|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-424 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 792.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDAaEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAAMKNVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 81 AEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 161 SRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLTNF 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI--EGDDLYLIPTAEVPLTNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 241 YRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYHV 320
Cdd:COG0172 238 HRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 321 ITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHVNLVHTLNGSGLAVGRTVAAILENY 400
Cdd:COG0172 318 VLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 1777084617 401 QNEDGTVTIPEALVPYMGGMTKIG 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 785.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDAaEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAAMKNVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPL-DVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 81 AEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 161 SRFVYYKGAGARLERAVYNFMLDQHAKE-GYEEMITPYLVNGESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLTN 239
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEhGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI--EDDDLYLIPTAEVPLTN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 240 FYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYH 319
Cdd:PRK05431 238 LHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 320 VITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDE-DGHVNLVHTLNGSGLAVGRTVAAILE 398
Cdd:PRK05431 318 VVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEgDGKPELVHTLNGSGLAVGRTLVAILE 397
|
410 420
....*....|....*....|....*.
gi 1777084617 399 NYQNEDGTVTIPEALVPYMGGMTKIG 424
Cdd:PRK05431 398 NYQQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-417 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 581.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDA-AEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAA-MKN 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVdIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIKKeLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 79 VGAEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 159 SGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLT 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKL--EDTDLYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 239 NFYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPY 318
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 319 HVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHVN-LVHTLNGSGLAVGRTVAAIL 397
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNkYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 1777084617 398 ENYQNEDGTVTIPEALVPYM 417
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
122-417 |
0e+00 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 523.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 122 REERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKVSGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNG 201
Cdd:cd00770 3 VEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 202 ESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLTNFYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQ 281
Cdd:cd00770 83 EVMEGTGQLPKFDEQLYKV--EGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 282 FNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYHVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQ 361
Cdd:cd00770 161 FEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDFQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1777084617 362 ARRAQIRYRDE-DGHVNLVHTLNGSGLAVGRTVAAILENYQNEDGTVTIPEALVPYM 417
Cdd:cd00770 241 ARRLNIRYRDKkDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
223-400 |
1.79e-46 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 157.96 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 223 EGEPMTLIPTAEVPLTNFYRDEILDGAQLPIYFTALSPAFRSEAGsagRDTRGLIRMHQFNKVEMVKFTKPEESFNELEK 302
Cdd:pfam00587 7 NGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 303 MTNDAENILKALDLPYHVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHVNLVHTL 382
Cdd:pfam00587 84 YIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMI 163
|
170
....*....|....*...
gi 1777084617 383 NGSGLAVGRTVAAILENY 400
Cdd:pfam00587 164 HRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-424 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 792.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDAaEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAAMKNVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 81 AEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKVSG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 161 SRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLTNF 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI--EGDDLYLIPTAEVPLTNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 241 YRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYHV 320
Cdd:COG0172 238 HRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 321 ITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHVNLVHTLNGSGLAVGRTVAAILENY 400
Cdd:COG0172 318 VLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 1777084617 401 QNEDGTVTIPEALVPYMGGMTKIG 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 785.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDAaEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAAMKNVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPL-DVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 81 AEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKVSG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 161 SRFVYYKGAGARLERAVYNFMLDQHAKE-GYEEMITPYLVNGESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLTN 239
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEhGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKI--EDDDLYLIPTAEVPLTN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 240 FYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYH 319
Cdd:PRK05431 238 LHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 320 VITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDE-DGHVNLVHTLNGSGLAVGRTVAAILE 398
Cdd:PRK05431 318 VVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEgDGKPELVHTLNGSGLAVGRTLVAILE 397
|
410 420
....*....|....*....|....*.
gi 1777084617 399 NYQNEDGTVTIPEALVPYMGGMTKIG 424
Cdd:PRK05431 398 NYQQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-417 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 581.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDA-AEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAA-MKN 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVdIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIKKeLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 79 VGAEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 159 SGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLT 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKL--EDTDLYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 239 NFYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPY 318
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 319 HVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHVN-LVHTLNGSGLAVGRTVAAIL 397
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNkYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 1777084617 398 ENYQNEDGTVTIPEALVPYM 417
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
122-417 |
0e+00 |
|
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. This domain It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. SerRS synthetase is a homodimer.
