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Conserved domains on  [gi|1002264484|ref|XP_015636579|]
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uncharacterized protein [Oryza sativa Japonica Group]

Protein Classification

tRNA_bind_EMAP-II_like domain-containing protein( domain architecture ID 10120044)

tRNA_bind_EMAP-II_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 94-194 7.48e-63

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


:

Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 192.44  E-value: 7.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  94 LLDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDA 173
Cdd:cd02799     5 RLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLCASNA 84

                          90       100
                  ....*....|....*....|.
gi 1002264484 174 SHENVELLTPPEGSVPGERVW 194
Cdd:cd02799    85 DHEKVELLEPPEGAKPGERVT 105
 
Name Accession Description Interval E-value
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 94-194 7.48e-63

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 192.44  E-value: 7.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  94 LLDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDA 173
Cdd:cd02799     5 RLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLCASNA 84

                          90       100
                  ....*....|....*....|.
gi 1002264484 174 SHENVELLTPPEGSVPGERVW 194
Cdd:cd02799    85 DHEKVELLEPPEGAKPGERVT 105
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 93-259 5.87e-61

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 205.40  E-value: 5.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  93 ALLDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASD 172
Cdd:PLN02610  641 SRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASN 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484 173 ASHENVELLTPPEGSVPGERVWFGTEDGKdrqseaasPNQV--QKKKIWESVQPHLRTSENCTAFLGEHPMRTSAGVVFC 250
Cdd:PLN02610  721 SDHTKVELVEPPESAAVGERVTFPGFEGE--------PDDVlnPKKKVWETLQPDLHTNSELVACYKDVPFTTSAGVCKV 792


                  ....*....
gi 1002264484 251 KTLQGARVS 259
Cdd:PLN02610  793 ASIANGSIR 801
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 97-192 7.63e-40

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 133.14  E-value: 7.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  97 IRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDASHE 176
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*.
gi 1002264484 177 NVELLTPPEGSVPGER 192
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 95-193 1.16e-25

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 97.88  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADTLYVEEVDVGEEQpRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDaS 174
Cdd:TIGR00399  40 VDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAED-D 117

                          90
                  ....*....|....*....
gi 1002264484 175 HENVELLTPPEGSVPGERV 193
Cdd:TIGR00399 118 GKVLFLLSPDQEAIAGERI 136
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
88-190 1.24e-21

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 93.77  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  88 VEEVAALLDIRVGRVVKAWRHPEADTLYVEEVDVGEEqPRTICSGLVNY----LPIDQLQDSNVIVLANLKPRNMRGIKS 163
Cdd:COG0073    35 FEKVGGLDGLRVGKVLEAEPHPNADKLLVLQVDVGEE-TRQIVCGAPNVyagdKVPEALVGAQVPGVVNLKPRKIRGVES 113

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002264484 164 NGMLMAASD----ASHENveLLTPPEGSVPG 190
Cdd:COG0073   114 EGMLCSAEElglgEDHDG--ILELPEDAPPG 142
 
Name Accession Description Interval E-value
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 94-194 7.48e-63

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 192.44  E-value: 7.48e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  94 LLDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDA 173
Cdd:cd02799     5 RLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLCASNA 84

                          90       100
                  ....*....|....*....|.
gi 1002264484 174 SHENVELLTPPEGSVPGERVW 194
Cdd:cd02799    85 DHEKVELLEPPEGAKPGERVT 105
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 93-259 5.87e-61

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 205.40  E-value: 5.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  93 ALLDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASD 172
Cdd:PLN02610  641 SRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASN 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484 173 ASHENVELLTPPEGSVPGERVWFGTEDGKdrqseaasPNQV--QKKKIWESVQPHLRTSENCTAFLGEHPMRTSAGVVFC 250
Cdd:PLN02610  721 SDHTKVELVEPPESAAVGERVTFPGFEGE--------PDDVlnPKKKVWETLQPDLHTNSELVACYKDVPFTTSAGVCKV 792


                  ....*....
gi 1002264484 251 KTLQGARVS 259
Cdd:PLN02610  793 ASIANGSIR 801
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 97-193 6.99e-42

The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.


Pssm-ID: 239066 [Multi-domain]  Cd Length: 99  Bit Score: 138.42  E-value: 6.99e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  97 IRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASD--AS 174
Cdd:cd02153     1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEElgLE 80

                          90
                  ....*....|....*....
gi 1002264484 175 HENVELLTPPEGSVPGERV 193
Cdd:cd02153    81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 97-192 7.63e-40

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 133.14  E-value: 7.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  97 IRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDASHE 176
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*.
gi 1002264484 177 NVELLTPPEGSVPGER 192
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 95-194 2.37e-29

tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.


Pssm-ID: 239199 [Multi-domain]  Cd Length: 105  Bit Score: 106.43  E-value: 2.37e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADTLYVEEVDVGEEqPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDAs 174
Cdd:cd02800     9 VDLRVGKVLEAERVEGSDKLLKLTVDLGEE-ERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAEDG- 86

                          90       100
                  ....*....|....*....|
gi 1002264484 175 hENVELLTPPEGSVPGERVW 194
Cdd:cd02800    87 -GKLKLLTPDEEVEPGSRVS 105
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 95-193 4.35e-29

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 115.25  E-value: 4.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADTLYVEEVDVGEEQpRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMR-GIkSNGMLMAASDA 173
Cdd:PRK00133  576 VDLRVAKIVEAEKVEGADKLLKLTLDLGEET-RQVFSGIKSAYDPEELVGKLVVMVANLAPRKMKfGV-SEGMVLAAGPG 653

