CS4F1_GEOSL
ID CS4F1_GEOSL Reviewed; 559 AA.
AC Q74H36;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=GSU0057;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
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 -!- 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}.
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DR EMBL; AE017180; AAR33392.1; -; Genomic_DNA.
DR RefSeq; NP_951119.1; NC_002939.5.
DR RefSeq; WP_010940735.1; NC_002939.5.
DR PDB; 7MI4; EM; 3.20 A; A/B/C/D=1-559.
DR PDB; 7MI5; EM; 3.57 A; A/B/C/D=1-559.
DR PDB; 7MI9; EM; 3.89 A; A/B/C/D=1-559.
DR PDB; 7MIB; EM; 5.80 A; A/B/C/D=1-559.
DR PDB; 7MID; EM; 3.56 A; A/B=1-559.
DR PDBsum; 7MI4; -.
DR PDBsum; 7MI5; -.
DR PDBsum; 7MI9; -.
DR PDBsum; 7MIB; -.
DR PDBsum; 7MID; -.
DR AlphaFoldDB; Q74H36; -.
DR SMR; Q74H36; -.
DR STRING; 243231.GSU0057; -.
DR PRIDE; Q74H36; -.
DR EnsemblBacteria; AAR33392; AAR33392; GSU0057.
DR KEGG; gsu:GSU0057; -.
DR PATRIC; fig|243231.5.peg.57; -.
DR eggNOG; COG1468; Bacteria.
DR eggNOG; COG1518; Bacteria.
DR HOGENOM; CLU_466793_0_0_7; -.
DR InParanoid; Q74H36; -.
DR OMA; FAYCPRL; -.
DR Proteomes; UP000000577; 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:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
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; 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; TIGR00372; cas4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Antiviral defense; DNA-binding; Endonuclease;
KW Exonuclease; Hydrolase; Iron; Iron-sulfur; Magnesium; Manganese;
KW Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..559
FT /note="CRISPR-associated exonuclease Cas4/endonuclease Cas1
FT fusion"
FT /id="PRO_0000417114"
FT REGION 1..198
FT /note="CRISPR-associated exonuclease Cas4"
FT REGION 224..559
FT /note="CRISPR-associated endonuclease Cas1"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 87
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 190
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 380
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 451
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT BINDING 466
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q02ML7"
FT HELIX 13..19
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 64..77
FT /evidence="ECO:0007829|PDB:7MI4"
FT TURN 78..81
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:7MI4"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 155..174
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 317..341
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 373..389
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 418..439
FT /evidence="ECO:0007829|PDB:7MI4"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:7MI4"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 468..482
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 502..516
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:7MI4"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:7MI4"
FT HELIX 531..546
FT /evidence="ECO:0007829|PDB:7MI4"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:7MI4"
SQ SEQUENCE 559 AA; 62515 MW; 0F9A00EDAE27344B CRC64;
MAETDGSIPL IPVRMLNEHV YCPRLAYLMW VQGEFSHNEF TVDGVIRHRR VDAGGGVLPS
ETQEDSRIHA RSVSLSSERL GITAKIDLVE GEGAYVSPVD YKRGKRPHVA GGAYEPERVQ
LCAQGLLLRE HGFASDGGAL YFVASRERVP VAFDDELIGR TLAAIDEMGR TALSGTMPPP
LEDSPKCPRC SLVGICLPDE VRFLSHLSVE PRPIIPADGR GLPLYVQSPK AYVRKDGDCL
VIEEERVRVA EARLGETSQV ALFGNATLTT AALHECLRRE IPVTWLSYGG WFMGHTVSTG
HRNVETRTYQ YQRSFDPETC LNLARRWIVA KIANCRTLLR RNWRGEGDEA KAPPGLLMSL
QDDMRHAMRA PSLEVLLGIE GASAGRYFQH FSRMLRGGDG EGMGFDFTTR NRRPPKDPVN
ALLSFAYAML TREWTVALAA VGLDPYRGFY HQPRFGRPAL ALDMMEPFRP LIADSTVLMA
INNGEIRTGD FVRSAGGCNL TDSARKRFIA GFERRMEQEV THPIFKYTIS YRRLLEVQAR
LLTRYLSGEI PAYPNFVTR
