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Database: UniProt
Entry: J9IIE3_9SPIT
LinkDB: J9IIE3_9SPIT
Original site: J9IIE3_9SPIT 
ID   J9IIE3_9SPIT            Unreviewed;       911 AA.
AC   J9IIE3;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 25.
DE   SubName: Full=Histidine ammonia-lyase {ECO:0000313|EMBL:EJY74423.1};
GN   ORFNames=OXYTRI_04321 {ECO:0000313|EMBL:EJY74423.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY74423.1};
RN   [1] {ECO:0000313|EMBL:EJY74423.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY74423.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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:EJY74423.1}.
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DR   EMBL; AMCR01013254; EJY74423.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9IIE3; -.
DR   EnsemblProtists; EJY74423; EJY74423; OXYTRI_04321.
DR   OrthoDB; 1030318at2759; -.
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); 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   PANTHER; PTHR10362; HISTIDINE AMMONIA-LYASE; 1.
DR   PANTHER; PTHR10362:SF7; HISTIDINE AMMONIA-LYASE; 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:0000313|EMBL:EJY74423.1}.
FT   REGION          252..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   911 AA;  102303 MW;  AF922FBD8AFFD356 CRC64;
     MQQTNSFKIN QLLLIKKITN SSVDSLDQAK VNSIYWIFDY ALLKARFPKL DTLCAIYCKM
     LEKEKMLQKD DKLPNDMNRL DVGHEESGQR VDLPSGYESY GKIILAFVHG LIYEDFTLEQ
     SRGHSPLLEK LNNMLFNFGM QHMMLGPQEV VFDLKLQELY SSARNTNNLF EEVLRFMSQV
     EIQNLVHMKK QQQIIHWIVT FCEKFLDILK ESVNENLSLF RLEDDAFPIM KSLIRLGQES
     LRTLNKKINV AAQRGDSEEE EKQHNANQND VIGSEQDQID AAEKGSNANS SSSDETEFQI
     VNAYKHPLES GSNYKPCRSF VVPDSERSIY STMNDGVQLR TLIDSLGYQI RDYEEIASKV
     AREKSDWQPL KQQKQSIIPL NGHDLTLEKL SLLGRGQSKI QIDDKTWKKL RATRDVVERL
     AKEPNEKPYY GINSGVGIFS NKKLTGQELK EFQVNLIRSH ATGIGENLDL DPARRILVLR
     INTLAKGLSG ISINTMERLI EFYNSGIVPQ IPSCGSVGAS GDLVPLSHIG LNLIGEGEIW
     NPTTASYENA VSVLREYDLK IAQLAEKDAL SLINGNQFIC GVGSVALEKS INIIKSIAPI
     SALTFLSMKG SPLSFDLTLQ RMRMHPGQAA IAAMMRELLP AGKTVTHSAE IQDPYSLKCI
     PQVHGPTLEA VVLTKDCLEI EMNSGSDNPM IFTEAPYLVS GGNFHGEYPA KQLDVLGLYV
     HEIGSLSSQR IKRLTNPTKN LGLPAFLVSQ GGLCSGMMTW ENVAASLVSE NKVLVYPASA
     DSAETCADKE DHVSMGSFSA KKAIMIADNV LQILAVELLG ATQALQHRYQ LEKDFDIYHP
     GLKNIFEMSK KISPILEKDR YTQPEYQELL EFISSGDLYD AVLEEMSNDW VNYDYANNVY
     DNPEIRKRIL Q
//
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