|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-424 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 845.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGEDLtDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEMREVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 81 EKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 161 SRFVFYKGAGARLERALISFMLDLHTdEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTNMH 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 241 RDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVM 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 321 SMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREpNGKPEHVHTLNGSGLAIGRTVAAILENY 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDE-DGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 228846882 401 QQEDGTIIIPEVLRPYMGGKTVIK 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 842.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGEDLtDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEMREVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPL-DVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 81 EKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 161 SRFVFYKGAGARLERALISFMLDLHTDEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTNMH 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 241 RDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVM 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 321 SMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREPNGKPEHVHTLNGSGLAIGRTVAAILENY 400
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....
gi 228846882 401 QQEDGTIIIPEVLRPYMGGKTVIK 424
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-417 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 649.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGE-DLTDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKD-AEALILEMRE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLsVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 79 VGEKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 159 TGSRFVFYKGAGARLERALISFMLDLHtDEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLL-EKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 239 MHRDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 319 VMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREPNGKPEHVHTLNGSGLAIGRTVAAILE 398
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 228846882 399 NYQQEDGTIIIPEVLRPYM 417
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-417 |
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: 563.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 120 DNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTGSRFVFYKGAGARLERALISFMLDLHTdEHGYEEVLPPYM 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 200 VNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTNMHRDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 280 QFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 228846882 360 QARRANIRFRREPNGKPEHVHTLNGSGLAIGRTVAAILENYQQEDGTIIIPEVLRPYM 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 ... |
213-400 |
4.38e-54 |
|
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: 177.99 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 213 KFEEDafriESEDYFLIPTAEVPVTNMHRDEILNKEQLPIRYAAFSSCFRSEAGsagRDTRGLIRQHQFNKVELVKFVKP 292
Cdd:pfam00587 2 KVEDE----NGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 293 EDSYEELEKLTNDAERVLQLLELPYRVMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREp 372
Cdd:pfam00587 75 GQSPDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDE- 153
|
170 180
....*....|....*....|....*...
gi 228846882 373 NGKPEHVHTLNGSGLAIGRTVAAILENY 400
Cdd:pfam00587 154 DNESKFPYMIHRAGLGVERFLAAILENN 181
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SerS |
COG0172 |
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ... |
1-424 |
0e+00 |
|
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439942 [Multi-domain] Cd Length: 421 Bit Score: 845.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGEDLtDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEMREVG 80
Cdd:COG0172 1 MLDIKLIRENPEAVKEALAKRGFDL-DVDELLELDEERRELQTEVEELRAERNALSKEIGKAKKKGEEAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 81 EKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTG 160
Cdd:COG0172 80 EEIKELEEELKELEEELDELLLSIPNLPHESVPVGKDESDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 161 SRFVFYKGAGARLERALISFMLDLHTdEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTNMH 240
Cdd:COG0172 160 SRFYVLKGDGARLERALIQFMLDLHT-EHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEGDDLYLIPTAEVPLTNLH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 241 RDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVM 320
Cdd:COG0172 239 RDEILDEEDLPLRYTAYTPCFRREAGSYGRDTRGLIRQHQFDKVEMVQFVKPEDSYEELEELTAHAEEILQKLGLPYRVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 321 SMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREpNGKPEHVHTLNGSGLAIGRTVAAILENY 400
Cdd:COG0172 319 LLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDE-DGKPEFVHTLNGSGLAVGRTLVAILENY 397
|
410 420
....*....|....*....|....
