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Conserved domains on  [gi|149274610|ref|NP_612387|]
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ferredoxin-fold anticodon-binding domain-containing protein 1 [Homo sapiens]

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 3.96e-53

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: 179.27  E-value: 3.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610    7 LLVGEGNFSFAAALSEtldQSTQLTATCLQRPAELARD-PLAWENLQCLRERGIDVRFGVDCTQLADVFELHEREFDQIY 85
Cdd:pfam10354   1 LLVGEGDFSFSLSLAE---NHGPLTATSLDSEEELLEKyPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610   86 FIFPHCGRKA-----GVAKNRELLAKFFQSCADVLAEEGEVHVALCRGQGgtpadkpqrewHNSWQVVAMAALGGLILSD 160
Cdd:pfam10354  78 FNFPHVGGKSkdqdrNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEP-----------YDSWNIEDLAKEAGLVLIR 146

                         170
                  ....*....|....*.
gi 149274610  161 VYPFSCKAVAGYKCTG 176
Cdd:pfam10354 147 SFKFDASDYPGYHHKR 162
PLN02788 super family cl33567
phenylalanine-tRNA synthetase
 491-624 3.83e-28

phenylalanine-tRNA synthetase


The actual alignment was detected with superfamily member PLN02788:

Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 116.79  E-value: 3.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610 491 LDLLAMLVWCISDWRMLWTFDNRFLKNFVPGKIEP-FKSHSLYPPCYvHDVSFWIDqkKGFDELEFHTVARAVSQDTIIS 569
Cdd:PLN02788 271 LERLAMVLFDIPDIRLFWSDDERFTSQFKEGQLGVkFKPYSKYPPCY-KDISFWIS--DEFTENNLCEVVRGIAGDLVEE 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149274610 570 IQFLSRFQHPKTQQVSLCYRLTYQTCDKALTQQQVASMQSQFRKEIQQHLYVIPR 624
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 3.96e-53

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: 179.27  E-value: 3.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610    7 LLVGEGNFSFAAALSEtldQSTQLTATCLQRPAELARD-PLAWENLQCLRERGIDVRFGVDCTQLADVFELHEREFDQIY 85
Cdd:pfam10354   1 LLVGEGDFSFSLSLAE---NHGPLTATSLDSEEELLEKyPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610   86 FIFPHCGRKA-----GVAKNRELLAKFFQSCADVLAEEGEVHVALCRGQGgtpadkpqrewHNSWQVVAMAALGGLILSD 160
Cdd:pfam10354  78 FNFPHVGGKSkdqdrNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEP-----------YDSWNIEDLAKEAGLVLIR 146

                         170
                  ....*....|....*.
gi 149274610  161 VYPFSCKAVAGYKCTG 176
Cdd:pfam10354 147 SFKFDASDYPGYHHKR 162
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 491-624 3.83e-28

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 116.79  E-value: 3.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610 491 LDLLAMLVWCISDWRMLWTFDNRFLKNFVPGKIEP-FKSHSLYPPCYvHDVSFWIDqkKGFDELEFHTVARAVSQDTIIS 569
Cdd:PLN02788 271 LERLAMVLFDIPDIRLFWSDDERFTSQFKEGQLGVkFKPYSKYPPCY-KDISFWIS--DEFTENNLCEVVRGIAGDLVEE 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149274610 570 IQFLSRFQHPKTQQVSLCYRLTYQTCDKALTQQQVASMQSQFRKEIQQHLYVIPR 624
Cdd:PLN02788 348 VKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 489-610 3.96e-24

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: 105.93  E-value: 3.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610  489 MNLDLLAMLVWCISDWRMLWTFDNRFLKNFVPGK---IEPFKSHSLYPPCYvHDVSFWIDQKK----GFDELEFHTVARA 561
Cdd:TIGR00469 320 LGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDlhlIPKFKPISHHPGCF-NDLAFWLPEDIeddaGFHENDFMDIIRN 398

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 149274610  562 VSQDTIISIQFLSRFQHPKTQQVSLCYRLTYQTCDKALTQQQVASMQSQ 610
Cdd:TIGR00469 399 IAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDM 447
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 530-624 5.03e-20

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: 84.78  E-value: 5.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610   530 SLYPPCYvHDVSFWIDqkKGFDELEFHTVARAVSQDTIISIQFLSRFQH-PKTQQVSLCYRLTYQTCDKALTQQQVASMQ 608
Cdd:smart00896   1 SKFPAVR-RDLAFVVD--EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIH 77

                           90
                   ....*....|....*.
gi 149274610   609 SQFRKEIQQHLYVIPR 624
Cdd:smart00896  78 DKIVAALEKKFGAELR 93
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 530-624 8.44e-15

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: 70.20  E-value: 8.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610  530 SLYPPCYVhDVSFWIDQKKGFDELEfhTVARAVSQDTIISIQFLSRFQHPK--TQQVSLCYRLTYQTCDKALTQQQVASM 607
Cdd:pfam03147   1 SKYPAVRR-DLAFVVDEDVPAADIL--KAIREAGGELLESVELFDVYRGEKipEGKKSLAFRLTFQSPERTLTDEEVNAI 77

