSELFVFIfselpkrfAHEIELVRK-QYPVEEFKLpkDGKMVRLTYKEGI-------------EMLRAAGKEIGdFE 420
Cdd:PRK00484 279 MDLTEELIRHL--------AQAVLGTTKvTYQGTEIDF--GPPFKRLTMVDAIkeytgvdfddmtdEEARALAKELG-IE 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   421 DLSTEN-----EKFLGKLVRDKYDTDFYILDkFPLEIRPFyTMPDPANPKYSNSYDFFMRGEEILSG----------AQR 485
Cdd:PRK00484 348 VEKSWGlgkliNELFEEFVEPKLIQPTFITD-YPVEISPL-AKRHREDPGLTERFELFIGGREIANAfselndpidqRER 425
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323011   486 IHDHALLQER--MKAHGLspeDpglKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:PRK00484 426 FEAQVEAKEAgdDEAMFM---D---EDFLRALEYGMPPTGGLGIGIDRLVMLLTDSPSIRDVILFP 485
LysU COG1190
Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA ...
247-549 1.25e-15

Lysyl-tRNA synthetase (class II) [Translation, ribosomal structure and biogenesis]; Lysyl-tRNA synthetase (class II) is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 440803 [Multi-domain]  Cd Length: 495  Bit Score: 79.69  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  247 IFRIQAGVCELFREYLATKKFTEVHTPKLlgAPSEGGSSV--FeVTYFKG---KAYLAQSPQFNKQQLIVADFERVYEIG 321
Cdd:COG1190 173 TFRKRSKIIRAIRRFLDERGFLEVETPML--QPIAGGAAArpF-ITHHNAldmDLYLRIAPELYLKRLIVGGFERVFEIG 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  322 PVFRAENSNThRHMTEFTGLDMEMAFEEhYHEVLDTLSELFVFIFSELPKrfAHEIELvrkqypveefklpkDGKMV--- 398
Cdd:COG1190 250 RNFRNEGIDT-THNPEFTMLELYQAYAD-YNDMMDLTEELIREAAEAVLG--TTKVTY--------------QGQEIdls 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  399 ----RLTYKEGIEmlRAAGKeigDFEDLSTENE-----------------------KFLGKLVRDKYDTDFYILDkFPLE 451
Cdd:COG1190 312 ppwrRITMVEAIK--EATGI---DVTPLTDDEElralakelgievdpgwgrgklidELFEELVEPKLIQPTFVTD-YPVE 385
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  452 IRPFyTMPDPANPKYSNSYDFFMRGEEILSG----------AQRIHDhallQERMKAHGlSPEDPGL-KDYCDGFSYGCP 520
Cdd:COG1190 386 VSPL-AKRHRDDPGLTERFELFIAGREIANAfselndpidqRERFEE----QLELKAAG-DDEAMPMdEDFLRALEYGMP 459
                       330       340
                ....*....|....*....|....*....
gi 6323011  521 PHAGGGIGLERVVMFYLDLKNIRRASLFP 549
Cdd:COG1190 460 PTGGLGIGIDRLVMLLTDSPSIRDVILFP 488
Asp_Lys_Asn_RS_N cd04100
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ...
108-199 1.94e-15

Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239766 [Multi-domain]  Cd Length: 85  Bit Score: 71.44  E-value: 1.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  108 EVLFRARVHNTRQQGAtLAFLTLRQQASLIQGLVKANKEGtiskNMVKWAGSLNLESIVLVRGIVKKVDEPIksATVQNL 187
Cdd:cd04100   1 EVTLAGWVHSRRDHGG-LIFIDLRDGSGIVQVVVNKEELG----EFFEEAEKLRTESVVGVTGTVVKRPEGN--LATGEI 73
                        90
                ....*....|..
gi 6323011  188 EIHITKIYTISE 199
Cdd:cd04100  74 ELQAEELEVLSK 85
PTZ00417 PTZ00417
lysine-tRNA ligase; Provisional
229-557 3.39e-15

