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Conserved domains on  [gi|446358046|ref|WP_000435901|]
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MULTISPECIES: serine-tRNA(Ala) deacylase AlaX [Bacillus]

Protein Classification

alanyl-tRNA editing protein( domain architecture ID 11458347)

alanyl-tRNA editing protein functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) or Gly-tRNA(Ala)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AlaX COG2872
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ...
1-228 1.88e-87

Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 442119 [Multi-domain]  Cd Length: 238  Bit Score: 264.75  E-value: 1.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   1 MEQKLYYTDAYKQDFTTKVIkqdyDKDGNLYVILNETVFYPTGGGQPHDTGTL--NG--IAVLGVEEVDEEIRHFIAEQ- 75
Cdd:COG2872    1 MTELLYLEDSYLKEFEATVT----AVTEEGGVVLDRTAFYPTGGGQPGDTGTLvwDGkeIRVVDVRKEDGEIVHVLEGAp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  76 --LHTEEVEGKINWERRFDHMQQHAAQHILSAAFWDYFNIPTIGFHLGKETVTIDLETENLHAETVEKAVQIANKIVFEN 153
Cdd:COG2872   77 lpEVGDEVTGEIDWERRYRHMRLHTALHLLSAVVYREYGAPVTGGQIGEDRARIDFDLPEFDEEDLEEIEAEANELIAAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 154 HPILIKWMNLEEAKTLP-LRK-----EPTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWER-NKGGIRLTFIA 226
Cdd:COG2872  157 LPVRIYWITREELEAIPgLVRtmsvlPPPGVGRVRIVEIGGVDLQPCGGTHVANTGEIGRIKITKIEKkGKGNRRVYFTL 236

                 ..
gi 446358046 227 GW 228
Cdd:COG2872  237 GE 238
DHHA1 pfam02272
DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
259-394 6.13e-11

DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA1 for DHH associated domain. This domain is diagnostic of DHH subfamily 1 members. This domains is also found in alanyl tRNA synthetase, suggesting that this domain may have an RNA binding function. The domain is about 60 residues long and contains a conserved GG motif.


:

Pssm-ID: 396724 [Multi-domain]  Cd Length: 139  Bit Score: 59.76  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  259 VAQLLTSQKENKKAMQTMTEKLLYTEANELLQQPTKIHAG-ILISKVFTNRSMQEIAKLSAIITEQ-QEHAITYFVIENE 336
Cdd:pfam02272   1 LESLNEELKELEKELEELKEALALLKAKELLEKAEEINGVkVLVAEVGEGWDAGALGIAADRLKKKlGDPVIVLVAKEDG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446358046  337 DKLQCILACGKTVTLDMNALLKEALPTIEGKGGGnKKSARGGGKAMMSGDEFLNQLIS 394
Cdd:pfam02272  81 DKVKVSARSSKDKGVDAGELLKEVAAILGGGGGG-HDLAAGAGIDAEKLDEALELLEE 137
 
Name Accession Description Interval E-value
AlaX COG2872
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ...
1-228 1.88e-87

Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442119 [Multi-domain]  Cd Length: 238  Bit Score: 264.75  E-value: 1.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   1 MEQKLYYTDAYKQDFTTKVIkqdyDKDGNLYVILNETVFYPTGGGQPHDTGTL--NG--IAVLGVEEVDEEIRHFIAEQ- 75
Cdd:COG2872    1 MTELLYLEDSYLKEFEATVT----AVTEEGGVVLDRTAFYPTGGGQPGDTGTLvwDGkeIRVVDVRKEDGEIVHVLEGAp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  76 --LHTEEVEGKINWERRFDHMQQHAAQHILSAAFWDYFNIPTIGFHLGKETVTIDLETENLHAETVEKAVQIANKIVFEN 153
Cdd:COG2872   77 lpEVGDEVTGEIDWERRYRHMRLHTALHLLSAVVYREYGAPVTGGQIGEDRARIDFDLPEFDEEDLEEIEAEANELIAAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 154 HPILIKWMNLEEAKTLP-LRK-----EPTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWER-NKGGIRLTFIA 226
Cdd:COG2872  157 LPVRIYWITREELEAIPgLVRtmsvlPPPGVGRVRIVEIGGVDLQPCGGTHVANTGEIGRIKITKIEKkGKGNRRVYFTL 236

