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Conserved domains on  [gi|17542084|ref|NP_500549|]
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serine--tRNA ligase [Caenorhabditis elegans]

Protein Classification

class-II aminoacyl-tRNA synthetase family protein( domain architecture ID 1270)

class-II aminoacyl-tRNA synthetase family protein contains a class II tRNA amino-acyl synthetase-like catalytic core domain

PubMed:  8274143|10447505
SCOP:  4001782

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 131-423 3.63e-98

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.


The actual alignment was detected with superfamily member cd00770:

Pssm-ID: 444800 [Multi-domain]  Cd Length: 297  Bit Score: 296.01  E-value: 3.63e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 131 QAKIVAEWGEKRE------DECLTAEKLvqTWRSLLHPTDASGQRSYVFLGALASLEKALLDYAHERVCALGFRPITVPD 204
Cdd:cd00770   1 DNVEIRRWGEPRVfdfkpkDHVELGEKL--DILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 205 IVSGEVTQACGvmQRSDHPIQ-YTLAGEESHtkLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASEAK- 282
Cdd:cd00770  79 LVRKEVMEGTG--QLPKFDEQlYKVEGEDLY--LIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRg 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 283 LYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSAS 362
Cdd:cd00770 155 LFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCS 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542084 363 NCTDFQSRRLGIKYK-TADGTTKYAHTCNGTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:cd00770 235 NCTDFQARRLNIRYRdKKDGKKQYVHTLNGTALATPRTIVAILENYQT-EDGSVVIPEVLRP 295
 
Name Accession Description Interval E-value
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
 131-423 3.63e-98

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: 296.01  E-value: 3.63e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 131 QAKIVAEWGEKRE------DECLTAEKLvqTWRSLLHPTDASGQRSYVFLGALASLEKALLDYAHERVCALGFRPITVPD 204
Cdd:cd00770   1 DNVEIRRWGEPRVfdfkpkDHVELGEKL--DILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 205 IVSGEVTQACGvmQRSDHPIQ-YTLAGEESHtkLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASEAK- 282
Cdd:cd00770  79 LVRKEVMEGTG--QLPKFDEQlYKVEGEDLY--LIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRg 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 283 LYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSAS 362
Cdd:cd00770 155 LFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCS 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542084 363 NCTDFQSRRLGIKYK-TADGTTKYAHTCNGTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:cd00770 235 NCTDFQARRLNIRYRdKKDGKKQYVHTLNGTALATPRTIVAILENYQT-EDGSVVIPEVLRP 295
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
 54-423 2.10e-87

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: 272.65  E-value: 2.10e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  54 KNLEAIRENILNRKGVGDIDKV------------------HKKWAV---IQKMMKSGE------KQTNG-----AVSEQK 101
Cdd:COG0172   9 ENPEAVKEALAKRGFDLDVDELleldeerrelqteveelrAERNALskeIGKAKKKGEeaealiAEVKElkeeiKELEEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 102 YKQLWDELYDEAILIPNMTQDGVPRG-SEDQAKIVAEWGEKRE-D----------ECL------TAEKLvqtwrsllhpt 163
Cdd:COG0172  89 LKELEEELDELLLSIPNLPHESVPVGkDESDNVEVRRWGEPREfDfepkdhwelgEKLgildfeRAAKV----------- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 164 daSGQRSYVFLGALASLEKAL----LDYAHERvcalGFRPITVPDIVSGEVTQacGVMQRSDHpiqytlaGEES-HTK-- 236
Cdd:COG0172 158 --SGSRFYVLKGDGARLERALiqfmLDLHTEH----GYTEVIPPYLVNEESMY--GTGQLPKF-------EEDLyKIEgd 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 237 ---LSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRteisksaSEA----K----LYRVHEFSKVEMFVVSTPEQSAA 305
Cdd:COG0172 223 dlyLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFR-------REAgsygRdtrgLIRQHQFDKVEMVQFVKPEDSYE 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 306 ELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTADGTTKY 385
Cdd:COG0172 296 ELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEF 375

                       410       420       430
                ....*....|....*....|....*....|....*...
gi 17542084 386 AHTCNGTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:COG0172 376 VHTLNGSGLAVGRTLVAILENYQQ-ADGSVRIPEVLRP 412
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 54-423 1.03e-83

