|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00326 |
PTZ00326 |
phenylalanyl-tRNA synthetase alpha chain; Provisional |
1-484 |
0e+00 |
|
phenylalanyl-tRNA synthetase alpha chain; Provisional
Pssm-ID: 240361 [Multi-domain] Cd Length: 494 Bit Score: 769.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 1 MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARV 80
Cdd:PTZ00326 2 MQKELEENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 81 FRSIPPEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKER 156
Cdd:PTZ00326 81 WQKLKEGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 157 SELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQ 236
Cdd:PTZ00326 161 KELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 237 IFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNW 314
Cdd:PTZ00326 241 ILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 315 KLDEARKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGV 390
Cdd:PTZ00326 321 KLEEARKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 391 LREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYG 470
Cdd:PTZ00326 401 IREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYG 480
|
490
....*....|....
gi 13676326 471 INNIRELVGHKVNL 484
Cdd:PTZ00326 481 IKNIRDLFGHKVDL 494
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
209-483 |
7.71e-116 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 341.48 E-value: 7.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 209 PYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlql 288
Cdd:pfam01409 1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 289 pmdyvqrvkrthsqggygsqgykynwkldEARKNLLRTHTTSASARALYrlaqKKPFTPVKYFSIDRVFRNETLDATHLA 368
Cdd:pfam01409 77 -----------------------------VARRLLLRTHTTPVQARTLA----KKPKPPIKIFSIGRVFRRDQVDATHLP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 369 EFHQIEGVVADHGLTLGHLMGVLREFFTKL-GIT-QLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPM 446
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 13676326 447 GLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVN 483
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLR 240
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
225-483 |
1.64e-115 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 339.52 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 225 HPLLKVRSQFRQIFLEMGFTEMPTdNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAealqlpmdyvqrvkrthsqgg 304
Cdd:cd00496 1 HPLNKVIEEIEDIFVSMGFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 305 ygsqgykynwkldearKNLLRTHTTSASARALYRLaqkkpFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTL 384
Cdd:cd00496 59 ----------------RLLLRTHTSAVQARALAKL-----KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 385 GHLMGVLREFFTKLG--ITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLE 462
Cdd:cd00496 118 ADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLE 197
|
250 260
....*....|....*....|.
gi 13676326 463 RPTMIKYGINNIRELVGHKVN 483
Cdd:cd00496 198 RLAMLKYGIPDIRLFYSNDLR 218
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
190-482 |
2.74e-109 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 326.58 E-value: 2.74e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 190 TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHP 269
Cdd:TIGR00468 37 TKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDIFLGLGFTEET-GPEVETDFWNFDALNIPQDHP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 270 ARDQHDTFFLRDpaealqlpmdyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrlaQKKPFTPVK 349
Cdd:TIGR00468 116 ARDMQDTFYIKD---------------------------------------RLLLRTHTTAVQLRTM----EEQEKPPIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 350 YFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKL-GITQLRFKPAYNPYTEPSMEVFSYHQGLKK 428
Cdd:TIGR00468 153 IFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13676326 429 WVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 482
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRDLYENDL 286
|
|
| PheS |
COG0016 |
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ... |
216-478 |
4.38e-57 |
|
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439787 [Multi-domain] Cd Length: 339 Bit Score: 192.96 E-value: 4.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 216 GVLPDSGHLHPLLKVRSQFRQIFLEMGFT-----EmptdnfIESSFWNFDALFQPQQHPARDQHDTFFLRDpaealqlpm 290
