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Database: UniProt
Entry: S9W1N9_SCHCR
LinkDB: S9W1N9_SCHCR
Original site: S9W1N9_SCHCR 
ID   S9W1N9_SCHCR            Unreviewed;       756 AA.
AC   S9W1N9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=cysteine--tRNA ligase {ECO:0000256|ARBA:ARBA00012832};
DE            EC=6.1.1.16 {ECO:0000256|ARBA:ARBA00012832};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031499};
GN   ORFNames=SPOG_00352 {ECO:0000313|EMBL:EPY51930.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY51930.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY51930.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   EMBL; KE546990; EPY51930.1; -; Genomic_DNA.
DR   RefSeq; XP_013023315.1; XM_013167861.1.
DR   AlphaFoldDB; S9W1N9; -.
DR   STRING; 653667.S9W1N9; -.
DR   EnsemblFungi; EPY51930; EPY51930; SPOG_00352.
DR   GeneID; 25034684; -.
DR   eggNOG; KOG2007; Eukaryota.
DR   HOGENOM; CLU_013528_3_1_1; -.
DR   OMA; YEGLGWA; -.
DR   OrthoDB; 2140072at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:EnsemblFungi.
DR   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00435; cysS; 1.
DR   PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EPY51930.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          38..454
FT                   /note="tRNA synthetases class I catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01406"
FT   COILED          654..681
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   756 AA;  85953 MW;  F88130CF4DBF6EFC CRC64;
     MSSEKSQLSP WFAPTGHKTE LNVFNTITHS KVPFKTNGSM VTWYCCGPTV YDASHMGHAR
     NYVTTDILRR ILQSYFGYNV TFVQNVTDID DKIILRARQQ YLFEQYKQQN EHNYASPTVK
     AKVTEAWLAY AKKNLPESPQ SVDEWSNWLA THDITTLALA APKVPLYADS LTQGVEGLKI
     AEEAKSEDSE LFWSKVQEVL IPVLDSELGN TVTDPAIFRK LSAYWENDYN EDMRALNVLP
     PTTVTRVSEF VPEIVEYVQK IIDRGYAYPV TDGSVYFDTE AFSKGGHFYA KLEPWNKGNR
     DLIAEGEGSL AALTGKKRPG DFALWKSSKP GEPSWDSPWS NGRPGWHIEC SVMASAVLGP
     NVDIHSGGVD LAFPHHDNEL AQSEAYHDCP QWINYFLHTG HLHIEGQKMS KSLKNFITIK
     EILKKFTPRQ LRLAFLLQQW NSQLDFKDAL LAHVLNVEQT LENFFQNVRA LNIESQGLSQ
     QGGHVTEKYG ELERQLLNDL QTAQRNAHSA LCDNFNTPLV MFHIDSLVGK SNIYIRDVGQ
     KPCTRLLNEI AMWITKMLQV FGLDDEGRPN AIGWSSKSSA SVSNSNDAIP YVRAVSTFRD
     RIRELCIAKA PIQEILQACD VFRDYDMAEL GVSLNDRQQG PALIKLVDPQ VLIQARDQKI
     AEEQEKEAKK LKAKAEQENK YIERIMKGKV APSEMFKLFE EFLSFDESGF PTKVRAEDGS
     EVELPKSRKK KLQKEYTTQE KLHKEYLAYI EKKNQD
//
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