|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 652.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKKDPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMMDNVERISQ 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 81 DLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 161 GWPAYKNQGVCLEWALLTYLLNKQR-EHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGF 239
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDD--LYLIPTAEVPLTNL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 240 HSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRL 319
Cdd:PRK05431 239 HRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 320 SLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNR-GKMHFVHTLNGSGLATPRLFVAILEN 398
Cdd:PRK05431 319 VLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGdGKPELVHTLNGSGLAVGRTLVAILEN 398
|
410 420
....*....|....*....|....*.
gi 499409919 399 NQQEDGSVIIPEVLRPYLENQEVLLP 424
Cdd:PRK05431 399 YQQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| 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: 638.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKKDPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMMDNVERISQ 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 81 DLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 161 GWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGFH 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDD--LYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 241 SQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRLS 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 321 LLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNRGKMHFVHTLNGSGLATPRLFVAILENNQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|..
gi 499409919 401 QEDGSVIIPEVLRPYLENQEVL 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 |
4.06e-167 |
|
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: 470.50 E-value: 4.06e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 120 NQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGSGWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVK 199
Cdd:cd00770 2 NVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 200 HEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGFHSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVH 279
Cdd:cd00770 82 KEVMEGTGQLPKFDEQLYKVEGED--LYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 280 QFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499409919 360 QSRRSETRYKDNR-GKMHFVHTLNGSGLATPRLFVAILENNQQEDGSVIIPEVLRPYL 416
Cdd:cd00770 240 QARRLNIRYRDKKdGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
6.48e-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: 467.23 E-value: 6.48e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKK--DPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGED-VSSMMDNVER 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARglSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 78 ISQDLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKT 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 158 SGSGWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLN 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTD--LYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 238 GFHSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPY 317
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 318 RLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNR-GKMHFVHTLNGSGLATPRLFVAIL 396
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNkGKNKYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 499409919 397 ENNQQEDGSVIIPEVLRPYL 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 ... |
217-399 |
5.77e-47 |
|
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: 159.50 E-value: 5.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 217 YRVED-GEQSLYLIPTAEVVLNGFHSQEIFSEKDLPIYYAAFTPCFRREAGAAgahERGLVRVHQFHKVEMFAFTTPDQA 295
Cdd:pfam00587 1 YKVEDeNGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGD---TRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 296 DQAYEKMLAVVEDILTELQLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNRGKM 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES 157
|
170 180
....*....|....*....|....
gi 499409919 376 HFVHTLNGSGLATPRLFVAILENN 399
Cdd:pfam00587 158 KFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 652.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKKDPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMMDNVERISQ 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 81 DLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 161 GWPAYKNQGVCLEWALLTYLLNKQR-EHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGF 239
Cdd:PRK05431 161 RFYVLKGDGARLERALIQFMLDLHTeEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDD--LYLIPTAEVPLTNL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 240 HSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRL 319
Cdd:PRK05431 239 HRDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 320 SLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNR-GKMHFVHTLNGSGLATPRLFVAILEN 398
Cdd:PRK05431 319 VLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGdGKPELVHTLNGSGLAVGRTLVAILEN 398
|
410 420
....*....|....*....|....*.
gi 499409919 399 NQQEDGSVIIPEVLRPYLENQEVLLP 424
Cdd:PRK05431 399 YQQADGSVTIPEVLRPYMGGLEVIPP 424
|
|
| 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: 638.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKKDPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMMDNVERISQ 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDLDVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 81 DLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGS 160
Cdd:COG0172 81 EIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 161 GWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGFH 240
Cdd:COG0172 161 RFYVLKGDGARLERALIQFMLDLHTEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDD--LYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 241 SQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRLS 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 321 LLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNRGKMHFVHTLNGSGLATPRLFVAILENNQ 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEFVHTLNGSGLAVGRTLVAILENYQ 398
|
410 420
....*....|....*....|..