                          90
                  ....*....|....*..
gi 149274610  608 QSQFRKEIQQHLYVIPR 624
Cdd:pfam03147  78 IEKIVEALEKKFGAELR 94
 
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 3.96e-53

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: 179.27  E-value: 3.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610    7 LLVGEGNFSFAAALSEtldQSTQLTATCLQRPAELARD-PLAWENLQCLRERGIDVRFGVDCTQLADVFELHEREFDQIY 85
Cdd:pfam10354   1 LLVGEGDFSFSLSLAE---NHGPLTATSLDSEEELLEKyPNAEENLEELEELGVTVLFGVDATKLGLHPRLKGRRFDRII 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610   86 FIFPHCGRKA-----GVAKNRELLAKFFQSCADVLAEEGEVHVALCRGQGgtpadkpqrewHNSWQVVAMAALGGLILSD 160
Cdd:pfam10354  78 FNFPHVGGKSkdqdrNIRKNQELLLGFFKSAKELLKPGGEIHVTLFEGEP-----------YDSWNIEDLAKEAGLVLIR 146

                         170
                  ....*....|....*.
gi 149274610  161 VYPFSCKAVAGYKCTG 176
Cdd:pfam10354 147 SFKFDASDYPGYHHKR 162
PLN02788 PLN02788
phenylalanine-tRNA synthetase
 491-624 3.83e-28

phenylalanine-tRNA synthetase


Pssm-ID: 215422 [Multi-domain]  Cd Length: 402  Bit Score: 116.79  E-value: 3.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610 491 LDLLAMLVWCISDWRMLWTFDNRFLKNFVPGKIEP-FKSHSLYPPCYvHDVSFWIDqkKGFDELEFHTVARAVSQDTIIS 569
Cdd:PLN02788 271 LERLAMVLFDIPDIRLFWSDDERFTSQFKEGQLGVkFKPYSKYPPCY-KDISFWIS--DEFTENNLCEVVRGIAGDLVEE 347

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149274610 570 IQFLSRFQHPKTQQVSLCYRLTYQTCDKALTQQQVASMQSQFRKEIQQHLYVIPR 624
Cdd:PLN02788 348 VKLIDNFTNPKKGKTSHCYRIVYRSMERSLTDEEINALQDKVREEVQKKLGVELR 402
pheS_mito TIGR00469
phenylalanyl-tRNA synthetase, mitochondrial; Unlike all other known phenylalanyl-tRNA ...
 489-610 3.96e-24

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: 105.93  E-value: 3.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610  489 MNLDLLAMLVWCISDWRMLWTFDNRFLKNFVPGK---IEPFKSHSLYPPCYvHDVSFWIDQKK----GFDELEFHTVARA 561
Cdd:TIGR00469 320 LGLDRIAMLLFDIPDIRLFWSNDEGFLRQFSEGDlhlIPKFKPISHHPGCF-NDLAFWLPEDIeddaGFHENDFMDIIRN 398

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 149274610  562 VSQDTIISIQFLSRFQHPKTQQVSLCYRLTYQTCDKALTQQQVASMQSQ 610
Cdd:TIGR00469 399 IAGDLVEQIKLVDKFKHPKTGKKSMCFRINYQHMDRNLTNAEVNEIHDM 447
FDX-ACB smart00896
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 530-624 5.03e-20

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: 84.78  E-value: 5.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610   530 SLYPPCYvHDVSFWIDqkKGFDELEFHTVARAVSQDTIISIQFLSRFQH-PKTQQVSLCYRLTYQTCDKALTQQQVASMQ 608
Cdd:smart00896   1 SKFPAVR-RDLAFVVD--EDVPAAELLDAIREAGGDLLEDVRLFDVYEGgIPEGKKSLAYRLTYQSPDRTLTDEEVNAIH 77

                           90
                   ....*....|....*.
gi 149274610   609 SQFRKEIQQHLYVIPR 624
Cdd:smart00896  78 DKIVAALEKKFGAELR 93
FDX-ACB pfam03147
Ferredoxin-fold anticodon binding domain; This is the anticodon binding domain found in some ...
 530-624 8.44e-15

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: 70.20  E-value: 8.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149274610  530 SLYPPCYVhDVSFWIDQKKGFDELEfhTVARAVSQDTIISIQFLSRFQHPK--TQQVSLCYRLTYQTCDKALTQQQVASM 607
Cdd:pfam03147   1 SKYPAVRR-DLAFVVDEDVPAADIL--KAIREAGGELLESVELFDVYRGEKipEGKKSLAFRLTFQSPERTLTDEEVNAI 77

                          90
                  ....*....|....*..
gi 149274610  608 QSQFRKEIQQHLYVIPR 624
Cdd:pfam03147  78 IEKIVEALEKKFGAELR 94
 
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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