lysine-tRNA ligase; Provisional


Pssm-ID: 173607 [Multi-domain]  Cd Length: 585  Bit Score: 78.51  E-value: 3.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   229 DTRLDYRVIDLRTVTNQA---IFRIQAGVCELFREYLATKKFTEVHTPkLLGAPSEGGSSVFEVTYFKG---KAYLAQSP 302
Cdd:PTZ00417 231 DTEIRYRQRYLDLMINEStrsTFITRTKIINYLRNFLNDRGFIEVETP-TMNLVAGGANARPFITHHNDldlDLYLRIAT 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   303 QFNKQQLIVADFERVYEIGPVFRAEN-SNTHRhmTEFTGLDMEMAFEEHYHEVL---DTLSELFVFIFSEL--------P 370
Cdd:PTZ00417 310 ELPLKMLIVGGIDKVYEIGKVFRNEGiDNTHN--PEFTSCEFYWAYADFYDLIKwseDFFSQLVMHLFGTYkilynkdgP 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   371 KRFAHEIELVrKQYP----VEE--------FKLPKDG-----KMVRLTYKEGIEMlraagkeigdfedlstENEKFLGKL 433
Cdd:PTZ00417 388 EKDPIEIDFT-PPYPkvsiVEElekltntkLEQPFDSpetinKMINLIKENKIEM----------------PNPPTAAKL 450
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   434 VrDKYDTDFyILDKFPleIRPFYTMPDP-----------ANPKYSNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLS 502
Cdd:PTZ00417 451 L-DQLASHF-IENKYP--NKPFFIIEHPqimsplakyhrSKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFSAQQKD 526
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323011   503 PEDPGLK------DYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPrdpkRLRP 557
Cdd:PTZ00417 527 REKGDAEafqfdaAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNCIKDVILFP----TMRP 583
PLN02532 PLN02532
asparagine-tRNA synthetase
274-550 1.03e-14

asparagine-tRNA synthetase


Pssm-ID: 215291 [Multi-domain]  Cd Length: 633  Bit Score: 77.22  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   274 KLLGAPSEGGSSV-FEVTYFKGKAYLAQSPQFNKQQLIVAdFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEhYH 352
Cdd:PLN02532 349 KLKTGTSVKADKLsFSKDFFSRPTYLTVSGRLHLESYACA-LGNVYTFGPRFRADRIDSARHLAEMWMVEVEMAFSE-LE 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   353 EVLDTLSELFVFIFSELPKRFAHEIELVRKQYP---VEEFKLPKDGKMVRLTYKEGIEMLRAAGKEigDFED-------L 422
Cdd:PLN02532 427 DAMNCAEDYFKFLCKWVLENCSEDMKFVSKRIDktiSTRLEAIISSSLQRISYTEAVDLLKQATDK--KFETkpewgiaL 504
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   423 STENEKFLGKlvrdkydtDFY----ILDKFPLEIRPFYTMPDPaNPKYSNSYDFFM-RGEEILSGAQRIHDHALLQERMK 497
Cdd:PLN02532 505 TTEHLSYLAD--------EIYkkpvIIYNYPKELKPFYVRLND-DGKTVAAFDLVVpKVGTVITGSQNEERMDILNARIE 575
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6323011   498 AHGLSPEDpgLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPR 550
Cdd:PLN02532 576 ELGLPREQ--YEWYLDLRRHGTVKHSGFSLGFELMVLFATGLPDVRDAIPFPR 626
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
230-549 1.55e-11