gi 499409919 401 QEDGSVIIPEVLRPYLENQEVL 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 |
4.06e-167 |
|
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: 470.50 E-value: 4.06e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 120 NQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGSGWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVK 199
Cdd:cd00770 2 NVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPFLVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 200 HEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGFHSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVH 279
Cdd:cd00770 82 KEVMEGTGQLPKFDEQLYKVEGED--LYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 280 QFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 499409919 360 QSRRSETRYKDNR-GKMHFVHTLNGSGLATPRLFVAILENNQQEDGSVIIPEVLRPYL 416
Cdd:cd00770 240 QARRLNIRYRDKKdGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-416 |
6.48e-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: 467.23 E-value: 6.48e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKK--DPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGED-VSSMMDNVER 77
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARglSVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 78 ISQDLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKT 157
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 158 SGSGWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLN 237
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLLEKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTD--LYLIPTAEVPLT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 238 GFHSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPY 317
Cdd:TIGR00414 239 NLHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 318 RLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNR-GKMHFVHTLNGSGLATPRLFVAIL 396
Cdd:TIGR00414 319 RVVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNkGKNKYVHTLNGTALAIGRTIVAIL 398
|
410 420
....*....|....*....|
gi 499409919 397 ENNQQEDGSVIIPEVLRPYL 416
Cdd:TIGR00414 399 ENYQTEDGSVEIPEVLRKYL 418
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-424 |
4.77e-101 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 309.93 E-value: 4.77e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 2 LDIKLIRKAPEECETRLRKKDPLISLQPILDLDKEIRHLKTETEALQSQRKLLSNQIhKAKAQGEDVSSMMDNVERISQD 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSNANLELVLELYENMLALQKEVERLRAERNAVANKM-KGKLEPSERQALVEEGKNLKEG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 82 LAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTgNQVIKQVGALPTFSFTPKHHVELNQKLQILDFKLPAKTSGSG 161
Cdd:PLN02320 146 LVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVGGEDS-SAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVSGSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 162 WPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDG-QYYRVEDGEQSLylIPTAEVVLNGFH 240
Cdd:PLN02320 225 FYYLKNEAVLLEMALVNWTLSEVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCL--IGTAEIPVGGIH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 241 SQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRLS 320
Cdd:PLN02320 303 MDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFKTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 321 LLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRY-------------KDNRGKMHFVHTLNGSGLA 387
Cdd:PLN02320 383 DMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYrpseppqtnpkkgKGSLGPTKFVHTLNATACA 462
|
410 420 430
....*....|....*....|....*....|....*..
gi 499409919 388 TPRLFVAILENNQQEDGSVIIPEVLRPYLENQEVLLP 424
Cdd:PLN02320 463 VPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIKP 499
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-422 |
1.76e-93 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 288.53 E-value: 1.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIR----KAPE---ECETRlRKKDPLIsLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMMD 73
Cdd:PLN02678 1 MLDINLFReekgGDPElirESQRR-RFASVEL-VDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 74 NVERISQDLAKLEPLLEQKESTLQDMLVRLPNYPDEDVPVCPDKTGNQVIKQVGaLPTFSFTPKHHVELNQKLQILDFKL 153
Cdd:PLN02678 79 ETKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWG-EKRQEPKLKNHVDLVELLGIVDTER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 154 PAKTSGSGWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVE-DGEQSlYLIPTA 232
Cdd:PLN02678 158 GADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVTgEGDDK-YLIATS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 233 EVVLNGFHSQEIFSEKDLPIYYAAFTPCFRREAGAAGAHERGLVRVHQFHKVEMFAFTTPDQAD--QAYEKMLAVVEDIL 310
Cdd:PLN02678 237 EQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGNEswEMHEEMLKNSEDFY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 311 TELQLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRY---KDNRGKMHFVHTLNGSGLA 387
Cdd:PLN02678 317 QSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYgqkKSNEQTKQYVHLLNSTLTA 396
|
410 420 430
....*....|....*....|....*....|....*
gi 499409919 388 TPRLFVAILENNQQEDGsVIIPEVLRPYLENQEVL 422
Cdd:PLN02678 397 TERTLCCILENYQTEDG-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 ... |
217-399 |
5.77e-47 |
|
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: 159.50 E-value: 5.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 217 YRVED-GEQSLYLIPTAEVVLNGFHSQEIFSEKDLPIYYAAFTPCFRREAGAAgahERGLVRVHQFHKVEMFAFTTPDQA 295
Cdd:pfam00587 1 YKVEDeNGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGD---TRGLIRVRQFHQDDAHIFHAPGQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 296 DQAYEKMLAVVEDILTELQLPYRLSLLSTGDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNRGKM 375
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNES 157
|
170 180
....*....|....*....|....
