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Conserved domains on  [gi|1387731998|gb|PWA25162|]
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hypothetical protein CCH79_00005121, partial [Gambusia affinis]

Protein Classification

single-stranded DNA-binding protein( domain architecture ID 10137679)

single-stranded DNA (ssDNA)-binding protein plays a key role in DNA replication, recombination, and repair

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 49-165 5.41e-56

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


:

Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 172.32  E-value: 5.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRQD---LFIILRDFSGLTQILVPQKDSAISMKAAlcDLSVESVVKVTGTVRRRP 125
Cdd:cd04317     1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEFELAE--KLRNESVIQVTGKVRARP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1387731998 126 DGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:cd04317    79 EGTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVS 118
 
Name Accession Description Interval E-value
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 49-165 5.41e-56

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 172.32  E-value: 5.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRQD---LFIILRDFSGLTQILVPQKDSAISMKAAlcDLSVESVVKVTGTVRRRP 125
Cdd:cd04317     1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEFELAE--KLRNESVIQVTGKVRARP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1387731998 126 DGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:cd04317    79 EGTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVS 118
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 49-165 1.38e-48

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 165.17  E-value: 1.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVPQKDSAISMKAALcDLSVESVVKVTGTVRRR 124
Cdd:COG0173     3 RTHYCGELRESDVGQEVTLSGWVHRRR-DHggliFIDLRDRYGITQVVFDPDDSAEAFEKAE-KLRSEYVIAVTGKVRAR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1387731998 125 PDGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:COG0173    81 PEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVS 121
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 48-165 2.03e-46

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 159.46  E-value: 2.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  48 FRTHTCGELRSHHVGEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVpqkDSAISMKAALCDLSVESVVKVTGTVRR 123
Cdd:PRK00476    3 MRTHYCGELRESHVGQTVTLCGWVHRRR-DHggliFIDLRDREGIVQVVF---DPDAEAFEVAESLRSEYVIQVTGTVRA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1387731998 124 RPDGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:PRK00476   79 RPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVS 120
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 65-147 4.72e-10

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 53.01  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  65 VTLCGWVQYLRQD----LFIILRDFSGLTQILVPQKDSAISMKaalcDLSVESVVKVTGTVRRRpdgqenkamPTGDVEV 140
Cdd:pfam01336   1 VTVAGRVTSIRRSggklLFLTLRDGTGSIQVVVFKEEAEKLAK----KLKEGDVVRVTGKVKKR---------KGGELEL 67


                  ....*..
gi 1387731998 141 LAENVEV 147
Cdd:pfam01336  68 VVEEIEL 74
 
Name Accession Description Interval E-value
EcAspRS_like_N cd04317
EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli ...
 49-165 5.41e-56

EcAspRS_like_N: N-terminal, anticodon recognition domain of the type found in Escherichia coli aspartyl-tRNA synthetase (AspRS), the human mitochondrial (mt) AspRS-2, the discriminating (D) Thermus thermophilus AspRS-1, and the nondiscriminating (ND) Helicobacter pylori AspRS. These homodimeric enzymes are class2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. Human mtAspRS participates in mitochondrial biosynthesis; this enzyme been shown to charge E.coli native tRNAsp in addition to in vitro transcribed human mitochondrial tRNAsp. T. thermophilus is rare among bacteria in having both a D_AspRS and a ND_AspRS. H.pylori ND-AspRS can charge both tRNAASp and tRNAAsn, it is fractionally more efficient at aminoacylating tRNAAsp over tRNAAsn. The H.pylori genome does not contain AsnRS.


Pssm-ID: 239812 [Multi-domain]  Cd Length: 135  Bit Score: 172.32  E-value: 5.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRQD---LFIILRDFSGLTQILVPQKDSAISMKAAlcDLSVESVVKVTGTVRRRP 125
Cdd:cd04317     1 RTHYCGELRESHVGQEVTLCGWVQRRRDHgglIFIDLRDRYGIVQVVFDPEEAPEFELAE--KLRNESVIQVTGKVRARP 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1387731998 126 DGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:cd04317    79 EGTVNPKLPTGEIEVVASELEVLNKAKTLPFEIDDDVNVS 118
AspS COG0173
Aspartyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Aspartyl-tRNA ...
 49-165 1.38e-48