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 263.08  E-value: 1.03e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   54 KNLEAIRENILNRKGVGDIDKV------------------HKKWAV---IQKMMKSGE------KQTNG-----AVSEQK 101
Cdd:PRK05431   9 ENPEAVKEALAKRGFPLDVDELleldeerrelqteleelqAERNALskeIGQAKRKGEdaealiAEVKElkeeiKALEAE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  102 YKQLWDELYDEAILIPNMTQDGVPRG-SEDQAKIVAEWGEKRE-D----------ECL------TAEKLvqtwrsllhpt 163
Cdd:PRK05431  89 LDELEAELEELLLRIPNLPHDSVPVGkDEDDNVEVRRWGEPREfDfepkdhwelgEKLgildfeRAAKV----------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  164 daSGQRSYVFLGALASLEKALLDYA---HerVCALGFRPITVPDIVSGEVTQACGvmQRSDHPIQ-YTLagEESHTKLSG 239
Cdd:PRK05431 158 --SGSRFYVLKGDGARLERALIQFMldlH--TEEHGYTEVIPPYLVNEESMYGTG--QLPKFEEDlYKI--EDDDLYLIP 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  240 TAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRteisksaSEA----K----LYRVHEFSKVEMFVVSTPEQSAAELDYLV 311
Cdd:PRK05431 230 TAEVPLTNLHRDEILDEEELPLKYTAYSPCFR-------SEAgsagRdtrgLIRVHQFDKVELVKFTKPEDSYAELEELT 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  312 EVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTA-DGTTKYAHTCN 390
Cdd:PRK05431 303 ANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEgDGKPELVHTLN 382

                        410       420       430
                 ....*....|....*....|....*....|...
gi 17542084  391 GTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:PRK05431 383 GSGLAVGRTLVAILENYQQ-ADGSVTIPEVLRP 414
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
 54-423 8.51e-83

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: 260.76  E-value: 8.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084    54 KNLEAIRENiLNRK--------GVGDIDKVHKKWAVIQKMMKSGEKQTNgavSEQKYKQLWDELYDEAILIPNMTQDGVP 125
Cdd:TIGR00414  40 KKLLSEIEE-LQAKrnelskqiGKAKGQKKDKIEEIKKELKELKEELTE---LSAALKALEAELQDKLLSIPNIPHESVP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   126 RGSEDQAKI-VAEWGEKRE------DECLTAEKLvqTWRSLLHPTDASGQRSYVFLGALASLEKALLDYAHERVCALGFR 198
Cdd:TIGR00414 116 VGKDEEDNLeVKRWGTPPVfdfkpkPHWELGEKL--GGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   199 PITVPDIVSGEVTQACGVMQRSDHPIqYTLAGEESHtkLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSA 278
Cdd:TIGR00414 194 EIYPPYLVNEESLDGTGQLPKFEEDI-FKLEDTDLY--LIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   279 SEAK-LYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGE 357
Cdd:TIGR00414 271 KDTKgLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYRE 350

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542084   358 VSSASNCTDFQSRRLGIKYKT-ADGTTKYAHTCNGTALASTRALISVLETFQnDKKGLGELPEPLRK 423
Cdd:TIGR00414 351 ISSCSNCTDFQARRLNIRYKDkNKGKNKYVHTLNGTALAIGRTIVAILENYQ-TEDGSVEIPEVLRK 416
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 226-407 2.98e-28

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: 109.81  E-value: 2.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   226 YTLAGEESHTK-LSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASeaKLYRVHEFSKVEMFVVSTPEQSA 304
Cdd:pfam00587   1 YKVEDENGDELaLKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTR--GLIRVRQFHQDDAHIFHAPGQSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   305 AELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTADGTTK 384
Cdd:pfam00587  79 DELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESK 158

                         170       180
                  ....*....|....*....|...
gi 17542084   385 YAHTCNGTALASTRALISVLETF 407
Cdd:pfam00587 159 FPYMIHRAGLGVERFLAAILENN 181
 
Name Accession Description Interval E-value
SerRS_core cd00770
Seryl-tRNA synthetase (SerRS) class II core catalytic domain. SerRS is responsible for the ...
 131-423 3.63e-98

