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Conserved domains on  [gi|15238286|ref|NP_196649|]
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tRNA synthetase-related / tRNA ligase-like protein [Arabidopsis thaliana]

Protein Classification

proline--tRNA ligase anticodon binding domain-containing protein( domain architecture ID 10096258)

proline--tRNA ligase anticodon binding domain-containing protein binds tRNA(Pro); proline--tRNA ligase catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro)

EC:  6.1.1.15
Gene Ontology:  GO:0006433|GO:0000049
PubMed:  12458790|10704480|10447505|1852601|8274143|2053131|10737860

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
 96-309 1.43e-70

ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.


:

Pssm-ID: 238439 [Multi-domain]  Cd Length: 202  Bit Score: 217.17  E-value: 1.43e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286  96 GLVFPPKVAPVQVVVIHVPIKgAADYQELCDACEAVESTLLGAGIRAEADIRDNYSCGWKYADQELTGVPLRIETGPRDL 175
Cdd:cd00862   1 GLVLPPRVAPIQVVIVPIGIK-DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286 176 ANDQVRIVTRDNGAKMDVKRGDLIEQVKDLLEKIQSNLYDVAKRKVEEcTQKVETWDEFVEALSQKKLILAPWCDKVEVE 255
Cdd:cd00862  80 EKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDA-TRIVDTWEEFKEALNEKGIVLAPWCGEEECE 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15238286 256 KDVKRRTRgdetggggggAKTLCTPLEQPELGEETLCFASGKPAKKWSYWGRSY 309
Cdd:cd00862 159 EEIKEETA----------ATILCIPFDEAKLEEGGKCVVCGRPAKAYARFAKSY 202
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 16-47 1.05e-04

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 cd00778:

Pssm-ID: 444800 [Multi-domain]  Cd Length: 261  Bit Score: 42.97  E-value: 1.05e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 15238286  16 DFGKWYSEACRFGELVEYYEsVKGCYILKPSG 47
Cdd:cd00778   1 DFSEWYTEVITKAELIDYGP-VKGCMVFRPYG 31
 
Name Accession Description Interval E-value
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
 96-309 1.43e-70

ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.


Pssm-ID: 238439 [Multi-domain]  Cd Length: 202  Bit Score: 217.17  E-value: 1.43e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286  96 GLVFPPKVAPVQVVVIHVPIKgAADYQELCDACEAVESTLLGAGIRAEADIRDNYSCGWKYADQELTGVPLRIETGPRDL 175
Cdd:cd00862   1 GLVLPPRVAPIQVVIVPIGIK-DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286 176 ANDQVRIVTRDNGAKMDVKRGDLIEQVKDLLEKIQSNLYDVAKRKVEEcTQKVETWDEFVEALSQKKLILAPWCDKVEVE 255
Cdd:cd00862  80 EKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDA-TRIVDTWEEFKEALNEKGIVLAPWCGEEECE 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15238286 256 KDVKRRTRgdetggggggAKTLCTPLEQPELGEETLCFASGKPAKKWSYWGRSY 309
Cdd:cd00862 159 EEIKEETA----------ATILCIPFDEAKLEEGGKCVVCGRPAKAYARFAKSY 202
ProRS-C_1 pfam09180
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 231-309 6.02e-23

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 462709  Cd Length: 67  Bit Score: 89.89  E-value: 6.02e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238286   231 WDEFVEALSQKKLILAPWCDKVEVEKDVKRRTrgdetgggggGAKTLCTPLEQPELGEEtlCFASGKPAKKWSYWGRSY 309
Cdd:pfam09180   1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET----------GATSRCIPFDQEEEGGK--CIVCGKPAKKWVLFARSY 67
ProRS-C_1 smart00946
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 231-309 2.49e-19