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


Pssm-ID: 439943 [Multi-domain]  Cd Length: 589  Bit Score: 165.17  E-value: 1.38e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVPQKDSAISMKAALcDLSVESVVKVTGTVRRR 124
Cdd:COG0173     3 RTHYCGELRESDVGQEVTLSGWVHRRR-DHggliFIDLRDRYGITQVVFDPDDSAEAFEKAE-KLRSEYVIAVTGKVRAR 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1387731998 125 PDGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:COG0173    81 PEGTVNPKLPTGEIEVLASELEILNKAKTPPFQIDDDTDVS 121
aspS PRK00476
aspartyl-tRNA synthetase; Validated
 48-165 2.03e-46

aspartyl-tRNA synthetase; Validated


Pssm-ID: 234775 [Multi-domain]  Cd Length: 588  Bit Score: 159.46  E-value: 2.03e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  48 FRTHTCGELRSHHVGEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVpqkDSAISMKAALCDLSVESVVKVTGTVRR 123
Cdd:PRK00476    3 MRTHYCGELRESHVGQTVTLCGWVHRRR-DHggliFIDLRDREGIVQVVF---DPDAEAFEVAESLRSEYVIQVTGTVRA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1387731998 124 RPDGQENKAMPTGDVEVLAENVEVFNTCRKLPFEIKDFVKVS 165
Cdd:PRK00476   79 RPEGTVNPNLPTGEIEVLASELEVLNKSKTLPFPIDDEEDVS 120
PLN02903 PLN02903
aminoacyl-tRNA ligase
 9-158 1.36e-29

aminoacyl-tRNA ligase


Pssm-ID: 215490 [Multi-domain]  Cd Length: 652  Bit Score: 113.34  E-value: 1.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998   9 HQASGRGQHLVCRAPVrqlSSANRLHTPPSATTGLSSLSF--RTHTCGELRSHHVGEKVTLCGWVQYLRQD---LFIILR 83
Cdd:PLN02903   20 LARKRTTLLSTSSAAS---SAATVIPVVSAVDSMSSQLTWpsRSHLCGALSVNDVGSRVTLCGWVDLHRDMgglTFLDVR 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1387731998  84 DFSGLTQIlVPQKDSAISMKAALCDLSVESVVKVTGTVRRRPDGQENKAMPTGDVEVLAENVEVFNTC-RKLPFEI 158
Cdd:PLN02903   97 DHTGIVQV-VTLPDEFPEAHRTANRLRNEYVVAVEGTVRSRPQESPNKKMKTGSVEVVAESVDILNVVtKSLPFLV 171
aspC PRK05159
aspartyl-tRNA synthetase; Provisional
 49-163 3.15e-24

aspartyl-tRNA synthetase; Provisional


Pssm-ID: 235354 [Multi-domain]  Cd Length: 437  Bit Score: 97.18  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVPQKDSAISMKAALcDLSVESVVKVTGTVRrr 124
Cdd:PRK05159    3 KRHLTSELTPELDGEEVTLAGWVHEIR-DLggiaFLILRDRSGIIQVVVKKKVDEELFETIK-KLKRESVVSVTGTVK-- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1387731998 125 pdgqENKAMPTGdVEVLAENVEVFNT-CRKLPFEIKDFVK 163
Cdd:PRK05159   79 ----ANPKAPGG-VEVIPEEIEVLNKaEEPLPLDISGKVL 113
Asp_Lys_Asn_RS_N cd04100
Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA ...
 64-150 1.56e-23

Asp_Lys_Asn_RS_N: N-terminal, anticodon recognition domain of class 2b aminoacyl-tRNA synthetases (aaRSs). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. Class 2b aaRSs include the homodimeric aspartyl-, asparaginyl-, and lysyl-tRNA synthetases (AspRS, AsnRS, and LysRS). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Included in this group are archeal and archeal-like AspRSs which are non-discriminating and can charge both tRNAAsp and tRNAAsn. E. coli cells have two isoforms of LysRSs (LysS and LysU) encoded by two distinct genes, which are differentially regulated. The cytoplasmic and the mitochondrial isoforms of human LysRS are encoded by a single gene. Yeast cytoplasmic and mitochondrial LysRSs participate in mitochondrial import of cytoplasmic tRNAlysCUU. In addition to their housekeeping role, human LysRS may function as a signaling molecule that activates immune cells. Tomato LysRS may participate in a process possibly connected to conditions of oxidative-stress conditions or heavy metal uptake. It is known that human tRNAlys and LysRS are specifically packaged into HIV-1 suggesting a role for LysRS in tRNA packaging. AsnRS is immunodominant antigen of the filarial nematode Brugia malayai and is of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239766 [Multi-domain]  Cd Length: 85  Bit Score: 88.39  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  64 KVTLCGWVQYLRQD---LFIILRDFSGLTQILVPQKDSAISMKAALcDLSVESVVKVTGTVRRRPDGQenkaMPTGDVEV 140
Cdd:cd04100     1 EVTLAGWVHSRRDHgglIFIDLRDGSGIVQVVVNKEELGEFFEEAE-KLRTESVVGVTGTVVKRPEGN----LATGEIEL 75

                          90
                  ....*....|
gi 1387731998 141 LAENVEVFNT 150
Cdd:cd04100    76 QAEELEVLSK 85
AsnS COG0017
Aspartyl/asparaginyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; ...
 49-160 4.90e-23