gi 499409919 376 HFVHTLNGSGLATPRLFVAILENN 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 |
3.57e-33 |
|
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: 124.43 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 169 GVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDG-----EQSLYLIPTAEVVLNGFHSQE 243
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelrDTDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 244 IFSEKDLPIYYAAFTPCFRREAGAAgaheRGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQLPYRLSLLS 323
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 324 TGDMSFT--------ASKTIDAEVWLPGQQSYYEVSSISQCTDFQSRRSETRYKDNRGKmhFVHTLNGSGLATPRLFVAI 395
Cdd:cd00670 157 DPFFGRGgkrgldagRETVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGGG--RAHTGCGGAGGEERLVLAL 234
|
.
gi 499409919 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 |
9.07e-26 |
|
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: 100.36 E-value: 9.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 1 MLDIKLIRKAPEECETRLRKK--DPLIsLQPILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMMDNVERI 78
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRgvDVLD-VDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKEL 79
|
90 100
....*....|....*....|....*....
gi 499409919 79 SQDLAKLEPLLEQKESTLQDMLVRLPNYP 107
Cdd:pfam02403 80 KDELKALEAELKELEAELDKLLLTIPNIP 108
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
174-391 |
9.54e-20 |
|
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: 87.17 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 174 WALLTYLLNKQ-REHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVEDGEqsLYLIPTAEVVLNGFHSQEIFsekDLPI 252
Cdd:cd00768 2 RSKIEQKLRRFmAELGFQEVETPIVEREPLLEKAGHEPKDLLPVGAENEED--LYLRPTLEPGLVRLFVSHIR---KLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 253 YYAAFTPCFRREAgaagaHERGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTEL--QLPYRLSLLSTGDMSFT 330
Cdd:cd00768 77 RLAEIGPAFRNEG-----GRRGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALgiKLDIVFVEKTPGEFSPG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499409919 331 -ASKTIDAEVWLPgQQSYYEVSSISQCTDFQSRRSETRYKDNRGKMHFVHTLNGsGLATPRL 391
Cdd:cd00768 152 gAGPGFEIEVDHP-EGRGLEIGSGGYRQDEQARAADLYFLDEALEYRYPPTIGF-GLGLERL 211
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
139-340 |
6.71e-13 |
|
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: 68.73 E-value: 6.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 139 HVELNQKLQILDFklpAKTSGSGWPAYKNQGVCLEWALLTYLLNKQREHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYR 218
Cdd:cd00771 2 HRRLGGELELFFF---FDEAGPGLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETSGHWDHYRENMFP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 219 VEDGEQSLYLIPtaevvLNGFHSQEIF-----SEKDLPIYYAAFTPCFRREA-GAAGaherGLVRVHQFHKVEMFAFTTP 292
Cdd:cd00771 79 FEEEDEEYGLKP-----MNCPGHCLIFkskprSYRDLPLRLAEFGTVHRYEQsGALH----GLTRVRGFTQDDAHIFCTP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 499409919 293 DQADQAYEKMLAVVEDILTELQL-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 |
1.08e-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: 62.00 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 185 REHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRV------EDGEQSLYLIPTAEVVLNGFHSQEIFSEKDLPIYYAAFT 258
Cdd:cd00772 47 KEHGAQNALFPFFILASFLEKEAEHDEGFSKELAVfkdagdEELEEDFALRPTLEENIGEIAAKFIKSWKDLPQHLNQIG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 259 PCFRREAGAagahERGLVRVHQFHKVEMFAF-TTPDQADQAYEKMLAVVEDILTEL-QLPYRLSLLSTGDMSFTASKTID 336
