CAS6L_PYRHO
ID CAS6L_PYRHO Reviewed; 239 AA.
AC O58088;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Putative CRISPR-associated endoribonuclease-like protein Cas6nc;
DE Short=PhCas6nc;
GN Name=cas6nc; OrderedLocusNames=PH0350;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN PRESENCE AND ABSENCE OF RNA,
RP SUBUNIT, RNA-BINDING, AND LACK OF FUNCTION AS AN ENDORIBONUCLEASE.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=22238224; DOI=10.1002/pro.2028;
RA Wang R., Zheng H., Preamplume G., Shao Y., Li H.;
RT "The impact of CRISPR repeat sequence on structures of a Cas6 protein-RNA
RT complex.";
RL Protein Sci. 21:405-417(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 sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA), also
CC called psiRNA (prokaryotic silencing) in this organism (Potential).
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer; homodimer when crystallized in the presence of crRNA.
CC Varying the crRNA sequence varies degree of oligomerization and
CC structure. {ECO:0000269|PubMed:22238224}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE
CC family. {ECO:0000305}.
CC -!- CAUTION: No in vitro nuclease activity has been observed against crRNA
CC for this protein. {ECO:0000305|PubMed:22238224}.
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DR EMBL; BA000001; BAA29424.1; -; Genomic_DNA.
DR PIR; C71142; C71142.
DR RefSeq; WP_010884439.1; NC_000961.1.
DR PDB; 3QJJ; X-ray; 2.80 A; A/B=1-239.
DR PDB; 3QJL; X-ray; 2.70 A; A/B=1-239.
DR PDB; 3QJP; X-ray; 3.30 A; A=1-239.
DR PDBsum; 3QJJ; -.
DR PDBsum; 3QJL; -.
DR PDBsum; 3QJP; -.
DR AlphaFoldDB; O58088; -.
DR SMR; O58088; -.
DR STRING; 70601.3256741; -.
DR PRIDE; O58088; -.
DR EnsemblBacteria; BAA29424; BAA29424; BAA29424.
DR GeneID; 1444226; -.
DR KEGG; pho:PH0350; -.
DR eggNOG; arCOG04342; Archaea.
DR OMA; HWDLYPH; -.
DR OrthoDB; 59332at2157; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.1890; -; 1.
DR InterPro; IPR010156; CRISPR-assoc_prot_Cas6.
DR InterPro; IPR045747; CRISPR-assoc_prot_Cas6_N_sf.
DR PANTHER; PTHR36984; PTHR36984; 1.
DR Pfam; PF01881; Cas_Cas6; 1.
DR PIRSF; PIRSF005054; PF1131; 1.
DR TIGRFAMs; TIGR01877; cas_cas6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; RNA-binding.
FT CHAIN 1..239
FT /note="Putative CRISPR-associated endoribonuclease-like
FT protein Cas6nc"
FT /id="PRO_0000417973"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3QJJ"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3QJL"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3QJL"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:3QJL"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:3QJL"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 181..193
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 200..211
FT /evidence="ECO:0007829|PDB:3QJL"
FT HELIX 213..222
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:3QJL"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3QJL"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:3QJL"
SQ SEQUENCE 239 AA; 27476 MW; 719DF6CB8E9E22FB CRC64;
MRIEVKLLPL KDNPILPFNY NYEVYSQILE KVNSIEPTIA KLLSSPHGFW TFSRIIVRKR
KILPDKGIEI LSDDVSLYIS SSNEDIIRAI AEAVEKSPEF KIGELSFLVG DIKAIKVKEL
GKENVFSTLS PIVVRTVKFE GNKLRHWDLY PHDELFMDRL RKVMILRYSE VMGETPKDRD
FTIEVLKFKP TRLMVGSSYI RGSLMVFRYA GSEEIARFGY ENGFGEKTGL GFGMVKLIE
