FRS2/YFL022C Protein Information

Standard Name	Frs2p
Systematic Name	Yfl022cp
ORF Classification	Verified
Description	Alpha subunit of cytoplasmic phenylalanyl-tRNA synthetase, forms a tetramer with Frs1p to form active enzyme; evolutionarily distant from mitochondrial phenylalanyl-tRNA synthetase based on protein sequence, but substrate binding is similar (1, 2)
Name Description	phenylalanyl (F)-tRNA Synthetase
Gene Product	cytoplasmic phenylalanyl-tRNA synthetase alpha subunit 1

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	503
Molecular Weight (Da)	57,511
Isoelectric Point (pI)	5.6

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Frs2p (InterPro)
Physical Interactions	There are 24 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000016831C \| P15625 MIPS: YFL022C NCBI: 1174509 \| 14318497 \| 172947 \| 836732 \| NP_116631.1 GenBank/EMBL/DDBJ: DAA12418.1 \| D50617 \| J03965
External Classifications	EC: 6.1.1.20 [Phenylalanine--tRNA ligase]

Amino Acid Sequence (or in FASTA format)
1 MSDFQLEILK KLDELDEIKS TLATFPQHGS QDVLSALNSL KAHNKLEFSK 51 VDTVTYDLTK EGAQILNEGS YEIKLVKLIQ ELGQLQIKDV MSKLGPQVGK 101 VGQARAFKNG WIAKNASNEL ELSAKLQNTD LNELTDETQS ILAQIKNNSH 151 LDSIDAKILN DLKKRKLIAQ GKITDFNVTK GPEFSTDLTK LETDLTSDMV 201 STNAYKDLKF KPYNFNSQGV QISSGALHPL NKVREEFRQI FFSMGFTEMP 251 SNQYVETGFW NFDALYVPQQ HPARDLQDTF YIKDPLTADL PDDKTYMDNI 301 KAVHEQGRFG SIGYRYNWKP EECQKLVLRT HSTAISARML HDLAKDPKPT 351 RLFSIDRVFR NEAVDATHLA EFHQVEGVLA DYNITLGDLI KFMEEFFERM 401 GVTGLRFKPT YNPYTEPSME IFSWHEGLQK WVEIGNSGMF RPEMLESMGL 451 PKDLRVLGWG LSLERPTMIK YKVQNIRELL GHKVSLDFIE TNPAARLDED 501 LYE*

Amino Acid Sequence (or in FASTA format)

       1  MSDFQLEILK KLDELDEIKS TLATFPQHGS QDVLSALNSL KAHNKLEFSK
      51  VDTVTYDLTK EGAQILNEGS YEIKLVKLIQ ELGQLQIKDV MSKLGPQVGK
     101  VGQARAFKNG WIAKNASNEL ELSAKLQNTD LNELTDETQS ILAQIKNNSH
     151  LDSIDAKILN DLKKRKLIAQ GKITDFNVTK GPEFSTDLTK LETDLTSDMV
     201  STNAYKDLKF KPYNFNSQGV QISSGALHPL NKVREEFRQI FFSMGFTEMP
     251  SNQYVETGFW NFDALYVPQQ HPARDLQDTF YIKDPLTADL PDDKTYMDNI
     301  KAVHEQGRFG SIGYRYNWKP EECQKLVLRT HSTAISARML HDLAKDPKPT
     351  RLFSIDRVFR NEAVDATHLA EFHQVEGVLA DYNITLGDLI KFMEEFFERM
     401  GVTGLRFKPT YNPYTEPSME IFSWHEGLQK WVEIGNSGMF RPEMLESMGL
     451  PKDLRVLGWG LSLERPTMIK YKVQNIRELL GHKVSLDFIE TNPAARLDED
     501  LYE*

external links for Frs2p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastGFP
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Frs2p

1)	Sanni A, et al. (1988) Structure and expression of the genes encoding the alpha and beta subunits of yeast phenylalanyl-tRNA synthetase. J Biol Chem 263(30):15407-15
2)	Aphasizhev R, et al. (1996) Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site. Biochemistry 35(1):117-23