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Conserved domains on  [gi|1365260312|ref|WP_106383917|]
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MULTISPECIES: YtpR family tRNA-binding protein [Streptococcus]

Protein Classification

DUF4479 and tRNA-binding domain-containing protein( domain architecture ID 10632253)

DUF4479 and tRNA-binding domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 96-200 1.53e-44

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: 143.80  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLKTIVALPGAMMPKGNLIFPGELRGEKSFGMMCSPRE 175
Cdd:cd02796     1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPNVRAGDKVVVALPGAVLPGGLKIKKRKLRGVESEGMLCSAKE 80

                          90       100
                  ....*....|....*....|....*
gi 1365260312 176 LQLPNapQKRGIIELASSEVVGTAF 200
Cdd:cd02796    81 LGLGE--DSDGIIELPEDAPVGTDI 103
DUF4479 pfam14794
Domain of unknown function (DUF4479); This domain family is found in bacteria, and is ...
 21-91 3.98e-28

Domain of unknown function (DUF4479); This domain family is found in bacteria, and is approximately 70 amino acids in length. The family is found in association with pfam01588.


:

Pssm-ID: 434215 [Multi-domain]  Cd Length: 71  Bit Score: 100.72  E-value: 3.98e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1365260312  21 GQGVKLAAERKGNVARIYRLDNGETVAWNIFQVSNLFNITERGQVFLTDEEISILNQELSQAGFEPELVND 91
Cdd:pfam14794   1 PDREEQTVERKGDVVRIFDEETGETVGYNIFNASSYLEIEGNGQVELTEEQVAKLNEALAKNGFEEELEVD 71
 
Name Accession Description Interval E-value
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 96-200 1.53e-44

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: 143.80  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLKTIVALPGAMMPKGNLIFPGELRGEKSFGMMCSPRE 175
Cdd:cd02796     1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPNVRAGDKVVVALPGAVLPGGLKIKKRKLRGVESEGMLCSAKE 80

                          90       100
                  ....*....|....*....|....*
gi 1365260312 176 LQLPNapQKRGIIELASSEVVGTAF 200
Cdd:cd02796    81 LGLGE--DSDGIIELPEDAPVGTDI 103
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 67-200 8.85e-40

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 144.16  E-value: 8.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  67 LTDEEISilnQELSQAGFEPELVNDLSP---KFVVGEIVKMVAHPDSDHLNICQVKVAaDKVVQIIAGAPNAKVGLKTIV 143
Cdd:PRK00629   16 ISSEELA---EALTMIGLEVEGVEDVAAglsGVVVGKVLECEKHPNADKLRVCQVDVG-EEPLQIVCGAPNVRAGDKVPV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1365260312 144 ALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNapQKRGIIELASSEVVGTAF 200
Cdd:PRK00629   92 ALPGAVLPGGFKIKKAKLRGVESEGMLCSASELGLSD--DHDGIIELPEDAPVGTDA 146
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 67-198 1.15e-33

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: 126.64  E-value: 1.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  67 LTDEEISILNQ---ELSQAGFEPELVNDLSPKF---VVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLK 140
Cdd:TIGR00472  11 YVPLSEIDNEEiaeALTSIGLEVEAVIPFSKPLkgvVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCGAPNVEAGKK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1365260312 141 TIVALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNapQKRGIIELASSEVVGT 198
Cdd:TIGR00472  91 VAVALPGAKLPNGLKIKKSKLRGVESEGMLCSESELGLDE--KSDGIIVLDEDAPLGT 146
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
65-201 1.46e-28

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 112.26  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  65 VFLTDEEISilnQELSQAGFEPELVNDLSP--KFVVGEIVKMVAHPDSDHLNICQVKVAaDKVVQIIAGAPNAKVGLKTI 142
Cdd:COG0073    14 LDLSPEELA---EKLTMAGIEVEDFEKVGGldGLRVGKVLEAEPHPNADKLLVLQVDVG-EETRQIVCGAPNVYAGDKVP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1365260312 143 VALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNAPQkrGIIELASSEVVGTAFD 201
Cdd:COG0073    90 EALVGAQVPGVVNLKPRKIRGVESEGMLCSAEELGLGEDHD--GILELPEDAPPGDDAE 146
DUF4479 pfam14794
Domain of unknown function (DUF4479); This domain family is found in bacteria, and is ...
 21-91 3.98e-28

Domain of unknown function (DUF4479); This domain family is found in bacteria, and is approximately 70 amino acids in length. The family is found in association with pfam01588.


Pssm-ID: 434215 [Multi-domain]  Cd Length: 71  Bit Score: 100.72  E-value: 3.98e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1365260312  21 GQGVKLAAERKGNVARIYRLDNGETVAWNIFQVSNLFNITERGQVFLTDEEISILNQELSQAGFEPELVND 91
Cdd:pfam14794   1 PDREEQTVERKGDVVRIFDEETGETVGYNIFNASSYLEIEGNGQVELTEEQVAKLNEALAKNGFEEELEVD 71
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 96-199 5.59e-13

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: 62.26  E-value: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLKtIVALPGAMMPKGNlifPGELRGEKSFGMMCSPRE 175
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEE-LVGRLVVVVANLK---PAKLRGVESEGMILSAEE 76

                          90       100
                  ....*....|....*....|....
gi 1365260312 176 LqlpnAPQKRGIIELASSEVVGTA 199
Cdd:pfam01588  77 L----DGGSVGLLEPPADVPPGTK 96
 
Name Accession Description Interval E-value
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 96-200 1.53e-44

