|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-426 |
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: 821.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRGFQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGEDIAPLLADVDRMGS 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 81 ELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKLSGA 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 161 RFALMRGPIARLHRALAQFMINLHTaEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDgeaDLYLIPTAEVSLTN 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGD---DLYLIPTAEVPLTN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 241 IVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYR 320
Cdd:COG0172 237 LHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 321 VLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRnPETGKPELVHTLNGSGLAVGRTLVAVLE 400
Cdd:COG0172 317 VVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYR-DEDGKPEFVHTLNGSGLAVGRTLVAILE 395
|
410 420
....*....|....*....|....*.
gi 489188236 401 NYQQADGSIRVPEVLKPYMAGIEVIG 426
Cdd:COG0172 396 NYQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-426 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 818.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRGFQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGEDIAPLLADVDRMGS 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 81 ELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKLSGA 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 161 RFALMRGPIARLHRALAQFMINLHTAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDgeaDLYLIPTAEVSLTN 240
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDD---DLYLIPTAEVPLTN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 241 IVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYR 320
Cdd:PRK05431 238 LHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 321 VLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNPETGKPELVHTLNGSGLAVGRTLVAVLE 400
Cdd:PRK05431 318 VVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILE 397
|
410 420
....*....|....*....|....*.
gi 489188236 401 NYQQADGSIRVPEVLKPYMAGIEVIG 426
Cdd:PRK05431 398 NYQQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-419 |
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: 617.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRG--FQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGED-IAPLLADVDR 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlsVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 78 MGSELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKL 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 158 SGARFALMRGPIARLHRALAQFMINLHtAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIgRDGeaDLYLIPTAEVS 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLL-EKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKL-EDT--DLYLIPTAEVP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 238 LTNIVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLEL 317
Cdd:TIGR00414 237 LTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 318 PYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNPETGKPELVHTLNGSGLAVGRTLVA 397
Cdd:TIGR00414 317 PYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVA 396
|
410 420
....*....|....*....|..
gi 489188236 398 VLENYQQADGSIRVPEVLKPYM 419
Cdd:TIGR00414 397 ILENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
119-419 |
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: 511.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 119 ANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKLSGARFALMRGPIARLHRALAQFMINLHTaEHGYEEAYTPYL 198
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 199 VQAPALQGTGQLPKFEEDLFKIGRDgeaDLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMI 278
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGE---DLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 279 RQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNC 358
Cdd:cd00770 157 RVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNC 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489188236 359 GDFQARRMQARYRNPETGKPELVHTLNGSGLAVGRTLVAVLENYQQADGSIRVPEVLKPYM 419
Cdd:cd00770 237 TDFQARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 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 ... |
218-402 |
2.88e-51 |
|
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: 170.67 E-value: 2.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 218 FKIGRDGEADLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSEAGasgRDTRGMIRQHQFDKVEMVQIVDPATS 297
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 298 YEALEGLTANAERVLQLLELPYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNpETGK 377
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKD-EDNE 156
|
170 180
....*....|....*....|....*
gi 489188236 378 PELVHTLNGSGLAVGRTLVAVLENY 402
Cdd:pfam00587 157 SKFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-426 |
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: 821.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRGFQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGEDIAPLLADVDRMGS 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 81 ELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKLSGA 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 161 RFALMRGPIARLHRALAQFMINLHTaEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDgeaDLYLIPTAEVSLTN 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGD---DLYLIPTAEVPLTN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 241 IVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYR 320
Cdd:COG0172 237 LHRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 321 VLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRnPETGKPELVHTLNGSGLAVGRTLVAVLE 400
Cdd:COG0172 317 VVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYR-DEDGKPEFVHTLNGSGLAVGRTLVAILE 395
|
410 420
....*....|....*....|....*.
gi 489188236 401 NYQQADGSIRVPEVLKPYMAGIEVIG 426
Cdd:COG0172 396 NYQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-426 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 818.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRGFQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGEDIAPLLADVDRMGS 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 81 ELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKLSGA 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 161 RFALMRGPIARLHRALAQFMINLHTAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDgeaDLYLIPTAEVSLTN 240
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDD---DLYLIPTAEVPLTN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 241 IVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYR 320
Cdd:PRK05431 238 LHRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 321 VLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNPETGKPELVHTLNGSGLAVGRTLVAVLE 400
Cdd:PRK05431 318 VVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILE 397
|
410 420
....*....|....*....|....*.