                 ..
gi 446358046 227 GW 228
Cdd:COG2872  237 GE 238
a_tRNA_ed_AlaXM NF040865
alanyl-tRNA editing protein AlaXM;
3-218 1.28e-60

alanyl-tRNA editing protein AlaXM;


Pssm-ID: 468802 [Multi-domain]  Cd Length: 234  Bit Score: 195.91  E-value: 1.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   3 QKLYYTDAYKQDFTTKVIKqdydKDGNlYVILNETVFYPTGGGQPHDTGTLNG----IAVLGVEEVDEEIRHFIAEQLHT 78
Cdd:NF040865   2 EKLYLEDSYLKEFDATVVR----VKGN-GVVLDRTAFYPTGGGQPHDTGTLVRddkeFRVVDVRKEGGEIAHVVDRAPGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  79 ---EEVEGKINWERRFDHMQQHAAQHILSAAFWDYFNIPTIGFHLGKETVTIDLETENLHAETVEKAVQIANKIVFENHP 155
Cdd:NF040865  77 kpgDKVKGEIDWDRRYRLMRYHTASHILSAVLYREYGALITGGQISPDKARVDFSLENFDRELLEEIIEEANEIIAEGIE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358046 156 ILIKWMNLEEAKTLP----LRKE-PTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWErNKG 218
Cdd:NF040865 157 VKIYWLPREEALKIPglvrLAKRlPPEIEEVRIVEIEGVDIQADGGTHVKNTGEIGEIKILKRE-NKG 223
alaS TIGR00344
alanine--tRNA ligase; The model describes alanine--tRNA ligase. This enzyme catalyzes the ...
4-379 1.97e-46

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: 170.25  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046    4 KLYYTDAykqDFTTKVIKQDYDkdGNL----------YVILNETVFYPTGGGQPHDTGTLNG----IAVLGVEEVDEEIR 69
Cdd:TIGR00344 446 FLGYDDL---EFEAKVIGLFDD--GYLveqalagqsvYVILDQTPFYAESGGQIGDTGYLIAndgkFRVVDVQKPNGVVF 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   70 HFIAEQLHTEE----VEGKINWERRFDHMQQHAAQHILSAAFWDyfnipTIGFHL-------GKETVTIDL-ETENLHAE 137
Cdd:TIGR00344 521 HFGEVEGGSLKvgdkVIAVIDEKRRFRIMRNHSATHLLHAALQK-----VLGNHVwqagslvSFKKLRFDFsHFRALTRE 595
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  138 TVEKAVQIANKIVFENHPILIKWMNLEEAKTLP----LRKEPTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGW 213
Cdd:TIGR00344 596 ELEEIEDLANEQILANIPIKVIFMDLDEAKRKGafalFGEKYVPGEKVRVVSVGDFSVELCGGTHVRNTGEIGLFKIVKE 675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  214 ERNKGGI-RLTFIAGWRTLKLMGQQQQIMKDVSKQLNSSEADIPAKVAQLLTSQKENKKAMQTMTEKLLYTEANELLQQP 292
Cdd:TIGR00344 676 SGIAAGVrRIEAVTGEAAIEYLNEQEDKLKELADILKVTPNELPKKVERFFEEWKALQKELESLKLKIADQKIDELKDKA 755
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  293 TKIHAGILISKVFTNRSMQEIAKLSAIITEQQEHAITYFVIENEDKLQCILACGK---TVTLDMNALLKEALPTIEGKGG 369
Cdd:TIGR00344 756 ETINGVKVLVEVVDAKDMKSLKTMADRLKSKLGSAIYVLASFAEGKVKLVCGVSNdvlTKKIKAGELINQIAQVLGGKGG 835
                         410
                  ....*....|
gi 446358046  370 GNKKSARGGG 379
Cdd:TIGR00344 836 GRPDFAQGGG 845
PLN02961 PLN02961
alanine-tRNA ligase
28-224 2.65e-13

