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Database: UniProt
Entry: A0A1A0FCF1_9GAMM
LinkDB: A0A1A0FCF1_9GAMM
Original site: A0A1A0FCF1_9GAMM 
ID   A0A1A0FCF1_9GAMM        Unreviewed;       224 AA.
AC   A0A1A0FCF1;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=MPN domain-containing protein {ECO:0000259|PROSITE:PS50249};
GN   ORFNames=ADS46_16695 {ECO:0000313|EMBL:OAZ97213.1};
OS   Halomonas sp. G11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1684425 {ECO:0000313|EMBL:OAZ97213.1, ECO:0000313|Proteomes:UP000092250};
RN   [1] {ECO:0000313|EMBL:OAZ97213.1, ECO:0000313|Proteomes:UP000092250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G11 {ECO:0000313|EMBL:OAZ97213.1,
RC   ECO:0000313|Proteomes:UP000092250};
RA   Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA   Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA   Eddine Masmoudi A.S., Cherif A.;
RT   "Genomic basis for crude oil degradation, heavy metal resistance and high
RT   salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT   Tunisian Chott El-Djerid salt lake.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the UPF0758 family.
CC       {ECO:0000256|RuleBase:RU003797}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAZ97213.1}.
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DR   EMBL; LYXG01000018; OAZ97213.1; -; Genomic_DNA.
DR   RefSeq; WP_066319410.1; NZ_LYXG01000018.1.
DR   AlphaFoldDB; A0A1A0FCF1; -.
DR   OrthoDB; 9804482at2; -.
DR   Proteomes; UP000092250; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08071; MPN_DUF2466; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   InterPro; IPR037518; MPN.
DR   InterPro; IPR025657; RadC_JAB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR001405; UPF0758.
DR   InterPro; IPR020891; UPF0758_CS.
DR   InterPro; IPR046778; UPF0758_N.
DR   NCBIfam; TIGR00608; radc; 1.
DR   PANTHER; PTHR30471; DNA REPAIR PROTEIN RADC; 1.
DR   PANTHER; PTHR30471:SF3; UPF0758 PROTEIN YEES-RELATED; 1.
DR   Pfam; PF04002; RadC; 1.
DR   Pfam; PF20582; UPF0758_N; 1.
DR   SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR   SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR   PROSITE; PS50249; MPN; 1.
DR   PROSITE; PS01302; UPF0758; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          102..224
FT                   /note="MPN"
FT                   /evidence="ECO:0000259|PROSITE:PS50249"
SQ   SEQUENCE   224 AA;  24770 MW;  6902472BBBCDD991 CRC64;
     MGINHWPEGE RPREKLLNLG AQALSDAELL AIFLRVGVQG RSAVDLARDL LASFGGLRQL
     LEADQERFCD ARGLGSAKFA QLQATLELSR RHLAAQLARG EALTSPTLVR HYLSAQLRHL
     GHEEFAVLFL DTQHRIIRYE SLFRGTLDSA SVYPREVAKR ALAHNAGAVI LAHNHPSGVA
     EPSDADRRIT DRLKEALALF DVRVLDHFVV GDGDVVSFAE RGWL
//
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