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Conserved domains on  [gi|564350613|ref|XP_006238048|]
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probable arginine--tRNA ligase, mitochondrial isoform X1 [Rattus norvegicus]

Protein Classification

arginine--tRNA ligase( domain architecture ID 11414312)

arginine--tRNA ligase catalyzes the esterification reaction between L-arginine and its cognate tRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
65-575 1.19e-157

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


:

Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 463.08  E-value: 1.19e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  65 AQRLAEKLKCDTVVTAIS-AGPRTLNFKINRALLTkAVLQQVTEDGSKYGlkselFSDLPQ-KRIVVEFSSPNIAKKFHV 142
Cdd:COG0018   60 AEEIAEALDADPLVEKVEiAGPGFINFFLSPAALA-AVLKEILADGEDYG-----RSDAGKgKKVVVEYVSANPTKPLHV 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 143 GHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEE-KLQANPLQHLFDVYVQVNKEATDDKNVTK 221
Cdd:COG0018  134 GHLRGAVIGDALARILEAAGYDVTRENYINDAGTQIGKLALSLERYGEEEiEPESKPDGYLGDLYVKFHKEYEEDPELED 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 222 LAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKS--QDVLKLLDSKGLLQKtAKGNVVV 299
Cdd:COG0018  214 IARELLAKLEPGDEEALELWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGavEEVVEELKEKGLLYE-SDGALWV 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 300 DVSETGDLsSVCTVMRSDGTSLYATRDLAAAIHRKDKYNFDTMIYVADKGQKRHFQQVFQMLKIMGHEWAERCQHVPFGI 379
Cdd:COG0018  293 RLTEFGDD-KDRVLVKSDGTYTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGM 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 380 VKG-----MKTRRGEVTFLEDVLNEVQSRMLQNMASikttKKMENPRETAEKVGLAALIIQDFRGLLLSDYQFSWDRVFQ 454
Cdd:COG0018  372 VNLrdgekMSTRAGTVVTLDDLLDEAVERAREIIEE----KSEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALS 447
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 455 SRGDTGVFLQYTHARLCSL----EETFgcGYLNDFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLtlsH 530
Cdd:COG0018  448 FEGNTNPYVQYAHARICSIlrkaGEEL--DGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLY---E 522
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 564350613 531 LAAVAHK---TLQV-KDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:COG0018  523 LAKAFHSfynACRIlKAEDEELRAARLALVAATAQVLKNGLGLLGISAP 571
 
Name Accession Description Interval E-value
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
65-575 1.19e-157

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


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 463.08  E-value: 1.19e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  65 AQRLAEKLKCDTVVTAIS-AGPRTLNFKINRALLTkAVLQQVTEDGSKYGlkselFSDLPQ-KRIVVEFSSPNIAKKFHV 142
Cdd:COG0018   60 AEEIAEALDADPLVEKVEiAGPGFINFFLSPAALA-AVLKEILADGEDYG-----RSDAGKgKKVVVEYVSANPTKPLHV 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 143 GHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEE-KLQANPLQHLFDVYVQVNKEATDDKNVTK 221
Cdd:COG0018  134 GHLRGAVIGDALARILEAAGYDVTRENYINDAGTQIGKLALSLERYGEEEiEPESKPDGYLGDLYVKFHKEYEEDPELED 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 222 LAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKS--QDVLKLLDSKGLLQKtAKGNVVV 299
Cdd:COG0018  214 IARELLAKLEPGDEEALELWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGavEEVVEELKEKGLLYE-SDGALWV 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 300 DVSETGDLsSVCTVMRSDGTSLYATRDLAAAIHRKDKYNFDTMIYVADKGQKRHFQQVFQMLKIMGHEWAERCQHVPFGI 379
Cdd:COG0018  293 RLTEFGDD-KDRVLVKSDGTYTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGM 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 380 VKG-----MKTRRGEVTFLEDVLNEVQSRMLQNMASikttKKMENPRETAEKVGLAALIIQDFRGLLLSDYQFSWDRVFQ 454
Cdd:COG0018  372 VNLrdgekMSTRAGTVVTLDDLLDEAVERAREIIEE----KSEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALS 447
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 455 SRGDTGVFLQYTHARLCSL----EETFgcGYLNDFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLtlsH 530
Cdd:COG0018  448 FEGNTNPYVQYAHARICSIlrkaGEEL--DGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLY---E 522
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 564350613 531 LAAVAHK---TLQV-KDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:COG0018  523 LAKAFHSfynACRIlKAEDEELRAARLALVAATAQVLKNGLGLLGISAP 571
argS TIGR00456
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ...
56-575 5.86e-134

arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273085 [Multi-domain]  Cd Length: 563  Bit Score: 402.11  E-value: 5.86e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613   56 KSQLDTQDQAQRLAEKLKC-DTVVTAISAGPrTLNFKINRALLTKAVLQQVTEDGSKYGLKselfsDLPQKRIVVEFSSP 134
Cdd:TIGR00456  48 VLKKAPRQIAEEIVLKLKTgEIIEKVEAAGP-FINFFLSPQKLLERLIQKILTQKEKYGSK-----KLKNKKIIIEFSSA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  135 NIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEE--KLQANPLQHLFDVYVQVNKE 212
Cdd:TIGR00456 122 NPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGNEAlnIAVKKPDHGLEGFYVEINKR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  213 ATDDKNVTKLAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEYS--GESFYREKSQDVLKLLDSKGLLQ 290
Cdd:TIGR00456 202 LEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNIHFDSFVweGESVKNGMLPKVLEDLKEKGLVV 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  291 KtaKGNVVVDVSETGDLSSVcTVMRSDGTSLYATRDLAAAIHRKDKyNFDTMIYVADKGQKRHFQQVFQMLKIMGHeWAE 370
Cdd:TIGR00456 282 E--DGALWLDLTLFGDKKDR-VLQKSDGTYLYLTTDIAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY-KKK 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  371 RCQHVPFGIVKG--MKTRRGEVTFLEDVLNEVQSRMLQNMasikTTKKMENPRETAEKVGLAALIIQDFRGLLLSDYQFS 448
Cdd:TIGR00456 357 ELEHLNFGMVPLysMKTRRGNVISLDNLLDEASKRAGNVI----TIKNDLEEEKVADAVGIGAVRYFDLSKNRTTDYVFD 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  449 WDRVFQSRGDTGVFLQYTHARLCSLEETF---GCGYLNDFNVacLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYL 525
Cdd:TIGR00456 433 WDAMLSFEGNTAPYIQYAHARICSILRKAeidGEKLIADDFE--LLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYL 510
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 564350613  526 LTLSHLAAVAHKTLQVKDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:TIGR00456 511 YELASLFSSFYKACPVLDAENELAAARLALLKATRQTLKNGLDLLGIEPP 560
argS PRK01611
arginyl-tRNA synthetase; Reviewed
22-575 2.32e-119

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 362.55  E-value: 2.32e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  22 ESLIKSISAVPV--SKKEEVADFQLSVDSLLENNSHKSQLDTqdqAQRLAEKLKCDTVvtaisAGPRTLNFKINRALLTk 99
Cdd:PRK01611  19 AGGLPELPAVLIerPKDPEHGDYATNVAMQLAKKLKKNPREI---AEEIVEAIEKVEI-----AGPGFINFFLDPAALA- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 100 AVLQQVTEDGSKYGlkselFSDLPQ-KRIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQF 178
Cdd:PRK01611  90 ELVLAILEAGERYG-----RSDIGKgKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYYVNDAGTQI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 179 GLLGTGFQLFgyeeklqanplqhlfdvyvqvnkeatddknvtklaheffhrlelgdtqalalWQRFRDLSIEEYTQIYKR 258
Cdd:PRK01611 165 GMLIASLELL----------------------------------------------------WRKAVDISLDEIKEDLDR 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 259 LGIYFDEYS--GESFYREKSQDVLKLLDSKGLLQKTAKGNVVVDVSETGDLSSvCTVMRSDGTSLYATRDLAAAIHRKDk 336
Cdd:PRK01611 193 LGVHFDVWFseSELYYNGKVDEVVEDLKEKGLLYVESDGALWVRLTEFGDDKD-RVLIKSDGTYTYFTRDIAYHLYKFE- 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 337 yNFDTMIYVADKGQKRHFQQVFQMLKIMGHEWA--ERCQHVPFGIVKG-----MKTRRGEVTFLEDVLNEVQSRMLQNMA 409
Cdd:PRK01611 271 -RFDRVIYVVGADHHGHFKRLKAALKALGYDPDalEVLLHQMVGLVRGgegvkMSTRAGNVVTLDDLLDEAVGRARELIE 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 410 SikttkkmenpRETAEKVGLAALiiqdfRGLLLS-----DYQFSWDRVFQSRGDTGVFLQYTHARLCS-LEETFGCGYln 483
Cdd:PRK01611 350 E----------KEIAEAVGIDAV-----RYFDLSrsrdkDLDFDLDLALSFEGNNPPYVQYAHARICSiLRKAAEAGI-- 412
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 484 DFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLTlshLAAVAHK---TLQVKDSPPEVAGARLHLFKAVR 560
Cdd:PRK01611 413 DLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYE---LAGAFHSfynRVLLKDEEEELRNARLALVKATA 489
                        570
                 ....*....|....*
gi 564350613 561 SVLANGMKLLGITPL 575
Cdd:PRK01611 490 QVLKNGLDLLGISAP 504
tRNA-synt_1d pfam00750
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ...
124-449 3.40e-97

tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only arginyl tRNA synthetase.


Pssm-ID: 395607 [Multi-domain]  Cd Length: 348  Bit Score: 299.87  E-value: 3.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  124 QKRIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEEKLQANPLQHLF 203
Cdd:pfam00750  18 KKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKTLQEMPIQDLE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  204 DVYVQVNKEATDDKNVTKLAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEySGESFYREKSQDVLKLL 283
Cdd:pfam00750  98 DFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE-MGESLYNPMMNEIVKDF 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  284 DSKGLLQKTaKGNVVVDVSETGDLSSVcTVMRSDGTSLYATRDLAAAIHRKDKYNFDTMIYVADKGQKRHFQQVFQMLKI 363
Cdd:pfam00750 177 KKNGLVVEI-DGALVVFLDEFGKPMGV-IVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAILRK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  364 MGHEW-AERCQHVPFGIV-----KGMKTRRGEVTFLEDVLNEVQSRMLQNMASIKTTKKM--ENPRETAEKVGLAALIIQ 435
Cdd:pfam00750 255 AGYVPeSKDLEHINFGMVlgkdgKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDKILqaDELEAVADAVGIGAIKYA 334
                         330
                  ....*....|....
gi 564350613  436 DFRGLLLSDYQFSW 449
Cdd:pfam00750 335 DLSKNRTNDYIFDW 348
ArgRS_core cd00671
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ...
126-388 5.10e-69

catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.


Pssm-ID: 185675 [Multi-domain]  Cd Length: 212  Bit Score: 222.05  E-value: 5.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 126 RIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLfgyeeklqanplqhlfdv 205
Cdd:cd00671    1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 206 yvqvnkeatddknvtklaheffhrlelgdtqalalWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKSQDVLKLLDS 285
Cdd:cd00671   63 -----------------------------------WRKLVEESIKADLETYGRLDVRFDVWFGESSYLGLMGKVVELLEE 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 286 KGLLQKTaKGNVVVDVSETGDLSSVcTVMRSDGTSLYATRDLAAAIHRKdKYNFDTMIYVADKGQKRHFQQVFQMLKIMG 365
Cdd:cd00671  108 LGLLYEE-DGALWLDLTEFGDDKDR-VLVRSDGTYTYFTRDIAYHLDKF-ERGADKIIYVVGADHHGHFKRLFAALELLG 184
                        250       260
                 ....*....|....*....|....*...
gi 564350613 366 HEWAERCQHVPFGIVKG-----MKTRRG 388
Cdd:cd00671  185 YDEAKKLEHLLYGMVNLpkegkMSTRAG 212
DALR_1 smart00836
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
463-575 5.30e-30

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.


