|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
2-549 |
3.24e-179 |
|
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: 517.01 E-value: 3.24e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 2 ITQKISEELNKALAKMGIhDTQETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQ-DLFLEVNLQPP 80
Cdd:COG0018 3 IKEELAEAIAAALAALGA-GLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDAdPLVEKVEIAGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 81 GFLNFKLKAKDHENLLKQIYYEKDRFGQF-SKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYW 159
Cdd:COG0018 82 GFINFFLSPAALAAVLKEILADGEDYGRSdAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTRENY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 160 INDAGNQIDKLAMSVLvRYLQlQNINIQLPADAYHGQeihlvaqtLYQTYKNQFINV--------RLNEKYEiDDDIANQ 231
Cdd:COG0018 162 INDAGTQIGKLALSLE-RYGE-EEIEPESKPDGYLGD--------LYVKFHKEYEEDpelediarELLAKLE-PGDEEAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 232 EIKNFAVKYLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKI--KPYTYTLDGALWLKTTTFGDDKDRVLIKSDG 309
Cdd:COG0018 231 ELWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELkeKGLLYESDGALWVRLTEFGDDKDRVLVKSDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 310 SYTYFTPDIAYHDYKFNKTNTTKLIDVWGTDHLGYIARLKAAMNALGYDP-NNLEIVCAQVMKLvKNNQefKLSKRSGQS 388
Cdd:COG0018 311 TYTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPaKDLEHLLFGMVNL-RDGE--KMSTRAGTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 389 LTIKDLVE-----------------------IIGKDALRWFLGSSSMNSHVIIDVDIALS-KNNNNPlyYVQYAHARANQ 444
Cdd:COG0018 388 VTLDDLLDeaverareiieekseeekeeiaeQVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGNTNP--YVQYAHARICS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 445 VLNKQVYELDFKTD----LLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKVLS 520
Cdd:COG0018 466 ILRKAGEELDGLAEadlsLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELR 545
|
570 580
....*....|....*....|....*....
gi 493739754 521 AQRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:COG0018 546 AARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-549 |
1.54e-177 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 510.08 E-value: 1.54e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 1 MITQKISEELNKALAKMGIHDTQEtkILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEqdlflEVNLQPP 80
Cdd:PRK01611 4 DIKELLAEALAAALEAGGLPELPA--VLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAIE-----KVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 81 GFLNFKLKAKDHENLLKQIYYEKDRFGQF-SKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYW 159
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEAGERYGRSdIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 160 INDAGNQIDKLAMSVlvrylqlqniniqlpadayhgqeihlvaqtlyqtyknqfinvrlnekyeidddianQEIKNFAVK 239
Cdd:PRK01611 157 VNDAGTQIGMLIASL--------------------------------------------------------ELLWRKAVD 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 240 YLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKI--KPYTYTL-DGALWLKTTTFGDDKDRVLIKSDGSYTYFTP 316
Cdd:PRK01611 181 ISLDEIKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLkeKGLLYVEsDGALWVRLTEFGDDKDRVLIKSDGTYTYFTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 317 DIAYHDYKFNKTNttKLIDVWGTDHLGYIARLKAAMNALGYDPNNLEIVCAQVMKLVKNNQEFKLSKRSGQSLTIKDLVE 396
Cdd:PRK01611 261 DIAYHLYKFERFD--RVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 397 -----------------IIGKDALRWFLGSSSMNSHVIIDVDIALSKNNNNPLyYVQYAHARANQVLNK-QVYELDFKTD 458
Cdd:PRK01611 339 eavgrarelieekeiaeAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKaAEAGIDLLLA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 459 LLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKVLSAqRYTLVWCVKQVLANGL 538
Cdd:PRK01611 418 LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEEELRNA-RLALVKATAQVLKNGL 496
|
570
....*....|.