Cdd:COG0016 98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaegpE------IETDWYNFEALNIPPDHPARDMQDTFYIDD--------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 291 dyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrLAQKkpfTPVKYFSIDRVFRNETLDATHLAEF 370
Cdd:COG0016 163 ------------------------------GLLLRTHTSPVQIRTM--EKQK---PPIRIIAPGRVYRRDESDATHSPMF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 371 HQIEGVVADHGLTLGHLMGVLREFFTKL-GI-TQLRFKPAYNPYTEPSMEV-FSYHQGLKK---------WVEVGNSGVF 438
Cdd:COG0016 208 HQVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFICGGKgcrvckgtgWLEILGCGMV 287
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 13676326 439 RPEMLLPMGL-PENVSVIAWGLSLERPTMIKYGINNIRELV 478
Cdd:COG0016 288 HPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00326 |
PTZ00326 |
phenylalanyl-tRNA synthetase alpha chain; Provisional |
1-484 |
0e+00 |
|
phenylalanyl-tRNA synthetase alpha chain; Provisional
Pssm-ID: 240361 [Multi-domain] Cd Length: 494 Bit Score: 769.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 1 MADGQVAELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARV 80
Cdd:PTZ00326 2 MQKELEENTILSKLESENEIVNSLALAESLNIDHQKVVGAIKSLESAN-YITTEMKKSNTWTLTEEGEDYLKNGSPEYRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 81 FRSIPPEGLAQSELMRLPSG---KVGFSKAMSNKWIRVDKSAADGPRVFRVVDSMEDEVQRRLQLV-RGGQAEKLGEKER 156
Cdd:PTZ00326 81 WQKLKEGGISKADDAKKLGGkvaDIGLGNAMKKKWIKLNKGDKKVFLSRKLVDSVVDTVRLLLKIVaKGSQAEKIDSKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 157 SELRKRKLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQ 236
Cdd:PTZ00326 161 KELKKRKLATLEKIKYFVVTKGPKFAKEIKKQITDLTQEMLLNGSWKNAEFKEYNFNALGKKIGGGNLHPLLKVRREFRE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 237 IFLEMGFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPA--EALQLPMDYVQRVKRTHSQGGYGSQGYKYNW 314
Cdd:PTZ00326 241 ILLEMGFEEMPTNRYVESSFWNFDALFQPQQHPARDAQDTFFLSKPEtsKVNDLDDDYVERVKKVHEVGGYGSIGWRYDW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 315 KLDEARKNLLRTHTTSASARALYRLAQ----KKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGV 390
Cdd:PTZ00326 321 KLEEARKNILRTHTTAVSARMLYKLAQeykkTGPFKPKKYFSIDRVFRNETLDATHLAEFHQVEGFVIDRNLTLGDLIGT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 391 LREFFTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYG 470
Cdd:PTZ00326 401 IREFFRRIGITKLRFKPAFNPYTEPSMEIFGYHPGLKKWVEVGNSGIFRPEMLRPMGFPEDVTVIAWGLSLERPTMIKYG 480
|
490
....*....|....
gi 13676326 471 INNIRELVGHKVNL 484
Cdd:PTZ00326 481 IKNIRDLFGHKVDL 494
|
|
| PLN02853 |
PLN02853 |
Probable phenylalanyl-tRNA synthetase alpha chain |
8-496 |
0e+00 |
|
Probable phenylalanyl-tRNA synthetase alpha chain
Pssm-ID: 215458 [Multi-domain] Cd Length: 492 Bit Score: 768.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 8 ELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPE 87
Cdd:PLN02853 6 EALLGALSNNEEISDSGQFAASHGLDHNEVVGVIKSLHGFR-YVDAQDIKRETWVLTEEGKKYAAEGSPEVQLFAAVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 88 G-LAQSELMRL--PS-GKVGFSKAMSNKWIRVDKsaadGPRVFRVVDSMEDEVQRRLQLVRGGQAekLGEKERSEL-RKR 162
Cdd:PLN02853 85 GsISKDELQKKldPAvFDIGFKQAMKNKWLEMGG----KPQVSRKVQHVEDEVKELLLAIQEGKE--VDDKDIDALkKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 163 KLLAEVTLKTYWVSKGSAFSTSISKQETELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMG 242
Cdd:PLN02853 159 KLITLETWKGYSIKKGPNYAPERKKAATDLTREMLQSGDWKDLEFKEYNFNALGAPPEGGHLHPLLKVRQQFRKIFLQMG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 243 FTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEALQLPMDYVQRVKRTHSQGGYGSQGYKYNWKLDEARKN 322
Cdd:PLN02853 239 FEEMPTNNFVESSFWNFDALFQPQQHPARDSHDTFFLKAPATTRQLPEDYVERVKTVHESGGYGSIGYGYDWKREEANKN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 323 LLRTHTTSASARALYRLAQKkPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKLGITQ 402
Cdd:PLN02853 319 LLRTHTTAVSSRMLYKLAQK-GFKPKRYFSIDRVFRNEAVDRTHLAEFHQVEGLVCDRGLTLGDLIGVLEDFFSRLGMTK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 403 LRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 482
Cdd:PLN02853 398 LRFKPAYNPYTEPSMEIFSYHEGLKKWVEVGNSGMFRPEMLLPMGLPEDVNVIAWGLSLERPTMILYGIDNIRDLFGHKV 477
|
490
....*....|....