alanine-tRNA ligase


Pssm-ID: 178546 [Multi-domain]  Cd Length: 223  Bit Score: 68.57  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  28 GNLYVILNETVFYPTGGGQPHDTGTLNG------IAVLGVEEVDEEIRHF-------IAEQLHTE---EVEGKINWERRF 91
Cdd:PLN02961   1 GRIALVLDRTIFHPQGGGQPSDTGRIVIsggdtkFSVQDVRRKDGVVYHYgvfegsnPESASPFEagdEVTVTVDESRRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  92 DHMQQHAAQHILSAAFwdyFNI------PTIGFHLG-------KETVTIDlETENLHAEtVEKAvqiANKIVFENHPILI 158
Cdd:PLN02961  81 LHSRLHSAGHLLDVCM---ARVglgplePGKGYHFPdgpfveyKGKIPQG-ELDSKQDE-LEAE---ANELIAEGGKVSA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358046 159 KWMNLEEAKTL-----PLRKEPTMTENIRVVMienfDYNG--CGGTHPKRTGEVGPIQVLGWERNKGGIRLTF 224
Cdd:PLN02961 153 AVLPYDEAAELcggslPDYIAKDSTPRIVKIG----DSPGcpCGGTHVADVSEITSVKVTQIRVKKGVTRVSY 221
tRNA_SAD smart00863
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ...
181-221 1.50e-11

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 197931 [Multi-domain]  Cd Length: 43  Bit Score: 58.55  E-value: 1.50e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 446358046   181 IRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWERNKGGIR 221
Cdd:smart00863   1 VRVVSIGDFSVELCGGTHVPNTGEIGAFKILSVSGAYWGLQ 41
DHHA1 pfam02272
DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
259-394 6.13e-11

DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA1 for DHH associated domain. This domain is diagnostic of DHH subfamily 1 members. This domains is also found in alanyl tRNA synthetase, suggesting that this domain may have an RNA binding function. The domain is about 60 residues long and contains a conserved GG motif.


Pssm-ID: 396724 [Multi-domain]  Cd Length: 139  Bit Score: 59.76  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  259 VAQLLTSQKENKKAMQTMTEKLLYTEANELLQQPTKIHAG-ILISKVFTNRSMQEIAKLSAIITEQ-QEHAITYFVIENE 336
Cdd:pfam02272   1 LESLNEELKELEKELEELKEALALLKAKELLEKAEEINGVkVLVAEVGEGWDAGALGIAADRLKKKlGDPVIVLVAKEDG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446358046  337 DKLQCILACGKTVTLDMNALLKEALPTIEGKGGGnKKSARGGGKAMMSGDEFLNQLIS 394
Cdd:pfam02272  81 DKVKVSARSSKDKGVDAGELLKEVAAILGGGGGG-HDLAAGAGIDAEKLDEALELLEE 137
tRNA_SAD pfam07973
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ...
181-221 1.17e-10

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 429764 [Multi-domain]  Cd Length: 43  Bit Score: 56.30  E-value: 1.17e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446358046  181 IRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWERNKGGIR 221
Cdd:pfam07973   1 VRVVSIGDFDVDLCGGTHVPNTGEIGAFKILKGESKNKGLR 41
 
Name Accession Description Interval E-value
AlaX COG2872
Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis] ...
1-228 1.88e-87

Ser-tRNA(Ala) deacylase AlaX (editing enzyme) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442119 [Multi-domain]  Cd Length: 238  Bit Score: 264.75  E-value: 1.88e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   1 MEQKLYYTDAYKQDFTTKVIkqdyDKDGNLYVILNETVFYPTGGGQPHDTGTL--NG--IAVLGVEEVDEEIRHFIAEQ- 75
Cdd:COG2872    1 MTELLYLEDSYLKEFEATVT----AVTEEGGVVLDRTAFYPTGGGQPGDTGTLvwDGkeIRVVDVRKEDGEIVHVLEGAp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  76 --LHTEEVEGKINWERRFDHMQQHAAQHILSAAFWDYFNIPTIGFHLGKETVTIDLETENLHAETVEKAVQIANKIVFEN 153
Cdd:COG2872   77 lpEVGDEVTGEIDWERRYRHMRLHTALHLLSAVVYREYGAPVTGGQIGEDRARIDFDLPEFDEEDLEEIEAEANELIAAD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 154 HPILIKWMNLEEAKTLP-LRK-----EPTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWER-NKGGIRLTFIA 226
Cdd:COG2872  157 LPVRIYWITREELEAIPgLVRtmsvlPPPGVGRVRIVEIGGVDLQPCGGTHVANTGEIGRIKITKIEKkGKGNRRVYFTL 236

                 ..
gi 446358046 227 GW 228
Cdd:COG2872  237 GE 238
a_tRNA_ed_AlaXM NF040865
alanyl-tRNA editing protein AlaXM;
3-218 1.28e-60

alanyl-tRNA editing protein AlaXM;