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 198014  Cd Length: 67  Bit Score: 80.31  E-value: 2.49e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238286    231 WDEFVEALSQKKLILAPWCDKVEVEKDVKRRTrgdetgggggGAKTLCTPLEQPELGEEtlCFASGKPAKKWSYWGRSY 309
Cdd:smart00946   1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET----------GATIRCIPFDQDEEPGK--CVVCGKPAKKWVLFARSY 67
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 91-206 5.96e-17

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 80.90  E-value: 5.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286   91 HGDDKGLVFPPKVAPVQVVVIHVPIKGAADYQelcdACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIET 170
Cdd:PRK09194 454 NHDEKGIIWPKAIAPFDVHIVPVNMKDEEVKE----LAEKLYAELQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVV 528

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15238286  171 GPRDLANDQVRIVTRDNGAKMDVKRGDLIEQVKDLL 206
Cdd:PRK09194 529 GDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALK 564
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 99-204 9.35e-08

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: 53.11  E-value: 9.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286  99 FPPKVAPVQVVVIhvPIkgaADYQElcDACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETGPRDLAND 178
Cdd:COG0441 533 FPLWLAPVQVVVL--PI---SDKHA--DYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENG 604

                        90       100
                ....*....|....*....|....*.
gi 15238286 179 QVRIVTRDNGAKMDVKRGDLIEQVKD 204
Cdd:COG0441 605 TVSVRRRGGGDLGTMSLDEFIARLKE 630
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 16-47 1.05e-04

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: 42.97  E-value: 1.05e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 15238286  16 DFGKWYSEACRFGELVEYYEsVKGCYILKPSG 47
Cdd:cd00778   1 DFSEWYTEVITKAELIDYGP-VKGCMVFRPYG 31
 
Name Accession Description Interval E-value
ProRS_anticodon_zinc cd00862
ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and ...
 96-309 1.43e-70

ProRS Prolyl-anticodon binding domain, long version found predominantly in eukaryotes and archaea. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only, and an additional C-terminal zinc-binding domain specific to this subfamily of aaRSs.


Pssm-ID: 238439 [Multi-domain]  Cd Length: 202  Bit Score: 217.17  E-value: 1.43e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286  96 GLVFPPKVAPVQVVVIHVPIKgAADYQELCDACEAVESTLLGAGIRAEADIRDNYSCGWKYADQELTGVPLRIETGPRDL 175
Cdd:cd00862   1 GLVLPPRVAPIQVVIVPIGIK-DEKREEVLEAADELAERLKAAGIRVHVDDRDNYTPGWKFNDWELKGVPLRIEIGPRDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286 176 ANDQVRIVTRDNGAKMDVKRGDLIEQVKDLLEKIQSNLYDVAKRKVEEcTQKVETWDEFVEALSQKKLILAPWCDKVEVE 255
Cdd:cd00862  80 EKNTVVIVRRDTGEKKTVPLAELVEKVPELLDEIQEDLYERALEFRDA-TRIVDTWEEFKEALNEKGIVLAPWCGEEECE 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15238286 256 KDVKRRTRgdetggggggAKTLCTPLEQPELGEETLCFASGKPAKKWSYWGRSY 309
Cdd:cd00862 159 EEIKEETA----------ATILCIPFDEAKLEEGGKCVVCGRPAKAYARFAKSY 202
ProRS-C_1 pfam09180
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 231-309 6.02e-23

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 462709  Cd Length: 67  Bit Score: 89.89  E-value: 6.02e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238286   231 WDEFVEALSQKKLILAPWCDKVEVEKDVKRRTrgdetgggggGAKTLCTPLEQPELGEEtlCFASGKPAKKWSYWGRSY 309
Cdd:pfam09180   1 WEEFKEALEEKGFVLAPWCGDEECEDKIKEET----------GATSRCIPFDQEEEGGK--CIVCGKPAKKWVLFARSY 67
ProRS-C_1 smart00946
Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in ...
 231-309 2.49e-19

Prolyl-tRNA synthetase, C-terminal; Members of this family are predominantly found in prokaryotic prolyl-tRNA synthetase. They contain a zinc binding site, and adopt a structure consisting of alpha helices and antiparallel beta sheets arranged in 2 layers, in a beta-alpha-beta-alpha-beta motif.