gi 493739754 539 AIMKITPYDQM 549
Cdd:PRK01611 497 DLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
2-549 |
1.46e-135 |
|
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: 405.19 E-value: 1.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 2 ITQKISEELNKALAKMGIHDtqETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQDLFLEVNLQPPG 81
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSK--ESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 82 FLNFKLKAKDH-ENLLKQIYYEKDRFGQFSKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWI 160
Cdd:TIGR00456 79 FINFFLSPQKLlERLIQKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 161 NDAGNQIDKLAMSVLVRYLQLQNINIQLPADAYHGQEIHlvaqtlyqtyknqfINVRLNEKYEIDD------------DI 228
Cdd:TIGR00456 159 NDWGRQFGLLALGVEKFGNEALNIAVKKPDHGLEGFYVE--------------INKRLEENEELEEearelfvklesgDE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 229 ANQEIKNFAVKYLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKIKPYTYTL-DGALWLKTTTFGDDKDRVLIKS 307
Cdd:TIGR00456 225 ETIKLWKRLVEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVeDGALWLDLTLFGDKKDRVLQKS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 308 DGSYTYFTPDIAYHDYKFnKTNTTKLIDVWGTDHLGYIARLKAAMNALGYDPNNLEIVCAQVMKLVK-----------NN 376
Cdd:TIGR00456 305 DGTYLYLTTDIAYHLDKL-ERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnvislDN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 377 QEFKLSKRSGQSLTIK------DLVEIIGKDALRWFLGSSSMNSHVIIDVDIALSkNNNNPLYYVQYAHARANQVLNKQV 450
Cdd:TIGR00456 384 LLDEASKRAGNVITIKndleeeKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLS-FEGNTAPYIQYAHARICSILRKAE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 451 Y---ELDFKTDLLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKvLSAQRYTLV 527
Cdd:TIGR00456 463 IdgeKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENE-LAAARLALL 541
|
570 580
....*....|....*....|..
gi 493739754 528 WCVKQVLANGLAIMKITPYDQM 549
Cdd:TIGR00456 542 KATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
115-386 |
2.78e-66 |
|
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: 213.96 E-value: 2.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 115 TYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWINDAGNQIDKLAMSvlvrylqlqniniqlpadayh 194
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILS--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 195 gqeihlvaqtlyqtyknqfinvrlnekYEIDDDIANQEIKnfavkyllnEIKNDLASINTFIDTYTSENWIRN-SGRILE 273
Cdd:cd00671 60 ---------------------------LEKWRKLVEESIK---------ADLETYGRLDVRFDVWFGESSYLGlMGKVVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 274 VLSKiKPYTYTLDGALWLKTTTFGDDKDRVLIKSDGSYTYFTPDIAYHDYKFNkTNTTKLIDVWGTDHLGYIARLKAAMN 353
Cdd:cd00671 104 LLEE-LGLLYEEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|....
gi 493739754 354 ALGYD-PNNLEIVCAQVMKLVKnnqEFKLSKRSG 386
Cdd:cd00671 182 LLGYDeAKKLEHLLYGMVNLPK---EGKMSTRAG 212
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
435-549 |
1.06e-36 |
|
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: 132.32 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 435 VQYAHARANQVLNK---QVYELDFKTD----LLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYA 507
Cdd:smart00836 1 VQYAHARICSILRKageAGETLPDIADadlsLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 493739754 508 NVKINNDNNKVLSAQRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:smart00836 81 RVRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
435-549 |
1.82e-34 |
|
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: 125.84 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 435 VQYAHARANQVLNK---QVYELDFKTDLLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKI 511
Cdd:pfam05746 1 LQYAHARICSILRKageLGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 493739754 512 NNDNNKVLsAQRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:pfam05746 81 LDEDNEER-NARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ArgS |
COG0018 |
Arginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Arginyl-tRNA ... |
2-549 |
3.24e-179 |
|
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: 517.01 E-value: 3.24e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 2 ITQKISEELNKALAKMGIhDTQETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQ-DLFLEVNLQPP 80
Cdd:COG0018 3 IKEELAEAIAAALAALGA-GLEEPDILVERPKDPEHGDYATNVAMQLAKPLKKNPREIAEEIAEALDAdPLVEKVEIAGP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 81 GFLNFKLKAKDHENLLKQIYYEKDRFGQF-SKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYW 159
Cdd:COG0018 82 GFINFFLSPAALAAVLKEILADGEDYGRSdAGKGKKVVVEYVSANPTKPLHVGHLRGAVIGDALARILEAAGYDVTRENY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 160 INDAGNQIDKLAMSVLvRYLQlQNINIQLPADAYHGQeihlvaqtLYQTYKNQFINV--------RLNEKYEiDDDIANQ 231
Cdd:COG0018 162 INDAGTQIGKLALSLE-RYGE-EEIEPESKPDGYLGD--------LYVKFHKEYEEDpelediarELLAKLE-PGDEEAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 232 EIKNFAVKYLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKI--KPYTYTLDGALWLKTTTFGDDKDRVLIKSDG 309
Cdd:COG0018 231 ELWKKAVDWSLEEIKEDLKRLGVEFDVWFSESSLYDSGAVEEVVEELkeKGLLYESDGALWVRLTEFGDDKDRVLVKSDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 310 SYTYFTPDIAYHDYKFNKTNTTKLIDVWGTDHLGYIARLKAAMNALGYDP-NNLEIVCAQVMKLvKNNQefKLSKRSGQS 388
Cdd:COG0018 311 TYTYFTTDIAYHLYKFERYGFDRVIYVVGADQHGHFKRLFAALKALGYDPaKDLEHLLFGMVNL-RDGE--KMSTRAGTV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 389 LTIKDLVE-----------------------IIGKDALRWFLGSSSMNSHVIIDVDIALS-KNNNNPlyYVQYAHARANQ 444
Cdd:COG0018 388 VTLDDLLDeaverareiieekseeekeeiaeQVGIDAVRYFDLSRSRDKDLDFDLDLALSfEGNTNP--YVQYAHARICS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 445 VLNKQVYELDFKTD----LLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKVLS 520
Cdd:COG0018 466 ILRKAGEELDGLAEadlsLLTEEEELALIKKLAQFPEVVEEAAEDLEPHRIANYLYELAKAFHSFYNACRILKAEDEELR 545
|
570 580
....*....|....*....|....*....