gi 489188236 401 NYQQADGSIRVPEVLKPYMAGIEVIG 426
Cdd:PRK05431 398 NYQQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-419 |
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: 617.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRG--FQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGED-IAPLLADVDR 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGlsVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 78 MGSELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKL 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 158 SGARFALMRGPIARLHRALAQFMINLHtAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIgRDGeaDLYLIPTAEVS 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLL-EKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKL-EDT--DLYLIPTAEVP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 238 LTNIVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLEL 317
Cdd:TIGR00414 237 LTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 318 PYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNPETGKPELVHTLNGSGLAVGRTLVA 397
Cdd:TIGR00414 317 PYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVA 396
|
410 420
....*....|....*....|..
gi 489188236 398 VLENYQQADGSIRVPEVLKPYM 419
Cdd:TIGR00414 397 ILENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
119-419 |
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: 511.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 119 ANVEVRRWGTPKTFDFEVKDHVALGERHGWLDFETAAKLSGARFALMRGPIARLHRALAQFMINLHTaEHGYEEAYTPYL 198
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 199 VQAPALQGTGQLPKFEEDLFKIGRDgeaDLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMI 278
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGE---DLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 279 RQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNC 358
Cdd:cd00770 157 RVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNC 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489188236 359 GDFQARRMQARYRNPETGKPELVHTLNGSGLAVGRTLVAVLENYQQADGSIRVPEVLKPYM 419
Cdd:cd00770 237 TDFQARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-425 |
3.88e-111 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 333.98 E-value: 3.88e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQ---EVAARLATRGFQ--LDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGEDIAPLLADV 75
Cdd:PLN02678 1 MLDINLFREEKGgdpELIRESQRRRFAsvELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 76 DRMGSELEEGKRQLDAIQGELDAMLLGIPNLPHESVPVGADEDANVEVRRWGTPKtFDFEVKDHVALGERHGWLDFETAA 155
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR-QEPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 156 KLSGARFALMRGPIARLHRALAQFMINLhTAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDGEaDLYLIPTAE 235
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLAF-LRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTGEGD-DKYLIATSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 236 VSLTNIVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPAT--SYEALEGLTANAERVLQ 313
Cdd:PLN02678 238 QPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGneSWEMHEEMLKNSEDFYQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 314 LLELPYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNPETG--KPELVHTLNGSGLAV 391
Cdd:PLN02678 318 SLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKKSNeqTKQYVHLLNSTLTAT 397
|
410 420 430
....*....|....*....|....*....|....
gi 489188236 392 GRTLVAVLENYQQADGsIRVPEVLKPYMAGIEVI 425
Cdd:PLN02678 398 ERTLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-425 |
5.21e-91 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 284.12 E-value: 5.21e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 2 LDPKLVRTQPQEVAARLATRGFQLDVARIEALEEQRKSVQTRTEQLQAERNA-------------RSKAIGQAKQRGEDI 68
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAvankmkgklepseRQALVEEGKNLKEGL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 69 APLLADVDRMGSELeegkrQLDAiqgeldamlLGIPNLPHESVPVGAdEDANVEVRRWGTPKTFDFEVKDHVALGERHGW 148
Cdd:PLN02320 147 VTLEEDLVKLTDEL-----QLEA---------QSIPNMTHPDVPVGG-EDSSAVRKEVGSPREFSFPIKDHLQLGKELDL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 149 LDFETAAKLSGARFALMRGPIARLHRALAQFMINlHTAEHGYEEAYTPYLVQAPALQGTGQLPKFEE-DLFKIgrDGeAD 227
