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Conserved domains on  [gi|68051723|ref|NP_941077|]
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ferredoxin-fold anticodon-binding domain-containing protein 1 homolog [Mus musculus]

Protein Classification

ferredoxin-fold anticodon-binding domain-containing protein 1( domain architecture ID 13767249)

ferredoxin-fold anticodon-binding domain-containing protein 1 contains a DUF2431 domain that belongs to the class I SAM-dependent methyltransferase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BMT5-like pfam10354
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
 7-176 1.24e-61

rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.


:

Pssm-ID: 463056  Cd Length: 162  Bit Score: 201.61  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723     7 LLVGEGNFSFAASLIDGLDPsvsVTATGFQHRAALEGD-PVALENLKRLRERGVEVRFGVDCTQLSHALPADDRDFDRIY 85
Cdd:pfam10354   1 LLVGEGDFSFSLSLAENHGP---LTATSLDSEEELLEKyPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723    86 FNFPHCGRKA-----GVAKNRELLAKFFQSCADVLAKAGEVHVTLCRGQGgtpadkpqrewHNSWQVVAMAALGGFILSD 160
Cdd:pfam10354  78 FNFPHVGGKSkdqdrNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEP-----------YDSWNIEDLAKEAGLVLIR 146

                         170
                  ....*....|....*.
gi 68051723   161 VCPFSCEAVPGYKCTG 176
Cdd:pfam10354 147 SFKFDASDYPGYHHKR 162
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
 489-622 2.40e-30

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 123.34  E-value: 2.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723  489 LDLLVMLAYGISDWRILWTFDNRFLKRFAPGKI-EHFKSYSLYPPCYvHDVSFWVDEkkAFDELEFHTVARAVSQDTVVS 567
Cdd:PLN02788 271 LERLAMVLFDIPDIRLFWSDDERFTSQFKEGQLgVKFKPYSKYPPCY-KDISFWISD--EFTENNLCEVVRGIAGDLVEE 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68051723  568 VQYRDRFQHPETRQVSLCYRLTYQTCDKALTPQLAAAMQSQFRKEIQRQLHVSPR 622
Cdd:PLN02788 348 VKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
 
Name Accession Description Interval E-value
BMT5-like pfam10354
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
 7-176 1.24e-61

rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.


Pssm-ID: 463056  Cd Length: 162  Bit Score: 201.61  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723     7 LLVGEGNFSFAASLIDGLDPsvsVTATGFQHRAALEGD-PVALENLKRLRERGVEVRFGVDCTQLSHALPADDRDFDRIY 85
Cdd:pfam10354   1 LLVGEGDFSFSLSLAENHGP---LTATSLDSEEELLEKyPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723    86 FNFPHCGRKA-----GVAKNRELLAKFFQSCADVLAKAGEVHVTLCRGQGgtpadkpqrewHNSWQVVAMAALGGFILSD 160
Cdd:pfam10354  78 FNFPHVGGKSkdqdrNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEP-----------YDSWNIEDLAKEAGLVLIR 146

                         170
                  ....*....|....*.
gi 68051723   161 VCPFSCEAVPGYKCTG 176
Cdd:pfam10354 147 SFKFDASDYPGYHHKR 162
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 489-622 2.40e-30

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 123.34  E-value: 2.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723  489 LDLLVMLAYGISDWRILWTFDNRFLKRFAPGKI-EHFKSYSLYPPCYvHDVSFWVDEkkAFDELEFHTVARAVSQDTVVS 567
Cdd:PLN02788 271 LERLAMVLFDIPDIRLFWSDDERFTSQFKEGQLgVKFKPYSKYPPCY-KDISFWISD--EFTENNLCEVVRGIAGDLVEE 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68051723  568 VQYRDRFQHPETRQVSLCYRLTYQTCDKALTPQLAAAMQSQFRKEIQRQLHVSPR 622
Cdd:PLN02788 348 VKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 487-613 8.37e-22

phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129561 [Multi-domain]  Cd Length: 460  Bit Score: 98.61  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723   487 INLDLLVMLAYGISDWRILWTFDNRFLKRFAPGK---IEHFKSYSLYPPCYvHDVSFWVDEKK----AFDELEFHTVARA 559
Cdd:TIGR00469 320 LGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDlhlIPKFKPISHHPGCF-NDLAFWLPEDIeddaGFHENDFMDIIRN 398

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68051723   560 VSQDTVVSVQYRDRFQHPETRQVSLCYRLTYQTCDKALT--------PQLAAAMQSQFRKEI 613
Cdd:TIGR00469 399 IAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTnaevneihDMIASALVDEFNVEI 460
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 528-622 7.30e-21

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 87.48  E-value: 7.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723    528 SLYPPCYvHDVSFWVDEKkaFDELEFHTVARAVSQDTVVSVQYRDRFQH-PETRQVSLCYRLTYQTCDKALTPQLAAAMQ 606
Cdd:smart00896   1 SKFPAVR-RDLAFVVDED--VPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIH 77

                           90
                   ....*....|....*.
gi 68051723    607 SQFRKEIQRQLHVSPR 622
Cdd:smart00896  78 DKIVAALEKKFGAELR 93
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 528-622 7.75e-18

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold.


