ID   A0A2P5ES45_TREOI        Unreviewed;      1276 AA.
AC   A0A2P5ES45;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=1,4-alpha-glucan-branching enzyme {ECO:0000313|EMBL:PON88358.1};
GN   ORFNames=TorRG33x02_159450 {ECO:0000313|EMBL:PON88358.1};
OS   Trema orientale (Charcoal tree) (Celtis orientalis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Trema.
OX   NCBI_TaxID=63057 {ECO:0000313|EMBL:PON88358.1, ECO:0000313|Proteomes:UP000237000};
RN   [1] {ECO:0000313|Proteomes:UP000237000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. RG33-2 {ECO:0000313|Proteomes:UP000237000};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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:PON88358.1}.
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DR   EMBL; JXTC01000107; PON88358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5ES45; -.
DR   STRING; 63057.A0A2P5ES45; -.
DR   InParanoid; A0A2P5ES45; -.
DR   OrthoDB; 1122263at2759; -.
DR   Proteomes; UP000237000; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   Gene3D; 2.60.40.3440; -; 1.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR044801; Filamin.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR38537; JITTERBUG, ISOFORM N; 1.
DR   PANTHER; PTHR38537:SF8; PROTEIN GAMETE EXPRESSED 2; 1.
DR   Pfam; PF17963; Big_9; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF81296; E set domains; 3.
DR   SUPFAM; SSF56529; FAH; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237000};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1276
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015176350"
FT   TRANSMEM        1003..1034
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REPEAT          564..602
FT                   /note="Filamin"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT   DOMAIN          1070..1266
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   1276 AA;  140508 MW;  9A1E437D9249D3D3 CRC64;
     MAVRMGVCIL ITIMALPFRF KLSNPQEVKG KPEFAFSWLN DKDTYKAGDI ATIKIKVLNN
     FDKLDKNAFK PTLSVSGKTG NSSYVSGVLT DLEGNPDDWN VFFTTITAGL FNVMINEDRY
     QVFDSSLHFQ VEPGRIYPSI CFASWMGYVN EFEAGARARV LILPKDAFGN NVTSTGEDPS
     SHNLTLSALY GNGSVADSPN VTRIGWNGSG YISIEFIVVK AGDFLLLVRS GNQALSGTPL
     PFKVNPGPLE VSNCVTKWNY EPNAWQLFSK MELFIHQQDQ YGNLVPGLYE FDAEVVEKET
     NLSIPVPDLY FEEVEPGIQL FSFSNLEPGN FLLKISDIKH NKSISNMPYA YTVFVGYCNG
     SNCVVNGTGL NNSVAGEVAE LSIYLRDSFL YPSPVEVERP QVQITREIDS YNVLPVIAPM
     QIINDSELAR GLRYGSNQAE VAPSPSVNLS DPSVGNLSVL ATSFNVTYTP DKSGIYSIRV
     FCGNIMLNGG HSFIKEVRAG EVNISLSGVV KFAPKVPKLI KNEVVVQLMD SFHNPVMSQQ
     SRLKLEVASS MKNTSGFSSS MFLDNNDGSY TGHYTAKDTG TYQICASFDG KRFSPCPFEV
     NVYSSEYFPR AFDDAISVWE DESTAFDALA NDFFAGDNAT ILEFSEPSHG SLLQYGRLLR
     YTPQKDYYGN DSFMYTISDI NGNLATASVN ISVLTIPPQF VSFPSQLQAT EDELSPKFGG
     FSGFEIRYSD MRENISVNLS AQSGTISLSP MPIQFWPIKN RLSVYKGDGE AKCLVLEGTV
     EVVNYALKSI QYFGNENFFG SDTVRISTRN TNGVNNMDVP VFLDPINDPP FINIPEFIIL
     KSNEEESLIY DSERDKFKFL IGDPDLQGFS GDDSFFMVIF SVEVDSGFLV TSLPAELINT
     TELRTMNSYR WQPLQTYVTI SKHFTVKANG IRFKGTINDC NSVMKQLFYN GGYHGTILTV
     TVNDMGNYGC YPDCSENVSV PLYAEANVNL IRRRPMSSFV SHALGSAIVI ESIVVLTLGV
     VLLSFTCKCA IVLVNERRNN AMLSTKIPEA ASLKGTAMAA SENPVKVGTK IVAVGRNYAA
     HAKELGNAVP KEPMLFLKPT SSYLEAGGTI EIPQPLEWLD HDVELAVVIG KRARDVPEDS
     AMDYVAGYAL ALDMTARQIQ APAKSAGLPW DIAKGQDTFT PISSFLPKAS VADPENLELW
     LKVDGEVKQQ GSTKDMIFKI PFLISHISSF MTLFEGDVIL TGTPEGVGPV KAGQKITAGI
     TNLLDVNFNV EKRKRQ
//