Pssm-ID: 468802 [Multi-domain]  Cd Length: 234  Bit Score: 195.91  E-value: 1.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   3 QKLYYTDAYKQDFTTKVIKqdydKDGNlYVILNETVFYPTGGGQPHDTGTLNG----IAVLGVEEVDEEIRHFIAEQLHT 78
Cdd:NF040865   2 EKLYLEDSYLKEFDATVVR----VKGN-GVVLDRTAFYPTGGGQPHDTGTLVRddkeFRVVDVRKEGGEIAHVVDRAPGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  79 ---EEVEGKINWERRFDHMQQHAAQHILSAAFWDYFNIPTIGFHLGKETVTIDLETENLHAETVEKAVQIANKIVFENHP 155
Cdd:NF040865  77 kpgDKVKGEIDWDRRYRLMRYHTASHILSAVLYREYGALITGGQISPDKARVDFSLENFDRELLEEIIEEANEIIAEGIE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358046 156 ILIKWMNLEEAKTLP----LRKE-PTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWErNKG 218
Cdd:NF040865 157 VKIYWLPREEALKIPglvrLAKRlPPEIEEVRIVEIEGVDIQADGGTHVKNTGEIGEIKILKRE-NKG 223
alaS TIGR00344
alanine--tRNA ligase; The model describes alanine--tRNA ligase. This enzyme catalyzes the ...
4-379 1.97e-46

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: 170.25  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046    4 KLYYTDAykqDFTTKVIKQDYDkdGNL----------YVILNETVFYPTGGGQPHDTGTLNG----IAVLGVEEVDEEIR 69
Cdd:TIGR00344 446 FLGYDDL---EFEAKVIGLFDD--GYLveqalagqsvYVILDQTPFYAESGGQIGDTGYLIAndgkFRVVDVQKPNGVVF 520
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046   70 HFIAEQLHTEE----VEGKINWERRFDHMQQHAAQHILSAAFWDyfnipTIGFHL-------GKETVTIDL-ETENLHAE 137
Cdd:TIGR00344 521 HFGEVEGGSLKvgdkVIAVIDEKRRFRIMRNHSATHLLHAALQK-----VLGNHVwqagslvSFKKLRFDFsHFRALTRE 595
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  138 TVEKAVQIANKIVFENHPILIKWMNLEEAKTLP----LRKEPTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGW 213
Cdd:TIGR00344 596 ELEEIEDLANEQILANIPIKVIFMDLDEAKRKGafalFGEKYVPGEKVRVVSVGDFSVELCGGTHVRNTGEIGLFKIVKE 675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  214 ERNKGGI-RLTFIAGWRTLKLMGQQQQIMKDVSKQLNSSEADIPAKVAQLLTSQKENKKAMQTMTEKLLYTEANELLQQP 292
Cdd:TIGR00344 676 SGIAAGVrRIEAVTGEAAIEYLNEQEDKLKELADILKVTPNELPKKVERFFEEWKALQKELESLKLKIADQKIDELKDKA 755
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  293 TKIHAGILISKVFTNRSMQEIAKLSAIITEQQEHAITYFVIENEDKLQCILACGK---TVTLDMNALLKEALPTIEGKGG 369
Cdd:TIGR00344 756 ETINGVKVLVEVVDAKDMKSLKTMADRLKSKLGSAIYVLASFAEGKVKLVCGVSNdvlTKKIKAGELINQIAQVLGGKGG 835
                         410
                  ....*....|
gi 446358046  370 GNKKSARGGG 379
Cdd:TIGR00344 836 GRPDFAQGGG 845
AlaS COG0013
Alanyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Alanyl-tRNA ...
31-380 1.14e-38

