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Database: UniProt
Entry: A0A094F7W8_9PEZI
LinkDB: A0A094F7W8_9PEZI
Original site: A0A094F7W8_9PEZI 
ID   A0A094F7W8_9PEZI        Unreviewed;       467 AA.
AC   A0A094F7W8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN   ORFNames=V497_06881 {ECO:0000313|EMBL:KFY55532.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY55532.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY55532.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY55532.1}.
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DR   EMBL; JPJZ01001148; KFY55532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094F7W8; -.
DR   STRING; 1420910.A0A094F7W8; -.
DR   HOGENOM; CLU_027272_2_1_1; -.
DR   OrthoDB; 2722228at2759; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000029268; 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:UP000029268}.
FT   DOMAIN          17..312
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          375..442
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   467 AA;  52350 MW;  B1D847182E028D52 CRC64;
     MAEKKADAPA AGMLWGGRFT GAIDPLMHKY NASIRYDKAL YKEDILGSIA FARANSKVGI
     LSEDEFKAIE GGLLQLMEEW KQGTFAIMPN DEDIHTANER RLGEVIGKDI AGKLHTGRSR
     NEQVVCDMRM WLRDRIREID SQLVDFLKVI TTRAEAEIDY LMPGYTHLQR AQPVRWSQWL
     MSYAAAFKQD LERLRQVFER VNLSPLGCGA LAGNVFGIDR DMIAKELGFS GITLNSMNTS
     AERDFLLDFL VWNSIFTNHV SRWAEDLIIY STSEFSFIRL ADAYSTGSSL MPNKFNGDSL
     ELLRGKSGRS FGQMAGLMMT LKGLPSCYNK DLQEGWEPML DSVQTVSDSL GIANGVLATL
     KVRPERMEAA LDKTMLATDV AEWLVRNKCP FREAHHISGR VVALSEKLEI SMDKLTLEQL
     QAIDSRFTAD IVKAFEYETS VEAKSSKGGT SRSAVLEQIQ IVRALLE
//
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