gi 228846882 401 QQEDGTIIIPEVLRPYMGGKTVIK 424
Cdd:COG0172 398 QQADGSVRIPEVLRPYMGGLEVIE 421
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1-424 |
0e+00 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 842.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGEDLtDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEMREVG 80
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAKRGFPL-DVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 81 EKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTG 160
Cdd:PRK05431 80 EEIKALEAELDELEAELEELLLRIPNLPHDSVPVGKDEDDNVEVRRWGEPREFDFEPKDHWELGEKLGILDFERAAKVSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 161 SRFVFYKGAGARLERALISFMLDLHTDEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTNMH 240
Cdd:PRK05431 160 SRFYVLKGDGARLERALIQFMLDLHTEEHGYTEVIPPYLVNEESMYGTGQLPKFEEDLYKIEDDDLYLIPTAEVPLTNLH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 241 RDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVM 320
Cdd:PRK05431 240 RDEILDEEELPLKYTAYSPCFRSEAGSAGRDTRGLIRVHQFDKVELVKFTKPEDSYAELEELTANAEEILQKLELPYRVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 321 SMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREPNGKPEHVHTLNGSGLAIGRTVAAILENY 400
Cdd:PRK05431 320 LLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEGDGKPELVHTLNGSGLAVGRTLVAILENY 399
|
410 420
....*....|....*....|....
gi 228846882 401 QQEDGTIIIPEVLRPYMGGKTVIK 424
Cdd:PRK05431 400 QQADGSVTIPEVLRPYMGGLEVIP 423
|
|
| serS |
TIGR00414 |
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ... |
1-417 |
0e+00 |
|
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam model tRNA-synt_2b. The seryl-tRNA synthetases of two archaeal species, Methanococcus jannaschii and Methanobacterium thermoautotrophicum, differ considerably and are included in a different model. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273066 [Multi-domain] Cd Length: 418 Bit Score: 649.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGE-DLTDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKD-AEALILEMRE 78
Cdd:TIGR00414 1 MLDRKLLRNNPDLVKESLKARGLsVDIDLEKLIALDDERKKLLSEIEELQAKRNELSKQIGKAKGQKKDkIEEIKKELKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 79 VGEKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKV 158
Cdd:TIGR00414 81 LKEELTELSAALKALEAELQDKLLSIPNIPHESVPVGKDEEDNLEVKRWGTPPVFDFKPKPHWELGEKLGGLDFDRAVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 159 TGSRFVFYKGAGARLERALISFMLDLHtDEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTN 238
Cdd:TIGR00414 161 TGSRFYYLKNDGAKLERALINFMLDLL-EKNGYQEIYPPYLVNEESLDGTGQLPKFEEDIFKLEDTDLYLIPTAEVPLTN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 239 MHRDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYR 318
Cdd:TIGR00414 240 LHRNEILEEEELPIKYTAHSPCFRSEAGSYGKDTKGLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 319 VMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREPNGKPEHVHTLNGSGLAIGRTVAAILE 398
Cdd:TIGR00414 320 VVNLCSGDLGFSAAKKYDLEVWMPGQNTYREISSCSNCTDFQARRLNIRYKDKNKGKNKYVHTLNGTALAIGRTIVAILE 399
|
410
....*....|....*....
gi 228846882 399 NYQQEDGTIIIPEVLRPYM 417
Cdd:TIGR00414 400 NYQTEDGSVEIPEVLRKYL 418
|
|
| SerRS_core |
cd00770 |
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ... |
120-417 |
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: 563.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 120 DNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTGSRFVFYKGAGARLERALISFMLDLHTdEHGYEEVLPPYM 199
Cdd:cd00770 1 DNVEIRRWGEPRVFDFKPKDHVELGEKLDILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLT-KRGFTPVIPPFL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 200 VNRASMTGTGQLPKFEEDAFRIESEDYFLIPTAEVPVTNMHRDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQH 279