gi 493739754 521 AQRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:COG0018 546 AARLALVAATAQVLKNGLGLLGISAPERM 574
|
|
| argS |
PRK01611 |
arginyl-tRNA synthetase; Reviewed |
1-549 |
1.54e-177 |
|
arginyl-tRNA synthetase; Reviewed
Pssm-ID: 234964 [Multi-domain] Cd Length: 507 Bit Score: 510.08 E-value: 1.54e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 1 MITQKISEELNKALAKMGIHDTQEtkILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEqdlflEVNLQPP 80
Cdd:PRK01611 4 DIKELLAEALAAALEAGGLPELPA--VLIERPKDPEHGDYATNVAMQLAKKLKKNPREIAEEIVEAIE-----KVEIAGP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 81 GFLNFKLKAKDHENLLKQIYYEKDRFGQF-SKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYW 159
Cdd:PRK01611 77 GFINFFLDPAALAELVLAILEAGERYGRSdIGKGKKVVVEYVSANPTGPLHVGHLRSAVIGDALARILEFAGYDVTREYY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 160 INDAGNQIDKLAMSVlvrylqlqniniqlpadayhgqeihlvaqtlyqtyknqfinvrlnekyeidddianQEIKNFAVK 239
Cdd:PRK01611 157 VNDAGTQIGMLIASL--------------------------------------------------------ELLWRKAVD 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 240 YLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKI--KPYTYTL-DGALWLKTTTFGDDKDRVLIKSDGSYTYFTP 316
Cdd:PRK01611 181 ISLDEIKEDLDRLGVHFDVWFSESELYYNGKVDEVVEDLkeKGLLYVEsDGALWVRLTEFGDDKDRVLIKSDGTYTYFTR 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 317 DIAYHDYKFNKTNttKLIDVWGTDHLGYIARLKAAMNALGYDPNNLEIVCAQVMKLVKNNQEFKLSKRSGQSLTIKDLVE 396
Cdd:PRK01611 261 DIAYHLYKFERFD--RVIYVVGADHHGHFKRLKAALKALGYDPDALEVLLHQMVGLVRGGEGVKMSTRAGNVVTLDDLLD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 397 -----------------IIGKDALRWFLGSSSMNSHVIIDVDIALSKNNNNPLyYVQYAHARANQVLNK-QVYELDFKTD 458
Cdd:PRK01611 339 eavgrarelieekeiaeAVGIDAVRYFDLSRSRDKDLDFDLDLALSFEGNNPP-YVQYAHARICSILRKaAEAGIDLLLA 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 459 LLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKVLSAqRYTLVWCVKQVLANGL 538
Cdd:PRK01611 418 LLTEEEEKELIKKLAEFPEVVESAAEELEPHRIANYLYELAGAFHSFYNRVLLKDEEEELRNA-RLALVKATAQVLKNGL 496
|
570
....*....|.