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: 296.01  E-value: 3.63e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 131 QAKIVAEWGEKRE------DECLTAEKLvqTWRSLLHPTDASGQRSYVFLGALASLEKALLDYAHERVCALGFRPITVPD 204
Cdd:cd00770   1 DNVEIRRWGEPRVfdfkpkDHVELGEKL--DILDFERGAKVSGSRFYYLKGDGALLERALINFALDFLTKRGFTPVIPPF 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 205 IVSGEVTQACGvmQRSDHPIQ-YTLAGEESHtkLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASEAK- 282
Cdd:cd00770  79 LVRKEVMEGTG--QLPKFDEQlYKVEGEDLY--LIATAEVPLAALHRDEILEEEELPLKYAGYSPCFRKEAGSAGRDTRg 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 283 LYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSAS 362
Cdd:cd00770 155 LFRVHQFEKVEQFVFTKPEESWEELEELISNAEEILQELGLPYRVVNICTGDLGFAAAKKYDIEAWMPGQGKYREISSCS 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17542084 363 NCTDFQSRRLGIKYK-TADGTTKYAHTCNGTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:cd00770 235 NCTDFQARRLNIRYRdKKDGKKQYVHTLNGTALATPRTIVAILENYQT-EDGSVVIPEVLRP 295
SerS COG0172
Seryl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Seryl-tRNA synthetase ...
 54-423 2.10e-87

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: 272.65  E-value: 2.10e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  54 KNLEAIRENILNRKGVGDIDKV------------------HKKWAV---IQKMMKSGE------KQTNG-----AVSEQK 101
Cdd:COG0172   9 ENPEAVKEALAKRGFDLDVDELleldeerrelqteveelrAERNALskeIGKAKKKGEeaealiAEVKElkeeiKELEEE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 102 YKQLWDELYDEAILIPNMTQDGVPRG-SEDQAKIVAEWGEKRE-D----------ECL------TAEKLvqtwrsllhpt 163
Cdd:COG0172  89 LKELEEELDELLLSIPNLPHESVPVGkDESDNVEVRRWGEPREfDfepkdhwelgEKLgildfeRAAKV----------- 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 164 daSGQRSYVFLGALASLEKAL----LDYAHERvcalGFRPITVPDIVSGEVTQacGVMQRSDHpiqytlaGEES-HTK-- 236
Cdd:COG0172 158 --SGSRFYVLKGDGARLERALiqfmLDLHTEH----GYTEVIPPYLVNEESMY--GTGQLPKF-------EEDLyKIEgd 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 237 ---LSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRteisksaSEA----K----LYRVHEFSKVEMFVVSTPEQSAA 305
Cdd:COG0172 223 dlyLIPTAEVPLTNLHRDEILDEEDLPLRYTAYTPCFR-------REAgsygRdtrgLIRQHQFDKVEMVQFVKPEDSYE 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 306 ELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTADGTTKY 385
Cdd:COG0172 296 ELEELTAHAEEILQKLGLPYRVVLLCTGDLGFSAAKTYDLEVWLPGQNKYREISSCSNCTDFQARRLNIRYRDEDGKPEF 375

                       410       420       430
                ....*....|....*....|....*....|....*...
gi 17542084 386 AHTCNGTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:COG0172 376 VHTLNGSGLAVGRTLVAILENYQQ-ADGSVRIPEVLRP 412
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 54-423 1.03e-83

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 263.08  E-value: 1.03e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   54 KNLEAIRENILNRKGVGDIDKV------------------HKKWAV---IQKMMKSGE------KQTNG-----AVSEQK 101
Cdd:PRK05431   9 ENPEAVKEALAKRGFPLDVDELleldeerrelqteleelqAERNALskeIGQAKRKGEdaealiAEVKElkeeiKALEAE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  102 YKQLWDELYDEAILIPNMTQDGVPRG-SEDQAKIVAEWGEKRE-D----------ECL------TAEKLvqtwrsllhpt 163
Cdd:PRK05431  89 LDELEAELEELLLRIPNLPHDSVPVGkDEDDNVEVRRWGEPREfDfepkdhwelgEKLgildfeRAAKV----------- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  164 daSGQRSYVFLGALASLEKALLDYA---HerVCALGFRPITVPDIVSGEVTQACGvmQRSDHPIQ-YTLagEESHTKLSG 239
Cdd:PRK05431 158 --SGSRFYVLKGDGARLERALIQFMldlH--TEEHGYTEVIPPYLVNEESMYGTG--QLPKFEEDlYKI--EDDDLYLIP 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  240 TAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRteisksaSEA----K----LYRVHEFSKVEMFVVSTPEQSAAELDYLV 311
Cdd:PRK05431 230 TAEVPLTNLHRDEILDEEELPLKYTAYSPCFR-------SEAgsagRdtrgLIRVHQFDKVELVKFTKPEDSYAELEELT 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  312 EVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTA-DGTTKYAHTCN 390
Cdd:PRK05431 303 ANAEEILQKLELPYRVVLLCTGDLGFSAAKTYDLEVWLPSQNTYREISSCSNCTDFQARRANIRYRDEgDGKPELVHTLN 382