Pssm-ID: 238393 [Multi-domain] Cd Length: 297 Bit Score: 523.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 122 REERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKVSGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNG 201
Cdd:cd00770 3 VEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 202 ESMFGTGQFPKFTEDVYTMtnEGEPMTLIPTAEVPLTNFYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQ 281
Cdd:cd00770 83 EVMEGTGQLPKFDEQLYKV--EGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 282 FNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYHVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQ 361
Cdd:cd00770 161 FEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDFQ 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1777084617 362 ARRAQIRYRDE-DGHVNLVHTLNGSGLAVGRTVAAILENYQNEDGTVTIPEALVPYM 417
Cdd:cd00770 241 ARRLNIRYRDKkDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-421 |
7.69e-123 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 363.64 E-value: 7.69e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRE----NVQWAKDKLATRGIDAAEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAAM 76
Cdd:PLN02678 1 MLDINLFREekggDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 77 KNVGAEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESFSREERKWSTPReFDFEPLAHWDIGEKLGILDFERAA 156
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR-QEPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 157 KVSGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYTMTNEGEPMTLIPTAEVP 236
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTGEGDDKYLIATSEQP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 237 LTNFYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPE--ESFNELEKMTNDAENILKAL 314
Cdd:PLN02678 240 LCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNgnESWEMHEEMLKNSEDFYQSL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 315 DLPYHVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHV---NLVHTLNGSGLAVGR 391
Cdd:PLN02678 320 GIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKKSNEqtkQYVHLLNSTLTATER 399
|
410 420 430
....*....|....*....|....*....|
gi 1777084617 392 TVAAILENYQNEDGtVTIPEALVPYMGGMT 421
Cdd:PLN02678 400 TLCCILENYQTEDG-VRVPEVLQPFMGGIE 428
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-423 |
2.13e-93 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 290.29 E-value: 2.13e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 2 LDIRVIRENVQWAKDKLATRGiDAAEIDEVVALDEKRRALIVRTEELKKNRNAaseaIAVAKRNKEDATEQ---IAAMKN 78
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRN-SNANLELVLELYENMLALQKEVERLRAERNA----VANKMKGKLEPSERqalVEEGKN 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 79 VGAEIKELDAQLAEVKEKVDYILVRLPNFPNDSAPVGLDESfSREERKWSTPREFDFEPLAHWDIGEKLGILDFERAAKV 158
Cdd:PLN02320 142 LKEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDS-SAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 159 SGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKF-TEDVYTMtnEGEPMTLIPTAEVPL 237
Cdd:PLN02320 221 SGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGdNTQVYSI--DGSDQCLIGTAEIPV 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 238 TNFYRDEILDGAQLPIYFTALSPAFRSEAGSAGRDTRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLP 317
Cdd:PLN02320 299 GGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLH 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 318 YHVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDED-------------GHVNLVHTLNG 384
Cdd:PLN02320 379 FKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPSEppqtnpkkgkgslGPTKFVHTLNA 458
|
410 420 430
....*....|....*....|....*....|....*....
gi 1777084617 385 SGLAVGRTVAAILENYQNEDGTVTIPEALVPYMGGMTKI 423
Cdd:PLN02320 459 TACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELI 497
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
223-400 |
1.79e-46 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 157.96 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 223 EGEPMTLIPTAEVPLTNFYRDEILDGAQLPIYFTALSPAFRSEAGsagRDTRGLIRMHQFNKVEMVKFTKPEESFNELEK 302
Cdd:pfam00587 7 NGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 303 MTNDAENILKALDLPYHVITLATGDASFTSAKTYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRYRDEDGHVNLVHTL 382
Cdd:pfam00587 84 YIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESKFPYMI 163
|
170
....*....|....*...