Pssm-ID: 198014  Cd Length: 67  Bit Score: 80.31  E-value: 2.49e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238286    231 WDEFVEALSQKKLILAPWCDKVEVEKDVKRRTrgdetgggggGAKTLCTPLEQPELGEEtlCFASGKPAKKWSYWGRSY 309
Cdd:smart00946   1 LEEFKKALEEGKFVLAPWCGDEECEEKIKEET----------GATIRCIPFDQDEEPGK--CVVCGKPAKKWVLFARSY 67
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 107-205 4.66e-17

Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.


Pssm-ID: 460819 [Multi-domain]  Cd Length: 94  Bit Score: 74.93  E-value: 4.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286   107 QVVVIhvPIKGAADyqELCDACEAVESTLLGAGIRAEADIRdNYSCGWKYADQELTGVPLRIETGPRDLANDQVRIVTRD 186
Cdd:pfam03129   1 QVVVI--PLGEKAE--ELEEYAQKLAEELRAAGIRVELDDR-NESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRD 75

                          90
                  ....*....|....*....
gi 15238286   187 NGAKMDVKRGDLIEQVKDL 205
Cdd:pfam03129  76 TGEQETVSLDELVEKLKEL 94
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 91-206 5.96e-17

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 80.90  E-value: 5.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286   91 HGDDKGLVFPPKVAPVQVVVIHVPIKGAADYQelcdACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIET 170
Cdd:PRK09194 454 NHDEKGIIWPKAIAPFDVHIVPVNMKDEEVKE----LAEKLYAELQAAGIEVLLDDRKE-RPGVKFADADLIGIPHRIVV 528

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15238286  171 GPRDLANDQVRIVTRDNGAKMDVKRGDLIEQVKDLL 206
Cdd:PRK09194 529 GDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALK 564
PRK12325 PRK12325
prolyl-tRNA synthetase; Provisional
 93-203 7.03e-12

prolyl-tRNA synthetase; Provisional


Pssm-ID: 237059 [Multi-domain]  Cd Length: 439  Bit Score: 65.65  E-value: 7.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286   93 DDKGLVFPPKVAPVQVVVIHVPIKGAAdyqelCD-ACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETG 171
Cdd:PRK12325 333 DDKGIIWPESVAPFKVGIINLKQGDEA-----CDaACEKLYAALSAAGIDVLYDDTDE-RPGAKFATMDLIGLPWQIIVG 406

                         90       100       110
                 ....*....|....*....|....*....|..
gi 15238286  172 PRDLANDQVRIVTRDNGAKMDVKRGDLIEQVK 203
Cdd:PRK12325 407 PKGLAEGKVELKDRKTGEREELSVEAAINRLT 438
HGTP_anticodon cd00738
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ...
 105-200 3.68e-09

HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).


Pssm-ID: 238379 [Multi-domain]  Cd Length: 94  Bit Score: 53.17  E-value: 3.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286 105 PVQVVVIhvPIKGAADyqELCDACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETGPRDLANDQVRIVT 184
Cdd:cd00738   1 PIDVAIV--PLTDPRV--EAREYAQKLLNALLANGIRVLYDDRER-KIGKKFREADLRGVPFAVVVGEDELENGKVTVKS 75

                        90
                ....*....|....*.
gi 15238286 185 RDNGAKMDVKRGDLIE 200
Cdd:cd00738  76 RDTGESETLHVDELPE 91
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
 105-203 9.74e-09

ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238438 [Multi-domain]  Cd Length: 94  Bit Score: 51.82  E-value: 9.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286 105 PVQVVVIHVPIKGAADYQelcdACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETGPRDLANDQVRIVT 184
Cdd:cd00861   1 PFDVVIIPMNMKDEVQQE----LAEKLYAELQAAGVDVLLDDRNE-RPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKV 75