gi 13676326 483 NLQMVYDSPLCRLD 496
Cdd:PLN02853 478 DLGLIKRNPICRLG 491
|
|
| pheS |
PRK04172 |
phenylalanine--tRNA ligase subunit alpha; |
10-477 |
6.80e-156 |
|
phenylalanine--tRNA ligase subunit alpha;
Pssm-ID: 235239 [Multi-domain] Cd Length: 489 Bit Score: 452.75 E-value: 6.80e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 10 LLRRLEASDGgLDSAELAAELGMEHQAVVGAVKSLQALGeVIEAELRSTKHWELTAEGEEIAREGSHEARVFRSIPPEG- 88
Cdd:PRK04172 11 VLKALKELKE-ATLEELAEKLGLPPEAVMRAAEWLEEKG-LVKVEERVEEVYVLTEEGKKYAEEGLPERRLLNALKDGGe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 89 LAQSELMRLPSGKVGFSKAMSN----KWIRVDKSaadgpRVFRVVDSMEDEVQRRLQLVRGGQAEKLGEKER---SELRK 161
Cdd:PRK04172 89 VSLDELKEALLDKKEVGIALGNlarkGWAKIEKG-----KVILKPDAYEDPEEKALKALAEGDKEELSEEDLkvlKELKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 162 RKLLAEVTLKTYWVS---KG-SAFSTSISKQE--TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFR 235
Cdd:PRK04172 164 RKLVEEKERTERSVEltdAGlELLKEGIELKEeiTQLTPELLKSGEWKEKEFRPYNVKAPPPKIYPGKKHPYREFIDEVR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 236 QIFLEMGFTEMpTDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlQLPMDYVQRVKRTHSQGG-YGSQGYKYNW 314
Cdd:PRK04172 244 DILVEMGFEEM-KGPLVETEFWNFDALFQPQDHPAREMQDTFYLKYPGIG-DLPEELVERVKEVHEHGGdTGSRGWGYKW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 315 KLDEARKNLLRTHTTSASARALYRLAQKkpftPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREF 394
Cdd:PRK04172 322 DEDIAKRLVLRTHTTALSARYLASRPEP----PQKYFSIGRVFRPDTIDATHLPEFYQLEGIVMGEDVSFRDLLGILKEF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 395 FTKLGITQLRFKPAYNPYTEPSMEVFSYHQGLkKWVEVGNSGVFRPEMLLPMGLpeNVSVIAWGLSLERPTMIKYGINNI 474
Cdd:PRK04172 398 YKRLGFEEVKFRPAYFPFTEPSVEVEVYHEGL-GWVELGGAGIFRPEVLEPLGI--DVPVLAWGLGIERLAMLRLGLDDI 474
|
...
gi 13676326 475 REL 477
Cdd:PRK04172 475 RDL 477
|
|
| tRNA-synt_2d |
pfam01409 |
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too ... |
209-483 |
7.71e-116 |
|
tRNA synthetases class II core domain (F); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only phenylalanyl-tRNA synthetases. This is the core catalytic domain.
Pssm-ID: 396130 [Multi-domain] Cd Length: 245 Bit Score: 341.48 E-value: 7.71e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 209 PYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAEAlql 288
Cdd:pfam01409 1 PYDVTLPGRRIEPGGLHPLTRTLERIRDIFLGMGFEEVE-GPEVESDFYNFDALNIPQDHPARDMQDTFYLKKPLKP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 289 pmdyvqrvkrthsqggygsqgykynwkldEARKNLLRTHTTSASARALYrlaqKKPFTPVKYFSIDRVFRNETLDATHLA 368
Cdd:pfam01409 77 -----------------------------VARRLLLRTHTTPVQARTLA----KKPKPPIKIFSIGRVFRRDQVDATHLP 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 369 EFHQIEGVVADHGLTLGHLMGVLREFFTKL-GIT-QLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPM 446
Cdd:pfam01409 124 EFHQVEGLVVDENVTFADLKGVLEEFLRKFfGFEvKVRFRPSYFPFTEPSAEVDVYVCKLGGWLEVGGAGMVHPNVLEAV 203
|
250 260 270
....*....|....*....|....*....|....*..
