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Database: UniProt
Entry: Q7NAI1_MYCGA
LinkDB: Q7NAI1_MYCGA
Original site: Q7NAI1_MYCGA 
ID   Q7NAI1_MYCGA            Unreviewed;       308 AA.
AC   Q7NAI1;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000256|HAMAP-Rule:MF_01470};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01470};
GN   Name=cas1 {ECO:0000256|HAMAP-Rule:MF_01470,
GN   ECO:0000313|EMBL:AAP57025.2};
GN   ORFNames=MGA_0523 {ECO:0000313|EMBL:AAP57025.2};
OS   Mycoplasmoides gallisepticum (strain R(low / passage 15 / clone 2))
OS   (Mycoplasma gallisepticum).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=710127 {ECO:0000313|EMBL:AAP57025.2, ECO:0000313|Proteomes:UP000001418};
RN   [1] {ECO:0000313|EMBL:AAP57025.2, ECO:0000313|Proteomes:UP000001418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R(low / passage 15 / clone 2)
RC   {ECO:0000313|Proteomes:UP000001418};
RX   PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA   Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA   Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT   "The complete genome sequence of the avian pathogen Mycoplasma
RT   gallisepticum strain R(low).";
RL   Microbiology 149:2307-2316(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). Acts as
CC       a dsDNA endonuclease. Involved in the integration of spacer DNA into
CC       the CRISPR cassette. {ECO:0000256|HAMAP-Rule:MF_01470}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01470};
CC   -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer.
CC       {ECO:0000256|ARBA:ARBA00038592, ECO:0000256|HAMAP-Rule:MF_01470}.
CC   -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01470}.
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DR   EMBL; AE015450; AAP57025.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q7NAI1; -.
DR   KEGG; mga:MGA_0523; -.
DR   PATRIC; fig|233150.7.peg.754; -.
DR   HOGENOM; CLU_055263_1_0_14; -.
DR   OrthoDB; 9803119at2; -.
DR   Proteomes; UP000001418; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004520; F:DNA endonuclease activity; IEA:InterPro.
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   CDD; cd09720; Cas1_II; 1.
DR   Gene3D; 1.20.120.920; CRISPR-associated endonuclease Cas1, C-terminal domain; 1.
DR   Gene3D; 3.100.10.20; CRISPR-associated endonuclease Cas1, N-terminal domain; 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; IPR019855; CRISPR-assoc_Cas1_NMENI.
DR   NCBIfam; TIGR00287; cas1; 1.
DR   NCBIfam; TIGR03639; cas1_NMENI; 1.
DR   PANTHER; PTHR34353; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR   PANTHER; PTHR34353:SF2; CRISPR-ASSOCIATED ENDONUCLEASE CAS1 1; 1.
DR   Pfam; PF01867; Cas_Cas1; 1.
PE   3: Inferred from homology;
KW   Antiviral defense {ECO:0000256|ARBA:ARBA00023118, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01470};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01470};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001418}.
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         223
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
FT   BINDING         238
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01470"
SQ   SEQUENCE   308 AA;  36108 MW;  599E0F51CAB47587 CRC64;
     MQLPHPPEHL CSGFLFVMSK KVLEVSETEF ISLHLDTLIV RKHGARVTLP LKTLDTILIT
     NPYCNISVPL LNKIVENNIN LIVCNTKFQP TMQILPISSY YSNKNYLWQI RWTDEQKNQI
     WKQLVKLKII NYARLINHLN ITTDDNIEKL TNYYTNVVDG DLNNCEGHAA KLSFKLLYGE
     DFSRSQKDDI INKYLNYGYI VLMTYVSRTL VKNGLDNRIG IFHKSFNNHF ALSCDIMEPF
     RPIIDYLTFS YLIKNQNDDF KSYKKDLFIS FENFIFPNGK NLNQVIDMLI KAIINNKINE
     RDFNIDWS
//
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