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Database: UniProt
Entry: A0A2T7NU39_POMCA
LinkDB: A0A2T7NU39_POMCA
Original site: A0A2T7NU39_POMCA 
ID   A0A2T7NU39_POMCA        Unreviewed;       590 AA.
AC   A0A2T7NU39;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 14.
DE   RecName: Full=Par3/HAL N-terminal domain-containing protein {ECO:0000259|Pfam:PF12053};
GN   ORFNames=C0Q70_15175 {ECO:0000313|EMBL:PVD24690.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD24690.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD24690.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD24690.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD24690.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the PAL/histidase family.
CC       {ECO:0000256|ARBA:ARBA00007238}.
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:PVD24690.1}.
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DR   EMBL; PZQS01000009; PVD24690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7NU39; -.
DR   STRING; 400727.A0A2T7NU39; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg9.
DR   GO; GO:0016841; F:ammonia-lyase activity; IEA:InterPro.
DR   CDD; cd00332; PAL-HAL; 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 2.
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; IPR021922; Par3/HAL_N.
DR   InterPro; IPR022313; Phe/His_NH3-lyase_AS.
DR   PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR   PANTHER; PTHR10362:SF7; HISTIDINE AMMONIA-LYASE; 1.
DR   Pfam; PF00221; Lyase_aromatic; 2.
DR   Pfam; PF12053; Par3_HAL_N_term; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00488; PAL_HISTIDASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          1..75
FT                   /note="Par3/HAL N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12053"
SQ   SEQUENCE   590 AA;  65008 MW;  D56D4641D56E9956 CRC64;
     MKLSVRVRGD WFAVPCKGNE RLQWLGEETL RRYYKSRGGS GCAEEKVYEV RKAKGGAILD
     PDDLIKDVLD DDDFVTVGKF ISLDGNSLST DDLMRLGKGE YLIKLTVDAI QKVQKSRDLV
     DDILDSNQGV GPGLSPERTR MLLALRINVL AKGYSGISLE TLQQYIAAFN SSCLPWVPEK
     GTVGASGDLA PLSHLALGMI GEGKMWSPKS GWAEAKYVLE SHNLTPIKLK PKEGLALING
     TQLITSLGAE AVERSEAIAR QADVIAAMSL EVLKGTSRAF DSKIQAVRPH KGQIKVARQL
     RALLALGHLP VGGGRKSQIL QPCARRLHTQ VLPPGGNFHG EYPAKVLDYL AIAVHELSNM
     SERRLERLIN PALSELPAFL TPDGGLNSGF MIAHCTAAAL VSENKVLCHP ASVDSLTTSA
     GTEDHVSMGG FSARKCLRVV EHVEQVLAIE LLAACQALEF LRPLKTTAPL EEVHRLVRTL
     VKPWAKDRFM APDIDAITKL LQEEKIWHKV KPMIDHYHSV PKHRDTCFLP NHDPHQQSTT
     EWTDRRQASP YDSHFLLHQE GLRRQNLLYD GLKGGKAVIT MVKKKSISSN
//
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