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CAS5D_MANSM
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   03-AUG-2022, entry version 80.
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; Proteobacteria; 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RL   Unpublished observations (JAN-2015).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}.
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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   PRIDE; Q65TW5; -.
DR   EnsemblBacteria; AAU37595; AAU37595; MS0988.
DR   KEGG; msu:MS0988; -.
DR   eggNOG; ENOG502Z82V; Bacteria.
DR   HOGENOM; CLU_086014_0_0_6; -.
DR   OMA; YLGCREF; -.
DR   OrthoDB; 1619114at2; -.
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   InterPro; IPR021124; CRISPR-assoc_prot_Cas5.
DR   InterPro; IPR013422; CRISPR-assoc_prot_Cas5_N.
DR   InterPro; IPR010155; CRISPR-assoc_prot_Cas5d.
DR   Pfam; PF09704; Cas_Cas5d; 1.
DR   PIRSF; PIRSF029950; Cas_CT1134; 1.
DR   TIGRFAMs; TIGR01876; cas_Cas5d; 1.
DR   TIGRFAMs; TIGR02593; CRISPR_cas5; 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
 
 
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