gi 1777084617 383 NGSGLAVGRTVAAILENY 400
Cdd:pfam00587 164 HRAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-108 |
1.10e-35 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 126.93 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 1 MLDIRVIRENVQWAKDKLATRGIDAAEIDEVVALDEKRRALIVRTEELKKNRNAASEAIAVAKRNKEDATEQIAAMKNVG 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 1777084617 81 AEIKELDAQLAEVKEKVDYILVRLPNFP 108
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPNIP 108
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
170-397 |
6.97e-27 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 107.48 E-value: 6.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 170 GARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYTMTNEGE-----PMTLIPTAEVPLTNFYRDE 244
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRelrdtDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 245 ILDGAQLPIYFTALSPAFRSEAGSAgrdtRGLIRMHQFNKVEMVKFTKPEESFNELEKMTNDAENILKALDLPYhVITLA 324
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPV-RVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 325 TGDASFTSAK---------TYDIEVWLPAQNTYREISSCSDCTDFQARRAQIRyRDEDGHVNLVHTLNGSGLaVGRTVAA 395
Cdd:cd00670 156 DDPFFGRGGKrgldagretVVEFELLLPLPGRAKETAVGSANVHLDHFGASFK-IDEDGGGRAHTGCGGAGG-EERLVLA 233
|
..
gi 1777084617 396 IL 397
Cdd:cd00670 234 LL 235
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
171-343 |
8.36e-09 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 57.34 E-value: 8.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 171 ARLERAVYNFMLDQHAKE-GYEEMITPYLVNGESMFGTGQF----------------PKFTEDV--YTMTNEGEPMTLI- 230
Cdd:PRK00960 223 TKLFRAFEKLVIEEVLKPlGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcppkrdPEYFEEFvdEMMVKKEVPIEKLk 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 231 -----------PTAEVPLTNFYRDEILDGAQLPIYFTALS-PAFRSEAGSAgrdtRGLIRMHQFNKVEMVKFTKPEESFN 298
Cdd:PRK00960 303 eklrdpgyvlaPAQCEPFYQFFQGETVDVDELPIKFFDRSgWTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQVEE 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1777084617 299 ELEKMTNDAENILKALDLPYHVIT-----------LATGDASFTSAKTYDIEVWLP 343
Cdd:PRK00960 379 IRDELLKYAHILAEKLDLEYWREVgddpfylegrgLEDRGIEFPDVPKYEMELWLP 434
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
140-400 |
1.19e-07 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 52.94 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 140 HWDIGEKLGILDFERAAKvSGSRFVYYKGAgaRLERAVYNFMLDQHAKEGYEEMITPYLVNgESMFGT-GQFPKFTEDVY 218
Cdd:cd00771 2 HRRLGGELELFFFFDEAG-PGLPFWLPKGA--IIRNELEDFLRELQRKRGYQEVETPIIYN-KELWETsGHWDHYRENMF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 219 TMTNEGEPMTLIPTA---------EVPLTnfYRDeildgaqLPIYFTALSPAFRSEA-GSAGrdtrGLIR--------MH 280
Cdd:cd00771 78 PFEEEDEEYGLKPMNcpghclifkSKPRS--YRD-------LPLRLAEFGTVHRYEQsGALH----GLTRvrgftqddAH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 281 QFNKVEMVK----------------F----------TKPEESFNELE---KMTNDAENILKALDLPYhviTLATGDASFT 331
Cdd:cd00771 145 IFCTPDQIKeeikgvldlikevysdFgffdykvelsTRPEKFIGSDEvweKAEAALREALEEIGLPY---EINEGEGAFY 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1777084617 332 SAKtYDIEVwlpaQNTYREISSCSdcT---DFQ-ARRAQIRYRDEDG---HVNLVH-TLNGSglaVGRTVAAILENY 400
Cdd:cd00771 222 GPK-IDFHV----KDALGREWQCS--TiqlDFNlPERFDLTYIGEDGekkRPVMIHrAILGS---IERFIGILIEHY 288
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
181-398 |
1.12e-04 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 43.51 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 181 MLDQHAKE-GYEEMITPYLVNGESMFGTGQFPK-FTEDVYTMTNEG-----EPMTLIPTAEVPLTNFYRDEILDGAQLPI 253
Cdd:cd00772 41 VLDKMFKEhGAQNALFPFFILASFLEKEAEHDEgFSKELAVFKDAGdeeleEDFALRPTLEENIGEIAAKFIKSWKDLPQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 254 YFTALSPAFRSEAgsagRDTRGLIRMHQFNKVEMVKFTKPEESFN-ELEKMTNDAENILKALDLPYHVITLATGDASFTS 332
Cdd:cd00772 121 HLNQIGNKFRDEI----RPRFGFLRAREFIMKDGHSAHADAEEADeEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAG 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1777084617 333 A-KTYDIEVWLPAQNTYR-EISSCSDCTDFQARRAQIRYRDEDGHVNLVHTlNGSGLAVGRTVAAILE 398
Cdd:cd00772 197 AsKSREFEALMEDGKAKQaETGHIFGEGFARAFDLKAKFLDKDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
170-227 |
4.59e-04 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 42.33 E-value: 4.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1777084617 170 GARLERAVYNFMLDQHAKEGYEEMITPYLVNgESMFGT-GQFPKFTEDVYTMTNEGE-----PM 227
Cdd:COG0441 270 GAIIRRELEDYIREKHRKAGYQEVKTPHILD-RELWETsGHWDHYRENMFPTESDGEeyalkPM 332
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
207-327 |
6.29e-04 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 41.41 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 207 TGQFPKFTEDVYTMTN-EGEPMTLIPTAEVPLTNFYRDEILDGAQLPIYFTALSPAFRSEAgsagRDTRGLIRMHQFNKV 285
Cdd:cd00779 67 SGRWDAYGPELLRLKDrHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEI----RPRFGLMRGREFLMK 142
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1777084617 286 EMVKF-TKPEESFNELEKMTNDAENILKALDLPYHVITLATGD 327
Cdd:cd00779 143 DAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGA 185
|
|
| PLN02837 |
PLN02837 |
threonine-tRNA ligase |
140-325 |
2.07e-03 |
|
threonine-tRNA ligase
Pssm-ID: 215450 [Multi-domain] Cd Length: 614 Bit Score: 40.27 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 140 HWDIGEKLGILDFERAAkvsGSRFVYYKGAGARLERAVYNFMLDQHAKEGYEEMITPYLVNGESMFGTGQFPKFTEDVYT 219
Cdd:PLN02837 219 HRRLGQDLDLFSIQDDA---GGGLVFWHPKGAIVRHIIEDSWKKMHFEHGYDLLYTPHVAKADLWKTSGHLDFYKENMYD 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1777084617 220 -MTNEGEPMTLIPTAEVPLTNFYRDEILDGAQLPIYFTALSPAFRSEAGSAgrdTRGLIRMHQFNKVEMVKFTKPEESFN 298
Cdd:PLN02837 296 qMDIEDELYQLRPMNCPYHILVYKRKLHSYRDLPIRVAELGTVYRYELSGS---LHGLFRVRGFTQDDAHIFCLEDQIKD 372
|
170 180
....*....|....*....|....*..
gi 1777084617 299 ELEKMTNDAENILKALDLPYHVITLAT 325
Cdd:PLN02837 373 EIRGVLDLTEEILKQFGFSKYEINLST 399
|
|
| |
