CS13A_HERHM
ID CS13A_HERHM Reviewed; 1285 AA.
AC A0A0H5SJ89;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=CRISPR-associated endoribonuclease Cas13a {ECO:0000303|PubMed:28475872};
DE Short=EndoRNase;
DE EC=3.1.-.-;
DE AltName: Full=HheCas13a {ECO:0000303|PubMed:28475872};
GN Name=cas13a {ECO:0000303|PubMed:28475872}; ORFNames=HHT355_2368;
OS Herbinix hemicellulosilytica.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae; Herbinix.
OX NCBI_TaxID=1564487;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T3/55T;
RA Wibberg D.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP LACK OF FUNCTION IN CRRNA PROCESSING, FUNCTION IN TARGET SSRNA CLEAVAGE,
RP FUNCTION 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 usually transcribed from pre-
CC CRISPR RNA (crRNA) and processed into crRNA but this protein does not
CC have detectable pre-cRNA processing activity on any tested pre-crRNA
CC (PubMed:28475872). Cleaves linear target ssRNA in a pre-crRNA-dependent
CC fashion, preferentially before U residues (PubMed:28475872). Binding a
CC viable 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 uridine-prefering CRISPR-Cas system.
CC {ECO:0000305|PubMed:28475872}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas13a
CC family. {ECO:0000305}.
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DR EMBL; CVTD020000026; CRZ35554.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5SJ89; -.
DR SMR; A0A0H5SJ89; -.
DR EnsemblBacteria; CRZ35554; CRZ35554; HHT355_2368.
DR Proteomes; UP000236497; Unassembled WGS sequence.
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; Coiled coil; Endonuclease; Hydrolase; Nuclease;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1285
FT /note="CRISPR-associated endoribonuclease Cas13a"
FT /id="PRO_0000442267"
FT REGION 353..510
FT /note="HEPN-like fold 1"
FT /evidence="ECO:0000250|UniProtKB:C7NBY4"
FT REGION 794..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1285
FT /note="HEPN-like fold 2"
FT /evidence="ECO:0000250|UniProtKB:C7NBY4"
FT COILED 969..1004
FT /evidence="ECO:0000255"
SQ SEQUENCE 1285 AA; 152323 MW; 5C0F695BB0F17E08 CRC64;
MKLTRRRISG NSVDQKITAA FYRDMSQGLL YYDSEDNDCT DKVIESMDFE RSWRGRILKN
GEDDKNPFYM FVKGLVGSND KIVCEPIDVD SDPDNLDILI NKNLTGFGRN LKAPDSNDTL
ENLIRKIQAG IPEEEVLPEL KKIKEMIQKD IVNRKEQLLK SIKNNRIPFS LEGSKLVPST
KKMKWLFKLI DVPNKTFNEK MLEKYWEIYD YDKLKANITN RLDKTDKKAR SISRAVSEEL
REYHKNLRTN YNRFVSGDRP AAGLDNGGSA KYNPDKEEFL LFLKEVEQYF KKYFPVKSKH
SNKSKDKSLV DKYKNYCSYK VVKKEVNRSI INQLVAGLIQ QGKLLYYFYY NDTWQEDFLN
SYGLSYIQVE EAFKKSVMTS LSWGINRLTS FFIDDSNTVK FDDITTKKAK EAIESNYFNK
LRTCSRMQDH FKEKLAFFYP VYVKDKKDRP DDDIENLIVL VKNAIESVSY LRNRTFHFKE
SSLLELLKEL DDKNSGQNKI DYSVAAEFIK RDIENLYDVF REQIRSLGIA EYYKADMISD
CFKTCGLEFA LYSPKNSLMP AFKNVYKRGA NLNKAYIRDK GPKETGDQGQ NSYKALEEYR
ELTWYIEVKN NDQSYNAYKN LLQLIYYHAF LPEVRENEAL ITDFINRTKE WNRKETEERL
NTKNNKKHKN FDENDDITVN TYRYESIPDY QGESLDDYLK VLQRKQMARA KEVNEKEEGN
NNYIQFIRDV VVWAFGAYLE NKLKNYKNEL QPPLSKENIG LNDTLKELFP EEKVKSPFNI
KCRFSISTFI DNKGKSTDNT SAEAVKTDGK EDEKDKKNIK RKDLLCFYLF LRLLDENEIC
KLQHQFIKYR CSLKERRFPG NRTKLEKETE LLAELEELME LVRFTMPSIP EISAKAESGY
DTMIKKYFKD FIEKKVFKNP KTSNLYYHSD SKTPVTRKYM ALLMRSAPLH LYKDIFKGYY
LITKKECLEY IKLSNIIKDY QNSLNELHEQ LERIKLKSEK QNGKDSLYLD KKDFYKVKEY
VENLEQVARY KHLQHKINFE SLYRIFRIHV DIAARMVGYT QDWERDMHFL FKALVYNGVL
EERRFEAIFN NNDDNNDGRI VKKIQNNLNN KNRELVSMLC WNKKLNKNEF GAIIWKRNPI
AHLNHFTQTE QNSKSSLESL INSLRILLAY DRKRQNAVTK TINDLLLNDY HIRIKWEGRV
DEGQIYFNIK EKEDIENEPI IHLKHLHKKD CYIYKNSYMF DKQKEWICNG IKEEVYDKSI
LKCIGNLFKF DYEDKNKSSA NPKHT