Pssm-ID: 460826 [Multi-domain]  Cd Length: 94  Bit Score: 78.68  E-value: 7.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723   528 SLYPPCYVhDVSFWVDEKKAFDELEfhTVARAVSQDTVVSVQYRDRFQHP--ETRQVSLCYRLTYQTCDKALTPQLAAAM 605
Cdd:pfam03147   1 SKYPAVRR-DLAFVVDEDVPAADIL--KAIREAGGELLESVELFDVYRGEkiPEGKKSLAFRLTFQSPERTLTDEEVNAI 77

                          90
                  ....*....|....*..
gi 68051723   606 QSQFRKEIQRQLHVSPR 622
Cdd:pfam03147  78 IEKIVEALEKKFGAELR 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-125 4.27e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.41  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723  40 ALEGDPVALENLKRLRERGVEVRFGVDCTQLSHALPADDRDFDRIYFNFPHCGRKagvaknrELLAKFFQSCADVLAKAG 119
Cdd:cd02440  26 GVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV-------EDLARFLEEARRLLKPGG 98


                ....*.
gi 68051723 120 EVHVTL 125
Cdd:cd02440  99 VLVLTL 104
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 517-622 9.70e-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: 9.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723 517 APGKIEHFKSYSLYPPcyVH-DVSFWVDEKKAFDELEfhTVARAVSQDTVVSVQYRDRFQH---PETRQvSLCYRLTYQT 592
Cdd:COG0072 688 LARKVPKYKPISKFPA--VRrDLALVVDEDVPAADVL--DAIRKAAGKLLEDVRLFDVYEGkgvPEGKK-SLAFSLTLQD 762

                        90       100       110
                ....*....|....*....|....*....|
gi 68051723 593 CDKALTPQLAAAMQSQFRKEIQRQLHVSPR 622
Cdd:COG0072 763 PDRTLTDEEIDAAMDKIVAALEKKFGAELR 792
 
Name Accession Description Interval E-value
BMT5-like pfam10354
rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in ...
 7-176 1.24e-61

rRNA (uridine-N3-)-methyltransferase BTM5-like; This is the N-terminal domain found in proteins from plants, yeast and humans, including 25S rRNA (uridine-N(3))-methyltransferase BMT5 from S. cerevisiae and the poorly characterized Ferredoxin-fold anticodon-binding domain-containing protein 1 from human and Heavy metal-associated isoprenylated plant protein 41 from Arabidopsis. This domain has a characteriztic Rossmann-like fold of S-adenosyl-L-methionine (SAM) binding domains. BTM5 is a SAM-dependent methyltransferase that specifically methylates the N3 position of uridine in 25S rRNA.


Pssm-ID: 463056  Cd Length: 162  Bit Score: 201.61  E-value: 1.24e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723     7 LLVGEGNFSFAASLIDGLDPsvsVTATGFQHRAALEGD-PVALENLKRLRERGVEVRFGVDCTQLSHALPADDRDFDRIY 85
Cdd:pfam10354   1 LLVGEGDFSFSLSLAENHGP---LTATSLDSEEELLEKyPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723    86 FNFPHCGRKA-----GVAKNRELLAKFFQSCADVLAKAGEVHVTLCRGQGgtpadkpqrewHNSWQVVAMAALGGFILSD 160
Cdd:pfam10354  78 FNFPHVGGKSkdqdrNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEP-----------YDSWNIEDLAKEAGLVLIR 146

                         170
                  ....*....|....*.
gi 68051723   161 VCPFSCEAVPGYKCTG 176
Cdd:pfam10354 147 SFKFDASDYPGYHHKR 162
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 489-622 2.40e-30

