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Database: UniProt
Entry: A0A059LJS7_9CHLO
LinkDB: A0A059LJS7_9CHLO
Original site: A0A059LJS7_9CHLO 
ID   A0A059LJS7_9CHLO        Unreviewed;       359 AA.
AC   A0A059LJS7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
DE   Flags: Fragment;
GN   ORFNames=H632_c1439p0 {ECO:0000313|EMBL:KDD74274.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD74274.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD74274.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD74274.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
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:KDD74274.1}.
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DR   EMBL; AYPS01001439; KDD74274.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LJS7; -.
DR   OrthoDB; 304089at2759; -.
DR   Proteomes; UP000026042; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR32027; CYTOSINE DEAMINASE; 1.
DR   PANTHER; PTHR32027:SF0; CYTOSINE DEAMINASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000026042}.
FT   DOMAIN          57..153
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          200..320
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   REGION          150..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..188
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KDD74274.1"
SQ   SEQUENCE   359 AA;  38752 MW;  1C9AF324C1EA7229 CRC64;
     RVELQGVALV PLSFFRDAAA ARALAKKVAE HGGVLGAAVC CGDRGGFAED EFTTCAADRS
     ELLDRMFELA REMDLDLDFH ADENGNKPAR GLLEIASKTV QHGWQGRVVV GHVCSLAEQP
     HDQLRETLRA AREARLTVVS LPLVNQWTQD RVRRGGGSEG AGSGALGEDG RGGEDGRRDE
     DDENNGTLDK IAARSFSRAP RTPRRRGVTA LQELQAAGVA CALASDNTRD QFYAYGDLDM
     LEVLAQGVRA AHLDRPLGSW VLAGGQTPAR AMRLPGREGL CELRLGGPAD LVLFRARSYS
     ELFARPQADR VVVRGGRPLY LQPPPYEELD WTLEARGEEG GRDSEALKGR GSCGAEAQT
//
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