Cdd:PLN02320 212 FDFDAAAEVSGSKFYYLKNEAVLLEMALVNWTLS-EVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSI--DG-SD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 228 LYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSEAGASGRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTAN 307
Cdd:PLN02320 288 QCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQI 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 308 AERVLQLLELPYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYR-------NPETGKPEL 380
Cdd:PLN02320 368 EEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRpseppqtNPKKGKGSL 447
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 489188236 381 -----VHTLNGSGLAVGRTLVAVLENYQQADGSIRVPEVLKPYMAGIEVI 425
Cdd:PLN02320 448 gptkfVHTLNATACAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELI 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 ... |
218-402 |
2.88e-51 |
|
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: 170.67 E-value: 2.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 218 FKIGRDGEADLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSEAGasgRDTRGMIRQHQFDKVEMVQIVDPATS 297
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 298 YEALEGLTANAERVLQLLELPYRVLALCTGDMGFGATKTYDLEVWVPSQDKYREISSCSNCGDFQARRMQARYRNpETGK 377
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKD-EDNE 156
|
170 180
....*....|....*....|....*
gi 489188236 378 PELVHTLNGSGLAVGRTLVAVLENY 402
Cdd:pfam00587 157 SKFPYMIHRAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-107 |
7.56e-36 |
|
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: 127.70 E-value: 7.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 1 MLDPKLVRTQPQEVAARLATRG-FQLDVARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQRGEDIAPLLADVDRMG 79
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGvDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 489188236 80 SELEEGKRQLDAIQGELDAMLLGIPNLP 107
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 ... |
169-399 |
4.34e-26 |
|
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: 105.55 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 169 IARLHRALAQFMINLhTAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDGEA----DLYLIPTAEVSLTNIVSG 244
Cdd:cd00670 1 GTALWRALERFLDDR-MAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKGRElrdtDLVLRPAACEPIYQIFSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 245 QILDAKQLPLKFVAHTPCFRSEAgasgRDTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYRVLAL 324
Cdd:cd00670 80 EILSYRALPLRLDQIGPCFRHEP----SGRRGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 325 CTGDMGFGAT--------KTYDLEVWVPSQDKYREISSCSNCGDFQARRmqARYRNPETGKPELVHTLNGSGLaVGRTLV 396
Cdd:cd00670 156 DDPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFG--ASFKIDEDGGGRAHTGCGGAGG-EERLVL 232
|
...
gi 489188236 397 AVL 399
Cdd:cd00670 233 ALL 235
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
168-393 |
5.32e-19 |
|
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: 84.86 E-value: 5.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 168 PIARLHRALAQFMinlhtAEHGYEEAYTPYLVQAPALQGTGQLPKfEEDLFKIGRDGeaDLYLIPTAEVSLTNIVSGQIl 247
Cdd:cd00768 1 IRSKIEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGHEPK-DLLPVGAENEE--DLYLRPTLEPGLVRLFVSHI- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 248 daKQLPLKFVAHTPCFRSEAGasgrdTRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLE--LPYRVLALC 325
Cdd:cd00768 72 --RKLPLRLAEIGPAFRNEGG-----RRGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGikLDIVFVEKT 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489188236 326 TGDMGFG-ATKTYDLEVWVPSqDKYREISSCSNCGDFQARRmQARYRNPETGKPELVHTLNGsGLAVGR 393
Cdd:cd00768 145 PGEFSPGgAGPGFEIEVDHPE-GRGLEIGSGGYRQDEQARA-ADLYFLDEALEYRYPPTIGF-GLGLER 210
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
129-351 |
1.10e-10 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 63.11 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 129 PKTFDFEvKDHVALGERHGWLDfetaaklsgaRFAlMRG------PIARLHRALAQFMINLHTAEHGYEEAYTPYLVQAP 202
