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Conserved domains on  [gi|15232216|ref|NP_191557|]
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Nucleic acid-binding, OB-fold-like protein [Arabidopsis thaliana]

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 ...
 104-208 3.54e-59

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: 183.58  E-value: 3.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 104 ETANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLA 183
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                        90       100
                ....*....|....*....|....*
gi 15232216 184 ASDAAHENVELLVPPEGSVPGDRVW 208
Cdd:cd02799  81 ASNADHEKVELLEPPEGAKPGERVT 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 ...
 104-208 3.54e-59

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: 183.58  E-value: 3.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 104 ETANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLA 183
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                        90       100
                ....*....|....*....|....*
gi 15232216 184 ASDAAHENVELLVPPEGSVPGDRVW 208
Cdd:cd02799  81 ASNADHEKVELLEPPEGAKPGERVT 105
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 75-273 2.19e-53

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 184.98  E-value: 2.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   75 TAAPDAGttvSADESEKKSESQKEEENVKE--TANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVP 152
Cdd:PLN02610 610 KALSDGG---KKKQGKKAGGGGKSKAAAEReiDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIP 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216  153 LDLLQGASVVVLANLKPRNMRGVKSCGMLLAASDAAHENVELLVPPEGSVPGDRV-WFGNEEDLEQLPEPappnkvqKKK 231
Cdd:PLN02610 687 LEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTKVELVEPPESAAVGERVtFPGFEGEPDDVLNP-------KKK 759

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15232216  232 MWELVQPLLKTDASGVSMLKEHLMRTSSGLVTSKSLRNANIS 273
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 111-206 7.64e-37

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: 126.20  E-value: 7.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   111 IKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLAASDAAHE 190
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*.
gi 15232216   191 NVELLVPPEGSVPGDR 206
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 85-207 1.34e-22

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: 90.18  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216    85 SADESEKKSESQKEEENVKETANL-----LDIKVGRIVKAWQHEEADSLYVEEVDIGEaEPRIICSGLVKYVPLDLLQGA 159
Cdd:TIGR00399  11 GAKKKEKKDEGEKALEPQKETITIddfekVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGK 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15232216   160 SVVVLANLKPRNMRGVKSCGMLLAASDAAhENVELLVPPEGSVPGDRV 207
Cdd:TIGR00399  90 KVIVVANLKPAKLFGVKSEGMILAAEDDG-KVLFLLSPDQEAIAGERI 136
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
98-215 7.78e-21

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 91.84  E-value: 7.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216  98 EEENVKETANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEaEPRIICSGLVKY-----VPLDLLqGASVVVLANLKPRNM 172
Cdd:COG0073  31 EVEDFEKVGGLDGLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGAPNVyagdkVPEALV-GAQVPGVVNLKPRKI 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15232216 173 RGVKSCGMLLAASDAAHENVE--LLVPPEGSVPG-DRVWFGNEEDL 215
Cdd:COG0073 109 RGVESEGMLCSAEELGLGEDHdgILELPEDAPPGdDAEYLLLLDDV 154
 
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 ...
 104-208 3.54e-59

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: 183.58  E-value: 3.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 104 ETANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLA 183
Cdd:cd02799   1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                        90       100
                ....*....|....*....|....*
gi 15232216 184 ASDAAHENVELLVPPEGSVPGDRVW 208
Cdd:cd02799  81 ASNADHEKVELLEPPEGAKPGERVT 105
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 75-273 2.19e-53

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 184.98  E-value: 2.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   75 TAAPDAGttvSADESEKKSESQKEEENVKE--TANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVP 152
Cdd:PLN02610 610 KALSDGG---KKKQGKKAGGGGKSKAAAEReiDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIP 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216  153 LDLLQGASVVVLANLKPRNMRGVKSCGMLLAASDAAHENVELLVPPEGSVPGDRV-WFGNEEDLEQLPEPappnkvqKKK 231
Cdd:PLN02610 687 LEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDHTKVELVEPPESAAVGERVtFPGFEGEPDDVLNP-------KKK 759

