CS4F1_MYXXD
ID CS4F1_MYXXD Reviewed; 568 AA.
AC Q1CW50;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=CRISPR-associated exonuclease Cas4/endonuclease Cas1 fusion;
DE EC=3.1.-.-;
DE EC=3.1.12.1;
GN Name=cas4-cas1; OrderedLocusNames=MXAN_7260;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
RN [2]
RP DEVELOPMENTAL STAGE, INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=DK1622;
RX PubMed=17369305; DOI=10.1128/jb.00187-07;
RA Viswanathan P., Murphy K., Julien B., Garza A.G., Kroos L.;
RT "Regulation of dev, an operon that includes genes essential for Myxococcus
RT xanthus development and CRISPR-associated genes and repeats.";
RL J. Bacteriol. 189:3738-3750(2007).
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) (By
CC similarity). The Cas4 region acts as a ssDNA exonuclease, while the
CC Cas1 region acts as a dsDNA endonuclease. Involved in the integration
CC of spacer DNA into the CRISPR cassette (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q97TX9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC nucleoside 3'-phosphates.; EC=3.1.12.1;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:Q97TX9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Operon expression begins by 6 hours after
CC starvation has initiated development and is under strong negative
CC regulation by DevS. {ECO:0000269|PubMed:17369305}.
CC -!- INDUCTION: Part of an operon going from at least MXAN_7266 to MXAN_7259
CC that includes a CRISPR operon with transcription continuing into the
CC pre-crRNA locus. {ECO:0000269|PubMed:17369305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR-associated
CC exonuclease Cas4 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the CRISPR-associated
CC endonuclease Cas1 family. {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; CP000113; ABF90454.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1CW50; -.
DR SMR; Q1CW50; -.
DR STRING; 246197.MXAN_7260; -.
DR PRIDE; Q1CW50; -.
DR EnsemblBacteria; ABF90454; ABF90454; MXAN_7260.
DR KEGG; mxa:MXAN_7260; -.
DR eggNOG; COG1468; Bacteria.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_466793_0_0_7; -.
DR OMA; FAYCPRL; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004520; F:endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-UniRule.
DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.920; -; 1.
DR Gene3D; 3.100.10.20; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01470; Cas1; 1.
DR InterPro; IPR002729; CRISPR-assoc_Cas1.
DR InterPro; IPR042206; CRISPR-assoc_Cas1_C.
DR InterPro; IPR023844; CRISPR-assoc_Cas1_MYXAN.
DR InterPro; IPR042211; CRISPR-assoc_Cas1_N.
DR InterPro; IPR013343; CRISPR-assoc_prot_Cas4.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR Pfam; PF01867; Cas_Cas1; 1.
DR Pfam; PF01930; Cas_Cas4; 1.
DR TIGRFAMs; TIGR00287; cas1; 1.
DR TIGRFAMs; TIGR03983; cas1_MYXAN; 1.
DR TIGRFAMs; TIGR00372; cas4; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Antiviral defense; DNA-binding; Endonuclease; Exonuclease;
KW Hydrolase; Iron; Iron-sulfur; Magnesium; Manganese; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..568
FT /note="CRISPR-associated exonuclease Cas4/endonuclease Cas1
FT fusion"
FT /id="PRO_0000418218"
FT REGION 1..209
FT /note="CRISPR-associated exonuclease Cas4"
FT REGION 232..568
FT /note="CRISPR-associated endonuclease Cas1"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 108
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 201
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 207
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 459
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 474
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
SQ SEQUENCE 568 AA; 62762 MW; 5393C35C5BA0633B CRC64;
MSVVVTRYRG GGPQYMNASS TSPKPVVGEP SIRTHALHAL AYCERLFYLE EVEELRVADA
AVFAGRRLHV QLQEEGEHVE LELASEALGL HGRVDAVKTR EGTLVVYEHK RGRHAPGGDA
PEAWPSDRLQ AGAYALLVEE RFPGAPVECR VRYHQTDTTV RFPLDAALRG AVVAAVARAR
LLRASRERPP VTQEERKCAK CSLAPVCLPE EERQVVGEER PRLFPEDDVR QVLHVATPGT
RVGRAAEELV VTPPEGEGAP SRQPGRMVSA LIAHGAVQVS AQALAYCVEN DIGVHWFTSG
GRYLGGLGGG AGNVHRRLRQ FEALRQASVC LGLARRLVAA KLEGQLRFLL RASRGDSESR
QVLASAVRDL RALLPKCEEA PSLEVLLGLE GAGAARYFGA LPYLQGEDVD TRLRFEGRNR
RPPRDRFNAV LGFLFGLVHR EVEAAIRAVG LDVAFGFYHQ PRGTAGPLGL DVMELFRVPL
ADMPLVASVN RRAWDADADF EVTSEHVWLS KAGRAKAIEL YERRKRETWK NNVLGYSLSY
ARLVELEVRL LEKEWTGKPG LFATFRLR