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


Pssm-ID: 439788 [Multi-domain]  Cd Length: 430  Bit Score: 93.96  E-value: 4.90e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  49 RTHTCGELRSHHVGEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVPQKDSAIsmKAALCDLSVESVVKVTGTVRrr 124
Cdd:COG0017     1 KRTYIKDLLPEHVGQEVTVAGWVRTKR-DSggisFLILRDGSGFIQVVVKKDKLEN--FEEAKKLTTESSVEVTGTVV-- 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1387731998 125 pdgqENKAMPTGdVEVLAENVEVFNTCRK-LPFEIKD 160
Cdd:COG0017    76 ----ESPRAPQG-VELQAEEIEVLGEADEpYPLQPKR 107
ND_PkAspRS_like_N cd04316
ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the ...
 62-150 4.77e-19

ND_PkAspRS_like_N: N-terminal, anticodon recognition domain of the type found in the homodimeric non-discriminating (ND) Pyrococcus kodakaraensis aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. P. kodakaraensis AspRS is a class 2b aaRS. aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. P. kodakaraensis ND-AspRS can charge both tRNAAsp and tRNAAsn. Some of the enzymes in this group may be discriminating, based on the presence of homologs of asparaginyl-tRNA synthetase (AsnRS) in their completed genomes.


Pssm-ID: 239811 [Multi-domain]  Cd Length: 108  Bit Score: 77.35  E-value: 4.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  62 GEKVTLCGWVQYLRqDL----FIILRDFSGLTQILVPQKDSAISMKAALCDLSVESVVKVTGTVrrrpdgQENKAMPTGd 137
Cdd:cd04316    12 GEEVTVAGWVHEIR-DLggikFVILRDREGIVQVTAPKKKVDKELFKTVRKLSRESVISVTGTV------KAEPKAPNG- 83

                          90
                  ....*....|...
gi 1387731998 138 VEVLAENVEVFNT 150
Cdd:cd04316    84 VEIIPEEIEVLSE 96
PRK12820 PRK12820
bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; ...
 53-160 6.04e-17

bifunctional aspartyl-tRNA synthetase/aspartyl/glutamyl-tRNA amidotransferase subunit C; Provisional


Pssm-ID: 105955 [Multi-domain]  Cd Length: 706  Bit Score: 77.33  E-value: 6.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  53 CGELRSHHVGEKVTLCGWVQYLRQD---LFIILRDFSGLTQILVPQKDSAISMKAALCDLSVESVVKVTGTVRRRPDGQE 129
Cdd:PRK12820    9 CGHLSLDDTGREVCLAGWVDAFRDHgelLFIHLRDRNGFIQAVFSPEAAPADVYELAASLRAEFCVALQGEVQKRLEETE 88

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1387731998 130 NKAMPTGDVEVLAENVEVFNTCRKLPFEIKD 160
Cdd:PRK12820   89 NPHIETGDIEVFVRELSILAASEALPFAISD 119
asnC PRK03932
asparaginyl-tRNA synthetase; Validated
 56-147 1.61e-11

asparaginyl-tRNA synthetase; Validated


Pssm-ID: 235176 [Multi-domain]  Cd Length: 450  Bit Score: 61.28  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  56 LRSHHVGEKVTLCGWVQYLRQDL---FIILRDFSGLTQILVPQKDSAISMKAALcDLSVESVVKVTGTVRrrpdgqENKA 132
Cdd:PRK03932   10 LKGKYVGQEVTVRGWVRTKRDSGkiaFLQLRDGSCFKQLQVVKDNGEEYFEEIK-KLTTGSSVIVTGTVV------ESPR 82

                          90
                  ....*....|....*
gi 1387731998 133 MPTGdVEVLAENVEV 147
Cdd:PRK03932   83 AGQG-YELQATKIEV 96
PhAsnRS_like_N cd04319
PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus ...
 64-147 3.91e-10

PhAsnRS_like_N: N-terminal, anticodon recognition domain of the type found in Pyrococcus horikoshii AsnRS asparaginyl-tRNA synthetase (AsnRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The archeal enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose.


Pssm-ID: 239814 [Multi-domain]  Cd Length: 103  Bit Score: 54.07  E-value: 3.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  64 KVTLCGWVqYLRQDL----FIILRDFSGLTQILVPQKDSAISMKAALcDLSVESVVKVTGTVRRRPDGqenkamPTGdVE 139
Cdd:cd04319     1 KVTLAGWV-YRKREVgkkaFIVLRDSTGIVQAVFSKDLNEEAYREAK-KVGIESSVIVEGAVKADPRA------PGG-AE 71


                  ....*...
gi 1387731998 140 VLAENVEV 147
Cdd:cd04319    72 VHGEKLEI 79
tRNA_anti-codon pfam01336
OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic ...
 65-147 4.72e-10

OB-fold nucleic acid binding domain; This family contains OB-fold domains that bind to nucleic acids. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See pfam00152). Aminoacyl-tRNA synthetases catalyze the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain.


