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Conserved domains on  [gi|1731032771|gb|TYK20575|]
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alanine--tRNA ligase-like [Cucumis melo var. makuwa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02900 super family cl33594
alanyl-tRNA synthetase
30-237 1.20e-111

alanyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02900:

Pssm-ID: 215487 [Multi-domain]  Cd Length: 936  Bit Score: 341.22  E-value: 1.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  30 PRYPVSRIREVYLAVFKRQSPTRVNSSPCyhrrqllpLPHR------ARAsrgtltllttgtlpardvrwvsvvGMNQFK 103
Cdd:PLN02900    9 KEWPGDRIRRTFLSFFESKGHTFLPSSPL--------VPVDdptllfTNA------------------------GMNQFK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 104 PIFLGTVDPNTSLSKLTRACNTQKCIHAGGRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPT 183
Cdd:PLN02900   57 PIFLGTADPNTPLRKLPRATNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAIGWAWELLTKVYGLPA 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1731032771 184 DRIYATYFGGDEKagLAPDNEARDIWLKFLPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:PLN02900  137 DRLYATYFGGDEK--QAPDDEARAIWLDYLPEERVLPFGCKDNFWEMGDTGPCG 188
 
Name Accession Description Interval E-value
PLN02900 PLN02900
alanyl-tRNA synthetase
30-237 1.20e-111

alanyl-tRNA synthetase


Pssm-ID: 215487 [Multi-domain]  Cd Length: 936  Bit Score: 341.22  E-value: 1.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  30 PRYPVSRIREVYLAVFKRQSPTRVNSSPCyhrrqllpLPHR------ARAsrgtltllttgtlpardvrwvsvvGMNQFK 103
Cdd:PLN02900    9 KEWPGDRIRRTFLSFFESKGHTFLPSSPL--------VPVDdptllfTNA------------------------GMNQFK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 104 PIFLGTVDPNTSLSKLTRACNTQKCIHAGGRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPT 183
Cdd:PLN02900   57 PIFLGTADPNTPLRKLPRATNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAIGWAWELLTKVYGLPA 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1731032771 184 DRIYATYFGGDEKagLAPDNEARDIWLKFLPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:PLN02900  137 DRLYATYFGGDEK--QAPDDEARAIWLDYLPEERVLPFGCKDNFWEMGDTGPCG 188
AlaS COG0013
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA ...
98-237 1.53e-83

Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439784 [Multi-domain]  Cd Length: 880  Bit Score: 266.15  E-value: 1.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  98 GMNQFKPIFLGTVDPntslsKLTRACNTQKCIHAGGRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQ 177
Cdd:COG0013    42 GMVQFKPYFLGQEKP-----PYPRATTSQKCVRTGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEEAIAWAWELLTE 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731032771 178 VYKLPTDRIYATYFGGDEkaglapdnEARDIWLKF--LPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:COG0013   117 VLGLPKERLWVTVYEDDD--------EAYDIWKKEigVPEERIIRLGKKDNFWEMGDTGPCG 170
tRNA-synt_2c pfam01411
tRNA synthetases class II (A); Other tRNA synthetase sub-families are too dissimilar to be ...
37-237 2.44e-76

tRNA synthetases class II (A); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only alanyl-tRNA synthetases.


Pssm-ID: 279719 [Multi-domain]  Cd Length: 548  Bit Score: 240.26  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  37 IREVYLAVFKRQSPTRVNSSPcyhrrqLLPlphRARAsrgtltllttgtlparDVRWVSVvGMNQFKPIFLGTVDPntsl 116
Cdd:pfam01411   2 IRQTFLDFFEKKGHTRVPSSP------VVP---RNDP----------------TLLFTNA-GMNQFKPIFLGGVAK---- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 117 SKLTRACNTQKCIhaggRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPTDRIYATYFGGDEk 196
Cdd:pfam01411  52 PPYNRATNSQKCI----RAGDLENVGRTGRHHTFFEMLGNFSFGDYFKEEAIEYAWELLTKELGLPPERLYVTVFEWDD- 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1731032771 197 aglapdnEARDIWLKF--LPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:pfam01411 127 -------EAGPIWEKIvgGPEERILRFGDKDNFWEMGDTGPCG 162
AlaRS_core cd00673
Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is ...
34-237 2.25e-69

Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine 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 predicted structure and the presence of three characteristic sequence motifs.


