(data stored in SCRATCH3701 zone)

SWISSPROT: D5E946_METMS

ID   D5E946_METMS            Unreviewed;       265 AA.
AC   D5E946;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 36.
DE   RecName: Full=CRISPR-associated exonuclease Cas4 {ECO:0000256|RuleBase:RU365022};
DE            EC=3.1.12.1 {ECO:0000256|RuleBase:RU365022};
GN   OrderedLocusNames=Mmah_0162 {ECO:0000313|EMBL:ADE35697.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35697.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35697.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU365022}.
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         Evidence={ECO:0000256|RuleBase:RU365022};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU365022};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU365022};
CC       Note=Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
CC       {ECO:0000256|RuleBase:RU365022};
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000256|RuleBase:RU365022};
CC   -!- SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family.
CC       {ECO:0000256|RuleBase:RU365022}.
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DR   EMBL; CP001994; ADE35697.1; -; Genomic_DNA.
DR   RefSeq; WP_013036640.1; NC_014002.1.
DR   EnsemblBacteria; ADE35697; ADE35697; Mmah_0162.
DR   GeneID; 8982293; -.
DR   KEGG; mmh:Mmah_0162; -.
DR   eggNOG; arCOG00793; Archaea.
DR   eggNOG; ENOG4111MY4; LUCA.
DR   HOGENOM; HOG000121402; -.
DR   KO; K07464; -.
DR   OMA; FVEYVSF; -.
DR   OrthoDB; 84826at2157; -.
DR   BioCyc; MMAH547558:G1GHT-163-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.320.10; -; 1.
DR   InterPro; IPR013343; CRISPR-assoc_prot_Cas4.
DR   InterPro; IPR022765; Dna2/Cas4_DUF83.
DR   InterPro; IPR011604; Exonuc_phg/RecB_C.
DR   Pfam; PF01930; Cas_Cas4; 1.
DR   TIGRFAMs; TIGR00372; cas4; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E946.
DR   SWISS-2DPAGE; D5E946.
KW   Antiviral defense {ECO:0000256|RuleBase:RU365022};
KW   Exonuclease {ECO:0000256|RuleBase:RU365022};
KW   Hydrolase {ECO:0000256|RuleBase:RU365022};
KW   Iron {ECO:0000256|RuleBase:RU365022};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU365022};
KW   Manganese {ECO:0000256|RuleBase:RU365022};
KW   Metal-binding {ECO:0000256|RuleBase:RU365022};
KW   Nuclease {ECO:0000256|RuleBase:RU365022};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059}.
FT   DOMAIN          157..254
FT                   /note="Cas_Cas4"
FT                   /evidence="ECO:0000259|Pfam:PF01930"
SQ   SEQUENCE   265 AA;  30275 MW;  FB19A0A5F5E7FEB2 CRC64;
     MCAMFCETNS NVSEVVLYTK CPRKIYFTSR NEVISNEIEK PYIRHLLLKE LALSCAEIAV
     SKQEILPLLQ KRVEEIVQEI ITIYSDELEH IDENQFKDAL EDVYEVLPAI AGNLKNQFDE
     EMIELIKPVE IEPLMHSDKL NLSGAPSAII CSDKQKIPML IKTGNAPMQG VWKNDRIPLA
     AYSILTEERY DQPVNSAVLF YASQGQARSV RIRPAERREV LNILKRIEKI KEGKMPQAKR
     GKLCGYCPYE QMCQSQGDSL ASKFF
//

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