ID L9YZG8_9EURY Unreviewed; 191 AA.
AC L9YZG8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Phosphoesterase {ECO:0000256|RuleBase:RU362039};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU362039};
GN ORFNames=C486_12628 {ECO:0000313|EMBL:ELY78882.1};
OS Natrinema gari JCM 14663.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230459 {ECO:0000313|EMBL:ELY78882.1, ECO:0000313|Proteomes:UP000011592};
RN [1] {ECO:0000313|EMBL:ELY78882.1, ECO:0000313|Proteomes:UP000011592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14663 {ECO:0000313|EMBL:ELY78882.1,
RC ECO:0000313|Proteomes:UP000011592};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU362039};
CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. YfcE
CC family. {ECO:0000256|ARBA:ARBA00008950, ECO:0000256|RuleBase:RU362039}.
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:ELY78882.1}.
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DR EMBL; AOIJ01000053; ELY78882.1; -; Genomic_DNA.
DR RefSeq; WP_008456468.1; NZ_AOIJ01000053.1.
DR AlphaFoldDB; L9YZG8; -.
DR PATRIC; fig|1230459.4.peg.2519; -.
DR Proteomes; UP000011592; Unassembled WGS sequence.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00841; MPP_YfcE; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041802; MPP_YfcE.
DR InterPro; IPR020935; PdiEstase_YfcE_CS.
DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29.
DR NCBIfam; TIGR00040; yfcE; 1.
DR PANTHER; PTHR11124:SF12; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 29; 1.
DR PANTHER; PTHR11124; VACUOLAR SORTING PROTEIN VPS29; 1.
DR Pfam; PF12850; Metallophos_2; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS01269; UPF0025; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|RuleBase:RU362039};
KW Nuclease {ECO:0000256|ARBA:ARBA00022839}.
FT DOMAIN 2..144
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF12850"
FT REGION 168..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 191 AA; 20490 MW; 85C31D9492150A0D CRC64;
MIAIFSDTHS SRGHELEGDA LTAAREADTV IHAGDFTTEA ALEAFRTECD RLYAVHGNAD
NGVVRDRLPT ARVVEAGGVR FAVTHRRDGG ETGLAMFGRS RGADVVVFGH SHRPTVVESD
TVQLLNPGSH ADPRGNRPGF AVLEERPDGG LAGEIRDPDG TVIETVRILG ETGTPAEDDD
RSESHGQRED R
//
