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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//