gi 13676326 447 GLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKVN 483
Cdd:pfam01409 204 GIDEDYSGFAFGLGVERLAMLKYGIDDIRDLYENDLR 240
|
|
| PheRS_alpha_core |
cd00496 |
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class ... |
225-483 |
1.64e-115 |
|
Phenylalanyl-tRNA synthetase (PheRS) alpha chain catalytic core domain. PheRS belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure and the presence of three characteristic sequence motifs. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. While class II aaRSs generally aminoacylate the 3'-OH 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. PheRS is an alpha-2/ beta-2 tetramer.
Pssm-ID: 238277 [Multi-domain] Cd Length: 218 Bit Score: 339.52 E-value: 1.64e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 225 HPLLKVRSQFRQIFLEMGFTEMPTdNFIESSFWNFDALFQPQQHPARDQHDTFFLRDPAealqlpmdyvqrvkrthsqgg 304
Cdd:cd00496 1 HPLNKVIEEIEDIFVSMGFTEVEG-PEVETDFYNFDALNIPQDHPARDMQDTFYINDPA--------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 305 ygsqgykynwkldearKNLLRTHTTSASARALYRLaqkkpFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTL 384
Cdd:cd00496 59 ----------------RLLLRTHTSAVQARALAKL-----KPPIRIFSIGRVYRNDEIDATHLPEFHQIEGLVVDKGLTF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 385 GHLMGVLREFFTKLG--ITQLRFKPAYNPYTEPSMEVFSYHQGLKKWVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLE 462
Cdd:cd00496 118 ADLKGTLEEFAKELFgpITKVRFRPSYFPFTEPSFEVDVYCPGCLGWLEILGCGMVRPEVLENAGIDEEYSGFAFGIGLE 197
|
250 260
....*....|....*....|.
gi 13676326 463 RPTMIKYGINNIRELVGHKVN 483
Cdd:cd00496 198 RLAMLKYGIPDIRLFYSNDLR 218
|
|
| pheS |
TIGR00468 |
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are ... |
190-482 |
2.74e-109 |
|
phenylalanyl-tRNA synthetase, alpha subunit; Most phenylalanyl-tRNA synthetases are heterodimeric, with 2 alpha (pheS) and 2 beta (pheT) subunits. This model describes the alpha subunit, which shows some similarity to class II aminoacyl-tRNA ligases. Mitochondrial phenylalanyl-tRNA synthetase is a single polypeptide chain, active as a monomer, and similar to this chain rather than to the beta chain, but excluded from this model. An interesting feature of the alignment of all sequences captured by this model is a deep split between non-spirochete bacterial examples and all other examples; supporting this split is a relative deletion of about 50 residues in the former set between two motifs well conserved throughout the alignment. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273095 [Multi-domain] Cd Length: 293 Bit Score: 326.58 E-value: 2.74e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 190 TELSPEMISSGSWRDRPFKPYNFLAHGVLPDSGHLHPLLKVRSQFRQIFLEMGFTEMPtDNFIESSFWNFDALFQPQQHP 269
Cdd:TIGR00468 37 TKLKPELESAGLWSKLKFETYDVSLPGTKIYPGSLHPLTRVIDEIRDIFLGLGFTEET-GPEVETDFWNFDALNIPQDHP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 270 ARDQHDTFFLRDpaealqlpmdyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrlaQKKPFTPVK 349
Cdd:TIGR00468 116 ARDMQDTFYIKD---------------------------------------RLLLRTHTTAVQLRTM----EEQEKPPIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 350 YFSIDRVFRNETLDATHLAEFHQIEGVVADHGLTLGHLMGVLREFFTKL-GITQLRFKPAYNPYTEPSMEVFSYHQGLKK 428