Pssm-ID: 214846 [Multi-domain]  Cd Length: 122  Bit Score: 114.21  E-value: 5.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613   463 LQYTHARLCSL-----EETFGCGYLNDFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLTLSHLAAVAHK 537
Cdd:smart00836   1 VQYAHARICSIlrkagEAGETLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 564350613   538 TLQVKDSP-PEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:smart00836  81 RVRVLGEEnPELRKARLALLKAVRQVLANGLRLLGISAP 119
 
Name Accession Description Interval E-value
ArgS COG0018
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ...
65-575 1.19e-157

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


Pssm-ID: 439789 [Multi-domain]  Cd Length: 574  Bit Score: 463.08  E-value: 1.19e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  65 AQRLAEKLKCDTVVTAIS-AGPRTLNFKINRALLTkAVLQQVTEDGSKYGlkselFSDLPQ-KRIVVEFSSPNIAKKFHV 142
Cdd:COG0018   60 AEEIAEALDADPLVEKVEiAGPGFINFFLSPAALA-AVLKEILADGEDYG-----RSDAGKgKKVVVEYVSANPTKPLHV 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 143 GHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEE-KLQANPLQHLFDVYVQVNKEATDDKNVTK 221
Cdd:COG0018  134 GHLRGAVIGDALARILEAAGYDVTRENYINDAGTQIGKLALSLERYGEEEiEPESKPDGYLGDLYVKFHKEYEEDPELED 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 222 LAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKS--QDVLKLLDSKGLLQKtAKGNVVV 299
Cdd:COG0018  214 IARELLAKLEPGDEEALELWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGavEEVVEELKEKGLLYE-SDGALWV 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 300 DVSETGDLsSVCTVMRSDGTSLYATRDLAAAIHRKDKYNFDTMIYVADKGQKRHFQQVFQMLKIMGHEWAERCQHVPFGI 379
Cdd:COG0018  293 RLTEFGDD-KDRVLVKSDGTYTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPAKDLEHLLFGM 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 380 VKG-----MKTRRGEVTFLEDVLNEVQSRMLQNMASikttKKMENPRETAEKVGLAALIIQDFRGLLLSDYQFSWDRVFQ 454
Cdd:COG0018  372 VNLrdgekMSTRAGTVVTLDDLLDEAVERAREIIEE----KSEEEKEEIAEQVGIDAVRYFDLSRSRDKDLDFDLDLALS 447
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 455 SRGDTGVFLQYTHARLCSL----EETFgcGYLNDFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLtlsH 530
Cdd:COG0018  448 FEGNTNPYVQYAHARICSIlrkaGEEL--DGLAEADLSLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLY---E 522
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 564350613 531 LAAVAHK---TLQV-KDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:COG0018  523 LAKAFHSfynACRIlKAEDEELRAARLALVAATAQVLKNGLGLLGISAP 571
argS TIGR00456
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ...
56-575 5.86e-134

arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273085 [Multi-domain]  Cd Length: 563  Bit Score: 402.11  E-value: 5.86e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613   56 KSQLDTQDQAQRLAEKLKC-DTVVTAISAGPrTLNFKINRALLTKAVLQQVTEDGSKYGLKselfsDLPQKRIVVEFSSP 134
Cdd:TIGR00456  48 VLKKAPRQIAEEIVLKLKTgEIIEKVEAAGP-FINFFLSPQKLLERLIQKILTQKEKYGSK-----KLKNKKIIIEFSSA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  135 NIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEE--KLQANPLQHLFDVYVQVNKE 212
Cdd:TIGR00456 122 NPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYVNDWGRQFGLLALGVEKFGNEAlnIAVKKPDHGLEGFYVEINKR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  213 ATDDKNVTKLAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEYS--GESFYREKSQDVLKLLDSKGLLQ 290
Cdd:TIGR00456 202 LEENEELEEEARELFVKLESGDEETIKLWKRLVEYSLEGIKETYDRLNIHFDSFVweGESVKNGMLPKVLEDLKEKGLVV 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  291 KtaKGNVVVDVSETGDLSSVcTVMRSDGTSLYATRDLAAAIHRKDKyNFDTMIYVADKGQKRHFQQVFQMLKIMGHeWAE 370
Cdd:TIGR00456 282 E--DGALWLDLTLFGDKKDR-VLQKSDGTYLYLTTDIAYHLDKLER-GFDKMIYVWGSDHHLHIAQMFAILEKLGY-KKK 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  371 RCQHVPFGIVKG--MKTRRGEVTFLEDVLNEVQSRMLQNMasikTTKKMENPRETAEKVGLAALIIQDFRGLLLSDYQFS 448
Cdd:TIGR00456 357 ELEHLNFGMVPLysMKTRRGNVISLDNLLDEASKRAGNVI----TIKNDLEEEKVADAVGIGAVRYFDLSKNRTTDYVFD 432
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  449 WDRVFQSRGDTGVFLQYTHARLCSLEETF---GCGYLNDFNVacLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYL 525
Cdd:TIGR00456 433 WDAMLSFEGNTAPYIQYAHARICSILRKAeidGEKLIADDFE--LLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYL 510
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 564350613  526 LTLSHLAAVAHKTLQVKDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:TIGR00456 511 YELASLFSSFYKACPVLDAENELAAARLALLKATRQTLKNGLDLLGIEPP 560
argS PRK01611
arginyl-tRNA synthetase; Reviewed
22-575 2.32e-119

