|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-425 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 654.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKKDPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMISEVERISQ 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 81 DLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 161 GWPAYKNQGVMLEWALLTYLLNKQR-EHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLNGF 239
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDD--LYLIPTAEVPLTNL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 240 HSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRL 319
Cdd:PRK05431 239 HRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 320 SLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKD-SQGKMHFIHTLNGSGLATPRLFVAILEN 398
Cdd:PRK05431 319 VLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDeGDGKPELVHTLNGSGLAVGRTLVAILEN 398
|
410 420
....*....|....*....|....*..
gi 499316359 399 NQQKDGSVVIPEVLRPYLGNQEVLLPQ 425
Cdd:PRK05431 399 YQQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-422 |
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: 640.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKKDPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMISEVERISQ 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 81 DLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 161 GWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLNGFH 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDD--LYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 241 SQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRLS 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 321 LLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDSQGKMHFIHTLNGSGLATPRLFVAILENNQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|..
gi 499316359 401 QKDGSVVIPEVLRPYLGNQEVL 422
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVI 420
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-416 |
6.31e-168 |
|
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: 472.81 E-value: 6.31e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 120 NQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGSGWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVK 199
Cdd:cd00770 2 NVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 200 REILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVH 279
Cdd:cd00770 82 KEVMEGTGQLPKFDEQLYKVEGED--LYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 280 QFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499316359 360 QSRRSETRYKDSQ-GKMHFIHTLNGSGLATPRLFVAILENNQQKDGSVVIPEVLRPYL 416
Cdd:cd00770 240 QARRLNIRYRDKKdGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
3.08e-164 |
|
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: 468.00 E-value: 3.08e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKK--DPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMIS-EVER 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARglSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIKkELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 78 ISQDLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKT 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 158 SGSGWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLN 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTD--LYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 238 GFHSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPY 317
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 318 RLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDSQ-GKMHFIHTLNGSGLATPRLFVAIL 396
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNkGKNKYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 499316359 397 ENNQQKDGSVVIPEVLRPYL 416
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
216-399 |
1.22e-45 |
|
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: 156.03 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 216 YYCVEDGDQSLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACTPCFRREAGAagaNERGLVRVHQFNKVEMFAFTTPEQA 295
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASG---DTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 296 DQAYEKMLAVVEDILTELKLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDSQGKM 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES 157
|
170 180
....*....|....*....|....
gi 499316359 376 HFIHTLNGSGLATPRLFVAILENN 399
Cdd:pfam00587 158 KFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-425 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 654.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKKDPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMISEVERISQ 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 81 DLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 161 GWPAYKNQGVMLEWALLTYLLNKQR-EHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLNGF 239
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDD--LYLIPTAEVPLTNL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 240 HSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRL 319
Cdd:PRK05431 239 HRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 320 SLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKD-SQGKMHFIHTLNGSGLATPRLFVAILEN 398
Cdd:PRK05431 319 VLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDeGDGKPELVHTLNGSGLAVGRTLVAILEN 398
|
410 420
....*....|....*....|....*..
gi 499316359 399 NQQKDGSVVIPEVLRPYLGNQEVLLPQ 425
Cdd:PRK05431 399 YQQADGSVTIPEVLRPYMGGLEVIPPK 425
|
|
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-422 |
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: 640.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKKDPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMISEVERISQ 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 81 DLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 161 GWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLNGFH 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDD--LYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 241 SQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRLS 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 321 LLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDSQGKMHFIHTLNGSGLATPRLFVAILENNQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|..
gi 499316359 401 QKDGSVVIPEVLRPYLGNQEVL 422
Cdd:COG0172 399 QADGSVRIPEVLRPYMGGLEVI 420
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-416 |
6.31e-168 |
|
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: 472.81 E-value: 6.31e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 120 NQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGSGWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVK 199
Cdd:cd00770 2 NVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 200 REILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVH 279
Cdd:cd00770 82 KEVMEGTGQLPKFDEQLYKVEGED--LYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 280 QFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499316359 360 QSRRSETRYKDSQ-GKMHFIHTLNGSGLATPRLFVAILENNQQKDGSVVIPEVLRPYL 416
Cdd:cd00770 240 QARRLNIRYRDKKdGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
3.08e-164 |
|
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: 468.00 E-value: 3.08e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKK--DPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMIS-EVER 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARglSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDKIEEIKkELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 78 ISQDLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKT 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 158 SGSGWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDGDqsLYLIPTAEVVLN 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTD--LYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 238 GFHSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPY 317
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 318 RLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDSQ-GKMHFIHTLNGSGLATPRLFVAIL 396
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNkGKNKYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 499316359 397 ENNQQKDGSVVIPEVLRPYL 416
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-425 |
6.72e-102 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 312.24 E-value: 6.72e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 2 LDIKLIRKAPEECEIRLRKKDPNISLLPILDLDKEVRRLKTDSESLQSQRKLLSTQIhKAKAQGEDASNMISEVERISQD 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAVANKM-KGKLEPSERQALVEEGKNLKEG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 82 LEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSgNQVIKSVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGSG 161
Cdd:PLN02320 146 LVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDS-SAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVSGSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 162 WPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDG-QYYCVEDGDQSLylIPTAEVVLNGFH 240
Cdd:PLN02320 225 FYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCL--IGTAEIPVGGIH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 241 SQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRLS 320
Cdd:PLN02320 303 MDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFKTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 321 LLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRY-------------KDSQGKMHFIHTLNGSGLA 387
Cdd:PLN02320 383 DMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYrpseppqtnpkkgKGSLGPTKFVHTLNATACA 462
|
410 420 430
....*....|....*....|....*....|....*...