gi 493739754 539 AIMKITPYDQM 549
Cdd:PRK01611 497 DLLGISAPERM 507
|
|
| argS |
TIGR00456 |
arginyl-tRNA synthetase; This model recognizes arginyl-tRNA synthetase in every completed ... |
2-549 |
1.46e-135 |
|
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: 405.19 E-value: 1.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 2 ITQKISEELNKALAKMGIHDtqETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQDLFLEVNLQPPG 81
Cdd:TIGR00456 1 IKTLLKEEISQALLKAGLSK--ESEILVEETPNPEFGDYASNIAFPLAKVLKKAPRQIAEEIVLKLKTGEIIEKVEAAGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 82 FLNFKLKAKDH-ENLLKQIYYEKDRFGQFSKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWI 160
Cdd:TIGR00456 79 FINFFLSPQKLlERLIQKILTQKEKYGSKKLKNKKIIIEFSSANPAGPLHVGHLRNAIIGDSLARILEFLGYDVIREYYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 161 NDAGNQIDKLAMSVLVRYLQLQNINIQLPADAYHGQEIHlvaqtlyqtyknqfINVRLNEKYEIDD------------DI 228
Cdd:TIGR00456 159 NDWGRQFGLLALGVEKFGNEALNIAVKKPDHGLEGFYVE--------------INKRLEENEELEEearelfvklesgDE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 229 ANQEIKNFAVKYLLNEIKNDLASINTFIDTYTSENWIRNSGRILEVLSKIKPYTYTL-DGALWLKTTTFGDDKDRVLIKS 307
Cdd:TIGR00456 225 ETIKLWKRLVEYSLEGIKETYDRLNIHFDSFVWEGESVKNGMLPKVLEDLKEKGLVVeDGALWLDLTLFGDKKDRVLQKS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 308 DGSYTYFTPDIAYHDYKFnKTNTTKLIDVWGTDHLGYIARLKAAMNALGYDPNNLEIVCAQVMKLVK-----------NN 376
Cdd:TIGR00456 305 DGTYLYLTTDIAYHLDKL-ERGFDKMIYVWGSDHHLHIAQMFAILEKLGYKKKELEHLNFGMVPLYSmktrrgnvislDN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 377 QEFKLSKRSGQSLTIK------DLVEIIGKDALRWFLGSSSMNSHVIIDVDIALSkNNNNPLYYVQYAHARANQVLNKQV 450
Cdd:TIGR00456 384 LLDEASKRAGNVITIKndleeeKVADAVGIGAVRYFDLSKNRTTDYVFDWDAMLS-FEGNTAPYIQYAHARICSILRKAE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 451 Y---ELDFKTDLLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKvLSAQRYTLV 527
Cdd:TIGR00456 463 IdgeKLIADDFELLEEKEKELLKLLLQFPEVLEEAAEELEPHVLTNYLYELASLFSSFYKACPVLDAENE-LAAARLALL 541
|
570 580
....*....|....*....|..
gi 493739754 528 WCVKQVLANGLAIMKITPYDQM 549
Cdd:TIGR00456 542 KATRQTLKNGLDLLGIEPPERM 563
|
|
| ArgRS_core |
cd00671 |
catalytic core domain of arginyl-tRNA synthetases; Arginyl tRNA synthetase (ArgRS) catalytic ... |
115-386 |
2.78e-66 |
|
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: 213.96 E-value: 2.78e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 115 TYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWINDAGNQIDKLAMSvlvrylqlqniniqlpadayh 194
Cdd:cd00671 1 KILVEFVSANPTGPLHVGHLRNAIIGDSLARILEFLGYDVTREYYINDWGRQIGLLILS--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 195 gqeihlvaqtlyqtyknqfinvrlnekYEIDDDIANQEIKnfavkyllnEIKNDLASINTFIDTYTSENWIRN-SGRILE 273
Cdd:cd00671 60 ---------------------------LEKWRKLVEESIK---------ADLETYGRLDVRFDVWFGESSYLGlMGKVVE 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 274 VLSKiKPYTYTLDGALWLKTTTFGDDKDRVLIKSDGSYTYFTPDIAYHDYKFNkTNTTKLIDVWGTDHLGYIARLKAAMN 353
Cdd:cd00671 104 LLEE-LGLLYEEDGALWLDLTEFGDDKDRVLVRSDGTYTYFTRDIAYHLDKFE-RGADKIIYVVGADHHGHFKRLFAALE 181
|
250 260 270
....*....|....*....|....*....|....