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 67.30  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    230 TRLDYRVIDLrtVTN---QAIFRIQAGVCELFREYLATKKFTEVHTPKLlgAPSEGGSSV--FeVTYFKgkAY-----LA 299
Cdd:PRK02983  751 ARVRQRYLDL--AVNpeaRDLLRARSAVVRAVRETLVARGFLEVETPIL--QQVHGGANArpF-VTHIN--AYdmdlyLR 823
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    300 QSPQFNKQQLIVADFERVYEIGPVFRAENSNtHRHMTEFTGLDmemAFEEH--YHEVLDTLSELF----VFIFSElpkrf 373
Cdd:PRK02983  824 IAPELYLKRLCVGGVERVFELGRNFRNEGVD-ATHNPEFTLLE---AYQAHadYDTMRDLTRELIqnaaQAAHGA----- 894
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    374 aHEIELVRKQYPVEEFKLPKDGKMVrlTYKEGIEmlRAAGKEIG---DFEDL---------STENEKFLGKLVRDKYD-- 439
Cdd:PRK02983  895 -PVVMRPDGDGVLEPVDISGPWPVV--TVHDAVS--EALGEEIDpdtPLAELrklcdaagiPYRTDWDAGAVVLELYEhl 969
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    440 ----TD---FYIldKFPLEIRPFyTMPDPANPKYSNSYDFFMRGEEiLSGA---------QRihdhALLQER-MKAHGLS 502
Cdd:PRK02983  970 vedrTTfptFYT--DFPTSVSPL-TRPHRSDPGLAERWDLVAWGVE-LGTAyseltdpveQR----RRLTEQsLLAAGGD 1041
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 6323011    503 PEDPGL-KDYCDGFSYGCPPHAGGGIGLERVVMFyLDLKNIRRASLFP 549
Cdd:PRK02983 1042 PEAMELdEDFLQALEYAMPPTGGLGMGVDRLVML-LTGRSIRETLPFP 1088
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
258-531 2.30e-11

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


Pssm-ID: 238391 [Multi-domain]  Cd Length: 211  Bit Score: 63.29  E-value: 2.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  258 FREYLATKKFTEVHTPKLLGAPSEGGSSVFEVT------YFKGKAYLAQSPQFNKQQL----IVADFERVYEIGPVFRAE 327
Cdd:cd00768   9 LRRFMAELGFQEVETPIVEREPLLEKAGHEPKDllpvgaENEEDLYLRPTLEPGLVRLfvshIRKLPLRLAEIGPAFRNE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  328 NSNTH-RHMTEFTGLDMEMAFEEhyhevldtlselfvfifSELPKRFAHEIELVRkqypveefklpkdgkmvrltykegi 406
Cdd:cd00768  89 GGRRGlRRVREFTQLEGEVFGED-----------------GEEASEFEELIELTE------------------------- 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  407 EMLRAAGKEIgdfedlstenekflgklvrdkydtDFYILDKFPLEIRPFYtmpdpanpkYSNSYDFFM-----RGEEILS 481
Cdd:cd00768 127 ELLRALGIKL------------------------DIVFVEKTPGEFSPGG---------AGPGFEIEVdhpegRGLEIGS 173
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6323011  482 GAQRIHDHALLQErmkahglspedpgLKDYCDGFSYGCPPHAGGGIGLER 531
Cdd:cd00768 174 GGYRQDEQARAAD-------------LYFLDEALEYRYPPTIGFGLGLER 210
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
115-240 2.53e-08

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 52.91  E-value: 2.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  115 VHNTRQQGAtLAFLTLRQQASLIQglVKANKEgtiSKNMVKWAGSLNLESIVLVRGIVKKVDEP---IKSATvQNLEIHI 191
Cdd:cd04317  23 VQRRRDHGG-LIFIDLRDRYGIVQ--VVFDPE---EAPEFELAEKLRNESVIQVTGKVRARPEGtvnPKLPT-GEIEVVA 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6323011  192 TKIYTISETpEALPILLEDASrseaeaeaaglpVVNLDTRLDYRVIDLR 240
Cdd:cd04317  96 SELEVLNKA-KTLPFEIDDDV------------NVSEELRLKYRYLDLR 131
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
109-197 7.31e-08

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 49.54  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011    109 VLFRARVHNTRQQGATLAFLTLRQQASLIQglVKANKEgtiskNMVKWAGSLNLESIVLVRGIVKKVDEPiksatvqNLE 188
Cdd:pfam01336   1 VTVAGRVTSIRRSGGKLLFLTLRDGTGSIQ--VVVFKE-----EAEKLAKKLKEGDVVRVTGKVKKRKGG-------ELE 66

                  ....*....
gi 6323011    189 IHITKIYTI 197
Cdd:pfam01336  67 LVVEEIELL 75
PRK09350 PRK09350
elongation factor P--(R)-beta-lysine ligase;
259-544 1.34e-05

elongation factor P--(R)-beta-lysine ligase;