Cdd:TIGR00468 153 IFSPGRVFRNDTVDATHLPEFHQVEGLVIDKNISFTNLKGFLEEFLKKMfGETEIRFRPSYFPFTEPSAEIDVYCPEGKG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 13676326 429 WVEVGNSGVFRPEMLLPMGLPENVSVIAWGLSLERPTMIKYGINNIRELVGHKV 482
Cdd:TIGR00468 233 WLEVLGAGMFRPEVLEPMGIDPTYPGFAWGIGIERLAMLKYGITDIRDLYENDL 286
|
|
| PheS |
COG0016 |
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; ... |
216-478 |
4.38e-57 |
|
Phenylalanyl-tRNA synthetase alpha subunit [Translation, ribosomal structure and biogenesis]; Phenylalanyl-tRNA synthetase alpha subunit is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439787 [Multi-domain] Cd Length: 339 Bit Score: 192.96 E-value: 4.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 216 GVLPDSGHLHPLLKVRSQFRQIFLEMGFT-----EmptdnfIESSFWNFDALFQPQQHPARDQHDTFFLRDpaealqlpm 290
Cdd:COG0016 98 GRPRPLGSLHPLTQVIEEIEDIFVGMGFEvaegpE------IETDWYNFEALNIPPDHPARDMQDTFYIDD--------- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 291 dyvqrvkrthsqggygsqgykynwkldearKNLLRTHTTSASARALyrLAQKkpfTPVKYFSIDRVFRNETLDATHLAEF 370
Cdd:COG0016 163 ------------------------------GLLLRTHTSPVQIRTM--EKQK---PPIRIIAPGRVYRRDESDATHSPMF 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 371 HQIEGVVADHGLTLGHLMGVLREFFTKL-GI-TQLRFKPAYNPYTEPSMEV-FSYHQGLKK---------WVEVGNSGVF 438
Cdd:COG0016 208 HQVEGLVVDKGISFADLKGTLEEFAKAFfGEdVKVRFRPSYFPFTEPSAEVdISCFICGGKgcrvckgtgWLEILGCGMV 287
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 13676326 439 RPEMLLPMGL-PENVSVIAWGLSLERPTMIKYGINNIRELV 478
Cdd:COG0016 288 HPNVLRAVGIdPEEYSGFAFGMGIERLAMLKYGIDDIRLFF 328
|
|
| PheRS_DBD1 |
pfam18552 |
PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ... |
2-61 |
1.62e-24 |
|
PheRS DNA binding domain 1; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase (EC:6.1.1.20) N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNA-Phe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains.
Pssm-ID: 465796 [Multi-domain] Cd Length: 59 Bit Score: 96.10 E-value: 1.62e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 2 ADGQVAELLLRRLEAsDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAELRSTKHW 61
Cdd:pfam18552 1 MDKDLEEQILQYLEK-HGGVDSLDLAAELGVDHQKVVGAVKSLQALGDVITAEQRSSKHW 59
|
|
| PLN02788 |
PLN02788 |
phenylalanine-tRNA synthetase |
225-475 |
2.26e-19 |
|
phenylalanine-tRNA synthetase
Pssm-ID: 215422 [Multi-domain] Cd Length: 402 Bit Score: 90.21 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 225 HPLLKVRSQFRQIFLEM---GFTEMPTDNFIESSFWNFDALFQPQQHPARDQHDTFflrdpaealqlpmdYVQRvkrths 301
Cdd:PLN02788 68 HPLGILKNAIYDYFDENysnKFKKFDDLSPIVSTKQNFDDVLVPPDHVSRSYNDTY--------------YVDA------ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 302 qggygsqgykynwkldearKNLLRTHTTSASARALYRLAQKkpftpvkYFSIDRVFRNETLDATHLAEFHQIEGV----- 376
Cdd:PLN02788 128 -------------------QTVLRCHTSAHQAELLRAGHTH-------FLVTGDVYRRDSIDATHYPVFHQMEGVrvfsp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 377 --VADHGLTLGH---------LMGVLREFFtklGITQLRFKPAYNPYTEPSMEVFSYHQGlkKWVEVGNSGVFRPEMLLP 445
Cdd:PLN02788 182 eeWEASGLDGTDlaaedlkktLEGLARHLF---GDVEMRWVDAYFPFTNPSFELEIFFKG--EWLEVLGCGVTEQEILKN 256
|
250 260 270
....*....|....*....|....*....|..