Pssm-ID: 460164 [Multi-domain]  Cd Length: 75  Bit Score: 53.01  E-value: 4.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  65 VTLCGWVQYLRQD----LFIILRDFSGLTQILVPQKDSAISMKaalcDLSVESVVKVTGTVRRRpdgqenkamPTGDVEV 140
Cdd:pfam01336   1 VTVAGRVTSIRRSggklLFLTLRDGTGSIQVVVFKEEAEKLAK----KLKEGDVVRVTGKVKKR---------KGGELEL 67


                  ....*..
gi 1387731998 141 LAENVEV 147
Cdd:pfam01336  68 VVEEIEL 74
AsnRS_cyto_like_N cd04323
AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and ...
 64-147 7.90e-08

AsnRS_cyto_like_N: N-terminal, anticodon recognition domain of the type found in human and Saccharomyces cerevisiae cytoplasmic asparaginyl-tRNA synthetase (AsnRS), in Brugia malayai AsnRs and, in various putative bacterial AsnRSs. This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic synthesis, whereas the other exclusively with mitochondrial protein synthesis. AsnRS is immunodominant antigen of the filarial nematode B. malayai and of interest as a target for anti-parasitic drug design. Human AsnRS has been shown to be a pro-inflammatory chemokine which interacts with CCR3 chemokine receptors on T cells, immature dendritic cells and macrophages.


Pssm-ID: 239818 [Multi-domain]  Cd Length: 84  Bit Score: 47.61  E-value: 7.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  64 KVTLCGWVQYLRQD---LFIILRDFSGLTQILVPQKDSAISMKAAlcDLSVESVVKVTGTVRRRPdgqENKAMPTGdVEV 140
Cdd:cd04323     1 RVKVFGWVHRLRSQkklMFLVLRDGTGFLQCVLSKKLVTEFYDAK--SLTQESSVEVTGEVKEDP---RAKQAPGG-YEL 74


                  ....*..
gi 1387731998 141 LAENVEV 147
Cdd:cd04323    75 QVDYLEI 81
ScAspRS_mt_like_N cd04321
ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces ...
 64-150 1.28e-05

ScAspRS_mt_like_N: N-terminal, anticodon recognition domain of the type found in Saccharomyces cerevisiae mitochondrial (mt) aspartyl-tRNA synthetase (AspRS). This domain is a beta-barrel domain (OB fold) involved in binding the tRNA anticodon stem-loop. The enzymes in this fungal group are homodimeric class2b aminoacyl-tRNA synthetases (aaRSs). aaRSs catalyze the specific attachment of amino acids (AAs) to their cognate tRNAs during protein biosynthesis. This 2-step reaction involves i) the activation of the AA by ATP in the presence of magnesium ions, followed by ii) the transfer of the activated AA to the terminal ribose of tRNA. In the case of the class2b aaRSs, the activated AA is attached to the 3'OH of the terminal ribose. Eukaryotes contain 2 sets of aaRSs, both of which are encoded by the nuclear genome. One set concerns with cytoplasmic protein synthesis, whereas the other exclusively with mitochondrial protein synthesis. Mutations in the gene for S. cerevisiae mtAspRS result in a "petite" phenotype typical for a mutation in a nuclear gene that results in a non-functioning mitochondrial protein synthesis system.


Pssm-ID: 239816 [Multi-domain]  Cd Length: 86  Bit Score: 41.53  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998  64 KVTLCGWVQYlRQDL-----FIILRDFSG-LTQILVPQKDSAISMkaaLCDLSVESVVKVTGTVRRRpdgQENKAMPTGD 137
Cdd:cd04321     1 KVTLNGWIDR-KPRIvkklsFADLRDPNGdIIQLVSTAKKDAFSL---LKSITAESPVQVRGKLQLK---EAKSSEKNDE 73

                          90
                  ....*....|...
gi 1387731998 138 VEVLAENVEVFNT 150
Cdd:cd04321    74 WELVVDDIQTLNA 86
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
49-121 5.96e-04

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 39.56  E-value: 5.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1387731998   49 RTHTCGELRSHHVGEKVTLCGWVQYLR---QDLFIILRDFSGLTQILV----PQKDSAISMKAA--LCDLsvesvVKVTG 119
Cdd:PRK02983   638 PTHTVAEALDAPTGEEVSVSGRVLRIRdygGVLFADLRDWSGELQVLLdasrLEQGSLADFRAAvdLGDL-----VEVTG 712


                   ..
gi 1387731998  120 TV 121
Cdd:PRK02983   713 TM 714
 
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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