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Database: UniProt
Entry: F1LGE3_ASCSU
LinkDB: F1LGE3_ASCSU
Original site: F1LGE3_ASCSU 
ID   F1LGE3_ASCSU            Unreviewed;       140 AA.
AC   F1LGE3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   13-SEP-2023, entry version 31.
DE   SubName: Full=Arginine deiminase {ECO:0000313|EMBL:ADY49197.1};
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY49197.1};
RN   [1] {ECO:0000313|EMBL:ADY49197.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21685128; DOI=10.1101/gr.121426.111;
RA   Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA   Davis R.E.;
RT   "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT   functional diversification, and novel developmental profiles.";
RL   Genome Res. 21:1462-1477(2011).
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DR   EMBL; JI214696; ADY49197.1; -; mRNA.
DR   AlphaFoldDB; F1LGE3; -.
DR   GO; GO:0016990; F:arginine deiminase activity; IEA:InterPro.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   InterPro; IPR003876; Arg_deiminase.
DR   PANTHER; PTHR47271; ARGININE DEIMINASE; 1.
DR   PANTHER; PTHR47271:SF2; ARGININE DEIMINASE; 1.
DR   Pfam; PF02274; ADI; 1.
DR   PRINTS; PR01466; ARGDEIMINASE.
DR   SUPFAM; SSF55909; Pentein; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   REGION          117..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   140 AA;  15535 MW;  EC5C895163EEEBEA CRC64;
     MHLDTVFTQV DKDKFSVHPD AINEGMRIKV YKKDGDAVRI EEKQNVNLEE LLAEATGNDK
     VTLIPCGAGD PIASMREQWN DGANTLAIAP GEVVVYSRNP ITNEELRKQG IKVHVMSSSE
     LSRGRGGPRC MSMPLEREEL
//
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