ID V9G2J1_PHYPR Unreviewed; 461 AA.
AC V9G2J1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Argininosuccinate lyase {ECO:0000313|EMBL:ETI57691.1};
GN ORFNames=F443_00049 {ECO:0000313|EMBL:ETI57691.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI57691.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI57691.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI57691.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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:ETI57691.1}.
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DR EMBL; ANIZ01000011; ETI57691.1; -; Genomic_DNA.
DR AlphaFoldDB; V9G2J1; -.
DR EnsemblProtists; ETI57691; ETI57691; F443_00049.
DR eggNOG; KOG1316; Eukaryota.
DR HOGENOM; CLU_027272_2_1_1; -.
DR OrthoDB; 2722228at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:ETI57691.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT DOMAIN 14..306
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 369..436
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 461 AA; 50828 MW; AF00EC67ABE296B7 CRC64;
MTDAPKEAKK LWGGRFRGNV DPVMNKFNES LSVDKRMWRV DLDGSQAYAR ALEKSGVLTT
AEVDQIVAGL DKVGEEWAAG TFQPKDGDED IHTANERRLT EIIGAVGGKL HTGRSRNDQV
ATDVRLYLKR TIVGIQDGLK ELIGTANQLA ENNIDLLMPG FTHLQPAQPL RFSHWVLSHG
AALLRDADRL ADLTKRVDYM PLGNGALAGN SFGLDREALA KSLGFANVTP NSLDGVCDRD
FIAEFLFWAS MLMVHLSQLS EDLIIYNTLK FVTMADAYST GSSLMPQKKN PDALELLRGK
SGTVIGRLNG FLVTLKGLPR SYNKDLQEDK TALFDVVDTI QDCLQIATGV LATMTPHGDK
MRSFLVTEML ATDLAEYLVR KGVPFRETHH VAGAAVRLAE DKNKPLSTLT FEELSTLHPK
FEEDVLEVWN FDVSVERKNV TGGTSKSAVQ KQIADIKAWL A
//