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15232216  232 MWELVQPLLKTDASGVSMLKEHLMRTSSGLVTSKSLRNANIS 273
Cdd:PLN02610 760 VWETLQPDLHTNSELVACYKDVPFTTSAGVCKVASIANGSIR 801
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 111-207 2.77e-40

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: 134.95  E-value: 2.77e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 111 IKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLAASD--AA 188
Cdd:cd02153   1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEElgLE 80

                        90
                ....*....|....*....
gi 15232216 189 HENVELLVPPEGSVPGDRV 207
Cdd:cd02153  81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 111-206 7.64e-37

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: 126.20  E-value: 7.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   111 IKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLAASDAAHE 190
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEELDGG 80

                          90
                  ....*....|....*.
gi 15232216   191 NVELLVPPEGSVPGDR 206
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 86-207 1.08e-28

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 114.48  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   86 ADESEKKSESQKEEENVKETANL-----LDIKVGRIVKAWQHEEADSLYVEEVDIGEaEPRIICSGLVKYVPLDLLQGAS 160
Cdd:PRK00133 548 AKAAAAAAAAPLAEEPIAETISFddfakVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIKSAYDPEELVGKL 626

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15232216  161 VVVLANLKPRNMR-GVkSCGMLLAASDAAhENVELLVPPEGSVPGDRV 207
Cdd:PRK00133 627 VVMVANLAPRKMKfGV-SEGMVLAAGPGG-GDLFLLEPDEGAKPGMRV 672
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 109-208 1.96e-26

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: 99.50  E-value: 1.96e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 109 LDIKVGRIVKAWQHEEADSLYVEEVDIGEaEPRIICSGLVKYVPLDLLQGASVVVLANLKPRNMRGVKSCGMLLAASDAa 188
Cdd:cd02800   9 VDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAAEDG- 86

                        90       100
                ....*....|....*....|
gi 15232216 189 hENVELLVPPEGSVPGDRVW 208
Cdd:cd02800  87 -GKLKLLTPDEEVEPGSRVS 105
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 87-207 4.49e-24

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 101.03  E-value: 4.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   87 DESEKKSESQKEEENVKETANL--------LDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQG 158
Cdd:PRK12267 521 EQMEGSAPKEPEEKEKKPEKPEitiddfdkVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVG 600

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 15232216  159 ASVVVLANLKPRNMRGVKSCGMLLAASDAahENVELLVPPEGSVPGDRV 207
Cdd:PRK12267 601 KKVVVVANLKPAKLMGEESQGMILAAEDD--GKLTLLTVDKEVPNGSKV 647
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 85-207 1.34e-22

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: 90.18  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216    85 SADESEKKSESQKEEENVKETANL-----LDIKVGRIVKAWQHEEADSLYVEEVDIGEaEPRIICSGLVKYVPLDLLQGA 159
Cdd:TIGR00399  11 GAKKKEKKDEGEKALEPQKETITIddfekVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGK 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 15232216   160 SVVVLANLKPRNMRGVKSCGMLLAASDAAhENVELLVPPEGSVPGDRV 207
Cdd:TIGR00399  90 KVIVVANLKPAKLFGVKSEGMILAAEDDG-KVLFLLSPDQEAIAGERI 136
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
98-215 7.78e-21

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 91.84  E-value: 7.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216  98 EEENVKETANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEaEPRIICSGLVKY-----VPLDLLqGASVVVLANLKPRNM 172
Cdd:COG0073  31 EVEDFEKVGGLDGLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGAPNVyagdkVPEALV-GAQVPGVVNLKPRKI 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15232216 173 RGVKSCGMLLAASDAAHENVE--LLVPPEGSVPG-DRVWFGNEEDL 215
Cdd:COG0073 109 RGVESEGMLCSAEELGLGEDHdgILELPEDAPPGdDAEYLLLLDDV 154
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 109-207 3.77e-18