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: 147.89  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  31 YVILNETVFYPTGGGQPHDTGTLNG----IAVLGVE-EVDEEIRHF---IAEQLHT-EEVEGKINWERRFDHMQQHAAQH 101
Cdd:COG0013  493 EVVLDRTPFYAESGGQVGDTGTIEGdggvFEVTDTQkPPGGLIVHIgkvEEGELKVgDTVTAQVDAERRRAIARNHSATH 572
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 102 ILSAAFWDyfniptigfHLGkETVT-----IDLE--------TENLHAETVEKAVQIANKIVFENHPILIKWMNLEEAKt 168
Cdd:COG0013  573 LLHAALRE---------VLG-EHVTqagslVAPDrlrfdfshFEALTPEELAEIEDLVNEKIRENLPVETREMPLDEAK- 641
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 169 lplrKEPTMT-------ENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGwErnkGGI-----RLTFIAGWRTLKLMGQ 236
Cdd:COG0013  642 ----ALGAMAlfgekygDEVRVVSIGDFSRELCGGTHVSRTGDIGLFKIVS-E---SSVaagvrRIEAVTGEAALEYLRE 713
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 237 QQQIMKDVSKQLNSSEADIPAKVAQLLTSQKENKKAMQTMTEKLLYTEANELLQQPTKIHaGI-LISKVFTNRSMQEIAK 315
Cdd:COG0013  714 QEALLKELAELLKAPPEELPERVEALLEELKELEKELEQLKAKLASAAADDLLAQAEEIG-GVkVLAARVEGVDAKDLRD 792
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446358046 316 LSAIITEQQEHAITYFVIENEDKLQCILACGKTVT---LDMNALLKEALPTIEGKGGGNKKSARGGGK 380
Cdd:COG0013  793 LADDLKDKLGSGVVVLASVADGKVSLVAGVTKDLVkkgLKAGDLVKEVAKIVGGGGGGRPDMAQAGGK 860
PLN02961 PLN02961
alanine-tRNA ligase
28-224 2.65e-13

alanine-tRNA ligase


Pssm-ID: 178546 [Multi-domain]  Cd Length: 223  Bit Score: 68.57  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  28 GNLYVILNETVFYPTGGGQPHDTGTLNG------IAVLGVEEVDEEIRHF-------IAEQLHTE---EVEGKINWERRF 91
Cdd:PLN02961   1 GRIALVLDRTIFHPQGGGQPSDTGRIVIsggdtkFSVQDVRRKDGVVYHYgvfegsnPESASPFEagdEVTVTVDESRRK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  92 DHMQQHAAQHILSAAFwdyFNI------PTIGFHLG-------KETVTIDlETENLHAEtVEKAvqiANKIVFENHPILI 158
Cdd:PLN02961  81 LHSRLHSAGHLLDVCM---ARVglgplePGKGYHFPdgpfveyKGKIPQG-ELDSKQDE-LEAE---ANELIAEGGKVSA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446358046 159 KWMNLEEAKTL-----PLRKEPTMTENIRVVMienfDYNG--CGGTHPKRTGEVGPIQVLGWERNKGGIRLTF 224
Cdd:PLN02961 153 AVLPYDEAAELcggslPDYIAKDSTPRIVKIG----DSPGcpCGGTHVADVSEITSVKVTQIRVKKGVTRVSY 221
PLN02900 PLN02900
alanyl-tRNA synthetase
32-380 1.09e-12

alanyl-tRNA synthetase


Pssm-ID: 215487 [Multi-domain]  Cd Length: 936  Bit Score: 69.66  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  32 VILNETVFYPTGGGQPHDTGTL--NGIAVLGVEEVDEEIRHFiaeqLHT-----------EEVEGKINWERRFDHMQQHA 98
Cdd:PLN02900 524 IVLDKTSFYAESGGQIGDTGVLegSGGAVVEVSDVQKAGGFV----LHIgtvtegsvsvgDAVTCKVDYDRRRRIAPNHT 599
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  99 AQHILSAAFWDyfnipTIG------------------FHLGKETVTIDL-ETENLHAETVEKAVqiankivfenhPILIK 159
Cdd:PLN02900 600 ATHLLNSALKE-----VLGdhvdqkgslvafeklrfdFSHGKPMTPEELrEVESLVNEWIGDAL-----------PVEAK 663
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 160 WMNLEEAKTLP-LR-----KEPtmtENIRVVMI-ENFDYNGCGGTHPKRTGEVGPIQVLGWERNKGGI-RLTFIAGWRTL 231
Cdd:PLN02900 664 EMPLADAKRINgLRavfgeKYP---DPVRVVSVgGVYSMELCGGTHVSNTAEAEAFKLLSEEGIAKGIrRITAVTGGAAV 740
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 232 KLMGQQQQIMKDVSKQLNSSEADIPAKVAQLLTS---------------------QKENKKAMQTMTE---KLLYTEANE 287
Cdd:PLN02900 741 EAINAADSLERELDSALKVEGSDLEKKVASLKSRvdaavipaakkeeirarvsalQKELRAAQKEAAAlraKLAVAKATE 820
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046 288 LLQQPTKIHAGILISKV---FTNRSMQEIAklSAIITEQQEHAITYF-VIENEDKLQCILACGKTVT---LDMNALLKEA 360
Cdd:PLN02900 821 LASKALSAGKSVLVARLdvgVDAAALKEAA--EKVIAKLGDPAAVVLsSDEEKGKVSLVAAVPPGVVkkgLKAGKWLGAI 898
                        410       420
                 ....*....|....*....|.
gi 446358046 361 LPtIEGKGGGNKK-SARGGGK 380
Cdd:PLN02900 899 AK-LCGGGGGGKPgFAQGQGR 918
tRNA_SAD smart00863
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of ...
181-221 1.50e-11

