SYCM_MOUSE
ID SYCM_MOUSE Reviewed; 551 AA.
AC Q8BYM8; Q9D6U9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Probable cysteine--tRNA ligase, mitochondrial;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
DE Flags: Precursor;
GN Name=Cars2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30187.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK009937; BAB26596.1; -; mRNA.
DR EMBL; AK038968; BAC30187.1; ALT_INIT; mRNA.
DR RefSeq; NP_077210.1; NM_024248.1.
DR RefSeq; XP_006508956.1; XM_006508893.2.
DR AlphaFoldDB; Q8BYM8; -.
DR SMR; Q8BYM8; -.
DR BioGRID; 215045; 10.
DR STRING; 10090.ENSMUSP00000046453; -.
DR iPTMnet; Q8BYM8; -.
DR PhosphoSitePlus; Q8BYM8; -.
DR EPD; Q8BYM8; -.
DR MaxQB; Q8BYM8; -.
DR PaxDb; Q8BYM8; -.
DR PeptideAtlas; Q8BYM8; -.
DR PRIDE; Q8BYM8; -.
DR ProteomicsDB; 258787; -.
DR GeneID; 71941; -.
DR KEGG; mmu:71941; -.
DR UCSC; uc009kvh.2; mouse.
DR CTD; 79587; -.
DR MGI; MGI:1919191; Cars2.
DR eggNOG; KOG2007; Eukaryota.
DR InParanoid; Q8BYM8; -.
DR OrthoDB; 528822at2759; -.
DR PhylomeDB; Q8BYM8; -.
DR BioGRID-ORCS; 71941; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Cars2; mouse.
DR PRO; PR:Q8BYM8; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BYM8; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Metal-binding;
KW Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..551
FT /note="Probable cysteine--tRNA ligase, mitochondrial"
FT /id="PRO_0000250739"
FT MOTIF 65..75
FT /note="'HIGH' region"
FT MOTIF 302..306
FT /note="'KMSKS' region"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 203
FT /note="P -> PA (in Ref. 1; BAB26596)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="I -> T (in Ref. 1; BAB26596)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 551 AA; 61272 MW; E71AAB981EE23013 CRC64;
MLRARGPGPG ALLLRAALGL GRRGRSWQRP QGQDTGVQVH NSLTGRKEPL IVARSDAVSW
YSCGPTVYDH AHLGHACSYV RFDIIRRILT RVFGCNVVMA MSITDVDDKI IKRANEMNVT
PASLASLFEE EFKQDMAALK VLPPTVYLRV TENIPQIIAF IEGIIAHGHA YSTATGSVYF
DLHARGDKYG KLVNTVPSAT AEPGDSDKRH SSDFALWKAA KPQEVFWASP WGDGRPGWHI
ECSTMASEVF GSHLDIHTGG IDLAFPHHEN EIAQSEVFHQ CQQWGNYFLH SGHLHVKGTE
EKMSKSLKNY ITIKDFLKTF SPDVFRLFCL RTNYRSAIEY SDSTLVEAKH LLLGLASFVE
DARAYVKGQL TCGPVEEDVL WERLTSTKKA VKAALANDFD TPRAVNTILD LVHHANRQLR
AVSKEASGPR SPTVFGAIIS YVEQFFETVG ISLANRQCVS GDSSTVTLRC VVDELVRFRL
KVRQYALDTP GAAGEARKRQ LQERQPLLEA CDTLRQDLVT HGINVKDRGS AASTWELLDP
RTRHQKPGDR G