                        410       420       430
                 ....*....|....*....|....*....|...
gi 17542084  391 GTALASTRALISVLETFQNdKKGLGELPEPLRK 423
Cdd:PRK05431 383 GSGLAVGRTLVAILENYQQ-ADGSVTIPEVLRP 414
serS TIGR00414
seryl-tRNA synthetase; This model represents the seryl-tRNA synthetase found in most organisms. ...
 54-423 8.51e-83

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: 260.76  E-value: 8.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084    54 KNLEAIRENiLNRK--------GVGDIDKVHKKWAVIQKMMKSGEKQTNgavSEQKYKQLWDELYDEAILIPNMTQDGVP 125
Cdd:TIGR00414  40 KKLLSEIEE-LQAKrnelskqiGKAKGQKKDKIEEIKKELKELKEELTE---LSAALKALEAELQDKLLSIPNIPHESVP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   126 RGSEDQAKI-VAEWGEKRE------DECLTAEKLvqTWRSLLHPTDASGQRSYVFLGALASLEKALLDYAHERVCALGFR 198
Cdd:TIGR00414 116 VGKDEEDNLeVKRWGTPPVfdfkpkPHWELGEKL--GGLDFDRAVKVTGSRFYYLKNDGAKLERALINFMLDLLEKNGYQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   199 PITVPDIVSGEVTQACGVMQRSDHPIqYTLAGEESHtkLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSA 278
Cdd:TIGR00414 194 EIYPPYLVNEESLDGTGQLPKFEEDI-FKLEDTDLY--LIPTAEVPLTNLHRNEILEEEELPIKYTAHSPCFRSEAGSYG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   279 SEAK-LYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGE 357
Cdd:TIGR00414 271 KDTKgLIRVHQFNKVELVKFCKPEESAEELEEMTSDAEQILQELELPYRVVNLCSGDLGFSAAKKYDLEVWMPGQNTYRE 350

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17542084   358 VSSASNCTDFQSRRLGIKYKT-ADGTTKYAHTCNGTALASTRALISVLETFQnDKKGLGELPEPLRK 423
Cdd:TIGR00414 351 ISSCSNCTDFQARRLNIRYKDkNKGKNKYVHTLNGTALAIGRTIVAILENYQ-TEDGSVEIPEVLRK 416
PLN02320 PLN02320
seryl-tRNA synthetase
 48-422 2.86e-82

seryl-tRNA synthetase


Pssm-ID: 177954 [Multi-domain]  Cd Length: 502  Bit Score: 261.78  E-value: 2.86e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   48 EFLLDEKNLEAIRENilnRKGVGDIDKVHKKWAVIQKMMKSGEKQTNGAVS-EQKYKQLWDELYDEAILIPNMTQDGVPR 126
Cdd:PLN02320 101 NMLALQKEVERLRAE---RNAVANKMKGKLEPSERQALVEEGKNLKEGLVTlEEDLVKLTDELQLEAQSIPNMTHPDVPV 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  127 GSEDQAKIVAEWGEKREDEcLTAEKLVQTWRSL-LHPTDA----SGQRSYVFLGALASLEKALLDYAHERVCALGFRPIT 201
Cdd:PLN02320 178 GGEDSSAVRKEVGSPREFS-FPIKDHLQLGKELdLFDFDAaaevSGSKFYYLKNEAVLLEMALVNWTLSEVMKKGFTPLT 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  202 VPDIVSGEVTQACGVMQRSDHPIQYTLagEESHTKLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASEA 281
Cdd:PLN02320 257 TPEIVRSSVVEKCGFQPRGDNTQVYSI--DGSDQCLIGTAEIPVGGIHMDSILLESALPLKYVAFSHCFRTEAGAAGAAT 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  282 K-LYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSS 360
Cdd:PLN02320 335 RgLYRVHQFSKVEMFVICRPEESESFHEELIQIEEDLFTSLGLHFKTLDMATADLGAPAYRKFDIEAWMPGLGRYGEISS 414