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: 77.67  E-value: 3.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 109 LDIKVGRIVKAWQHEEA-DSLYVEEVDIGEAEPRIICSGLVK-YVPLDLLqGASVVVLANLKPRNMRGVKSCGMLLAASD 186
Cdd:cd02798   9 VDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKyYKPEELI-GRQVVAVVNFPPKQIAGVLSEVLVLGADD 87

                        90       100
                ....*....|....*....|.
gi 15232216 187 AAhENVELLVPPEGSVPGDRV 207
Cdd:cd02798  88 EG-GEVVLLVPDREVPNGAKV 107
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 98-186 2.78e-14

phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This model represents the subfamily that includes the beta subunit from Bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the amino end. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273097 [Multi-domain]  Cd Length: 797  Bit Score: 72.32  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216    98 EEENVKETANLLD-IKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLV-----KYVPLdLLQGAsvvVLAN---LK 168
Cdd:TIGR00472  32 EVEAVIPFSKPLKgVVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCGAPnveagKKVAV-ALPGA---KLPNglkIK 107

                          90
                  ....*....|....*...
gi 15232216   169 PRNMRGVKSCGMLLAASD 186
Cdd:TIGR00472 108 KSKLRGVESEGMLCSESE 125
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 98-205 7.83e-13

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 68.27  E-value: 7.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216   98 EEENVKETANLLD-IKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIIC------SGLvkYVPLDLLqGAsvvVLAN---L 167
Cdd:PRK00629  31 EVEGVEDVAAGLSgVVVGKVLECEKHPNADKLRVCQVDVGEEPLQIVCgapnvrAGD--KVPVALP-GA---VLPGgfkI 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15232216  168 KPRNMRGVKSCGMLLAAS----DAAHENVELLvpPEGSVPGD 205
Cdd:PRK00629 105 KKAKLRGVESEGMLCSASelglSDDHDGIIEL--PEDAPVGT 144
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 111-186 4.30e-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: 60.99  E-value: 4.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216 111 IKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSG-----LVKYVPLdLLQGAsvvVLAN---LKPRNMRGVKSCGMLL 182
Cdd:cd02796   1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGapnvrAGDKVVV-ALPGA---VLPGglkIKKRKLRGVESEGMLC 76


                ....
gi 15232216 183 AASD 186
Cdd:cd02796  77 SAKE 80
PRK10089 PRK10089
chaperone CsaA;
109-207 2.71e-11

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 59.07  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216  109 LDIKVGRIVKAWQHEEADSL-YVEEVDIGEaEPRIICSG--LVK-YVPLDLLqGASVVVLANLKPRNMRGVKSCGMLLAA 184
Cdd:PRK10089  12 VDIRVGTIVEAEPFPEARKPaYKLWIDFGE-EIGVKQSSaqITPhYTPEELI-GKQVVAVVNFPPKQIAGFMSEVLVLGF 89

                         90       100
                 ....*....|....*....|...
gi 15232216  185 SDAAhENVELLVPPEGSVPGDRV 207
Cdd:PRK10089  90 EDED-GEVVLLTPDRPVPNGVKL 111
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 98-210 1.12e-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: 40.15  E-value: 1.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232216  98 EEENVKETANLLDIKVGRIVKAWQHEEADSLYVEEVDIGEAEPRIICSGLVKYVPLDLLQGASVVVLAN----LKPRNMR 173
Cdd:COG0072  32 EEEVEGAAAVVVGVVVVVVVVEEPHPDADDLVVVVVDVGGGEVLVVVCGAANVAVGVVVVAAPGGAVLPggfkIKKAKIR 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15232216 174 GVKSCGMLLAA-----SDAAHENVELlvPPEGSVPGD-RVWFG 210
Cdd:COG0072 112 GVESSGMLCSEeelglGEDHDGIIVL--PPDAPVGGDaREYLG 152
 
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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