Cdd:cd00770 80 VRKEVMEGTGQLPKFDEQLYKVEGEDLYLIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRGLFRVH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 280 QFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAF 359
Cdd:cd00770 160 QFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCSNCTDF 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 228846882 360 QARRANIRFRREPNGKPEHVHTLNGSGLAIGRTVAAILENYQQEDGTIIIPEVLRPYM 417
Cdd:cd00770 240 QARRLNIRYRDKKDGKKQYVHTLNGTALATPRTIVAILENYQTEDGSVVIPEVLRPYM 297
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
1-423 |
5.04e-124 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 366.72 E-value: 5.04e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRT----NFEEVKAKLQHRGEDLTDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEM 76
Cdd:PLN02678 1 MLDINLFREekggDPELIRESQRRRFASVELVDEVIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 77 REVGEKVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGETEDDNVVARTWGEvKEFAFEPKPHWDLATDLGILDFERAG 156
Cdd:PLN02678 81 KELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNDEANNAVVRTWGE-KRQEPKLKNHVDLVELLGIVDTERGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 157 KVTGSRFVFYKGAGARLERALISFMLDLHTDEhGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRI--ESEDYFLIPTAEV 234
Cdd:PLN02678 160 DVAGGRGYYLKGAGVLLNQALINFGLAFLRKR-GYTPLQTPFFMRKDVMAKCAQLAQFDEELYKVtgEGDDKYLIATSEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 235 PVTNMHRDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPED--SYEELEKLTNDAERVLQL 312
Cdd:PLN02678 239 PLCAYHRGDWIDPKELPIRYAGYSTCFRKEAGSHGRDTLGIFRVHQFEKVEQFCITSPNGneSWEMHEEMLKNSEDFYQS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 313 LELPYRVMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREPNG--KPEHVHTLNGSGLAIG 390
Cdd:PLN02678 319 LGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQSRRLEIRYGQKKSNeqTKQYVHLLNSTLTATE 398
|
410 420 430
....*....|....*....|....*....|...
gi 228846882 391 RTVAAILENYQQEDGtIIIPEVLRPYMGGKTVI 423
Cdd:PLN02678 399 RTLCCILENYQTEDG-VRVPEVLQPFMGGIEFL 430
|
|
| PLN02320 |
PLN02320 |
seryl-tRNA synthetase |
2-424 |
9.66e-99 |
|
seryl-tRNA synthetase
Pssm-ID: 177954 [Multi-domain] Cd Length: 502 Bit Score: 303.77 E-value: 9.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 2 LDIKFLRTNFEEVKAKLQHRGEDlTDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVlKREKKDAEALILEMREVGE 81
Cdd:PLN02320 67 IDFKWIRDNKEAVAINIRNRNSN-ANLELVLELYENMLALQKEVERLRAERNAVANKMKG-KLEPSERQALVEEGKNLKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 82 KVKDLDNELRTVEEDLERLMLSIPNIPHESAPVGeTEDDNVVARTWGEVKEFAFEPKPHWDLATDLGILDFERAGKVTGS 161
Cdd:PLN02320 145 GLVTLEEDLVKLTDELQLEAQSIPNMTHPDVPVG-GEDSSAVRKEVGSPREFSFPIKDHLQLGKELDLFDFDAAAEVSGS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 162 RFVFYKGAGARLERALISFMLDlHTDEHGYEEVLPPYMVNRASMTGTGQLPKFEE-DAFRIESEDYFLIPTAEVPVTNMH 240
Cdd:PLN02320 224 KFYYLKNEAVLLEMALVNWTLS-EVMKKGFTPLTTPEIVRSSVVEKCGFQPRGDNtQVYSIDGSDQCLIGTAEIPVGGIH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 241 RDEILNKEQLPIRYAAFSSCFRSEAGSAGRDTRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVM 320
Cdd:PLN02320 303 MDSILLESALPLKYVAFSHCFRTEAGAAGAATRGLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFKTL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 321 SMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFR-REPN-----------GKPEHVHTLNGSGLA 388
Cdd:PLN02320 383 DMATADLGAPAYRKFDIEAWMPGLGRYGEISSASNCTDYQSRRLGIRYRpSEPPqtnpkkgkgslGPTKFVHTLNATACA 462
|
410 420 430
....*....|....*....|....*....|....*.
