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Database: UniProt
Entry: R1GWI4_BOTPV
LinkDB: R1GWI4_BOTPV
Original site: R1GWI4_BOTPV 
ID   R1GWI4_BOTPV            Unreviewed;       725 AA.
AC   R1GWI4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Putative phenylalanine ammonia-lyase protein {ECO:0000313|EMBL:EOD50449.1};
GN   ORFNames=UCRNP2_2780 {ECO:0000313|EMBL:EOD50449.1};
OS   Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS   (Neofusicoccum parvum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Neofusicoccum.
OX   NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD50449.1, ECO:0000313|Proteomes:UP000013521};
RN   [1] {ECO:0000313|Proteomes:UP000013521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX   PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT   vascular pathogen associated with grapevine cankers.";
RL   Genome Announc. 1:E0033913-E0033913(2013).
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {ECO:0000256|ARBA:ARBA00007238, ECO:0000256|RuleBase:RU003954}.
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DR   EMBL; KB915980; EOD50449.1; -; Genomic_DNA.
DR   RefSeq; XP_007582081.1; XM_007582019.1.
DR   AlphaFoldDB; R1GWI4; -.
DR   STRING; 1287680.R1GWI4; -.
DR   KEGG; npa:UCRNP2_2780; -.
DR   eggNOG; KOG0222; Eukaryota.
DR   HOGENOM; CLU_014801_3_1_1; -.
DR   OMA; GNFHGDY; -.
DR   OrthoDB; 1030318at2759; -.
DR   Proteomes; UP000013521; 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; IPR022313; Phe/His_NH3-lyase_AS.
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.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|RuleBase:RU003954, ECO:0000313|EMBL:EOD50449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013521}.
SQ   SEQUENCE   725 AA;  77711 MW;  3756F441F8770AAE CRC64;
     MGDHRIPADL AAMAAAAHAR STHTSWSCLQ ADKLSGGSTI VLDGQSLTIA QLVAVAKHGS
     QPVLDKSPSI INRIDKSVEM LKRHLGRGDL VYGVNTGYGG SADVRTDDVY SLQQALVQHQ
     QSGVLTINDT ARSLLGPNQA ALRQPEDFGS LSMPTSWVKG LMVSRVNSII RGHSAVSLPV
     IEAIMAFLHH DITPVIPLRG SISASGDLQP LAYVAGALEG SPDIFVRVGG NPPVIMSASE
     ALKSYNLRPV VLAAKEGLGL LNGTAASVSA ASLAIYEANH LALLTQALTA MGVEALCGTA
     ESFSPFIANV RPHRGQVEAA ANIHGFLQGS RLASGLEAQG QKDMHISGLC QDRYPLRTSS
     QWIGPQLEDL LLANEQISVE LNSTTDNPLI DAEADTIYHG GNFQAASITS AMEKVRTSIQ
     MLGKLLFAQG VELINSNLNR GLPPNLAADD PSLSFACKGI DINLAAYMSE LGYLANPVSS
     HVQSAELHNQ AVNSLALISA RYTLQSIEVL SQMCAAYLFA LCQALDLRVL QAEFLAEAYP
     LFTVAATAAL DRAKDSAAAD GPEKLLNEVW NALKDTWNAS TSMDLAPRAE KSARAAVLVF
     QYRVGCASTL VHELEAELAQ TLQRTYAQLR DRMFAQHEVI TPQYLGSAAS KMYAFVRGEL
     RVKFHRGLVE YPNYVVKTEE GAPKPSLPVE ERRIIGSEVS VIYEALRAGL LHRPVMEALN
     QNGIF
//
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