arginyl-tRNA synthetase; Reviewed


Pssm-ID: 234964 [Multi-domain]  Cd Length: 507  Bit Score: 362.55  E-value: 2.32e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  22 ESLIKSISAVPV--SKKEEVADFQLSVDSLLENNSHKSQLDTqdqAQRLAEKLKCDTVvtaisAGPRTLNFKINRALLTk 99
Cdd:PRK01611  19 AGGLPELPAVLIerPKDPEHGDYATNVAMQLAKKLKKNPREI---AEEIVEAIEKVEI-----AGPGFINFFLDPAALA- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 100 AVLQQVTEDGSKYGlkselFSDLPQ-KRIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQF 178
Cdd:PRK01611  90 ELVLAILEAGERYG-----RSDIGKgKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYYVNDAGTQI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 179 GLLGTGFQLFgyeeklqanplqhlfdvyvqvnkeatddknvtklaheffhrlelgdtqalalWQRFRDLSIEEYTQIYKR 258
Cdd:PRK01611 165 GMLIASLELL----------------------------------------------------WRKAVDISLDEIKEDLDR 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 259 LGIYFDEYS--GESFYREKSQDVLKLLDSKGLLQKTAKGNVVVDVSETGDLSSvCTVMRSDGTSLYATRDLAAAIHRKDk 336
Cdd:PRK01611 193 LGVHFDVWFseSELYYNGKVDEVVEDLKEKGLLYVESDGALWVRLTEFGDDKD-RVLIKSDGTYTYFTRDIAYHLYKFE- 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 337 yNFDTMIYVADKGQKRHFQQVFQMLKIMGHEWA--ERCQHVPFGIVKG-----MKTRRGEVTFLEDVLNEVQSRMLQNMA 409
Cdd:PRK01611 271 -RFDRVIYVVGADHHGHFKRLKAALKALGYDPDalEVLLHQMVGLVRGgegvkMSTRAGNVVTLDDLLDEAVGRARELIE 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 410 SikttkkmenpRETAEKVGLAALiiqdfRGLLLS-----DYQFSWDRVFQSRGDTGVFLQYTHARLCS-LEETFGCGYln 483
Cdd:PRK01611 350 E----------KEIAEAVGIDAV-----RYFDLSrsrdkDLDFDLDLALSFEGNNPPYVQYAHARICSiLRKAAEAGI-- 412
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 484 DFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLTlshLAAVAHK---TLQVKDSPPEVAGARLHLFKAVR 560
Cdd:PRK01611 413 DLLLALLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYE---LAGAFHSfynRVLLKDEEEELRNARLALVKATA 489
                        570
                 ....*....|....*
gi 564350613 561 SVLANGMKLLGITPL 575
Cdd:PRK01611 490 QVLKNGLDLLGISAP 504
PLN02286 PLN02286
arginine-tRNA ligase
65-575 1.79e-101

