ID CAS5D_MANSM Reviewed; 225 AA.
AC Q65TW5;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=CRISPR pre-crRNA endoribonuclease Cas5d {ECO:0000303|PubMed:23006625};
DE EC=3.1.-.-;
DE AltName: Full=Pre-crRNA processing endonuclease Cas5d;
GN Name=cas5d {ECO:0000303|PubMed:23006625}; OrderedLocusNames=MS0988;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
RN [2]
RP PROBABLE REACTION MECHANISM, AND COFACTOR.
RA MacMillan A.M.;
RL Unpublished observations (JAN-2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 2-225, AND FUNCTION.
RC STRAIN=MBEL55E;
RX PubMed=23006625; DOI=10.1261/rna.033100.112;
RA Garside E.L., Schellenberg M.J., Gesner E.M., Bonanno J.B., Sauder J.M.,
RA Burley S.K., Almo S.C., Mehta G., MacMillan A.M.;
RT "Cas5d processes pre-crRNA and is a member of a larger family of CRISPR RNA
RT endonucleases.";
RL RNA 18:2020-2028(2012).
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 spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). This
CC protein is a sequence-specific endonuclease that cleaves pre-crRNA at
CC G21 into mature crRNA. Does not cleave pre-crRNA associated with the
CC T.thermophilus strain HB27 Cas5 protein (AC Q746C2) CRISPR locus
CC (PubMed:23006625). The reaction mechanism may proceed by an
CC intramolecular attack of the 2'-hydroxyl group of G21 on the scissile
CC phosphodiester, cutting the precursor 3' to G21 residue yielding 5'-
CC hydroxyl and 2' and/or 3' ends lacking a hydroxyl group (perhaps a
CC 2'/3' cyclic phosphodiester) (Ref.2). {ECO:0000269|PubMed:23006625,
CC ECO:0000303|Ref.2}.
CC -!- COFACTOR:
CC Note=Does not require a metal cofactor. {ECO:0000303|Ref.2};
CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas5 family.
CC Subtype I-C/Dvulg subfamily. {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; AE016827; AAU37595.1; -; Genomic_DNA.
DR RefSeq; WP_011200165.1; NC_006300.1.
DR PDB; 3KG4; X-ray; 1.95 A; A=2-225.
DR PDBsum; 3KG4; -.
DR AlphaFoldDB; Q65TW5; -.
DR SMR; Q65TW5; -.
DR STRING; 221988.MS0988; -.
DR KEGG; msu:MS0988; -.
DR eggNOG; ENOG502Z82V; Bacteria.
DR HOGENOM; CLU_086014_0_0_6; -.
DR OrthoDB; 5621871at2; -.
DR EvolutionaryTrace; Q65TW5; -.
DR Proteomes; UP000000607; Chromosome.
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.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:InterPro.
DR CDD; cd09752; Cas5_I-C; 1.
DR Gene3D; 3.30.70.2660; -; 1.
DR InterPro; IPR021124; CRISPR-assoc_prot_Cas5.
DR InterPro; IPR013422; CRISPR-assoc_prot_Cas5_N.
DR InterPro; IPR010155; CRISPR-assoc_prot_Cas5d.
DR NCBIfam; TIGR01876; cas_Cas5d; 1.
DR NCBIfam; TIGR02593; CRISPR_cas5; 1.
DR Pfam; PF09704; Cas_Cas5d; 1.
DR PIRSF; PIRSF029950; Cas_CT1134; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Endonuclease; Hydrolase; Nuclease;
KW RNA-binding.
FT CHAIN 1..225
FT /note="CRISPR pre-crRNA endoribonuclease Cas5d"
FT /id="PRO_0000418432"
FT STRAND 5..14
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3KG4"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 105..122
FT /evidence="ECO:0007829|PDB:3KG4"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3KG4"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 182..193
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:3KG4"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:3KG4"
SQ SEQUENCE 225 AA; 25831 MW; 403FAF4FFA9C3326 CRC64;
MANRIRLHIW GDYACFTRPE MKVERVSYDV ITPSAARGIL SAIHWKPAIN WVIDKIYVLK
PIRFESVRRN ELGAKISESK VSGAMKRKSV ADLYTVIEDD RQQRAATVLK DVAYVIEAHA
VMTSKAGVDE NTTKHIEMFK RRALKGQCFQ QPCMGVREFP AHFALIDDND PLPLSQLSES
EFNRDLGWML HDIDFEHGNT PHFFRAELKN GVIDVPPFYA EEVKR
//
