|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-426 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 791.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPLSSELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKDmgTAEKLKAEVGEL 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGE--DAEALIAEVKEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 81 KDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLA 160
Cdd:PRK05431 79 KEEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 161 GARFTVLKGPLARLERALGQFMLDLHTTEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTTDGR-WLIPTAEVPLTNL 239
Cdd:PRK05431 159 GSRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDlYLIPTAEVPLTNL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 240 VAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRT 319
Cdd:PRK05431 239 HRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 320 VVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKSTRFVHTLNGSGVAVGRALIAVMEN 399
Cdd:PRK05431 319 VLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILEN 398
|
410 420
....*....|....*....|....*..
gi 189083559 400 YQQEDGSIHIPEALQPYIGGLTRIEKA 426
Cdd:PRK05431 399 YQQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| 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: 786.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPLSSELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKDmgTAEKLKAEVGEL 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGE--EAEALIAEVKEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 81 KDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLA 160
Cdd:COG0172 79 KEEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 161 GARFTVLKGPLARLERALGQFMLDLHTtEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTT-DGRWLIPTAEVPLTNL 239
Cdd:COG0172 159 GSRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEgDDLYLIPTAEVPLTNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 240 VAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRT 319
Cdd:COG0172 238 HRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 320 VVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKsTRFVHTLNGSGVAVGRALIAVMEN 399
Cdd:COG0172 318 VLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGK-PEFVHTLNGSGLAVGRTLVAILEN 396
|
410 420
....*....|....*....|....*
gi 189083559 400 YQQEDGSIHIPEALQPYIGGLTRIE 424
Cdd:COG0172 397 YQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| 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: 558.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPLSS--ELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKDMGTAEkLKAEVG 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDleKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEE-IKKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 79 ELKDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAK 158
Cdd:TIGR00414 80 ELKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 159 LAGARFTVLKGPLARLERALGQFMLDLHTtEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTTDGR-WLIPTAEVPLT 237
Cdd:TIGR00414 160 VTGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDlYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 238 NLVAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPF 317
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 318 RTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKSTRFVHTLNGSGVAVGRALIAVM 397
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 189083559 398 ENYQQEDGSIHIPEALQPYI 417
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
121-417 |
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: 509.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 121 DNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLAGARFTVLKGPLARLERALGQFMLDLHTtEHGYTEVMPPLM 200
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 201 VRDEAVYGTGQLPKFSEDLFRTT-DGRWLIPTAEVPLTNLVAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEgEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 280 QFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083559 360 QGRRMNARYRPEGEKSTRFVHTLNGSGVAVGRALIAVMENYQQEDGSIHIPEALQPYI 417
Cdd:cd00770 240 QARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 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 ... |
228-400 |
2.91e-43 |
|
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: 149.87 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 228 LIPTAEVPLTNLVAEEIVDMKGLPLRFTALTPCFRSEAGsagRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAE 307
Cdd:pfam00587 13 LKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 308 EVLKRLGLPFRTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKStRFVHTLNGSGV 387
Cdd:pfam00587 90 RVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES-KFPYMIHRAGL 168
|
170
....*....|...
gi 189083559 388 AVGRALIAVMENY 400
Cdd:pfam00587 169 GVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-426 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 791.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPLSSELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKDmgTAEKLKAEVGEL 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGE--DAEALIAEVKEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 81 KDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLA 160
Cdd:PRK05431 79 KEEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 161 GARFTVLKGPLARLERALGQFMLDLHTTEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTTDGR-WLIPTAEVPLTNL 239
Cdd:PRK05431 159 GSRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDlYLIPTAEVPLTNL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 240 VAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRT 319
Cdd:PRK05431 239 HRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 320 VVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKSTRFVHTLNGSGVAVGRALIAVMEN 399
Cdd:PRK05431 319 VLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILEN 398
|
410 420
....*....|....*....|....*..