gi 493739754 354 ALGYD-PNNLEIVCAQVMKLVKnnqEFKLSKRSG 386
Cdd:cd00671 182 LLGYDeAKKLEHLLYGMVNLPK---EGKMSTRAG 212
|
|
| Anticodon_Ia_Arg |
cd07956 |
Anticodon-binding domain of arginyl tRNA synthetases; This domain is found in arginyl tRNA ... |
396-549 |
5.94e-37 |
|
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: 134.26 E-value: 5.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 396 EIIGKDALRWFLGSSSMNSHVIIDVDIALSKNNNnPLYYVQYAHARANQVLNKQVYELDFKTD----LLTETRERELLNQ 471
Cdd:cd07956 1 EEVGVGAVKYQDLSNKRIKDYTFDWERMLSFEGD-TGPYLQYAHARLCSILRKAGETIEAEADadlsLLPEPDERDLILL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493739754 472 LHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKINNDNNKVLSAqRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:cd07956 80 LAKFPEVVKNAAETLEPHTIATYLFDLAHAFSKFYNACPVLGAEEELRNA-RLALVAAARQVLANGLDLLGIEAPERM 156
|
|
| DALR_1 |
smart00836 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
435-549 |
1.06e-36 |
|
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: 132.32 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 435 VQYAHARANQVLNK---QVYELDFKTD----LLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYA 507
Cdd:smart00836 1 VQYAHARICSILRKageAGETLPDIADadlsLLTEPEEWALLLKLARFPEVLEAAAEQLEPHRLANYLYDLAAAFHSFYN 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 493739754 508 NVKINNDNNKVLSAQRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:smart00836 81 RVRVLGEENPELRKARLALLKAVRQVLANGLRLLGISAPERM 122
|
|
| DALR_1 |
pfam05746 |
DALR anticodon binding domain; This all alpha helical domain is the anticodon binding domain ... |
435-549 |
1.82e-34 |
|
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: 125.84 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 435 VQYAHARANQVLNK---QVYELDFKTDLLTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYYANVKI 511
Cdd:pfam05746 1 LQYAHARICSILRKageLGINLDIDADLLTEEEEKELLKALLQFPEVLEEAAEELEPHRLANYLYELASAFHSFYNNCRV 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 493739754 512 NNDNNKVLsAQRYTLVWCVKQVLANGLAIMKITPYDQM 549
Cdd:pfam05746 81 LDEDNEER-NARLALLKAVRQVLKNGLDLLGIEAPEKM 117
|
|
| Arg_tRNA_synt_N |
pfam03485 |
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of ... |
6-87 |
4.36e-21 |
|
Arginyl tRNA synthetase N terminal domain; This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition.
Pssm-ID: 460943 [Multi-domain] Cd Length: 83 Bit Score: 87.29 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 6 ISEELNKALAKMGIHDTQETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQ-DLFLEVNLQPPGFLN 84
Cdd:pfam03485 1 LKKAIAKALSKLGGPDLELIDIVIETPKNPKFGDYATNVAMQLAKKLKKNPREIAEEIAEKLEKsDIIEKVEVAGPGFIN 80
|
...
gi 493739754 85 FKL 87
Cdd:pfam03485 81 FFL 83
|
|
| Arg_tRNA_synt_N |
smart01016 |
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl ... |
2-87 |
6.90e-18 |
|
Arginyl tRNA synthetase N terminal dom; This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition.
Pssm-ID: 214975 [Multi-domain] Cd Length: 85 Bit Score: 78.40 E-value: 6.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 2 ITQKISEELNKALAKMGIhdtqETKILVDKTKNIKFGDFYTNIAMILSKKNNKSSLEIAKEIANNFEQ-DLFLEVNLQPP 80
Cdd:smart01016 3 LKEAIAEALKKALGVEGE----PIDIALERPKDPDHGDYATNVAFRLAKKLKKNPRELAEEIAEKLPKsDLVEKVEIAGP 78
|
....*..
