ID SYCC_HUMAN Reviewed; 748 AA. AC P49589; Q53XI8; Q5HYE4; Q9HD24; Q9HD25; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 31-JAN-2002, sequence version 3. DT 22-APR-2020, entry version 186. DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic; DE EC=6.1.1.16; DE AltName: Full=Cysteinyl-tRNA synthetase; DE Short=CysRS; GN Name=CARS1 {ECO:0000312|HGNC:HGNC:1493}; Synonyms=CARS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=7987009; DOI=10.3109/10425179409020847; RA Cruzen M.E., Arfin S.M.; RT "Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA RT synthetase."; RL DNA Seq. 4:243-248(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=11347887; DOI=10.1515/bc.2001.049; RA Davidson E., Caffarella J., Vitseva O., Hou Y.M., King M.P.; RT "Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl- RT tRNA synthetase."; RL Biol. Chem. 382:399-406(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cervix; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP CHROMOSOMAL TRANSLOCATION WITH ALK. RX PubMed=12112524; DOI=10.1002/gcc.10033; RA Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B., RA De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.; RT "Identification of novel fusion partners of ALK, the anaplastic lymphoma RT kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic RT tumor."; RL Genes Chromosomes Cancer 34:354-362(2002). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-503, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-79 (ISOFORM 3), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-307, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-305 AND SER-307, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). 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 -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P49589-1; Sequence=Displayed; CC Name=2; CC IsoId=P49589-2; Sequence=VSP_006312; CC Name=3; CC IsoId=P49589-3; Sequence=VSP_043571; CC -!- DISEASE: Note=A chromosomal aberration involving CARS is associated CC with inflammatory myofibroblastic tumors (IMTs). Translocation CC t(2;11)(p23;p15) with ALK. CC -!- MISCELLANEOUS: [Isoform 2]: Found in 20% of the mRNAs. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA73901.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/CARSID484.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L06845; AAA73901.1; ALT_FRAME; mRNA. DR EMBL; AF288206; AAG00578.1; -; mRNA. DR EMBL; AF288207; AAG00579.1; -; mRNA. DR EMBL; BT009913; AAP88915.1; -; mRNA. DR EMBL; AK302644; BAG63885.1; -; mRNA. DR EMBL; BX647906; CAI46108.1; -; mRNA. DR EMBL; AC108448; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC131971; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471158; EAX02541.1; -; Genomic_DNA. DR EMBL; BC002880; AAH02880.1; -; mRNA. DR CCDS; CCDS41600.1; -. [P49589-3] DR CCDS; CCDS41602.1; -. [P49589-2] DR CCDS; CCDS7742.1; -. [P49589-1] DR RefSeq; NP_001014437.1; NM_001014437.2. [P49589-3] DR RefSeq; NP_001742.1; NM_001751.5. [P49589-1] DR RefSeq; NP_644802.1; NM_139273.3. [P49589-2] DR SMR; P49589; -. DR BioGrid; 107283; 66. DR IntAct; P49589; 20. DR MINT; P49589; -. DR STRING; 9606.ENSP00000369897; -. DR ChEMBL; CHEMBL4105937; -. DR DrugBank; DB00151; Cysteine. DR iPTMnet; P49589; -. DR MetOSite; P49589; -. DR PhosphoSitePlus; P49589; -. DR SwissPalm; P49589; -. DR BioMuta; CARS; -. DR DMDM; 20141641; -. DR EPD; P49589; -. DR jPOST; P49589; -. DR MassIVE; P49589; -. DR MaxQB; P49589; -. DR PaxDb; P49589; -. DR PeptideAtlas; P49589; -. DR PRIDE; P49589; -. DR ProteomicsDB; 56023; -. [P49589-1] DR ProteomicsDB; 56024; -. [P49589-2] DR ProteomicsDB; 56025; -. [P49589-3] DR Antibodypedia; 1044; 222 antibodies. DR DNASU; 833; -. DR Ensembl; ENST00000278224; ENSP00000278224; ENSG00000110619. [P49589-2] DR Ensembl; ENST00000380525; ENSP00000369897; ENSG00000110619. [P49589-3] DR Ensembl; ENST00000397111; ENSP00000380300; ENSG00000110619. [P49589-1] DR Ensembl; ENST00000612826; ENSP00000482336; ENSG00000278191. [P49589-3] DR