Cdd:PRK00960 188 KREITFD-GDPTEEAEKLGWVK----------RFP-GRGqwfytpPMTKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 203 ALQGTGQL------------PKFEEDLFKigrdgEADLYLIPTAEVSLTNI----------------------VSGQILD 248
Cdd:PRK00960 256 VMYKMRYLeglpegmyyvcpPKRDPEYFE-----EFVDEMMVKKEVPIEKLkeklrdpgyvlapaqcepfyqfFQGETVD 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 249 AKQLPLKFVAHT-PCFRSEAGASgrdtRGMIRQHQFDKVEMVQIVDPATSYEALEGLTANAERVLQLLELPYRVLALCT- 326
Cdd:PRK00960 331 VDELPIKFFDRSgWTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQVEEIRDELLKYAHILAEKLDLEYWREVGDDp 406
|
250 260 270
....*....|....*....|....*....|....*
gi 489188236 327 ----------GDMGFGATKTYDLEVWVPSQDKYRE 351
Cdd:PRK00960 407 fylegrgledRGIEFPDVPKYEMELWLPYRGDERK 441
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
187-400 |
4.14e-08 |
|
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: 53.91 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 187 EHGYEEAYTPYLVQAPALQGTGQLPK-FEEDLFKI----GRDGEADLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTP 261
Cdd:cd00772 48 EHGAQNALFPFFILASFLEKEAEHDEgFSKELAVFkdagDEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIGN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 262 CFRSEAgasgRDTRGMIRQHQFDKVEMVQIVDPATSY--EALEGLTANAERVLQLLELPYRVLALCTGDMGFGATKTYDL 339
Cdd:cd00772 128 KFRDEI----RPRFGFLRAREFIMKDGHSAHADAEEAdeEFLNMLSAYAEIARDLAAIDFIEGEADEGAKFAGASKSREF 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489188236 340 EVWVpsQDKYR---EISSCSNCGDFQARRMQARYRNpETGKPELVHTlNGSGLAVGRTLVAVLE 400
Cdd:cd00772 204 EALM--EDGKAkqaETGHIFGEGFARAFDLKAKFLD-KDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
187-400 |
9.66e-08 |
|
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: 52.96 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 187 EHGYEEAYTPYLVQAPALQGTGQLPKFEEDLFKIGRDGEADLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSE 266
Cdd:cd00779 47 KIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDRHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 267 AgasgRDTRGMIRQHQFDKVEMVQI-VDPATSYEALEGLTANAERVLQLLELPYRVLALCTGDMGFGATKtydlEVWVPS 345
Cdd:cd00779 127 I----RPRFGLMRGREFLMKDAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSH----EFHVLS 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489188236 346 QDKYR---EISSCSNCGDFQARRMQARYRNpETGKPELVHTlnGS-GLAVGRTLVAVLE 400
Cdd:cd00779 199 PLKITkgiEVGHIFQLGTKYSKALGATFLD-ENGKPKPLEM--GCyGIGVSRLLAAIIE 254
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
138-271 |
1.37e-04 |
|
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: 43.69 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 138 DHVALGERHGWLDFETAAKlSGARFALMRGpiARLHRALAQFMINLHtAEHGYEEAYTPYLVQAPALQGTGQLPKFEEDL 217
Cdd:cd00771 1 DHRRLGGELELFFFFDEAG-PGLPFWLPKG--AIIRNELEDFLRELQ-RKRGYQEVETPIIYNKELWETSGHWDHYRENM 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489188236 218 FKIGRDGEaDLYLIPTAEVSLTNIVSGQILDAKQLPLKFVAHTPCFRSEagASG 271
Cdd:cd00771 77 FPFEEEDE-EYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYE--QSG 127
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
28-104 |
7.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 28 ARIEALEEQRKSVQTRTEQLQAERNARSKAIGQAKQR-----GEDIAPLLADVDRMGSELEEGKRQLDAIQGELDAMLLG 102
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
..
gi 489188236 103 IP 104
Cdd:COG4913 375 LP 376
|
|
| TerB_C |
pfam15615 |
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain ... |
10-111 |
8.92e-03 |
|
TerB-C domain; TerB-C occurs C-terminal of TerB in TerB-N containing proteins. This domain displays multiple conserved acidic residues (TerBC). The presence of conserved acidic residues in both TerB-N and TerB-C suggests that they, like the TerB domain, might also chelate metals. These two domains may also occur together in the same protein independently of TerB.
Pssm-ID: 434814 [Multi-domain] Cd Length: 143 Bit Score: 36.57 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489188236 10 QPQEVAARLATRGFQLDVARIEALEEQRKSVQtrtEQLqaernarsKAIGQAKQRGEDIAPLLADVDRMGSELEEGKRQ- 88
Cdd:pfam15615 2 EEVEEAAEAARKGISLDLDRIAAIQEETAAVS---ALL--------AEIFVEEETEEALTEIDEEPESEEAETALADKVd 70
|
90 100
....*....|....*....|....*
gi 489188236 89 --LDAIQGELDAMLLGIPNLPHESV 111
Cdd:pfam15615 71 egLDEAHSALLRLLLARAQWPREEL 95
|
|
| |
