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Database: UniProt
Entry: A0A1S6IUF8_9FIRM
LinkDB: A0A1S6IUF8_9FIRM
Original site: A0A1S6IUF8_9FIRM 
ID   A0A1S6IUF8_9FIRM        Unreviewed;       247 AA.
AC   A0A1S6IUF8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=CRISPR-associated endoribonuclease {ECO:0000256|PIRNR:PIRNR005054};
GN   ORFNames=B0537_04425 {ECO:0000313|EMBL:AQS58400.1};
OS   Desulforamulus ferrireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS58400.1, ECO:0000313|Proteomes:UP000189464};
RN   [1] {ECO:0000313|EMBL:AQS58400.1, ECO:0000313|Proteomes:UP000189464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSS09 {ECO:0000313|EMBL:AQS58400.1,
RC   ECO:0000313|Proteomes:UP000189464};
RX   PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA   Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT   "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT   sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT   compost.";
RL   Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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).
CC       {ECO:0000256|PIRNR:PIRNR005054}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas6/Cse3/CasE
CC       family. {ECO:0000256|ARBA:ARBA00005937, ECO:0000256|PIRNR:PIRNR005054}.
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DR   EMBL; CP019698; AQS58400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S6IUF8; -.
DR   STRING; 1833852.B0537_04425; -.
DR   KEGG; dfg:B0537_04425; -.
DR   OrthoDB; 9797488at2; -.
DR   Proteomes; UP000189464; 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   CDD; cd21140; Cas6_I-like; 1.
DR   Gene3D; 3.30.70.1890; -; 1.
DR   Gene3D; 3.30.70.1900; -; 1.
DR   InterPro; IPR049435; Cas_Cas6_C.
DR   InterPro; IPR010156; CRISPR-assoc_prot_Cas6.
DR   InterPro; IPR045747; CRISPR-assoc_prot_Cas6_N_sf.
DR   NCBIfam; TIGR01877; cas_cas6; 1.
DR   PANTHER; PTHR36984; CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS6 1; 1.
DR   PANTHER; PTHR36984:SF1; CRISPR-ASSOCIATED ENDORIBONUCLEASE CAS6 1; 1.
DR   Pfam; PF21350; Cas6_I-A; 1.
DR   Pfam; PF01881; Cas_Cas6_C; 1.
DR   PIRSF; PIRSF005054; PF1131; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189464};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          123..242
FT                   /note="CRISPR associated protein Cas6 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01881"
FT   ACT_SITE        28
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005054-50"
FT   ACT_SITE        40
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005054-50"
FT   SITE            52
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005054-1"
SQ   SEQUENCE   247 AA;  27974 MW;  680D2EA497E74314 CRC64;
     MHLYIKFTSQ EDIEVPVRYN HLLQAALYET IDPPLAAFLH DKGYQSHGRS FKLFTFSRLN
     GKFKMIKEKN MLRFCGDICL TVTSPVADFC HSIANRLFKL GQIRLGRQSL DVKALTTRQY
     TVQSERVILR TLSPVVTYST FLRPEGRKYT CYFQPGEPDY NQLIENNLRK KYLAFYQVEA
     PPGAVTVTAL SPMKLNIVNY KDTVIKGYSG KLAITGPNEL LQMAVDAGIG SKNSQGFGCV
     EVVEKQI
//
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