Ensembl; ENST00000632612; ENSP00000487923; ENSG00000278191. [P49589-2] DR Ensembl; ENST00000633248; ENSP00000488657; ENSG00000278191. [P49589-1] DR GeneID; 833; -. DR KEGG; hsa:833; -. DR UCSC; uc001lxf.4; human. [P49589-1] DR CTD; 833; -. DR DisGeNET; 833; -. DR GeneCards; CARS1; -. DR HGNC; HGNC:1493; CARS1. DR HPA; ENSG00000110619; Low tissue specificity. DR MalaCards; CARS1; -. DR MIM; 123859; gene. DR neXtProt; NX_P49589; -. DR OpenTargets; ENSG00000110619; -. DR Orphanet; 178342; Inflammatory myofibroblastic tumor. DR PharmGKB; PA26079; -. DR eggNOG; KOG2007; Eukaryota. DR eggNOG; COG0215; LUCA. DR GeneTree; ENSGT00390000006347; -. DR HOGENOM; CLU_013528_3_3_1; -. DR InParanoid; P49589; -. DR KO; K01883; -. DR OMA; FHNDMKS; -. DR OrthoDB; 528822at2759; -. DR PhylomeDB; P49589; -. DR TreeFam; TF300384; -. DR Reactome; R-HSA-379716; Cytosolic tRNA aminoacylation. DR ChiTaRS; CARS; human. DR GenomeRNAi; 833; -. DR Pharos; P49589; Tbio. DR PRO; PR:P49589; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P49589; protein. DR Bgee; ENSG00000110619; Expressed in endothelial cell and 229 other tissues. DR ExpressionAtlas; P49589; baseline and differential. DR Genevisible; P49589; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IDA:UniProtKB. DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome. DR CDD; cd00672; CysRS_core; 1. DR Gene3D; 3.40.50.620; -; 2. 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 Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding; KW Chromosomal rearrangement; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Proto-oncogene; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000244|PubMed:22814378" FT CHAIN 2..748 FT /note="Cysteine--tRNA ligase, cytoplasmic" FT /id="PRO_0000159550" FT MOTIF 57..67 FT /note="'HIGH' region" FT MOTIF 406..410 FT /note="'KMSKS' region" FT METAL 55 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 348 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 373 FT /note="Zinc" FT /evidence="ECO:0000250" FT METAL 377 FT /note="Zinc" FT /evidence="ECO:0000250" FT BINDING 409 FT /note="ATP" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000244|PubMed:22814378" FT MOD_RES 19 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:24275569" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569" FT MOD_RES 503 FT /note="N6-acetyllysine" FT /evidence="ECO:0000244|PubMed:19608861" FT MOD_RES 746 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231" FT VAR_SEQ 9 FT /note="G -> APDYRSILSISDEAARAQALNEHLSTRSYVQGYSLSQADVDAFRQLS FT APPADPQLFHVARWFRHIEALLGSPCGKGQPCRLQAS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:17974005" FT /id="VSP_043571" FT VAR_SEQ 705..748 FT /note="GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ -> VSMV FT CPHMTWRAKSSAKGKPRS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11347887, FT ECO:0000303|PubMed:7987009" FT /id="VSP_006312" FT MOD_RES P49589-3:79 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:20068231" SQ SEQUENCE 748 AA; 85473 MW; D0B7A29EC03AA87F CRC64; MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV TWYCCGPTVY DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD KIIKRARQNH LFEQYREKRP EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ MLERIQHAVQ LATEPLEKAV QSRLTGEEVN SCVEVLLEEA KDLLSDWLDS TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR VSEYVPEIVN FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA MAGTLLGASM DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL TIAGCKMSKS LKNFITIKDA LKKHSARQLR LAFLMHSWKD TLDYSSNTME SALQYEKFLN EFFLNVKDIL RAPVDITGQF EKWGEEEAEL NKNFYDKKTA IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN QALLENIALY LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK IAREQKVPEI LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE REEKRRVEEE KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK FDENGLPTHD MEGKELSKGQ AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ //