A5DVN7 (A5DVN7_LODEL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Arginyl-tRNA synthetase EMBL EDK43245.1

Gene names

ORF Names:

LELG_01423 EMBL EDK43245.1

Organism

Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) [Complete proteome]

Taxonomic identifier

379508 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Debaryomycetaceae › Lodderomyces

Protein attributes

Sequence length	672 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. RuleBase RU003489

Ontologies

Keywords
Biological process	Protein biosynthesis RuleBase RU003489
Ligand	ATP-binding RuleBase RU003489 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase RuleBase RU003489 EMBL EDK43245.1 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW arginine-tRNA ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	A5DVN7 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: DBD421BDDD789D48	FASTA	672	77,298
	10 20 30 40 50 60 MQILKRTVSK PSAFFSLNLI KVSLTNLLIP LYRHHHCYYH HQHNIKSFSR TMSVSAISDE 70 80 90 100 110 120 LKKLGLSQPD PVKESLPEYN IVDVFKNYIT DELHRITEAD KSIIFDALDT PKVLDQGDII 130 140 150 160 170 180 VALPRLRIKG IKPNEKSQEW AEQFNKGKFI SEARPQGVFI QFFFNRSLVY DLVIKDVLKR 190 200 210 220 230 240 KTEYGYLPLG VGKKAIVEFS SPNIAKPFHA GHLRSTIIGG FISNLYEKLG WEVVRINYLG 250 260 270 280 290 300 DWGKQFGLLA VGFEKYGSEE QLAKDPINHL FEVYVKVNND VREEASEATG EPAVADAADA 310 320 330 340 350 360 DEKKVQASST NEKARQFFRR MEDGDESALK IWRRFRDLSI DKYIDTYARL NIKYDYYSGE 370 380 390 400 410 420 SQVPQEKMKE ATKLFEDKGL VHVDRGAKLI DLTKFNKKLG KALVEKSDGT SLYLTRDVGE 430 440 450 460 470 480 AIKRYETYKF DKMIYVIASQ QDLHCQQFFE ILKQMGFEWA KNLEHINFGM VQGMSTRKGN 490 500 510 520 530 540 VVFLDNILQE TKEKMHDVMK KNADKYAQIE EPDKIAELVG ISAVMIQDFQ SKRILNYEFK 550 560 570 580 590 600 WDRMTSFEGD TGPYLQYAHS RLSSMQRKSD ISEEELENAN FDLLTEPCAA NLVRTLLQYP 610 620 630 640 650 660 DIIRRASHNN EPSTIVTYLF TLCHIVSQCY DILWVAGQER EVATARLALY AATKQVIYNG 670 MTLLGLTPVE RM

References

[1]

"Evolution of pathogenicity and sexual reproduction in eight Candida genomes." Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S., Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I., Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C., Fitzpatrick D.A., de Groot P.W.J. , Harris D., Hoyer L.L., Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A. Nature 459:657-662(2009) [PubMed: 19465905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 11503 / CBS 2605 / IFO 1676 / JCM 1781 / NRRL YB-4239 and ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH981525 Genomic DNA. Translation: EDK43245.1.
RefSeq	XP_001526595.1. XM_001526545.1.
3D structure databases
ProteinModelPortal	A5DVN7.
SMR	A5DVN7. Positions 60-672.
ModBase	Search...
Protein-protein interaction databases
STRING	A5DVN7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5234647.
KEGG	lel:LELG_01423.
Phylogenomic databases
OMA	MQKNEEK.
OrthoDB	EOG4FR40V.
Family and domain databases
HAMAP	MF_00123. Arg_tRNA_synth. [Tree]
InterPro	IPR001412. aa-tRNA-synth_I_CS. IPR001278. Arg-tRNA-synth_Ia. IPR015945. Arg-tRNA-synth_Ia_core. IPR005148. Arg-tRNA-synth_N. IPR008909. DALR_anticod-bd. IPR014729. Rossmann-like_a/b/a_fold. IPR009080. tRNAsynth_1a_anticodon-bd. [Graphical view]
Gene3D	G3DSA:3.30.1360.70. Arg-tRNA-synth_Ic_N. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KO	K01887.
PANTHER	PTHR11956. Arg_tRNA-synt_1c. 1 hit.
Pfam	PF05746. DALR_1. 1 hit. PF00750. tRNA-synt_1d. 1 hit. [Graphical view]
PRINTS	PR01038. TRNASYNTHARG.
SMART	SM01016. Arg_tRNA_synt_N. 1 hit. SM00836. DALR_1. 1 hit. [Graphical view]
SUPFAM	SSF55190. Arg-tRNA-synth_Ic_N. 1 hit. SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMs	TIGR00456. ArgS. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A5DVN7_LODEL

Accession

Primary (citable) accession number: A5DVN7

Entry history

Integrated into UniProtKB/TrEMBL:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	January 25, 2012
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)