arginine-tRNA ligase


Pssm-ID: 215160 [Multi-domain]  Cd Length: 576  Bit Score: 318.51  E-value: 1.79e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  65 AQRLAEKLKCDTVVTAIS-AGPRTLNFKINRALLTKAVlQQVTEDGSKyglksELFSDLPQKRIVVEFSSPNIAKKFHVG 143
Cdd:PLN02286  62 AQAIVKNLPASEMIESTSvAGPGFVNVRLSASWLAKRI-ERMLVDGID-----TWAPTLPVKRAVVDFSSPNIAKEMHVG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 144 HLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLgtgfqlfgyeeklqanpLQHLFDVYvqVNKEATDDKNVTKL- 222
Cdd:PLN02286 136 HLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQFGML-----------------IEHLFEKF--PNWESVSDQAIGDLq 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 223 -------------------AHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEySGESFYREKSQDVLKLL 283
Cdd:PLN02286 197 efykaakkrfdedeefkarAQQAVVRLQGGDPEYRAAWAKICEISRREFEKVYQRLRVELEE-KGESFYNPYIPGVIEEL 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 284 DSKGLLQKTaKGNVVVDVSetgDLSSVCTVMRSDGTSLYATRDLAAAIHRKDKYNFDTMIYVADKGQKRHFQQVFQMLKI 363
Cdd:PLN02286 276 ESKGLVVES-DGARVIFVE---GFDIPLIVVKSDGGFNYASTDLAALWYRLNEEKAEWIIYVTDVGQQQHFDMVFKAAKR 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 364 MGheWAE-----RCQHVPFGIVKG-----MKTRRGEVTFLEDVLNEVQSRMLQNMASiKTTKKMENPRE---TAEKVGLA 430
Cdd:PLN02286 352 AG--WLPedtypRLEHVGFGLVLGedgkrFRTRSGEVVRLVDLLDEAKSRSKAALIE-RGKDSEWTPEEleqAAEAVGYG 428
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 431 ALIIQDFRGLLLSDYQFSWDRVFQSRGDTGVFLQYTHARLCSLEETFGCGY--LNDFNVACLQEPQSVSILQHLLRFDEV 508
Cdd:PLN02286 429 AVKYADLKNNRLTNYTFSFDQMLDLKGNTAVYLLYAHARICSIIRKSGKDIdeLKKTGKIVLDHPDERALGLHLLQFPEV 508
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564350613 509 LYTASQDLQPKHIVSYLLTLSHLAAVAHKTLQVKDSPPEVagARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:PLN02286 509 VEEACTDLLPNRLCEYLYNLSEKFTKFYSNCKVNGSEEET--SRLLLCEATAIVMRKCFHLLGITPL 573
tRNA-synt_1d pfam00750
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ...
124-449 3.40e-97

tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only arginyl tRNA synthetase.


Pssm-ID: 395607 [Multi-domain]  Cd Length: 348  Bit Score: 299.87  E-value: 3.40e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  124 QKRIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLFGYEEKLQANPLQHLF 203
Cdd:pfam00750  18 KKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAGLEKYQDEKTLQEMPIQDLE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  204 DVYVQVNKEATDDKNVTKLAHEFFHRLELGDTQALALWQRFRDLSIEEYTQIYKRLGIYFDEySGESFYREKSQDVLKLL 283
Cdd:pfam00750  98 DFYREAKKHYDEEEEFAERARNYVVKLQSGDEYWRRMWKLIVDITMTQNQRLYDRLDVTLTE-MGESLYNPMMNEIVKDF 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  284 DSKGLLQKTaKGNVVVDVSETGDLSSVcTVMRSDGTSLYATRDLAAAIHRKDKYNFDTMIYVADKGQKRHFQQVFQMLKI 363
Cdd:pfam00750 177 KKNGLVVEI-DGALVVFLDEFGKPMGV-IVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDSRQSQHMQQAFAILRK 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  364 MGHEW-AERCQHVPFGIV-----KGMKTRRGEVTFLEDVLNEVQSRMLQNMASIKTTKKM--ENPRETAEKVGLAALIIQ 435
Cdd:pfam00750 255 AGYVPeSKDLEHINFGMVlgkdgKPFKTRKGGTVKLADLLDEALERALQLIMEKNKDKILqaDELEAVADAVGIGAIKYA 334
                         330
                  ....*....|....
gi 564350613  436 DFRGLLLSDYQFSW 449
Cdd:pfam00750 335 DLSKNRTNDYIFDW 348
ArgRS_core cd00671
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ...
126-388 5.10e-69

catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine.