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: 143.80  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLKTIVALPGAMMPKGNLIFPGELRGEKSFGMMCSPRE 175
Cdd:cd02796     1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPNVRAGDKVVVALPGAVLPGGLKIKKRKLRGVESEGMLCSAKE 80

                          90       100
                  ....*....|....*....|....*
gi 1365260312 176 LQLPNapQKRGIIELASSEVVGTAF 200
Cdd:cd02796    81 LGLGE--DSDGIIELPEDAPVGTDI 103
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 67-200 8.85e-40

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 144.16  E-value: 8.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  67 LTDEEISilnQELSQAGFEPELVNDLSP---KFVVGEIVKMVAHPDSDHLNICQVKVAaDKVVQIIAGAPNAKVGLKTIV 143
Cdd:PRK00629   16 ISSEELA---EALTMIGLEVEGVEDVAAglsGVVVGKVLECEKHPNADKLRVCQVDVG-EEPLQIVCGAPNVRAGDKVPV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1365260312 144 ALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNapQKRGIIELASSEVVGTAF 200
Cdd:PRK00629   92 ALPGAVLPGGFKIKKAKLRGVESEGMLCSASELGLSD--DHDGIIELPEDAPVGTDA 146
pheT_bact TIGR00472
phenylalanyl-tRNA synthetase, beta subunit, non-spirochete bacterial; Every known example of ...
 67-198 1.15e-33

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: 126.64  E-value: 1.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  67 LTDEEISILNQ---ELSQAGFEPELVNDLSPKF---VVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLK 140
Cdd:TIGR00472  11 YVPLSEIDNEEiaeALTSIGLEVEAVIPFSKPLkgvVVGKVLEVEPHPNADKLKVCKVDIGEKEMLQIVCGAPNVEAGKK 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1365260312 141 TIVALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNapQKRGIIELASSEVVGT 198
Cdd:TIGR00472  91 VAVALPGAKLPNGLKIKKSKLRGVESEGMLCSESELGLDE--KSDGIIVLDEDAPLGT 146
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
65-201 1.46e-28

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 112.26  E-value: 1.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  65 VFLTDEEISilnQELSQAGFEPELVNDLSP--KFVVGEIVKMVAHPDSDHLNICQVKVAaDKVVQIIAGAPNAKVGLKTI 142
Cdd:COG0073    14 LDLSPEELA---EKLTMAGIEVEDFEKVGGldGLRVGKVLEAEPHPNADKLLVLQVDVG-EETRQIVCGAPNVYAGDKVP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1365260312 143 VALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNAPQkrGIIELASSEVVGTAFD 201
Cdd:COG0073    90 EALVGAQVPGVVNLKPRKIRGVESEGMLCSAEELGLGEDHD--GILELPEDAPPGDDAE 146
DUF4479 pfam14794
Domain of unknown function (DUF4479); This domain family is found in bacteria, and is ...
 21-91 3.98e-28

Domain of unknown function (DUF4479); This domain family is found in bacteria, and is approximately 70 amino acids in length. The family is found in association with pfam01588.


Pssm-ID: 434215 [Multi-domain]  Cd Length: 71  Bit Score: 100.72  E-value: 3.98e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1365260312  21 GQGVKLAAERKGNVARIYRLDNGETVAWNIFQVSNLFNITERGQVFLTDEEISILNQELSQAGFEPELVND 91
Cdd:pfam14794   1 PDREEQTVERKGDVVRIFDEETGETVGYNIFNASSYLEIEGNGQVELTEEQVAKLNEALAKNGFEEELEVD 71
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 96-198 1.63e-24

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: 92.20  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNA-----KVGLKTIVALPgammpkgnlIFPGELRGEKSFGMM 170
Cdd:cd02153     1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVyppeeLVGKKVVVAVN---------LKPKKLRGVESEGML 71

                          90       100
                  ....*....|....*....|....*...
gi 1365260312 171 CSPRELQLPNapQKRGIIELASSEVVGT 198
Cdd:cd02153    72 LSAEELGLEE--GSVGILELPEDAPVGD 97
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 67-200 9.05e-18

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: 80.98  E-value: 9.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  67 LTDEEISILNQELSQAGFEPELVNDLSPKFVVGEIVKMV-----AHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLKT 141
Cdd:COG0072    11 LVEEAALLEELLLLLTGEGLEEEEVEGAAAVVVGVVVVVvvveePHPDADDLVVVVVDVGGGEVLVVVCGAANVAVGVVV 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1365260312 142 IVALPGAMMPKGNLIFPGELRGEKSFGMMCSPRELQLPNApqKRGIIELASSEVVGTAF 200
Cdd:COG0072    91 VAAPGGAVLPGGFKIKKAKIRGVESSGMLCSEEELGLGED--HDGIIVLPPDAPVGGDA 147
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 96-199 5.59e-13

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: 62.26  E-value: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGAPNAKVGLKtIVALPGAMMPKGNlifPGELRGEKSFGMMCSPRE 175
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEE-LVGRLVVVVANLK---PAKLRGVESEGMILSAEE 76

                          90       100
                  ....*....|....*....|....
gi 1365260312 176 LqlpnAPQKRGIIELASSEVVGTA 199
Cdd:pfam01588  77 L----DGGSVGLLEPPADVPPGTK 96
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 96-171 3.67e-05

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: 41.44  E-value: 3.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1365260312  96 FVVGEIVKMVAHPDSDHLNICQVKVAADKVVQIIAGApnakVGLKTIVALPGAMMPKGNLIFPGELRGEKSFGM-MC 171
Cdd:cd02799     8 IRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGL----VKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMvLC 80
 
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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