SYC_SCHPO
ID SYC_SCHPO Reviewed; 754 AA.
AC Q09860;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN ORFNames=SPAC29E6.06c, SPAC30.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; Z66525; CAA91428.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB66469.1; -; Genomic_DNA.
DR PIR; T38507; S62512.
DR RefSeq; NP_594564.1; NM_001019993.2.
DR AlphaFoldDB; Q09860; -.
DR SMR; Q09860; -.
DR BioGRID; 279172; 3.
DR STRING; 4896.SPAC29E6.06c.1; -.
DR iPTMnet; Q09860; -.
DR MaxQB; Q09860; -.
DR PaxDb; Q09860; -.
DR PRIDE; Q09860; -.
DR EnsemblFungi; SPAC29E6.06c.1; SPAC29E6.06c.1:pep; SPAC29E6.06c.
DR GeneID; 2542721; -.
DR KEGG; spo:SPAC29E6.06c; -.
DR PomBase; SPAC29E6.06c; -.
DR VEuPathDB; FungiDB:SPAC29E6.06c; -.
DR eggNOG; KOG2007; Eukaryota.
DR HOGENOM; CLU_013528_3_1_1; -.
DR InParanoid; Q09860; -.
DR OMA; FHNDMKS; -.
DR PhylomeDB; Q09860; -.
DR PRO; PR:Q09860; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; ISS:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; ISS:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR CDD; cd00672; CysRS_core; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00435; cysS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..754
FT /note="Probable cysteine--tRNA ligase"
FT /id="PRO_0000159552"
FT REGION 664..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT MOTIF 408..412
FT /note="'KMSKS' region"
FT COMPBIAS 710..736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 754 AA; 85555 MW; 985E0301CC105358 CRC64;
MSTRNPAQSH WGVPKGQRTE LYVYNTLTHS KVPFVSNGSN LTWYCCGPTV YDASHMGHAR
NYVTTDILRR ILQSYFGYNI TFVQNVTDID DKIILRARQQ YLFEEYKKQQ GTNKSHSEAR
EKVTEAWFAY AKKNLPEPPS SMSEWPQWLA SHDIPTLAIN NPKLPMHVDA LKSALDALQV
SEASEIISLD GFWPKVQDVL VPLLDAELGS TVTDPAIFRK LAAYWEDDFN KDMANLNVLP
PTAVTRVSEY VPEIVDFVQR IIDRGYAYPV TDGSVYFDTE AFEKGGHFYA KLEPWNKGNR
ELIAEGEGSL AALTGKKRPG DFALWKASKP GEPSWDSPWS KGRPGWHIEC SVMASALLGS
NIDIHSGGID LAFPHHDNEL AQSEAYFDCP QWVNYFFHAG HLHIEGQKMS KSLKNFITIK
EILKKFTPRQ LRLAFLLQQW NTQLDFKETL LAYVLNIEQA LENFFRTVRA LMNETEGVSA
NGGHVPEKFD KLEIELLEKF QQTQQNTHLA LCDSFNTPLV MQHIDNLVTQ ANIYIREVGQ
QPCSRLLGQI ASWITSMLQI FGLDENGHPN AVGWSSSKGS SSENTDAMPY IRAVSSFRDR
VRELCIAKAS SQEILKACDI FRDYDMAALG VSFNDRPQGS ALVKLVDAEE LIAAREQKLE
EERAKQAKKA QAKAEQEKKQ VERVMKGKTS PSEMFKMFKE YLSFDEAGLP TKMRGEDGSE
IDVPKSRKKK LQKEYAQQEK LHKEYLSYIE SNKS