                        90
                ....*....|....*....
gi 15238286 185 RDNGAKMDVKRGDLIEQVK 203
Cdd:cd00861  76 RKTGEKEEISIDELLEFLQ 94
ThrRS_anticodon cd00860
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ...
 105-203 7.97e-08

ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238437 [Multi-domain]  Cd Length: 91  Bit Score: 49.04  E-value: 7.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286 105 PVQVVVIhvPIKGAADyqelcDACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETGPRDLANDQVRIVT 184
Cdd:cd00860   1 PVQVVVI--PVTDEHL-----DYAKEVAKKLSDAGIRVEVDLRNE-KLGKKIREAQLQKIPYILVVGDKEVETGTVSVRT 72

                        90
                ....*....|....*....
gi 15238286 185 RDNGAKMDVKRGDLIEQVK 203
Cdd:cd00860  73 RDGGDLGSMSLDEFIEKLK 91
ThrS COG0441
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ...
 99-204 9.35e-08

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: 53.11  E-value: 9.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286  99 FPPKVAPVQVVVIhvPIkgaADYQElcDACEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETGPRDLAND 178
Cdd:COG0441 533 FPLWLAPVQVVVL--PI---SDKHA--DYAKEVAKKLRAAGIRVEVDLRNE-KIGYKIREAQLQKVPYMLVVGDKEVENG 604

                        90       100
                ....*....|....*....|....*.
gi 15238286 179 QVRIVTRDNGAKMDVKRGDLIEQVKD 204
Cdd:COG0441 605 TVSVRRRGGGDLGTMSLDEFIARLKE 630
PRK12444 PRK12444
threonyl-tRNA synthetase; Reviewed
 96-203 2.24e-05

threonyl-tRNA synthetase; Reviewed


Pssm-ID: 183530 [Multi-domain]  Cd Length: 639  Bit Score: 45.89  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286   96 GLVFPPKVAPVQVVVIHVPIKGAADYqelcdaCEAVESTLLGAGIRAEADIRDNySCGWKYADQELTGVPLRIETGPRDL 175
Cdd:PRK12444 532 GGAFPAWLAPVQVKVIPVSNAVHVQY------ADEVADKLAQAGIRVERDERDE-KLGYKIREAQMQKIPYVLVIGDKEM 604

                         90       100
                 ....*....|....*....|....*...
gi 15238286  176 ANDQVRIVTRDNGAKMDVKRGDLIEQVK 203
Cdd:PRK12444 605 ENGAVNVRKYGEEKSEVIELDMFVESIK 632
ProRS_core_arch_euk cd00778
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ...
 16-47 1.05e-04

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: 42.97  E-value: 1.05e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 15238286  16 DFGKWYSEACRFGELVEYYEsVKGCYILKPSG 47
Cdd:cd00778   1 DFSEWYTEVITKAELIDYGP-VKGCMVFRPYG 31
GlyRS_anticodon cd00858
GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases ...
 97-207 1.22e-04

GlyRS Glycyl-anticodon binding domain. GlyRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.


Pssm-ID: 238435 [Multi-domain]  Cd Length: 121  Bit Score: 41.00  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238286  97 LVFPPKVAPVQVVVIhvPIKGAADYQELcdaCEAVESTLLGAGIRAEADirDNYSCGWKYADQELTGVPLRIETGPRDLA 176
Cdd:cd00858  18 LRLPPALAPIKVAVL--PLVKRDELVEI---AKEISEELRELGFSVKYD--DSGSIGRRYARQDEIGTPFCVTVDFDTLE 90

                        90       100       110
                ....*....|....*....|....*....|.
gi 15238286 177 NDQVRIVTRDNGAKMDVKRGDLIEQVKDLLE 207
Cdd:cd00858  91 DGTVTIRERDSMRQVRVKIEELPSYLRELIR 121
 
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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