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active form of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this SAD domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 197931 [Multi-domain]  Cd Length: 43  Bit Score: 58.55  E-value: 1.50e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 446358046   181 IRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWERNKGGIR 221
Cdd:smart00863   1 VRVVSIGDFSVELCGGTHVPNTGEIGAFKILSVSGAYWGLQ 41
DHHA1 pfam02272
DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called ...
259-394 6.13e-11

DHHA1 domain; This domain is often found adjacent to the DHH domain pfam01368 and is called DHHA1 for DHH associated domain. This domain is diagnostic of DHH subfamily 1 members. This domains is also found in alanyl tRNA synthetase, suggesting that this domain may have an RNA binding function. The domain is about 60 residues long and contains a conserved GG motif.


Pssm-ID: 396724 [Multi-domain]  Cd Length: 139  Bit Score: 59.76  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  259 VAQLLTSQKENKKAMQTMTEKLLYTEANELLQQPTKIHAG-ILISKVFTNRSMQEIAKLSAIITEQ-QEHAITYFVIENE 336
Cdd:pfam02272   1 LESLNEELKELEKELEELKEALALLKAKELLEKAEEINGVkVLVAEVGEGWDAGALGIAADRLKKKlGDPVIVLVAKEDG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446358046  337 DKLQCILACGKTVTLDMNALLKEALPTIEGKGGGnKKSARGGGKAMMSGDEFLNQLIS 394
Cdd:pfam02272  81 DKVKVSARSSKDKGVDAGELLKEVAAILGGGGGG-HDLAAGAGIDAEKLDEALELLEE 137
tRNA_SAD pfam07973
Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of ...
181-221 1.17e-10

Threonyl and Alanyl tRNA synthetase second additional domain; The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain.


Pssm-ID: 429764 [Multi-domain]  Cd Length: 43  Bit Score: 56.30  E-value: 1.17e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 446358046  181 IRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWERNKGGIR 221
Cdd:pfam07973   1 VRVVSIGDFDVDLCGGTHVPNTGEIGAFKILKGESKNKGLR 41
tRNA-synt_2c pfam01411
tRNA synthetases class II (A); Other tRNA synthetase sub-families are too dissimilar to be ...
1-89 5.07e-06

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: 48.43  E-value: 5.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046    1 MEQKLYYTDAYKQDFTTKVIKQDYDKDG-----NLYVILNETVFYPTGGGQPHDTGTLNG----IAVLGVEEVDEEIRHF 71
Cdd:pfam01411 447 TTEFLGYDDLESEAKILALPKDGEFVAEvlagqEGGVILDRTPFYAESGGQIGDTGYIIGdggeFRVTDVQKYGGVVVHK 526
                          90       100
                  ....*....|....*....|..
gi 446358046   72 I-AEQLHTEE---VEGKINWER 89
Cdd:pfam01411 527 GkLESGKLKVgdkVIAVIDEDR 548
PRK01584 PRK01584
alanyl-tRNA synthetase; Provisional
92-221 1.21e-03

alanyl-tRNA synthetase; Provisional


Pssm-ID: 234962 [Multi-domain]  Cd Length: 594  Bit Score: 40.91  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446358046  92 DHMQQ----HAAQHILSAAFWdyfniPTIGFHLGKETVTIDLE--------TENLHAETVEKAVQIANKIVFENHPILIK 159
Cdd:PRK01584 448 DHSYEttklHTATHLLHKALR-----LVLGDHVRQKGSNITAErlrfdfshPEKMTDDEIKKVEDIVNLQIKNDLSVKKE 522
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446358046 160 WMNLEEAKTLPLRK--EPTMTENIRVVMIENFDYNGCGGTHPKRTGEVGPIQVLGWERNKGGIR 221
Cdd:PRK01584 523 VMSLEEAREKGAMAlfGEKYEDIVKVYEIDGFSKEVCGGPHVENTGELGTFKIQKEQSSSSGVR 586
 
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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