                          90       100
                  ....*....|....*....|
gi 1002264484 174 ShENVELLTPPEGSVPGERV 193
Cdd:PRK00133  654 G-GDLFLLEPDEGAKPGMRV 672
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 95-193 1.16e-25

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 97.88  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADTLYVEEVDVGEEQpRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDaS 174
Cdd:TIGR00399  40 VDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAAED-D 117

                          90
                  ....*....|....*....
gi 1002264484 175 HENVELLTPPEGSVPGERV 193
Cdd:TIGR00399 118 GKVLFLLSPDQEAIAGERI 136
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 95-193 4.59e-25

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 103.73  E-value: 4.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDAs 174
Cdd:PRK12267  551 VELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAAEDD- 629

                          90
                  ....*....|....*....
gi 1002264484 175 hENVELLTPPEGSVPGERV 193
Cdd:PRK12267  630 -GKLTLLTVDKEVPNGSKV 647
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
88-190 1.24e-21

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 93.77  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  88 VEEVAALLDIRVGRVVKAWRHPEADTLYVEEVDVGEEqPRTICSGLVNY----LPIDQLQDSNVIVLANLKPRNMRGIKS 163
Cdd:COG0073    35 FEKVGGLDGLRVGKVLEAEPHPNADKLLVLQVDVGEE-TRQIVCGAPNVyagdKVPEALVGAQVPGVVNLKPRKIRGVES 113

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002264484 164 NGMLMAASD----ASHENveLLTPPEGSVPG 190
Cdd:COG0073   114 EGMLCSAEElglgEDHDG--ILELPEDAPPG 142
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 95-193 2.90e-21

tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.


Pssm-ID: 239197 [Multi-domain]  Cd Length: 107  Bit Score: 85.37  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEA-DTLYVEEVDVGEEQPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASDA 173
Cdd:cd02798     9 VDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLGADDE 88

                          90       100
                  ....*....|....*....|
gi 1002264484 174 ShENVELLTPPEGSVPGERV 193
Cdd:cd02798    89 G-GEVVLLVPDREVPNGAKV 107
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 97-172 1.31e-12

tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.


Pssm-ID: 239196 [Multi-domain]  Cd Length: 103  Bit Score: 62.53  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  97 IRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNyLPIDQLqdsnVIV------LAN---LKPRNMRGIKSNGML 167
Cdd:cd02796     1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPN-VRAGDK----VVValpgavLPGglkIKKRKLRGVESEGML 75


                  ....*
gi 1002264484 168 MAASD 172
Cdd:cd02796    76 CSAKE 80
PRK10089 PRK10089
chaperone CsaA;
95-193 1.38e-12

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 62.54  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADTL-YVEEVDVGEE-QPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASD 172
Cdd:PRK10089   12 VDIRVGTIVEAEPFPEARKPaYKLWIDFGEEiGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVLGFED 91

                          90       100
                  ....*....|....*....|.
gi 1002264484 173 AShENVELLTPPEGSVPGERV 193
Cdd:PRK10089   92 ED-GEVVLLTPDRPVPNGVKL 111
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 88-199 2.99e-11

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 63.27  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  88 VEEVAALLD-IRVGRVVKAWRHPEADTLYVEEVDVGEEqPRTICSGlvnylpidqlqDSNV-----IVLAN--------- 152
Cdd:PRK00629   35 VEDVAAGLSgVVVGKVLECEKHPNADKLRVCQVDVGEE-PLQIVCG-----------APNVragdkVPVALpgavlpggf 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002264484 153 -LKPRNMRGIKSNGMLMAAS----DASHENVELLtpPEGSVPGE--RVWFGTED 199
Cdd:PRK00629  103 kIKKAKLRGVESEGMLCSASelglSDDHDGIIEL--PEDAPVGTdaREYLGLDD 154
chap_CsaA TIGR02222
export-related chaperone protein CsaA; This model describes Bacillus subtilis CsaA, an ...
 95-193 1.49e-07

export-related chaperone protein CsaA; This model describes Bacillus subtilis CsaA, an export-related chaperone that interacts with the Sec system, and related proteins from a number of other bacteria and archaea. The crystal structure is known for the homodimer from Thermus thermophilus. [Protein fate, Protein folding and stabilization, Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131277 [Multi-domain]  Cd Length: 107  Bit Score: 48.57  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  95 LDIRVGRVVKAWRHPEADT-LYVEEVDVGEE-QPRTICSGLVNYLPIDQLQDSNVIVLANLKPRNMRGIKSNGMLMAASD 172
Cdd:TIGR02222   7 LDLRVGRIVRAEPFPEARKpAYKLWVDFGTEiGVKQSSAQITKLYKPEDLIGRLVVAVVNFPPKQIAGFLSEVLVLGVID 86

                          90       100
                  ....*....|....*....|.
gi 1002264484 173 aSHENVELLTPPEGSVPGERV 193
Cdd:TIGR02222  87 -EQGRVVLLQPDRPVPNGTKI 106
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 85-199 2.59e-03

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


Pssm-ID: 439842 [Multi-domain]  Cd Length: 793  Bit Score: 38.99  E-value: 2.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002264484  85 VPPVEEVAALLDIRVGRVVKAWRHPEADTLYVEEVDVGEEQPRTICSGLVNYLPIDqlqdsnVIVLA----------NLK 154
Cdd:COG0072    33 EEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVGV------VVVAApggavlpggfKIK 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002264484 155 PRNMRGIKSNGMLMAA-----SDASHENVELL--TPPEGSVpgeRVWFGTED 199
Cdd:COG0072   107 KAKIRGVESSGMLCSEeelglGEDHDGIIVLPpdAPVGGDA---REYLGLDD 155
 
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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