gi 189083559 400 YQQEDGSIHIPEALQPYIGGLTRIEKA 426
Cdd:PRK05431 399 YQQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| 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: 786.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPLSSELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKDmgTAEKLKAEVGEL 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGE--EAEALIAEVKEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 81 KDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLA 160
Cdd:COG0172 79 KEEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 161 GARFTVLKGPLARLERALGQFMLDLHTtEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTT-DGRWLIPTAEVPLTNL 239
Cdd:COG0172 159 GSRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEgDDLYLIPTAEVPLTNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 240 VAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRT 319
Cdd:COG0172 238 HRDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 320 VVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKsTRFVHTLNGSGVAVGRALIAVMEN 399
Cdd:COG0172 318 VLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGK-PEFVHTLNGSGLAVGRTLVAILEN 396
|
410 420
....*....|....*....|....*
gi 189083559 400 YQQEDGSIHIPEALQPYIGGLTRIE 424
Cdd:COG0172 397 YQQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| 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: 558.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPLSS--ELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKDMGTAEkLKAEVG 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLSVDIDleKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEE-IKKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 79 ELKDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAK 158
Cdd:TIGR00414 80 ELKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 159 LAGARFTVLKGPLARLERALGQFMLDLHTtEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTTDGR-WLIPTAEVPLT 237
Cdd:TIGR00414 160 VTGSRFYYLKNDGAKLERALINFMLDLLE-KNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDlYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 238 NLVAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPF 317
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 318 RTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKSTRFVHTLNGSGVAVGRALIAVM 397
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 189083559 398 ENYQQEDGSIHIPEALQPYI 417
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
121-417 |
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: 509.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 121 DNVELRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLAGARFTVLKGPLARLERALGQFMLDLHTtEHGYTEVMPPLM 200
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 201 VRDEAVYGTGQLPKFSEDLFRTT-DGRWLIPTAEVPLTNLVAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEgEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 280 QFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 189083559 360 QGRRMNARYRPEGEKSTRFVHTLNGSGVAVGRALIAVMENYQQEDGSIHIPEALQPYI 417
Cdd:cd00770 240 QARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-421 |
7.61e-107 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 323.19 E-value: 7.61e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRE----NPETLDKALAKRGAAP-LSSELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKdmGTAEKLKA 75
Cdd:PLN02678 1 MLDINLFREekggDPELIRESQRRRFASVeLVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAK--EDATELIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 76 EVGELKDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVELRRIGNPHnFSFQPKEHFELGEALGYMDFER 155
Cdd:PLN02678 79 ETKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGEKR-QEPKLKNHVDLVELLGIVDTER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 156 AAKLAGARFTVLKGPLARLERALGQFMLDLhTTEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTT---DGRWLIPTA 232
Cdd:PLN02678 158 GADVAGGRGYYLKGAGVLLNQALINFGLAF-LRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTgegDDKYLIATS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 233 EVPLTNLVAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSIT--DAESSVAEHERMTACAEEVL 310
Cdd:PLN02678 237 EQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITspNGNESWEMHEEMLKNSEDFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 311 KRLGLPFRTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPE--GEKSTRFVHTLNGSGVA 388
Cdd:PLN02678 317 QSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKksNEQTKQYVHLLNSTLTA 396
|
410 420 430
....*....|....*....|....*....|...
gi 189083559 389 VGRALIAVMENYQQEDGsIHIPEALQPYIGGLT 421
Cdd:PLN02678 397 TERTLCCILENYQTEDG-VRVPEVLQPFMGGIE 428
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-423 |
3.55e-99 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 305.31 E-value: 3.55e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 2 LDIKWIRENPETLDKALAKRGAAPLSSELIALDEKRREHVGKVQAAQERRNA-ASKEIGKAmaakDMGTAEKLKAEVGEL 80
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAvANKMKGKL----EPSERQALVEEGKNL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 81 KDFLAHAEEDERRLSKELSDALSTIPNIPLDDVPLGKDESDNVElRRIGNPHNFSFQPKEHFELGEALGYMDFERAAKLA 160
Cdd:PLN02320 143 KEGLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDSSAVR-KEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 161 GARFTVLKGPLARLERALGQFMLDlHTTEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTTDG--RWLIPTAEVPLTN 238
Cdd:PLN02320 222 GSKFYYLKNEAVLLEMALVNWTLS-EVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNTQVYSIDGsdQCLIGTAEIPVGG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 239 LVAEEIVDMKGLPLRFTALTPCFRSEAGSAGRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFR 318
Cdd:PLN02320 301 IHMDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 319 TVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRP---------EGEKS---TRFVHTLNGSG 386
Cdd:PLN02320 381 TLDMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRPseppqtnpkKGKGSlgpTKFVHTLNATA 460
|
410 420 430
....*....|....*....|....*....|....*..
gi 189083559 387 VAVGRALIAVMENYQQEDGSIHIPEALQPYIGGLTRI 423
Cdd:PLN02320 461 CAVPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELI 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 ... |
228-400 |
2.91e-43 |
|
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: 149.87 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 228 LIPTAEVPLTNLVAEEIVDMKGLPLRFTALTPCFRSEAGsagRDTRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAE 307
Cdd:pfam00587 13 LKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAPGQSPDELEDYIKLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 308 EVLKRLGLPFRTVVLCTGDMGFGAQRTYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKStRFVHTLNGSGV 387
Cdd:pfam00587 90 RVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES-KFPYMIHRAGL 168
|
170
....*....|...
