ID A0A165B6V4_9APHY Unreviewed; 561 AA.
AC A0A165B6V4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=PAL-domain-containing protein {ECO:0000313|EMBL:KZT00379.1};
GN ORFNames=LAESUDRAFT_666234 {ECO:0000313|EMBL:KZT00379.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT00379.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT00379.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT00379.1,
RC ECO:0000313|Proteomes:UP000076871};
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 PAL/histidase family.
CC {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR EMBL; KV427687; KZT00379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165B6V4; -.
DR STRING; 1314785.A0A165B6V4; -.
DR InParanoid; A0A165B6V4; -.
DR OrthoDB; 1030318at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016841; F:ammonia-lyase activity; IEA:InterPro.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:InterPro.
DR CDD; cd00332; PAL-HAL; 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 InterPro; IPR001106; Aromatic_Lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR005922; Phe_NH3-lyase.
DR InterPro; IPR023144; Phe_NH3-lyase_shielding_dom_sf.
DR NCBIfam; TIGR01226; phe_am_lyase; 1.
DR PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR PANTHER; PTHR10362:SF80; PHENYLALANINE AMMONIA-LYASE 2; 1.
DR Pfam; PF00221; Lyase_aromatic; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU003954};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
SQ SEQUENCE 561 AA; 61215 MW; 4D28EFDFB14AE623 CRC64;
MPESWVRGAI AIRINALIRG HSGCRWVVID ALQKLLAANV IPCPPLRQTI SASGDLGPLA
YIASALTGDR DCAVWDGEGK DRRIISSSVA LERHAISAIE FLPKEGLAVV NGTAPSCSVS
ALAIHDAHFL LLLSQATTAM CVEALLGALE SFHPFLHDVA RPHPGQIEVA ANIRRALAQS
RLVTQHVEGK AGDRLRQDRY SLRTAPQWIG PQVEELLSSH QTILTEINST TDNPILDASN
GRTTSFSGGN FQGTSLTIAM EKTRIALQHV GAIAYAQMVE LGSPHMSRGL APDVAANEPS
IDYGQKAMDM ACASYLAELS FISSTVSNHV QPAEMHNQSV NSLALISARY TMTAVQLTQM
IMANLLLSLC QAVDLRAMYK CFFDKLDGHI RTSLLATIQP ALSPLKVQEM TTLLRQQAEG
SFRETGTLDS GERFYVMCKP LVADVSSYLS TLTQEPNAFE QRHFDAHTFH VQLAASLSDA
WISNRSSFFD NGSAEELLGV GTRQLYRWVR QDLGVRMRRG IDFDEEGTDA VVSRIYAAIV
QGDVNNVLVK MFRDGDLELS V
//