gi 499316359 388 TPRLFVAILENNQQKDGSVVIPEVLRPYLGNQEVLLPQ 425
Cdd:PLN02320 463 VPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIKPK 500
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-422 |
8.68e-99 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 302.39 E-value: 8.68e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIR----KAPEECEIRLRKKDPNISLL-PILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMISEV 75
Cdd:PLN02678 1 MLDINLFReekgGDPELIRESQRRRFASVELVdEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 76 ERISQDLEKLEASLEEKNATLQDLLVRLPNYPEEDVPVCPDKSGNQVIKSVGaLPTFSFTPKHHVELNQKLQILDFKLPA 155
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWG-EKRQEPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 156 KTSGSGWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVE-DGDQSlYLIPTAEV 234
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTgEGDDK-YLIATSEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 235 VLNGFHSQEIFNEKDLPIYYAACTPCFRREAGAAGANERGLVRVHQFNKVEMFAFTTPEQAD--QAYEKMLAVVEDILTE 312
Cdd:PLN02678 239 PLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGNEswEMHEEMLKNSEDFYQS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 313 LKLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRY---KDSQGKMHFIHTLNGSGLATP 389
Cdd:PLN02678 319 LGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYgqkKSNEQTKQYVHLLNSTLTATE 398
|
410 420 430
....*....|....*....|....*....|...
gi 499316359 390 RLFVAILENNQQKDGsVVIPEVLRPYLGNQEVL 422
Cdd:PLN02678 399 RTLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
216-399 |
1.22e-45 |
|
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: 156.03 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 216 YYCVEDGDQSLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACTPCFRREAGAagaNERGLVRVHQFNKVEMFAFTTPEQA 295
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASG---DTRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 296 DQAYEKMLAVVEDILTELKLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDSQGKM 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES 157
|
170 180
....*....|....*....|....
gi 499316359 376 HFIHTLNGSGLATPRLFVAILENN 399
Cdd:pfam00587 158 KFPYMIHRAGLGVERFLAAILENN 181
|
|
| 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 ... |
169-396 |
1.93e-31 |
|
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: 119.80 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 169 GVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVEDG-----DQSLYLIPTAEVVLNGFHSQE 243
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelrDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 244 IFNEKDLPIYYAACTPCFRREAGAAganeRGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLPYRLSLLS 323
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 324 TGDMSFT--------ASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRsETRYKDSQGKMHFIHTLNGSGLaTPRLFVAI 395
Cdd:cd00670 157 DPFFGRGgkrgldagRETVVEFELLLPLPGRAKETAVGSANVHLDHFG-ASFKIDEDGGGRAHTGCGGAGG-EERLVLAL 234
|
.