gi 189083559 388 AVGRALIAVMENY 400
Cdd:pfam00587 169 GVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-109 |
1.53e-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: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 1 MLDIKWIRENPETLDKALAKRGAAPL-SSELIALDEKRREHVGKVQAAQERRNAASKEIGKAMAAKdmGTAEKLKAEVGE 79
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLdVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKK--EDADALIAEVKE 78
|
90 100 110
....*....|....*....|....*....|
gi 189083559 80 LKDFLAHAEEDERRLSKELSDALSTIPNIP 109
Cdd:pfam02403 79 LKDELKALEAELKELEAELDKLLLTIPNIP 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 ... |
172-386 |
2.15e-25 |
|
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: 103.62 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 172 ARLERALGQFMldlhtTEHGYTEVMPPLMVRDEAVYGTGQLPKFSEDLFRTTD-GRW-------LIPTAEVPLTNLVAEE 243
Cdd:cd00670 6 RALERFLDDRM-----AEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDkGRElrdtdlvLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 244 IVDMKGLPLRFTALTPCFRSEAGSAgrdtRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLGLPFRTVVLC 323
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189083559 324 TGDMGFGAQR--------TYDIEVWLPGQNTYREISSCSTCGDFQGRRMNARYRPEGEKstRFVHTLNGSG 386
Cdd:cd00670 157 DPFFGRGGKRgldagretVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGGG--RAHTGCGGAG 225
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
170-387 |
4.25e-13 |
|
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: 67.91 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 170 PLARLERALGQFMldlhtTEHGYTEVMPPLMVRDEAVYGTGQLPK--------FSEDLFrttdgrwLIPTAEVPLTNLVA 241
Cdd:cd00768 1 IRSKIEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGHEPKdllpvgaeNEEDLY-------LRPTLEPGLVRLFV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 242 EEIVDmkgLPLRFTALTPCFRSEAGSagrdtRGMLRQHQFLKVEMVSITDAESSVAEHERMTACAEEVLKRLG--LPFRT 319
Cdd:cd00768 69 SHIRK---LPLRLAEIGPAFRNEGGR-----RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGikLDIVF 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 189083559 320 VVLCTGDMGFG-AQRTYDIEVWLPgQNTYREISSCSTCGDFQGRRMNARYRPEGEKSTRFVHTLNGSGV 387
Cdd:cd00768 141 VEKTPGEFSPGgAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGFGLGL 208
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
209-328 |
2.84e-11 |
|
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: 63.36 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 209 TGQLPKFSEDLFRTTD--GRWLI--PTAEVPLTNLVAEEIVDMKGLPLRFTALTPCFRSEAgsagRDTRGMLRQHQFLKV 284
Cdd:cd00779 67 SGRWDAYGPELLRLKDrhGKEFLlgPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDEI----RPRFGLMRGREFLMK 142
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 189083559 285 EMVSI-TDAESSVAEHERMTACAEEVLKRLGLPFRTVVLCTGDMG 328
Cdd:cd00779 143 DAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIG 187
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
170-342 |
4.49e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 48.86 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 170 PLARLERALGQFMLDLHTTEHGYTEVMPPLMVRDEAVYGTGQL------------PKFSEDLFRTTdGRWLIPTAEVPLT 237
Cdd:PRK00960 221 PMTKLFRAFEKLVIEEVLKPLGFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFEEF-VDEMMVKKEVPIE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 238 NL----------------------VAEEIVDMKGLPLRFTALT-PCFRSEAGSAgrdtRGMLRQHQFLKVEMVSITDAES 294
Cdd:PRK00960 300 KLkeklrdpgyvlapaqcepfyqfFQGETVDVDELPIKFFDRSgWTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQ 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 189083559 295 SVAEHERMTACAEEVLKRLGLPFRTVVLCT-----------GDMGFGAQRTYDIEVWLP 342
Cdd:PRK00960 376 VEEIRDELLKYAHILAEKLDLEYWREVGDDpfylegrgledRGIEFPDVPKYEMELWLP 434
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
190-316 |
1.31e-03 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine 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. 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. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 40.28 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189083559 190 HGYTEVMPPlMVRDEAVYGTGQLPKFSEDLFRTTD--GRW--LIPTAEVPLTNLVAEEIVDMkGLPLRFTALTPCFRSEA 265
Cdd:cd00773 19 YGYEEIDTP-VFEYTELFLRKSGDEVSKEMYRFKDkgGRDlaLRPDLTAPVARAVAENLLSL-PLPLKLYYIGPVFRYER 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 189083559 266 GSAGRdtrgmLRQHQFLKVEMVS----ITDAEssvaeherMTACAEEVLKRLGLP 316
Cdd:cd00773 97 PQKGR-----YREFYQVGVEIIGsdspLADAE--------VIALAVEILEALGLK 138
|
|
| |
