ID   Y172_TRIV2              Reviewed;         243 AA.
AC   Q3MGT8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=UPF0758 protein Ava_0172;
GN   OrderedLocusNames=Ava_0172;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
CC   -!- SIMILARITY: Belongs to the UPF0758 family. {ECO:0000305}.
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DR   EMBL; CP000117; ABA19798.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3MGT8; -.
DR   SMR; Q3MGT8; -.
DR   STRING; 240292.Ava_0172; -.
DR   EnsemblBacteria; ABA19798; ABA19798; Ava_0172.
DR   KEGG; ava:Ava_0172; -.
DR   eggNOG; COG2003; Bacteria.
DR   HOGENOM; CLU_073529_0_2_3; -.
DR   OMA; AMPDYEL; -.
DR   Proteomes; UP000002533; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08071; MPN_DUF2466; 1.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   PANTHER; PTHR30471; PTHR30471; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF04002; RadC; 1.
DR   SMART; SM00278; HhH1; 1.
DR   TIGRFAMs; TIGR00608; radc; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01302; UPF0758; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..243
FT                   /note="UPF0758 protein Ava_0172"
FT                   /id="PRO_1000089789"
FT   DOMAIN          113..235
FT                   /note="MPN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   MOTIF           184..197
FT                   /note="JAMM motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ   SEQUENCE   243 AA;  26475 MW;  FC979A2EBDD79F73 CRC64;
     MTYCLRIADI PTNERPRERL MTHGPKVLAT AELIAILLGT GQGPGKLSAV GLGQYLLQEL
     GKNQRDPLAV LREVTPAELM QIPGIGPAKA TSILAAVELG KRTFQFRPLD KTPIDSPVAA
     VAALSQDLMW QNQERFAVLL LDVKNRLLGT QVITIGTATE TLASPREIFR EIIRQGATRT
     IVAHNHPSGN VEPSPEDIEL TRQLLAGAQL LGIPLLDHLI LGNGNHQSLR EVTTLWNDYP
     QGD