gi 228846882 389 IGRTVAAILENYQQEDGTIIIPEVLRPYMGGKTVIK 424
Cdd:PLN02320 463 VPRMIVCLLENYQQEDGSVVIPEPLRPFMGGLELIK 498
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
213-400 |
4.38e-54 |
|
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: 177.99 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 213 KFEEDafriESEDYFLIPTAEVPVTNMHRDEILNKEQLPIRYAAFSSCFRSEAGsagRDTRGLIRQHQFNKVELVKFVKP 292
Cdd:pfam00587 2 KVEDE----NGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEAS---GDTRGLIRVRQFHQDDAHIFHAP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 293 EDSYEELEKLTNDAERVLQLLELPYRVMSMCTGDLGFTAAKKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREp 372
Cdd:pfam00587 75 GQSPDELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDE- 153
|
170 180
....*....|....*....|....*...
gi 228846882 373 NGKPEHVHTLNGSGLAIGRTVAAILENY 400
Cdd:pfam00587 154 DNESKFPYMIHRAGLGVERFLAAILENN 181
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
1-108 |
2.49e-40 |
|
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: 139.26 E-value: 2.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 1 MLDIKFLRTNFEEVKAKLQHRGEDLTDFGRFEELDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEMREVG 80
Cdd:pfam02403 1 MLDIKLIRENPEAVKESLKKRGVDVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEVKELK 80
|
90 100
....*....|....*....|....*...
gi 228846882 81 EKVKDLDNELRTVEEDLERLMLSIPNIP 108
Cdd:pfam02403 81 DELKALEAELKELEAELDKLLLTIPNIP 108
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
171-397 |
5.58e-27 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 107.86 E-value: 5.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 171 ARLERALISFMLdlhtdEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRIESE-------DYFLIPTAEVPVTNMHRDE 243
Cdd:cd00670 6 RALERFLDDRMA-----EYGYQEILFPFLAPTVLFFKGGHLDGYRKEMYTFEDKgrelrdtDLVLRPAACEPIYQIFSGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 244 ILNKEQLPIRYAAFSSCFRSEAGSAgrdtRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLELPYRVMSMC 323
Cdd:cd00670 81 ILSYRALPLRLDQIGPCFRHEPSGR----RGLMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 324 TGDLGFTAA--------KKYDIEVWIPSYGTYREISSCSNFEAFQARRANIRFRREPNGKpehVHTLNGSGLAIGRTVAA 395
Cdd:cd00670 157 DPFFGRGGKrgldagreTVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGGGR---AHTGCGGAGGEERLVLA 233
|
..
gi 228846882 396 IL 397
Cdd:cd00670 234 LL 235
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
172-380 |
4.64e-16 |
|
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: 76.39 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 172 RLERALISFMldlhtDEHGYEEVLPPYMVNRASMTGTGQLPKfEEDAFR-IESEDYFLIPTAEVPVTNMHRDEIlnkEQL 250
Cdd:cd00768 4 KIEQKLRRFM-----AELGFQEVETPIVEREPLLEKAGHEPK-DLLPVGaENEEDLYLRPTLEPGLVRLFVSHI---RKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 251 PIRYAAFSSCFRSEAGSagrdtRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLE--LPYRVMSMCTGDLG 328
Cdd:cd00768 75 PLRLAEIGPAFRNEGGR-----RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGikLDIVFVEKTPGEFS 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 228846882 329 FTAAK-KYDIEVWIPSyGTYREISSCSNFEAFQARRANIRFRREPN--GKPEHVH 380
Cdd:cd00768 150 PGGAGpGFEIEVDHPE-GRGLEIGSGGYRQDEQARAADLYFLDEALeyRYPPTIG 203
|
|
| PRK00960 |
PRK00960 |
seryl-tRNA synthetase; Provisional |
34-349 |