Pssm-ID: 238360 [Multi-domain]  Cd Length: 232  Bit Score: 212.61  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  34 VSRIREVYLAVFKRQSPTRVNSSPcyhrrqLLPlphrarasrgtltllttgtlpaRD---VRWVSVvGMNQFKPIFLGTV 110
Cdd:cd00673     1 ASEIRETFLSFFEKKGHTRVPSSP------VVP----------------------RDdptLLFTNA-GMNQFKPIFLGEV 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 111 DPNTSlskltRACNTQKCIHAGGRHNdlddVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPTDRIYATY 190
Cdd:cd00673    52 PPPAN-----RLVNSQKCIRAGDIDN----VGKTGRHHTFFEMLGNFSFGDYFKEEAIAFAWELLTEVLGLPKDRLYVSV 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1731032771 191 FGGDEKAglapdnEARDIWLKFLPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:cd00673   123 FEGDDEE------EAIWWWKIGLPGIRIERIGFKDNFWEMGGNGPCG 163
alaS TIGR00344
alanine--tRNA ligase; The model describes alanine--tRNA ligase. This enzyme catalyzes the ...
98-237 2.31e-54

alanine--tRNA ligase; The model describes alanine--tRNA ligase. This enzyme catalyzes the reaction (tRNAala + L-alanine + ATP = L-alanyl-tRNAala + pyrophosphate + AMP). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273026 [Multi-domain]  Cd Length: 845  Bit Score: 186.43  E-value: 2.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  98 GMNQFKPIFLGTVDPNTSlskltRACNTQKCIhaggRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQ 177
Cdd:TIGR00344  37 GMAQFKPIFTGIVKPPSN-----RLTNAQPCI----RLNDLENVGRTARHHTLFEMLGNFSFGDYFKEEAIAFAWELLTE 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 178 VYKLPTDRIYATYFGGDEKAGLAPDNeardiwlKFLPAERVLPFGCKDNFWEMGDtGPCG 237
Cdd:TIGR00344 108 VLGLDKERLYVTVYEDDEEAYKIWEK-------IGIPADRIIKCDAKDNFWDMGD-GPCG 159
 
Name Accession Description Interval E-value
PLN02900 PLN02900
alanyl-tRNA synthetase
30-237 1.20e-111

alanyl-tRNA synthetase


Pssm-ID: 215487 [Multi-domain]  Cd Length: 936  Bit Score: 341.22  E-value: 1.20e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  30 PRYPVSRIREVYLAVFKRQSPTRVNSSPCyhrrqllpLPHR------ARAsrgtltllttgtlpardvrwvsvvGMNQFK 103
Cdd:PLN02900    9 KEWPGDRIRRTFLSFFESKGHTFLPSSPL--------VPVDdptllfTNA------------------------GMNQFK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 104 PIFLGTVDPNTSLSKLTRACNTQKCIHAGGRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPT 183
Cdd:PLN02900   57 PIFLGTADPNTPLRKLPRATNTQKCIRAGGKHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAIGWAWELLTKVYGLPA 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1731032771 184 DRIYATYFGGDEKagLAPDNEARDIWLKFLPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:PLN02900  137 DRLYATYFGGDEK--QAPDDEARAIWLDYLPEERVLPFGCKDNFWEMGDTGPCG 188
AlaS COG0013
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA ...
98-237 1.53e-83

Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439784 [Multi-domain]  Cd Length: 880  Bit Score: 266.15  E-value: 1.53e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  98 GMNQFKPIFLGTVDPntslsKLTRACNTQKCIHAGGRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQ 177
Cdd:COG0013    42 GMVQFKPYFLGQEKP-----PYPRATTSQKCVRTGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEEAIAWAWELLTE 116
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731032771 178 VYKLPTDRIYATYFGGDEkaglapdnEARDIWLKF--LPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:COG0013   117 VLGLPKERLWVTVYEDDD--------EAYDIWKKEigVPEERIIRLGKKDNFWEMGDTGPCG 170
tRNA-synt_2c pfam01411
tRNA synthetases class II (A); Other tRNA synthetase sub-families are too dissimilar to be ...
37-237 2.44e-76

tRNA synthetases class II (A); Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only alanyl-tRNA synthetases.