gi 493739754 81 GFLNFKL 87
Cdd:smart01016 79 GFINFFL 85
|
|
| PLN02286 |
PLN02286 |
arginine-tRNA ligase |
21-513 |
1.32e-15 |
|
arginine-tRNA ligase
Pssm-ID: 215160 [Multi-domain] Cd Length: 576 Bit Score: 79.69 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 21 DTQETKILVDKTKNIKFGDFYTNIAM----ILSKKNN--KSSLEIAKEIANNF-EQDLFLEVNLQPPGFLNFKLKAKD-H 92
Cdd:PLN02286 17 DEPSVEPLVAACTNPKFGDYQCNNAMglwsKLKGKGTsfKNPRAVAQAIVKNLpASEMIESTSVAGPGFVNVRLSASWlA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 93 ENLLKQIYYEKDRFG-QFSKKNITynIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWINDAGNQidkLA 171
Cdd:PLN02286 97 KRIERMLVDGIDTWApTLPVKRAV--VDFSSPNIAKEMHVGHLRSTIIGDTLARMLEFSGVEVLRRNHVGDWGTQ---FG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 172 MsvLVRYLqlqniniqlpADAY-HGQEIHLVA----QTLYQTYKNQFIN------------VRL---NEKY----EIDDD 227
Cdd:PLN02286 172 M--LIEHL----------FEKFpNWESVSDQAigdlQEFYKAAKKRFDEdeefkaraqqavVRLqggDPEYraawAKICE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 228 IANQEiknFAVKY-LLN-EIKNDLASI-NTFIDTYTSEnwIRNSGRILEVlskikpytytlDGAlwlkTTTFGDDKDRVL 304
Cdd:PLN02286 240 ISRRE---FEKVYqRLRvELEEKGESFyNPYIPGVIEE--LESKGLVVES-----------DGA----RVIFVEGFDIPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 305 I--KSDGSYTYFTPDIAYHDYKFNKTNTTKLI---DVWGTDHLGYIarLKAAMNAlGYDPNNLEIVCAQV-MKLVKNNQE 378
Cdd:PLN02286 300 IvvKSDGGFNYASTDLAALWYRLNEEKAEWIIyvtDVGQQQHFDMV--FKAAKRA-GWLPEDTYPRLEHVgFGLVLGEDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 379 FKLSKRSGQSLTIKDLV---EIIGKDALRWFLGSSSMNSHVIIDVDIALS---------KNN----------------NN 430
Cdd:PLN02286 377 KRFRTRSGEVVRLVDLLdeaKSRSKAALIERGKDSEWTPEELEQAAEAVGygavkyadlKNNrltnytfsfdqmldlkGN 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 431 PLYYVQYAHARANQVL---NKQVYELDFKTDL-LTETRERELLNQLHFYKQTIANAANNREPHRISNYLYDLAQIFHNYY 506
Cdd:PLN02286 457 TAVYLLYAHARICSIIrksGKDIDELKKTGKIvLDHPDERALGLHLLQFPEVVEEACTDLLPNRLCEYLYNLSEKFTKFY 536
|
....*..
gi 493739754 507 ANVKINN 513
Cdd:PLN02286 537 SNCKVNG 543
|
|
| tRNA-synt_1d |
pfam00750 |
tRNA synthetases class I (R); Other tRNA synthetase sub-families are too dissimilar to be ... |
104-404 |
7.03e-10 |
|
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: 60.66 E-value: 7.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 104 DRFGQFSKKNITYNIEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWINDAGNQIDKLAMSvLVRYLQ--- 180
Cdd:pfam00750 9 KGLGKASREKKKVVVDFSSPNIAKEMHVGHLRSTIIGDALSRLLEFLGHSVIRANHVGDWGTQFGMLIAG-LEKYQDekt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 181 LQNINIQLPADAYHGQEIHLVAQTLYQTYKNQFInVRLNEKyeiDDDIanQEIKNFAVKYLLNEIKNDLASINTFIdTYT 260
Cdd:pfam00750 88 LQEMPIQDLEDFYREAKKHYDEEEEFAERARNYV-VKLQSG---DEYW--RRMWKLIVDITMTQNQRLYDRLDVTL-TEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493739754 261 SENWIRNS-GRILEVLSKiKPYTYTLDGALWLKTTTFGDDKDRVLIKSDGSYTYFTPDIAYHDYKFNKTNTTKLIDVWGT 339
Cdd:pfam00750 161 GESLYNPMmNEIVKDFKK-NGLVVEIDGALVVFLDEFGKPMGVIVQKSDGGYLYTTTDIAAAKYRYETLHADRMLYVIDS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493739754 340 DHLGYIARLKAAMNALGYDPNNLEIVCAQV-MKLVKNNQEFKlsKRSGQSLTIKDLVEIIGKDALR 404
Cdd:pfam00750 240 RQSQHMQQAFAILRKAGYVPESKDLEHINFgMVLGKDGKPFK--TRKGGTVKLADLLDEALERALQ 303
|
|
| class_I_aaRS_core |
cd00802 |
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ... |
118-171 |
8.33e-04 |
|
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: 39.77 E-value: 8.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 493739754 118 IEYVSANPTGYLHIAHAANAIYGDILANLLKIYGYDVETEYWINDAGNQIDKLA 171
Cdd:cd00802 1 TTFSGITPNGYLHIGHLRTIVTFDFLAQAYRKLGYKVRCIALIDDAGGLIGDPA 54
|
|
| |
