CS13A_LACNK
ID CS13A_LACNK Reviewed; 1437 AA.
AC P0DPB7;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=CRISPR-associated endoribonuclease Cas13a {ECO:0000303|PubMed:28475872};
DE Short=EndoRNase;
DE EC=3.1.-.-;
DE AltName: Full=LbaCas13a {ECO:0000303|PubMed:28475872};
GN Name=cas13a {ECO:0000303|PubMed:28475872};
OS Lachnospiraceae bacterium (strain NK4A179).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=877424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NK4A179;
RG US DOE Joint Genome Institute;
RA Kelly W., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN CRRNA PROCESSING, FUNCTION IN TARGET SSRNA CLEAVAGE, FUNCTION
RP AS AN ENDORIBONUCLEASE, AND ACTIVITY REGULATION.
RX PubMed=28475872; DOI=10.1016/j.molcel.2017.04.008;
RA East-Seletsky A., O'Connell M.R., Burstein D., Knott G.J., Doudna J.A.;
RT "RNA targeting by functionally orthogonal type VI-A CRISPR-Cas enzymes.";
RL Mol. Cell 66:373-383(2017).
CC -!- FUNCTION: CRISPR (clustered regularly interspaced short palindromic
CC repeat), is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. Unlike
CC many single-component effectors, this CRISPR-Cas system targets RNA
CC (PubMed:28475872). CRISPR clusters are transcribed from pre-CRISPR RNA
CC (crRNA) and processed into crRNA by this protein (PubMed:28475872).
CC Cleaves linear target ssRNA in a pre-crRNA-dependent fashion,
CC preferentially around A residues (PubMed:28475872). Binding a viable
CC target RNA target activates this protein for non-specific RNA
CC degradation in vitro (called collateral RNA degradation), but it is not
CC very sensitive as it requires nanomolar levels of viable target RNA
CC (PubMed:28475872). {ECO:0000269|PubMed:28475872}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:C7NBY4};
CC Note=Pre-crRNA processing is metal independent, while crRNA-guided
CC target RNA cleavage is dependent on divalent metal.
CC {ECO:0000250|UniProtKB:C7NBY4};
CC -!- ACTIVITY REGULATION: Target RNA acts as an activator for non-specific
CC ssRNA degradation (PubMed:28475872). {ECO:0000269|PubMed:28475872}.
CC -!- DOMAIN: The target ssRNase active sites are probably within the 2 HEPN-
CC like folds, and the 2 folds interact in vivo.
CC {ECO:0000250|UniProtKB:C7NBY4}.
CC -!- MISCELLANEOUS: Part of a type VI-A adenine-prefering CRISPR-Cas system.
CC {ECO:0000305|PubMed:28475872}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas13a
CC family. {ECO:0000305}.
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; ATWC01000054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_022785443.1; NZ_ATWC01000054.1.
DR AlphaFoldDB; P0DPB7; -.
DR SMR; P0DPB7; -.
DR OrthoDB; 382328at2; -.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antiviral defense; Endonuclease; Hydrolase; Nuclease; Repeat; RNA-binding.
FT CHAIN 1..1437
FT /note="CRISPR-associated endoribonuclease Cas13a"
FT /id="PRO_0000442268"
FT REGION 460..626
FT /note="HEPN-like fold 1"
FT /evidence="ECO:0000250|UniProtKB:C7NBY4"
FT REGION 1101..1437
FT /note="HEPN-like fold 2"
FT /evidence="ECO:0000250|UniProtKB:C7NBY4"
FT REGION 1377..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 168661 MW; FB0E7920B74ECD34 CRC64;
MKISKVREEN RGAKLTVNAK TAVVSENRSQ EGILYNDPSR YGKSRKNDED RDRYIESRLK
SSGKLYRIFN EDKNKRETDE LQWFLSEIVK KINRRNGLVL SDMLSVDDRA FEKAFEKYAE
LSYTNRRNKV SGSPAFETCG VDAATAERLK GIISETNFIN RIKNNIDNKV SEDIIDRIIA
KYLKKSLCRE RVKRGLKKLL MNAFDLPYSD PDIDVQRDFI DYVLEDFYHV RAKSQVSRSI
KNMNMPVQPE GDGKFAITVS KGGTESGNKR SAEKEAFKKF LSDYASLDER VRDDMLRRMR
RLVVLYFYGS DDSKLSDVNE KFDVWEDHAA RRVDNREFIK LPLENKLANG KTDKDAERIR
KNTVKELYRN QNIGCYRQAV KAVEEDNNGR YFDDKMLNMF FIHRIEYGVE KIYANLKQVT
EFKARTGYLS EKIWKDLINY ISIKYIAMGK AVYNYAMDEL NASDKKEIEL GKISEEYLSG
ISSFDYELIK AEEMLQRETA VYVAFAARHL SSQTVELDSE NSDFLLLKPK GTMDKNDKNK
LASNNILNFL KDKETLRDTI LQYFGGHSLW TDFPFDKYLA GGKDDVDFLT DLKDVIYSMR
NDSFHYATEN HNNGKWNKEL ISAMFEHETE RMTVVMKDKF YSNNLPMFYK NDDLKKLLID
LYKDNVERAS QVPSFNKVFV RKNFPALVRD KDNLGIELDL KADADKGENE LKFYNALYYM
FKEIYYNAFL NDKNVRERFI TKATKVADNY DRNKERNLKD RIKSAGSDEK KKLREQLQNY
IAENDFGQRI KNIVQVNPDY TLAQICQLIM TEYNQQNNGC MQKKSAARKD INKDSYQHYK
MLLLVNLRKA FLEFIKENYA FVLKPYKHDL CDKADFVPDF AKYVKPYAGL ISRVAGSSEL
QKWYIVSRFL SPAQANHMLG FLHSYKQYVW DIYRRASETG TEINHSIAED KIAGVDITDV
DAVIDLSVKL CGTISSEISD YFKDDEVYAE YISSYLDFEY DGGNYKDSLN RFCNSDAVND
QKVALYYDGE HPKLNRNIIL SKLYGERRFL EKITDRVSRS DIVEYYKLKK ETSQYQTKGI
FDSEDEQKNI KKFQEMKNIV EFRDLMDYSE IADELQGQLI NWIYLRERDL MNFQLGYHYA
CLNNDSNKQA TYVTLDYQGK KNRKINGAIL YQICAMYING LPLYYVDKDS SEWTVSDGKE
STGAKIGEFY RYAKSFENTS DCYASGLEIF ENISEHDNIT ELRNYIEHFR YYSSFDRSFL
GIYSEVFDRF FTYDLKYRKN VPTILYNILL QHFVNVRFEF VSGKKMIGID KKDRKIAKEK
ECARITIREK NGVYSEQFTY KLKNGTVYVD ARDKRYLQSI IRLLFYPEKV NMDEMIEVKE
KKKPSDNNTG KGYSKRDRQQ DRKEYDKYKE KKKKEGNFLS GMGGNINWDE INAQLKN
