ID A0A165IEL2_9BASI Unreviewed; 463 AA.
AC A0A165IEL2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN ORFNames=CALCODRAFT_429307 {ECO:0000313|EMBL:KZT60470.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT60470.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT60470.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT60470.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR EMBL; KV423931; KZT60470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165IEL2; -.
DR STRING; 1353952.A0A165IEL2; -.
DR InParanoid; A0A165IEL2; -.
DR OrthoDB; 2722228at2759; -.
DR Proteomes; UP000076842; 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:KZT60470.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT DOMAIN 13..307
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 370..437
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 463 AA; 51934 MW; 4864830A0AB9045C CRC64;
MSDLPTKQKL WGGRFTGKTD PLMHEFNQSL KYDKRMYAVD IKGSIAYAKA NCQKGILTKD
EEAKMVAGLN AVLKEWEEGK FVIEADDEDI HTANERRLSE LIGPLGGKLH TGRSRNDQVA
TDMRMWLLDE VQNIEEALKD FLRVLTERAD KEVSVLMPGY THLQRGQPIR WSHFLCYHAF
SFASDLDRLR QLIPRISVLP LGSGALAGNP FSIDREFLRS ELGFASIAEN SMWGVADRDF
IVEFMMWASL CMTHMSRFAE DLIIYSTAEF GFVTLSDAYS TGSSIMPQKK NPDSLELLRG
KSGRVFGNMA GFMMTLKGLP ATYNKDLQED KEPLFDTVDN MAACLRIAEG VIATLNIHPE
KMQAALTMDM LATDLADYLV RKGTPFRETH HISGRAVALA EQLQIPLSEL TLAQYKELSG
KFEPDVKDVF DFEASVERRN AIGGPSKEMI ARQVGVLRGL IGK
//