gi 13676326 446 MGLPENVsviAW--GLSLERPTMIKYGINNIR 475
Cdd:PLN02788 257 NGRSDNV---AWafGLGLERLAMVLFDIPDIR 285
|
|
| PheRS_DBD3 |
pfam18553 |
PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ... |
75-131 |
1.07e-18 |
|
PheRS DNA binding domain 3; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. This domain belongs to a superfamily of 'winged helix' DNA-biding domains. The topology of DBD-1 and DBD-3 closely resembles the topology of the Z-DNA-binding domain Zalpha of double-stranded RNA (dsRNA) adenosine deaminase and other domains from DNA-binding proteins. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNAPhe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains.
Pssm-ID: 465797 [Multi-domain] Cd Length: 57 Bit Score: 79.62 E-value: 1.07e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 75 SHEARVFRSIPP-EGLAQSELMRL--PSGKVGFSKAMSNKWIRVDKsaaDGPRVFRVVDS 131
Cdd:pfam18553 1 SPEARVFNAVPPaGGISLKELMKLgdSVAKVGFGKAMKNKWIKKDK---GDGKVVRKVDS 57
|
|
| pheS_mito |
TIGR00469 |
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ... |
258-475 |
5.33e-10 |
|
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 129561 [Multi-domain] Cd Length: 460 Bit Score: 61.63 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 258 NFDALFQPQQHPARDQHDTFFlrdpaealqlpmdyvqrVKRTHsqggygsqgykynwkldearknLLRTHTTSASARALY 337
Cdd:TIGR00469 83 NFDNLGFPADHPGRQKSDCYY-----------------INEQH----------------------LLRAHTSAHELECFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 338 RLAQKKPFTPVKYFSIDRVFRNETLDATHLAEFHQIEGVV------ADHG---------------------------LTL 384
Cdd:TIGR00469 124 GGLDDSDNIKSGFLISADVYRRDEIDKTHYPVFHQADGAAirkrtkADLFekepgyiekfeedirgteadlnkenvkIIL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 385 GH------------------------------LMGVLREFFTK-------------LGITQLRFKPAYNPYTEPSMEVFS 421
Cdd:TIGR00469 204 DDdsiplkennpkqeyasdlavdlcehelkhsIEGITKDLFGKkissmiknkanntPKELKVRWIDAYFPFTAPSWEIEI 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 13676326 422 YHQGlkKWVEVGNSGVFRPEMLLPMGLPENVSV-IAWGLSLERPTMIKYGINNIR 475
Cdd:TIGR00469 284 WFKD--EWLELCGCGIIRHDILLRAGVHPSETIgWAFGLGLDRIAMLLFDIPDIR 336
|
|
| PheRS_DBD2 |
pfam18554 |
PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA ... |
134-166 |
7.81e-09 |
|
PheRS DNA binding domain 2; This is a DNA-binding fold domain found in Phenylalanyl-tRNA Synthetase N-terminal region. Mutational analysis indicate that DBD-1, 2 and 3 play critical roles in tRNA- Phe binding and recognition, i.e., from the drastic reduction of aminoacylation activity seen upon removal of the N-terminal domains. DBD-2 and DBD-3 constitute large insertions sequentially included between two neighboring antiparallel strands of the DBD-1 domain. Moreover, the DBD-3 pfam18553 is the domain insertion into DBD-2.