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 123.34  E-value: 2.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723  489 LDLLVMLAYGISDWRILWTFDNRFLKRFAPGKI-EHFKSYSLYPPCYvHDVSFWVDEkkAFDELEFHTVARAVSQDTVVS 567
Cdd:PLN02788 271 LERLAMVLFDIPDIRLFWSDDERFTSQFKEGQLgVKFKPYSKYPPCY-KDISFWISD--EFTENNLCEVVRGIAGDLVEE 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 68051723  568 VQYRDRFQHPETRQVSLCYRLTYQTCDKALTPQLAAAMQSQFRKEIQRQLHVSPR 622
Cdd:PLN02788 348 VKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 487-613 8.37e-22

phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA synthetases, the mitochondrial form demonstrated from yeast is monomeric. It is similar to but longer than the alpha subunit (PheS) of the alpha 2 beta 2 form found in Bacteria, Archaea, and eukaryotes, and shares the characteristic motifs of class II aminoacyl-tRNA ligases. This model models the experimental example from Saccharomyces cerevisiae (designated MSF1) and its orthologs from other eukaryotic species. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 129561 [Multi-domain]  Cd Length: 460  Bit Score: 98.61  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723   487 INLDLLVMLAYGISDWRILWTFDNRFLKRFAPGK---IEHFKSYSLYPPCYvHDVSFWVDEKK----AFDELEFHTVARA 559
Cdd:TIGR00469 320 LGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDlhlIPKFKPISHHPGCF-NDLAFWLPEDIeddaGFHENDFMDIIRN 398

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 68051723   560 VSQDTVVSVQYRDRFQHPETRQVSLCYRLTYQTCDKALT--------PQLAAAMQSQFRKEI 613
Cdd:TIGR00469 399 IAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTnaevneihDMIASALVDEFNVEI 460
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 528-622 7.30e-21

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold, consisting of an alpha+beta sandwich with anti-parallel beta-sheets (beta-alpha-beta x2).


Pssm-ID: 214893 [Multi-domain]  Cd Length: 93  Bit Score: 87.48  E-value: 7.30e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723    528 SLYPPCYvHDVSFWVDEKkaFDELEFHTVARAVSQDTVVSVQYRDRFQH-PETRQVSLCYRLTYQTCDKALTPQLAAAMQ 606
Cdd:smart00896   1 SKFPAVR-RDLAFVVDED--VPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIH 77

                           90
                   ....*....|....*.
gi 68051723    607 SQFRKEIQRQLHVSPR 622
Cdd:smart00896  78 DKIVAALEKKFGAELR 93
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 528-622 7.75e-18

Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold.


Pssm-ID: 460826 [Multi-domain]  Cd Length: 94  Bit Score: 78.68  E-value: 7.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723   528 SLYPPCYVhDVSFWVDEKKAFDELEfhTVARAVSQDTVVSVQYRDRFQHP--ETRQVSLCYRLTYQTCDKALTPQLAAAM 605
Cdd:pfam03147   1 SKYPAVRR-DLAFVVDEDVPAADIL--KAIREAGGELLESVELFDVYRGEkiPEGKKSLAFRLTFQSPERTLTDEEVNAI 77

                          90
                  ....*....|....*..
gi 68051723   606 QSQFRKEIQRQLHVSPR 622
Cdd:pfam03147  78 IEKIVEALEKKFGAELR 94
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 520-622 2.41e-03

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 40.92  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723  520 KIEHFKSYSLYPPcyVH-DVSFWVDEKKAFDELEfhTVARAVSQDTVVSVQYRDRFQ--HPETRQVSLCYRLTYQTCDKA 596
Cdd:PRK00629 689 KLPKYKPISKFPA--VRrDLALVVDEDVPAADIL--KAIKKAGGKLLESVELFDVYEgkGIGEGKKSLAFRLTFQDPDRT 764

                         90       100
                 ....*....|....*....|....*.
gi 68051723  597 LTPQLAAAMQSQFRKEIQRQLHVSPR 622
Cdd:PRK00629 765 LTDEEINAAMDKIVAALEEKFGAELR 790
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 40-125 4.27e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.41  E-value: 4.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723  40 ALEGDPVALENLKRLRERGVEVRFGVDCTQLSHALPADDRDFDRIYFNFPHCGRKagvaknrELLAKFFQSCADVLAKAG 119
Cdd:cd02440  26 GVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV-------EDLARFLEEARRLLKPGG 98


                ....*.
gi 68051723 120 EVHVTL 125
Cdd:cd02440  99 VLVLTL 104
PheT COG0072
Phenylalanyl-tRNA synthetase beta subunit [Translation, ribosomal structure and biogenesis]; ...
 517-622 9.70e-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: 9.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 68051723 517 APGKIEHFKSYSLYPPcyVH-DVSFWVDEKKAFDELEfhTVARAVSQDTVVSVQYRDRFQH---PETRQvSLCYRLTYQT 592
Cdd:COG0072 688 LARKVPKYKPISKFPA--VRrDLALVVDEDVPAADVL--DAIRKAAGKLLEDVRLFDVYEGkgvPEGKK-SLAFSLTLQD 762

                        90       100       110
                ....*....|....*....|....*....|
gi 68051723 593 CDKALTPQLAAAMQSQFRKEIQRQLHVSPR 622
Cdd:COG0072 763 PDRTLTDEEIDAAMDKIVAALEKKFGAELR 792
 
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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