Pssm-ID: 279719 [Multi-domain]  Cd Length: 548  Bit Score: 240.26  E-value: 2.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  37 IREVYLAVFKRQSPTRVNSSPcyhrrqLLPlphRARAsrgtltllttgtlparDVRWVSVvGMNQFKPIFLGTVDPntsl 116
Cdd:pfam01411   2 IRQTFLDFFEKKGHTRVPSSP------VVP---RNDP----------------TLLFTNA-GMNQFKPIFLGGVAK---- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 117 SKLTRACNTQKCIhaggRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPTDRIYATYFGGDEk 196
Cdd:pfam01411  52 PPYNRATNSQKCI----RAGDLENVGRTGRHHTFFEMLGNFSFGDYFKEEAIEYAWELLTKELGLPPERLYVTVFEWDD- 126
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1731032771 197 aglapdnEARDIWLKF--LPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:pfam01411 127 -------EAGPIWEKIvgGPEERILRFGDKDNFWEMGDTGPCG 162
AlaRS_core cd00673
Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is ...
34-237 2.25e-69

Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine 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 predicted structure and the presence of three characteristic sequence motifs.


Pssm-ID: 238360 [Multi-domain]  Cd Length: 232  Bit Score: 212.61  E-value: 2.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  34 VSRIREVYLAVFKRQSPTRVNSSPcyhrrqLLPlphrarasrgtltllttgtlpaRD---VRWVSVvGMNQFKPIFLGTV 110
Cdd:cd00673     1 ASEIRETFLSFFEKKGHTRVPSSP------VVP----------------------RDdptLLFTNA-GMNQFKPIFLGEV 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 111 DPNTSlskltRACNTQKCIHAGGRHNdlddVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQVYKLPTDRIYATY 190
Cdd:cd00673    52 PPPAN-----RLVNSQKCIRAGDIDN----VGKTGRHHTFFEMLGNFSFGDYFKEEAIAFAWELLTEVLGLPKDRLYVSV 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1731032771 191 FGGDEKAglapdnEARDIWLKFLPAERVLPFGCKDNFWEMGDTGPCG 237
Cdd:cd00673   123 FEGDDEE------EAIWWWKIGLPGIRIERIGFKDNFWEMGGNGPCG 163
alaS TIGR00344
alanine--tRNA ligase; The model describes alanine--tRNA ligase. This enzyme catalyzes the ...
98-237 2.31e-54

alanine--tRNA ligase; The model describes alanine--tRNA ligase. This enzyme catalyzes the reaction (tRNAala + L-alanine + ATP = L-alanyl-tRNAala + pyrophosphate + AMP). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273026 [Multi-domain]  Cd Length: 845  Bit Score: 186.43  E-value: 2.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  98 GMNQFKPIFLGTVDPNTSlskltRACNTQKCIhaggRHNDLDDVGKDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQ 177
Cdd:TIGR00344  37 GMAQFKPIFTGIVKPPSN-----RLTNAQPCI----RLNDLENVGRTARHHTLFEMLGNFSFGDYFKEEAIAFAWELLTE 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771 178 VYKLPTDRIYATYFGGDEKAGLAPDNeardiwlKFLPAERVLPFGCKDNFWEMGDtGPCG 237
Cdd:TIGR00344 108 VLGLDKERLYVTVYEDDEEAYKIWEK-------IGIPADRIIKCDAKDNFWDMGD-GPCG 159
PRK01584 PRK01584
alanyl-tRNA synthetase; Provisional
98-237 3.73e-31

alanyl-tRNA synthetase; Provisional


Pssm-ID: 234962 [Multi-domain]  Cd Length: 594  Bit Score: 120.26  E-value: 3.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731032771  98 GMNQFKPIFLGTVDPntslsKLTRACNTQKCIHAGgrhnDLDDVGkDTYHHTFFEMLGNWSFGDYFKKEAITWAWELLTQ 177
Cdd:PRK01584   41 GMHPLVPYLLGEPHP-----SGTRLVDVQKCLRTG----DIDEVG-DLSHLTFFEMLGNWSLGAYFKEESIKYSFEFLTS 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731032771 178 VYKL--PTDRIYATYFGGDEKAglAPDNEARDIWLKF-LPAERVLPFGCKDNFW-EMGDTGPCG 237
Cdd:PRK01584  111 PDYLniPKDKLYVTVFEGDEEI--PRDEETASVWESLgIPKDRIFYLSREHNWWgPVGETGPCG 172
 
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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