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17542084  361 ASNCTDFQSRRLGIKYKTAD-------------GTTKYAHTCNGTALASTRALISVLETFQNDkKGLGELPEPLR 422
Cdd:PLN02320 415 ASNCTDYQSRRLGIRYRPSEppqtnpkkgkgslGPTKFVHTLNATACAVPRMIVCLLENYQQE-DGSVVIPEPLR 488
PLN02678 PLN02678
seryl-tRNA synthetase
 71-422 7.74e-58

seryl-tRNA synthetase


Pssm-ID: 215364 [Multi-domain]  Cd Length: 448  Bit Score: 196.46  E-value: 7.74e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   71 DIDKVHKKwavIQKMMKSGE------KQTNG-----AVSEQKYKQLWDELYDEAILIPNMTQDGVPRGS-EDQAKIVAEW 138
Cdd:PLN02678  55 EFNKLNKE---VAKLKIAKEdateliAETKElkkeiTEKEAEVQEAKAALDAKLKTIGNLVHDSVPVSNdEANNAVVRTW 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  139 GEKREDECLT-----AEKL--VQTWRSllhpTDASGQRSYVFLGALASLEKALLDYAHERVCALGFRPITVPDIVSGEVT 211
Cdd:PLN02678 132 GEKRQEPKLKnhvdlVELLgiVDTERG----ADVAGGRGYYLKGAGVLLNQALINFGLAFLRKRGYTPLQTPFFMRKDVM 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  212 QACGVMQRSDHPIqYTLAGEESHTKLSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEI-SKSASEAKLYRVHEFS 290
Cdd:PLN02678 208 AKCAQLAQFDEEL-YKVTGEGDDKYLIATSEQPLCAYHRGDWIDPKELPIRYAGYSTCFRKEAgSHGRDTLGIFRVHQFE 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  291 KVEMFVVSTPE--QSAAELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQ 368
Cdd:PLN02678 287 KVEQFCITSPNgnESWEMHEEMLKNSEDFYQSLGIPYQVVSIVSGALNDAAAKKYDLEAWFPASKTYRELVSCSNCTDYQ 366

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 17542084  369 SRRLGIKY---KTADGTTKYAHTCNGTALASTRALISVLETFQNDkKGLgELPEPLR 422
Cdd:PLN02678 367 SRRLEIRYgqkKSNEQTKQYVHLLNSTLTATERTLCCILENYQTE-DGV-RVPEVLQ 421
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 226-407 2.98e-28

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: 109.81  E-value: 2.98e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   226 YTLAGEESHTK-LSGTAEMGIAAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASeaKLYRVHEFSKVEMFVVSTPEQSA 304
Cdd:pfam00587   1 YKVEDENGDELaLKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDTR--GLIRVRQFHQDDAHIFHAPGQSP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084   305 AELDYLVEVQKGTFQALGVHCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTADGTTK 384
Cdd:pfam00587  79 DELEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFYGPKLDFEVVFPSLGKQRQTGTIQNDGFRLPRRLGIRYKDEDNESK 158

                         170       180
                  ....*....|....*....|...
gi 17542084   385 YAHTCNGTALASTRALISVLETF 407
Cdd:pfam00587 159 FPYMIHRAGLGVERFLAAILENN 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 ...
 177-394 1.62e-13

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: 69.73  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 177 LASLEKALLDYAHERVCALGFRPITVPdIVSGEVTQACGVMQRSDHPIQYTLAGEESHTK-----LSGTAEMGIAAFLRG 251
Cdd:cd00670   1 GTALWRALERFLDDRMAEYGYQEILFP-FLAPTVLFFKGGHLDGYRKEMYTFEDKGRELRdtdlvLRPAACEPIYQIFSG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 252 RTFNQDQLPIRLVSLSRCFRTEISKSASeakLYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQLEMP 331
Cdd:cd00670  80 EILSYRALPLRLDQIGPCFRHEPSGRRG---LMRVREFRQVEYVVFGEPEEAEEERREWLELAEEIARELGLPVRVVVAD 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17542084 332 SEELGASAAR--------KFDIEAWMPGRKLYGEVSSASNCTDFQSRRLGIKYKTADGtTKYAHTCNGTAL 394
Cdd:cd00670 157 DPFFGRGGKRgldagretVVEFELLLPLPGRAKETAVGSANVHLDHFGASFKIDEDGG-GRAHTGCGGAGG 226
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 188-388 3.65e-10

