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Protein

Probable arginine--tRNA ligase, cytoplasmic

Gene

mrs1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.By similarity

Catalytic activityi

ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

GO - Molecular functioni

  1. arginine-tRNA ligase activity Source: GO_Central
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. arginyl-tRNA aminoacylation Source: GO_Central
  2. mitochondrial translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
Alternative name(s):
Arginyl-tRNA synthetase
Short name:
ArgRS
Gene namesi
Name:mrs1
Synonyms:rrs1
ORF Names:SPBC25B2.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC25B2.09c.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. cytosol Source: PomBase
  3. mitochondrion Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 618618Probable arginine--tRNA ligase, cytoplasmicPRO_0000151663Add
BLAST

Proteomic databases

MaxQBiO74781.
PaxDbiO74781.

Interactioni

Protein-protein interaction databases

BioGridi277075. 2 interactions.
MINTiMINT-4680727.
STRINGi4896.SPBC25B2.09c-1.

Structurei

3D structure databases

ProteinModelPortaliO74781.
SMRiO74781. Positions 10-618.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi149 – 16012"HIGH" regionAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0018.
HOGENOMiHOG000247211.
InParanoidiO74781.
KOiK01887.
OMAiACNKNEP.
OrthoDBiEOG7NKKV8.
PhylomeDBiO74781.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74781-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATSVDQISK SLSTLGLQDL PVFREADIHH NPVDVYRSYI SSELSKINGV
60 70 80 90 100
DVSLIYPALE TSISKDSADL NLPVPRLRVK GKPQELAQKW AEAFPKDLVE
110 120 130 140 150
VTANGIFLRF NFNGPSLTKL ILPIIWEQRE NYGRNESGSG KVAVIEFSSP
160 170 180 190 200
NIAKPFHAGH LRSTIIGSFL ANLHESQGWK VHRVNYLGDW GKQFGLLAIG
210 220 230 240 250
YKKYGDEDQL KSNPIRHLYD VYVKVNADAT EEDEKIQKDK AEAESKGLPY
260 270 280 290 300
TPPLSLHDKA REFFKRMEDG DEESLKVWAR FRDLSITKLK DTYDRLNIHY
310 320 330 340 350
DEYDGESQVS LELMNKMVDE LRSLNLIEED GGALLIDLSK HDKKLGKAIV
360 370 380 390 400
QKRDGTTLYL TRDIGTAYKR YEKYKFDKSI YVVSSQQDMY FSQLFKIFEL
410 420 430 440 450
MGFDWAKKCV HINYGLVQGM STRKGKAVFL DDIMEVAKEE MHKVMQKNEE
460 470 480 490 500
KYAQVENPEE VADIVGKTAI RIQDSTGKRI NNYAFDWSRM TSFEGDTGPY
510 520 530 540 550
LQYAHSRLSS VRRNVNYTDE EIMGANLELL TEPDAYDLVR LLGQYPDVLK
560 570 580 590 600
NAFRFQETST VVTYLFKLTH AVSKLYDILW VRGRERDIQL ARLALFGAAK
610
QVLNNGMTLL GLTPLERM
Length:618
Mass (Da):70,689
Last modified:November 1, 1998 - v1
Checksum:i69BDECEA3B2853F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3591Y → S in BAA13762. (PubMed:9501991)Curated
Sequence conflicti401 – 4011M → T in BAA13762. (PubMed:9501991)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21267.1.
D89099 mRNA. Translation: BAA13762.1.
PIRiT39985.
T42007.
RefSeqiNP_596077.1. NM_001021989.2.

Genome annotation databases

EnsemblFungiiSPBC25B2.09c.1; SPBC25B2.09c.1:pep; SPBC25B2.09c.
GeneIDi2540548.
KEGGispo:SPBC25B2.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21267.1.
D89099 mRNA. Translation: BAA13762.1.
PIRiT39985.
T42007.
RefSeqiNP_596077.1. NM_001021989.2.

3D structure databases

ProteinModelPortaliO74781.
SMRiO74781. Positions 10-618.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277075. 2 interactions.
MINTiMINT-4680727.
STRINGi4896.SPBC25B2.09c-1.

Proteomic databases

MaxQBiO74781.
PaxDbiO74781.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC25B2.09c.1; SPBC25B2.09c.1:pep; SPBC25B2.09c.
GeneIDi2540548.
KEGGispo:SPBC25B2.09c.

Organism-specific databases

PomBaseiSPBC25B2.09c.

Phylogenomic databases

eggNOGiCOG0018.
HOGENOMiHOG000247211.
InParanoidiO74781.
KOiK01887.
OMAiACNKNEP.
OrthoDBiEOG7NKKV8.
PhylomeDBiO74781.

Miscellaneous databases

NextBioi20801674.
PROiO74781.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.30.1360.70. 1 hit.
3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR001278. Arg-tRNA-ligase.
IPR005148. Arg-tRNA-synth_N.
IPR008909. DALR_anticod-bd.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR11956. PTHR11956. 1 hit.
PfamiPF05746. DALR_1. 1 hit.
PF00750. tRNA-synt_1d. 1 hit.
[Graphical view]
PRINTSiPR01038. TRNASYNTHARG.
SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
SM00836. DALR_1. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF55190. SSF55190. 1 hit.
TIGRFAMsiTIGR00456. argS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-476.
    Strain: PR745.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYRC_SCHPO
AccessioniPrimary (citable) accession number: O74781
Secondary accession number(s): P78751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: November 1, 1998
Last modified: February 4, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.