2.37e-09 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 234876 [Multi-domain] Cd Length: 517 Bit Score: 59.26 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 34 LDTRRRELLVQTEELKSKRNEVSQQISVLKREKKDAEALILEMREVGE---KVKDLDNELRTVEEDLERLMLSIPNiphe 110
Cdd:PRK00960 98 IEIDNYVITIPADGEKVIELEGLKVPPCVVEIEGEKGTIILIFKDVGEselKRNIIDRAIKLVEEKLEKLEDLTFY---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 111 sapVGETEDDNVVARTwgEVKEFAFEPKPHwDLATDLG-ILDFERAGKVtgsrfvFYKGAGARLERALISFMLDLHTDEH 189
Cdd:PRK00960 174 ---VGKAEPGTIVSES--KKREITFDGDPT-EEAEKLGwVKRFPGRGQW------FYTPPMTKLFRAFEKLVIEEVLKPL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 190 GYEEVLPPYMVNRASMTGTGQL------------PKFEEDAFRiESEDYFLIpTAEVPVTNMHR---------------- 241
Cdd:PRK00960 242 GFDECLFPKLIPLEVMYKMRYLeglpegmyyvcpPKRDPEYFE-EFVDEMMV-KKEVPIEKLKEklrdpgyvlapaqcep 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 242 ------DEILNKEQLPIRYAAFSS-CFRSEAGSAgrdtRGLIRQHQFNKVELVKFVKPEDSYEELEKLTNDAERVLQLLE 314
Cdd:PRK00960 320 fyqffqGETVDVDELPIKFFDRSGwTYRWEGGGA----HGLERVNEFHRIEIVWLGTPEQVEEIRDELLKYAHILAEKLD 395
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 228846882 315 LPYRVMSMCT-----------GDLGFTAAKKYDIEVWIPSYGTYRE 349
Cdd:PRK00960 396 LEYWREVGDDpfylegrgledRGIEFPDVPKYEMELWLPYRGDERK 441
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
139-319 |
3.87e-09 |
|
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: 57.56 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 139 PHWDLATDLGILDFERAgkvTGSRFVFYKGAGARLERALISFMLDLHtDEHGYEEVLPPYMVNRASMTGTGQLPKFEEDA 218
Cdd:cd00771 1 DHRRLGGELELFFFFDE---AGPGLPFWLPKGAIIRNELEDFLRELQ-RKRGYQEVETPIIYNKELWETSGHWDHYRENM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 219 FRIESED--YFLIPTAEVPVTNMHRDEILNKEQLPIRYAAFSSCFRSEA-GSAGrdtrGLIRQHQFNKVELVKFVKPEDS 295
Cdd:cd00771 77 FPFEEEDeeYGLKPMNCPGHCLIFKSKPRSYRDLPLRLAEFGTVHRYEQsGALH----GLTRVRGFTQDDAHIFCTPDQI 152
|
170 180
....*....|....*....|....*..
gi 228846882 296 YEELE---KLTNDAERVLQLLELPYRV 319
Cdd:cd00771 153 KEEIKgvlDLIKEVYSDFGFFDYKVEL 179
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
160-264 |
1.34e-06 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 50.42 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 160 GSRFVFYKGAGARLERALISFMLDLHtDEHGYEEVLPPYMVNR----ASmtgtGQLPKFEEDAF--RIESEDYFLIPtae 233
Cdd:COG0441 260 GPGLPFWHPKGAIIRRELEDYIREKH-RKAGYQEVKTPHILDRelweTS----GHWDHYRENMFptESDGEEYALKP--- 331
|
90 100 110
....*....|....*....|....*....|....*....
gi 228846882 234 vpvtnM---HRDEILNKEQ-----LPIRYAAFSSCFRSE 264
Cdd:COG0441 332 -----MncpGHILIYKSGLrsyrdLPLRLAEFGTVHRYE 365
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
178-398 |
3.63e-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: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 178 ISFMLDLHTDEHGYEEVLPPYMVNRASMTGTGQLPKFEEDAFRI---ESEDYFLIPTAEVPVTNMHRDEILNKEQLPIRY 254
Cdd:cd00779 37 IENIIREEMNKIGAQEILMPILQPAELWKESGRWDAYGPELLRLkdrHGKEFLLGPTHEEVITDLVANEIKSYKQLPLNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 255 AAFSSCFRSEAgsagRDTRGLIRQHQFnkveLVKfvkpeDSY------EELEK---LTNDA-ERVLQLLELPYRVMSMCT 324
Cdd:cd00779 117 YQIQTKFRDEI----RPRFGLMRGREF----LMK-----DAYsfdideESLEEtyeKMYQAySRIFKRLGLPFVKVEADS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 325 GDLGFTAAKKY----------DIEV-WIPSYGT-YReisscsnfEAFQARRANirfrrePNGKPEHVHTlnGS-GLAIGR 391
Cdd:cd00779 184 GAIGGSLSHEFhvlsplkitkGIEVgHIFQLGTkYS--------KALGATFLD------ENGKPKPLEM--GCyGIGVSR 247
|
....*..
