ID J9IGB2_9SPIT Unreviewed; 854 AA.
AC J9IGB2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE SubName: Full=Histidine ammonia-lyase {ECO:0000313|EMBL:EJY79937.1};
GN ORFNames=OXYTRI_22783 {ECO:0000313|EMBL:EJY79937.1};
OS Oxytricha trifallax.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY79937.1};
RN [1] {ECO:0000313|EMBL:EJY79937.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JRB310 {ECO:0000313|EMBL:EJY79937.1};
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:EJY79937.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMCR01008205; EJY79937.1; -; Genomic_DNA.
DR AlphaFoldDB; J9IGB2; -.
DR EnsemblProtists; EJY79937; EJY79937; OXYTRI_22783.
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:EJY79937.1}.
FT REGION 246..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 96307 MW; BB9B7B5E90A0F186 CRC64;
MESLTNQDIF YPKEAKFKNS MFLVLNESLR LQCFPKLSTV SAMLHMIETL DQSHLYDASH
IDVSDGKRYG LPREFDVHGR TFLAFIYSMI HEYTKRGSRK LVPFVDDIQS FLDIFYMGHL
HLNESQLQSP QIVDSEHQAT TQSNLNKLFD LLCFSDSKNL EEAEIQLQII KWIQDFVKQF
LSVLQKSSQE NNSLQSLYKD AHFILSSISI LSQTAAKFIK NKKIDFNMTQ KKTFNFELRD
NVDRVEEKKQ GTHSNNSTII PKPKSVGTKI GNERYQREII LPEDDFEIME MQLRNDDLRK
FFISELGYHF YEDQHEEKAI IPLNGHDLTL EKLSLLGRGQ SKIQLDDKTW KKLRATRDVV
ERLAKEPNEK PYYGINSGVG IFSNKKLTGQ ELKEFQVNLI RSHATGIGEN LDLDPARRIL
VLRINTLAKG LSGISINTME RLIEFYNSGI VPQIPSCGSV GASGDLVPLS HIGLNLIGEG
EIWNPTTASY ENAVSVLREY DLKIAQLAEK DALSLINGNQ FICGVGSVAL EKSINIIKSI
APISALTFLS MKGSPLSFDL TLQRMRMHPG QAAIAAMMRE LLPAGKTVTH SAEIQDPYSL
KCIPQVHGPT LEAVVLTKDC LEIEMNSGSD NPMIFTEAPY LVSGGNFHGE YPAKQLDVLG
LYVHEIGSLS SQRIKRLTNP TKNLGLPAFL VSQGGLCSGM MTWENVAASL VSENKVLVYP
ASADSAETCA DKEDHVSMGS FSAKKAIMIA DNVLQILAVE LLGATQALQH RYQLEKDFDI
YHPGLKNIFE MSKKISPILE KDRYTQPEYQ ELLEFISSGD LYDAVLEEMS NDWVNYDYAN
NVYDNPEIRK RILQ
//