Pssm-ID: 465798 [Multi-domain] Cd Length: 33 Bit Score: 50.87 E-value: 7.81e-09
10 20 30
....*....|....*....|....*....|...
gi 13676326 134 DEVQRRLQLVRGGQAEKLGEKERSELRKRKLLA 166
Cdd:pfam18554 1 DEVQEQLKLIQEGKGDSLSDKVKNELKKRKLLQ 33
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
347-464 |
1.12e-06 |
|
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: 49.42 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 347 PVKYFSIDRVFRNE--TLDATHLAEFHQIEGVVA----DHGLTLGHLMGVLREFFTKLGIT-QLRFKPAYN-----PYTE 414
Cdd:cd00768 75 PLRLAEIGPAFRNEggRRGLRRVREFTQLEGEVFgedgEEASEFEELIELTEELLRALGIKlDIVFVEKTPgefspGGAG 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 13676326 415 PSMEVFSYHqGLKKWVEVGNSGVFRPE--------MLLPMGLPENVSVIAWGLSLERP 464
Cdd:cd00768 155 PGFEIEVDH-PEGRGLEIGSGGYRQDEqaraadlyFLDEALEYRYPPTIGFGLGLERL 211
|
|
| tRNA-synt_2 |
pfam00152 |
tRNA synthetases class II (D, K and N); |
349-434 |
1.15e-04 |
|
tRNA synthetases class II (D, K and N);
Pssm-ID: 425487 [Multi-domain] Cd Length: 318 Bit Score: 44.09 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 349 KYFSIDRVFRNETLDATHLAEFHQIEGVVADhgLTLGHLMGVLREFFTKL-----GITQLRFKPAYNPYTEPsMEVFSYH 423
Cdd:pfam00152 92 RVFQIARCFRDEDLRTDRQPEFTQLDLEMSF--VDYEDVMDLTEELIKEIfkeveGIAKELEGGTLLDLKKP-FPRITYA 168
|
90
....*....|.
gi 13676326 424 QGLKKWVEVGN 434
Cdd:pfam00152 169 EAIEKLNGKDV 179
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
8-54 |
1.05e-03 |
|
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
Pssm-ID: 429896 [Multi-domain] Cd Length: 52 Bit Score: 37.03 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 13676326 8 ELLLRRLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVIEAE 54
Cdd:pfam08279 1 LQILQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEAE 47
|
|
| MntR |
COG1321 |
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription]; |
13-73 |
1.11e-03 |
|
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
Pssm-ID: 440932 [Multi-domain] Cd Length: 135 Bit Score: 39.42 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13676326 13 RLEASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVieaELRSTKHWELTAEGEEIARE 73
Cdd:COG1321 17 ELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLV---EYEPYGGITLTEEGRELALR 74
|
|
| MarR |
COG1846 |
DNA-binding transcriptional regulator, MarR family [Transcription]; |
10-91 |
2.91e-03 |
|
DNA-binding transcriptional regulator, MarR family [Transcription];
Pssm-ID: 441451 [Multi-domain] Cd Length: 142 Bit Score: 38.03 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 10 LLRRLeASDGGLDSAELAAELGMEHQAVVGAVKSLQALGEVI----EAELRSTKHwELTAEGEEIARE-----GSHEARV 80
Cdd:COG1846 43 VLAAL-AEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVErepdPEDRRAVLV-RLTEKGRALLEEarpalEALLAEL 120
|
90
....*....|.
gi 13676326 81 FRSIPPEGLAQ 91
Cdd:COG1846 121 LAGLSEEELEA 131
|
|
| MarR_2 |
pfam12802 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
9-50 |
5.57e-03 |
|
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.
Pssm-ID: 432797 [Multi-domain] Cd Length: 60 Bit Score: 35.26 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 13676326 9 LLLRRLEASdGGLDSAELAAELGMEHQAVVGAVKSLQALGEV 50
Cdd:pfam12802 9 RVLLALARN-PGLTVAELARRLGISKQTVSRLVKRLEAKGLV 49
|
|
| LysRS_core |
cd00775 |
Lys_tRNA synthetase (LysRS) class II core domain. Class II LysRS is a dimer which attaches a ... |
349-428 |
9.55e-03 |
|
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: 38.33 E-value: 9.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13676326 349 KYFSIDRVFRNETLDATHLAEFHQIEGVVA--DH----GLTLGHLMGVLREFFTKLGIT----QLRFKPaynPYtepsmE 418
Cdd:cd00775 78 RVYEIGRNFRNEGIDLTHNPEFTMIEFYEAyaDYndmmDLTEDLFSGLVKKINGKTKIEyggkELDFTP---PF-----K 149
|
90
....*....|
gi 13676326 419 VFSYHQGLKK 428
Cdd:cd00775 150 RVTMVDALKE 159
|
|
| |