gi 228846882 392 TVAAILE 398
Cdd:cd00779 248 LLAAIIE 254
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
178-398 |
4.11e-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.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 45.05 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 178 ISFMLDLHTDEHGYEEVLPPYMVNRASMTGTGQLPK--------FEEDAFRIESEDYFLIPTAEVPVTNMHRDEILNKEQ 249
Cdd:cd00772 38 IENVLDKMFKEHGAQNALFPFFILASFLEKEAEHDEgfskelavFKDAGDEELEEDFALRPTLEENIGEIAAKFIKSWKD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 250 LPIRYAAFSSCFRSEAgsagRDTRGLIRQHQFNKVELVKFVKPEDSYEE--LEKLTNDAERVLQLLELPYRVMSMCTGDL 327
Cdd:cd00772 118 LPQHLNQIGNKFRDEI----RPRFGFLRAREFIMKDGHSAHADAEEADEefLNMLSAYAEIARDLAAIDFIEGEADEGAK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 228846882 328 GFTAAKKYDIEVwIPSYGTYREISSCSNFEAFQARRANIRFR-REPNGKPEHVHTlNGSGLAIGRTVAAILE 398
Cdd:cd00772 194 FAGASKSREFEA-LMEDGKAKQAETGHIFGEGFARAFDLKAKfLDKDGKEKFFEM-GCWGIGISRFIGAIIE 263
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
165-340 |
6.78e-05 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 45.15 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 165 FYKGAGARLERALISFMLDlHTDEHGYEEVLPPYMVNRASMTGTGQLPKFEED--AFRIESEDYFLIPTAEVPVTNMHRD 242
Cdd:PLN02908 315 FFLPHGARIYNKLMDFIRE-QYWERGYDEVITPNIYNMDLWETSGHAAHYKENmfVFEIEKQEFGLKPMNCPGHCLMFAH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 243 EILNKEQLPIRYAAFSSCFRSEAGSAgrdTRGLIRQHQFNKVELVKFVKPEDSYEELEKltndaerVLQLLELPYRVMSM 322
Cdd:PLN02908 394 RVRSYRELPLRLADFGVLHRNELSGA---LTGLTRVRRFQQDDAHIFCREDQIKDEVKG-------VLDFLDYVYEVFGF 463
|
170 180
....*....|....*....|.
gi 228846882 323 cTGDLGF-TAAKKY--DIEVW 340
Cdd:PLN02908 464 -TYELKLsTRPEKYlgDLETW 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-100 |
1.83e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 228846882 32 EELDTRRRELlvqtEELKSKRNEVSQQISVLKREKKDAEALILEMREVGEKVKDLDNELRTVEEDLERL 100
Cdd:PRK03918 518 EELEKKAEEY----EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
9-107 |
3.55e-03 |
|
chromosome segregation protein SMC, common bacterial 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. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 228846882 9 TNFEEVKAKLQHRGEDLTdfGRFEELDTRRRELlvqTEELKSKRNEVSQQISVLKREKKDAEALILEMREVGEKVKDLDN 88
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLA--AEIEELEELIEEL---ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
90 100
....*....|....*....|....*.
gi 228846882 89 ELR-------TVEEDLERLMLSIPNI 107
Cdd:TIGR02168 916 ELEelreklaQLELRLEGLEVRIDNL 941
|
|
| |