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: 59.44  E-value: 3.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 188 AHERVCALGFRPITVPdivsgEVTQAcGVMQRSDHPIQYTLAGEESHTK---LSGTAEMGIAAFLRGRTFnqdQLPIRLV 264
Cdd:cd00768   9 LRRFMAELGFQEVETP-----IVERE-PLLEKAGHEPKDLLPVGAENEEdlyLRPTLEPGLVRLFVSHIR---KLPLRLA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 265 SLSRCFRTEISKsaseAKLYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGV--HCRQLEMPSEELGASAA-R 341
Cdd:cd00768  80 EIGPAFRNEGGR----RGLRRVREFTQLEGEVFGEDGEEASEFEELIELTEELLRALGIklDIVFVEKTPGEFSPGGAgP 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17542084 342 KFDIEAWMPGRKlYGEVSSASNCTDFQSRRLGIKYKTADGTTKYAHT 388
Cdd:cd00768 156 GFEIEVDHPEGR-GLEIGSGGYRQDEQARAADLYFLDEALEYRYPPT 201
GlyRS-like_core cd00774
Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a ...
 248-354 1.38e-04

Glycyl-tRNA synthetase (GlyRS)-like class II core catalytic domain. GlyRS functions as a homodimer in eukaryotes, archaea and some bacteria and as a heterotetramer in the remainder of prokaryotes. It is responsible for the attachment of glycine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP binding and hydrolysis. This alignment contains only sequences from the GlyRS form which homodimerizes. The heterotetramer glyQ is in a different family of class II aaRS. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the N-terminus of the accessory subunit of mitochondrial polymerase gamma (Pol gamma b). Pol gamma b stimulates processive DNA synthesis and is functional as a homodimer, which can associate with the catalytic subunit Pol gamma alpha to form a heterotrimer. Despite significant both structural and sequence similarity with GlyRS, Pol gamma b lacks conservation of several class II functional residues.


Pssm-ID: 238397 [Multi-domain]  Cd Length: 254  Bit Score: 43.35  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084 248 FLRGRTFNQDQLPIRLVSLSRCFRTEISKSASeakLYRVHEFSKVEMFVVSTPEQSAAELDYLVEVQKGTFQALGVHCRQ 327
Cdd:cd00774  95 FKNLLEFNRRKLPFGVAQIGKSFRNEISPRNG---LFRVREFTQAEIEFFVDPEKSHPWFDYWADQRLKWLPKFAQSPEN 171

                        90       100       110
                ....*....|....*....|....*....|
gi 17542084 328 LEM---PSEELGASAARKFDIEAWMPGRKL 354
Cdd:cd00774 172 LRLtdhEKEELAHYANETLDYFYAFPHGFL 201
PRK00960 PRK00960
seryl-tRNA synthetase; Provisional
 248-425 2.24e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 234876 [Multi-domain]  Cd Length: 517  Bit Score: 43.47  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  248 FLRGRTFNQDQLPIRLVSLS-RCFRTEiskSASEAKLYRVHEFSKVEMFVVSTPEQS--------------AAELD--YL 310
Cdd:PRK00960 323 FFQGETVDVDELPIKFFDRSgWTYRWE---GGGAHGLERVNEFHRIEIVWLGTPEQVeeirdellkyahilAEKLDleYW 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  311 VEVQKGTF--QALGVHCRQLEMPSeelgasaARKFDIEAWMPGRKLYG---EVSSAS-NCTDFQSrrlGIKYKTADGTTK 384
Cdd:PRK00960 400 REVGDDPFylEGRGLEDRGIEFPD-------VPKYEMELWLPYRGDERkwvAVTSANvHGTHFVE---GFNIKDYKGRKL 469

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17542084  385 YAhTCNGTALasTRALISVLEtfqndKKGL--GELPEPLRKRV 425
Cdd:PRK00960 470 WT-GCTGYGL--ERWVIGFLA-----QKGFdpENWPEEIRKRV 504
PRK04173 PRK04173
glycyl-tRNA synthetase; Provisional
 240-367 4.42e-03

glycyl-tRNA synthetase; Provisional


Pssm-ID: 235240 [Multi-domain]  Cd Length: 456  Bit Score: 39.34  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17542084  240 TAEmGI-AAFLRGRTFNQDQLPIRLVSLSRCFRTEISKSASeakLYRVHEFSKVEM--FVvsTPEQSAAELDYLVEVQKG 316
Cdd:PRK04173 166 TAQ-GIfVNFKNVLRTARKKLPFGIAQIGKSFRNEITPRNF---IFRTREFEQMELefFV--KPGTDNEWFAYWIELRKN 239

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17542084  317 TFQALGV---HCRQLEMPSEELGASAARKFDIEAWMPGRKLYGEVSSASNCTDF 367
Cdd:PRK04173 240 WLLDLGIdpeNLRFREHLPEELAHYSKATWDIEYKFPFGRFWGELEGIANRTDY 293
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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