Pssm-ID: 185675 [Multi-domain]  Cd Length: 212  Bit Score: 222.05  E-value: 5.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 126 RIVVEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGFQLfgyeeklqanplqhlfdv 205
Cdd:cd00671    1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILSLEK------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 206 yvqvnkeatddknvtklaheffhrlelgdtqalalWQRFRDLSIEEYTQIYKRLGIYFDEYSGESFYREKSQDVLKLLDS 285
Cdd:cd00671   63 -----------------------------------WRKLVEESIKADLETYGRLDVRFDVWFGESSYLGLMGKVVELLEE 107
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 286 KGLLQKTaKGNVVVDVSETGDLSSVcTVMRSDGTSLYATRDLAAAIHRKdKYNFDTMIYVADKGQKRHFQQVFQMLKIMG 365
Cdd:cd00671  108 LGLLYEE-DGALWLDLTEFGDDKDR-VLVRSDGTYTYFTRDIAYHLDKF-ERGADKIIYVVGADHHGHFKRLFAALELLG 184
                        250       260
                 ....*....|....*....|....*...
gi 564350613 366 HEWAERCQHVPFGIVKG-----MKTRRG 388
Cdd:cd00671  185 YDEAKKLEHLLYGMVNLpkegkMSTRAG 212
Anticodon_Ia_Arg cd07956
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ...
425-575 7.83e-40

Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA synthetases (ArgRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. ArgRS catalyzes the transfer of arginine to the 3'-end of its tRNA.


Pssm-ID: 153410 [Multi-domain]  Cd Length: 156  Bit Score: 142.35  E-value: 7.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613 425 EKVGLAALIIQDFRGLLLSDYQFSWDRVFQSRGDTGVFLQYTHARLCSLEETFGCGY--LNDFNVACLQEPQSVSILQHL 502
Cdd:cd07956    1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGDTGPYLQYAHARLCSILRKAGETIeaEADADLSLLPEPDERDLILLL 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564350613 503 LRFDEVLYTASQDLQPKHIVSYLLTLSHLAAVAHKTLQVKDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:cd07956   81 AKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEELRNARLALVAAARQVLANGLDLLGIEAP 153
DALR_1 smart00836
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
463-575 5.30e-30

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain of Arginyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids.


Pssm-ID: 214846 [Multi-domain]  Cd Length: 122  Bit Score: 114.21  E-value: 5.30e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613   463 LQYTHARLCSL-----EETFGCGYLNDFNVACLQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLTLSHLAAVAHK 537
Cdd:smart00836   1 VQYAHARICSIlrkagEAGETLPDIADADLSLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 564350613   538 TLQVKDSP-PEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:smart00836  81 RVRVLGEEnPELRKARLALLKAVRQVLANGLRLLGISAP 119
DALR_1 pfam05746
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ...
463-575 1.30e-21

DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteriztic conserved amino acids.


Pssm-ID: 399042 [Multi-domain]  Cd Length: 117  Bit Score: 90.40  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564350613  463 LQYTHARLCSLEETFGcgYLNDFNVAC---LQEPQSVSILQHLLRFDEVLYTASQDLQPKHIVSYLLTLSHLAAVAHKTL 539
Cdd:pfam05746   1 LQYAHARICSILRKAG--ELGINLDIDadlLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNC 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564350613  540 QVKDSPPEVAGARLHLFKAVRSVLANGMKLLGITPL 575
Cdd:pfam05746  79 RVLDEDNEERNARLALLKAVRQVLKNGLDLLGIEAP 114
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
129-185 4.51e-11

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


Pssm-ID: 173901 [Multi-domain]  Cd Length: 143  Bit Score: 60.96  E-value: 4.51e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564350613 129 VEFSSPNIAKKFHVGHLRSTIIGNFIANLKEALGHQVTRINYIGDWGMQFGLLGTGF 185
Cdd:cd00802    1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPANKK 57
 
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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