Pssm-ID: 236474 [Multi-domain]  Cd Length: 306  Bit Score: 47.23  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   259 REYLATKKFTEVHTPKLLGAP-SEGGSSVFEvTYFKG-------KAYLAQSPQFNKQQLIVADFERVYEIGPVFRAENSN 330
Cdd:PRK09350  16 RRFFADRGVLEVETPILSQATvTDIHLVPFE-TRFVGpgasqgkTLWLMTSPEYHMKRLLAAGSGPIFQICKSFRNEEAG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   331 THrHMTEFTGLDMemaFEEHY--HEVLDTLSELFVFIFselpkrFAHEIELVRKQYPVEEF----KLPKDgkmvrltyke 404
Cdd:PRK09350  95 RY-HNPEFTMLEW---YRPHYdmYRLMNEVDDLLQQVL------DCEPAESLSYQQAFLRYlgidPLSAD---------- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   405 gIEMLRAAGKEIGDFEDLSTEnekflgklvrDKYDTDFYILdkFPLEIRP---------FYTMP---------DPANPKY 466
Cdd:PRK09350 155 -KTQLREVAAKLGLSNIADEE----------EDRDTLLQLL--FTFGVEPnigkekptfVYHFPasqaalakiSTEDHRV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011   467 SNSYDFFMRGEEILSGAQRIHDHALLQERMKAHGLSPEDPGLKDY------CDGFSYGCPPHAGGGIGLERVVMFYLDLK 540
Cdd:PRK09350 222 AERFEVYFKGIELANGFHELTDAREQRQRFEQDNRKRAARGLPQQpidenlIAALEAGLPDCSGVALGVDRLIMLALGAE 301

                 ....
gi 6323011   541 NIRR 544
Cdd:PRK09350 302 SISE 305
ND_PkAspRS_like_N cd04316
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ...
107-206 2.90e-05

ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.


Pssm-ID: 239811 [Multi-domain]  Cd Length: 108  Bit Score: 43.46  E-value: 2.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323011  107 KEVLFRARVHNTRQQGAtLAFLTLRQQASLIQglVKANKEgTISKNMVKWAGSLNLESIVLVRGIVKkvDEPIKSATVqn 186
Cdd:cd04316  13 EEVTVAGWVHEIRDLGG-IKFVILRDREGIVQ--VTAPKK-KVDKELFKTVRKLSRESVISVTGTVK--AEPKAPNGV-- 84
                        90       100
                ....*....|....*....|
gi 6323011  187 lEIHITKIYTISETPEALPI 206
Cdd:cd04316  85 -EIIPEEIEVLSEAKTPLPL 103
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
24-46 4.60e-03

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 40.01  E-value: 4.60e-03
                         10        20
                 ....*....|....*....|...
gi 6323011    24 EDGKPLSKKALKKLQKEQEKQRK 46
Cdd:PTZ00399 617 ADGEEISKKERKKLSKEYDKQAK 639
NatA_aux_su pfam12569
N-terminal acetyltransferase A, auxiliary subunit; This entry represents N-terminal ...
31-102 9.77e-03

N-terminal acetyltransferase A, auxiliary subunit; This entry represents N-terminal acetyltransferase A (NatA) auxiliary subunit (also known as NMDA receptor-regulated protein 1), which is a non-catalytic component of the NatA N-terminal acetyltransferase that catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-terminal acetylation plays a role in normal eukaryotic translation and processing, protecting against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and NAT5 to the ribosome, and may present the N terminus of nascent polypeptides for acetylation.


Pssm-ID: 463630 [Multi-domain]  Cd Length: 514  Bit Score: 38.79  E-value: 9.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323011     31 KKALKKLQKEQekqrKKEERAlqlEAEREAREKKAAAEDTAKDNYGKlplIQSRDSDRTGQKRVKFVD-LDEA 102
Cdd:pfam12569 411 KKARKKQKKAE----KKAEKE---EAEKAAKKKKKKAEKKAKGEDGE---TKKEDPDPLGEKLAQTEDpLEEA 473
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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