Cdd:cd00772 127 NKFRDEIRP----RFGFLRAREFIMKDGHSAhADAEEADEEFLNMLSAYAEIARDLaAIDFIEGEADEGAKFAGASKSRE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499409919 337 AEVWLP-GQQSYYEVSSISQCTDFQSRRSETRYKDNRGKMHFVHTlNGSGLATPRLFVAILE 397
Cdd:cd00772 203 FEALMEdGKAKQAETGHIFGEGFARAFDLKAKFLDKDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
239-354 |
2.28e-06 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 49.63 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 239 FHSQEIFSEKDLPI-YYAAFTPCFRREAGaaGAHerGLVRVHQFHKVEMFAFTTPDQADQAYEKMLAVVEDILTELQL-- 315
Cdd:PRK00960 323 FFQGETVDVDELPIkFFDRSGWTYRWEGG--GAH--GLERVNEFHRIEIVWLGTPEQVEEIRDELLKYAHILAEKLDLey 398
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 499409919 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 ... |
186-327 |
2.87e-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: 45.26 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 186 EHGFQLWLPPLLVKHEILFGSGQIPKFDGQYYRVED-GEQSLYLIPTAEVVLNGFHSQEIFSEKDLPIYYAAFTPCFRRE 264
Cdd:cd00779 47 KIGAQEILMPILQPAELWKESGRWDAYGPELLRLKDrHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNLYQIQTKFRDE 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499409919 265 AgaagaheR---GLVRVHQFHKVEMFAF-TTPDQADQAYEKMLAVVEDILTELQLPYRLSLLSTGDM 327
Cdd:cd00779 127 I-------RprfGLMRGREFLMKDAYSFdIDEESLEETYEKMYQAYSRIFKRLGLPFVKVEADSGAI 186
|
|
| ProRS_core_arch_euk |
cd00778 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
174-396 |
3.33e-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 archaea, the cytoplasm of eukaryotes and some bacteria.
Pssm-ID: 238401 [Multi-domain] Cd Length: 261 Bit Score: 45.28 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 174 WALLTYLLNKQ-REHGFQLWLPPLLV-KHEILFGSGQIPKFDGQYYRVEDG-----EQSLYLIPTAEVVLNGFHSQEIFS 246
Cdd:cd00778 35 WENIQKILDKEiKETGHENVYFPLLIpESELEKEKEHIEGFAPEVAWVTHGgleelEEPLALRPTSETAIYPMFSKWIRS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 247 EKDLPIYYAAFTPCFRREAgaagAHERGLVRVHQFHKVEMF-AFTTPDQADQAYEKMLAVVEDILTELQ-LPYRLSLLST 324
Cdd:cd00778 115 YRDLPLKINQWVNVFRWET----KTTRPFLRTREFLWQEGHtAHATEEEAEEEVLQILDLYKEFYEDLLaIPVVKGRKTE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499409919 325 GDMSFTASKTIDAEVWLPGQQSYYEVSSISQCTDFqSRRSETRYKDNRGKMHFVHTlNGSGLATpRLFVAIL 396
Cdd:cd00778 191 WEKFAGADYTYTIEAMMPDGRALQSGTSHNLGQNF-SKAFDIKYQDKDGQKEYVHQ-TSWGIST-RLIGAII 259
|
|
| DASH_Dad2 |
pfam08654 |
DASH complex subunit Dad2; The DASH complex is a ~10 subunit microtubule-binding complex that ... |
37-104 |
4.49e-03 |
|
DASH complex subunit Dad2; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro.
Pssm-ID: 430134 Cd Length: 99 Bit Score: 36.42 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 37 IRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSSMM---DNVER-ISQDLAKL-------------EPLLEQKESTLQDM 99
Cdd:pfam08654 14 LKQLRDLSATLANQLEELSEKLSTLADGTEAVASVManwDSVLRaISMASLKLlqyaennaadeeeDTSEEEEEDPLPET 93
|
....*
gi 499409919 100 LVRLP 104
Cdd:pfam08654 94 LVRIP 98
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-112 |
5.90e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499409919 4 IKLIRKAPEECETRLRKKDPLIS-LQ-PILDLDKEIRHLKTETEALQSQRKLLSNQIHKAKAQGEDVSsmmdnvERISQD 81
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEeLEaALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR------KRLSEL 922
|
90 100 110
....*....|....*....|....*....|.
gi 499409919 82 LAKLEPLLEQkESTLQDMLVRLPNYPDEDVP 112
Cdd:TIGR02169 923 KAKLEALEEE-LSEIEDPKGEDEEIPEEELS 952
|
|
| |