gi 499316359 396 L 396
Cdd:cd00670 235 L 235
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-107 |
4.67e-27 |
|
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: 104.21 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 1 MLDIKLIRKAPEECEIRLRKKDPNISLL-PILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMISEVERIS 79
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVdELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 499316359 80 QDLEKLEASLEEKNATLQDLLVRLPNYP 107
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPNIP 108
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
139-340 |
3.64e-11 |
|
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: 63.72 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 139 HVELNQKLQILDFklpAKTSGSGWPAYKNQGVMLEWALLTYLLNKQREHGFQLWLPPLLVKREILFGSGQIPKFDGQYYC 218
Cdd:cd00771 2 HRRLGGELELFFF---FDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 219 VEDGDQSLYLIPtaevvLNGFHSQEIFNEK-----DLPIYYAACTPCFRREA-GAAGanerGLVRVHQFNKVEMFAFTTP 292
Cdd:cd00771 79 FEEEDEEYGLKP-----MNCPGHCLIFKSKprsyrDLPLRLAEFGTVHRYEQsGALH----GLTRVRGFTQDDAHIFCTP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499316359 293 EQADQAYEKMLAVVEDILTELKL-PYRLSlLSTGDMSFTASKtidaEVW 340
Cdd:cd00771 150 DQIKEEIKGVLDLIKEVYSDFGFfDYKVE-LSTRPEKFIGSD----EVW 193
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
185-397 |
4.27e-10 |
|
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: 60.07 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 185 REHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCV------EDGDQSLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACT 258
Cdd:cd00772 47 KEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVfkdagdEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 259 PCFRREAgaagANERGLVRVHQFNKVEMFAF-TTPEQADQAYEKMLAVVEDILTEL-KLPYRLSLLSTGDMSFTASKTID 336
Cdd:cd00772 127 NKFRDEI----RPRFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIARDLaAIDFIEGEADEGAKFAGASKSRE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499316359 337 AEVWLP-GQQSYYEVSSISQCTDFQSRRSETRYKDSQGKMHFIHTlNGSGLATPRLFVAILE 397
Cdd:cd00772 203 FEALMEdGKAKQAETGHIFGEGFARAFDLKAKFLDKDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
239-354 |
6.45e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 48.09 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 239 FHSQEIFNEKDLPI-YYAACTPCFRREAGAAganeRGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKL-- 315
Cdd:PRK00960 323 FFQGETVDVDELPIkFFDRSGWTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQVEEIRDELLKYAHILAEKLDLey 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499316359 316 -------PYRLS--LLSTGDMSFTASKTIDAEVWLP---GQQSYYEVSSIS 354
Cdd:PRK00960 399 wrevgddPFYLEgrGLEDRGIEFPDVPKYEMELWLPyrgDERKWVAVTSAN 449
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
186-397 |
4.19e-05 |
|
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: 44.87 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 186 EHGFQLWLPPLLVKREILFGSGQIPKFDGQYYCVED-GDQSLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACTPCFRRE 264
Cdd:cd00779 47 KIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDrHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 265 AgaagaNER-GLVRVHQFNKVEMFAF-TTPEQADQAYEKMLAVVEDILTELKLPYRLSLLSTGDMSFTASKTIDAEVWLP 342
Cdd:cd00779 127 I-----RPRfGLMRGREFLMKDAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAIGGSLSHEFHVLSPLK 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 499316359 343 GQQSyYEVSSISQCTDFQSRRSETRYKDSQGKMHFIHTlnGS-GLATPRLFVAILE 397
Cdd:cd00779 202 ITKG-IEVGHIFQLGTKYSKALGATFLDENGKPKPLEM--GCyGIGVSRLLAAIIE 254
|
|
| PRK04173 |
PRK04173 |
glycyl-tRNA synthetase; Provisional |
266-359 |
4.39e-03 |
|
glycyl-tRNA synthetase; Provisional
Pssm-ID: 235240 [Multi-domain] Cd Length: 456 Bit Score: 39.34 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 266 GAAGANE----RGLVRVHQFNKVEMFAFTTPEQADQAYEKMLAVVEDILTELKLP---YRLSLLSTGDMSFTASKTIDAE 338
Cdd:PRK04173 193 GKSFRNEitprNFIFRTREFEQMELEFFVKPGTDNEWFAYWIELRKNWLLDLGIDpenLRFREHLPEELAHYSKATWDIE 272
|
90 100
....*....|....*....|.
gi 499316359 339 VWLPGQQSYYEVSSISQCTDF 359
Cdd:PRK04173 273 YKFPFGRFWGELEGIANRTDY 293
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
223-396 |
7.59e-03 |
|
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 archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 37.96 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 223 DQSLYLIPTAEVVLNGFHSQEIFNEKDLPIYYAACTPCFRREAgaagANERGLVRVHQFnkveMF-----AFTTPEQADQ 297
Cdd:cd00778 91 EEPLALRPTSETAIYPMFSKWIRSYRDLPLKINQWVNVFRWET----KTTRPFLRTREF----LWqeghtAHATEEEAEE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499316359 298 AYEKMLAVVEDILTELK-LPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFqSRRSETRYKDSQGKMH 376
Cdd:cd00778 163 EVLQILDLYKEFYEDLLaIPVVKGRKTEWEKFAGADYTYTIEAMMPDGRALQSGTSHNLGQNF-SKAFDIKYQDKDGQKE 241
|
170 180
....*....|....*....|
gi 499316359 377 FIHTlNGSGLATpRLFVAIL 396
Cdd:cd00778 242 YVHQ-TSWGIST-RLIGAII 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
30-103 |
8.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 8.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499316359 30 ILDLDKEVRRLKTDSESLQSQRKLLSTQIHKAKAQGEDASNMI----SEVERISQDLEKLEASLEEKNATLQDLLVRL 103
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELealqAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
|
| |
