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Database: UniProt
Entry: A0A0F8VSS8_9EURO
LinkDB: A0A0F8VSS8_9EURO
Original site: A0A0F8VSS8_9EURO 
ID   A0A0F8VSS8_9EURO        Unreviewed;       473 AA.
AC   A0A0F8VSS8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN   ORFNames=ARAM_003062 {ECO:0000313|EMBL:KKK26291.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26291.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK26291.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26291.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) 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:KKK26291.1}.
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DR   EMBL; JZBS01000478; KKK26291.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8VSS8; -.
DR   STRING; 308745.A0A0F8VSS8; -.
DR   OrthoDB; 2722228at2759; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000034291; 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   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          26..319
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          382..449
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   473 AA;  52839 MW;  430240F502F4087A CRC64;
     MSGPKAVAEN MLWGGRFTRL TTFTRFVEGL DPLMVQYNQS LPYDRILWRQ DIAGSIAFAR
     ANAKTGILSA REFSEIERGF RQIAEEWSTN TFVIQENDED IHTANERRLS EIIGKEIGGK
     LHTGRSRNEQ IATDMRLWLR DELRKLEGFL SDLVKVSIAR AESEIDYLMP GYTHLQKAQP
     VRWAHWLLSH ATAFADELKR LREVTKRVNR SPLGTGALAG NPFHIDREAM AKELGFDGLL
     YNSMNAVGDR DFAMETMQWG SSFMLKISRW AEDLIIYSSL EFGYVRLSDA YSTGSSLMPQ
     KKNADSLELL RGKAGRAFGH MAGLMCTIKG LPTTYNKDLQ ESVEPLLDHI KTVGDSIQIA
     TGVLSTLTVI PEKMVAALTP EMLATEFADY LVRKGVPFRE GHHISGRVVA LAESTGVPMD
     QLSLAQLKGI DARFGDDVRT CLDYERAVEL KDAIGGCSKR AVLEQTSVLK GLL
//
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