ID A0A1R3ILT2_COCAP Unreviewed; 1204 AA.
AC A0A1R3ILT2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN ORFNames=CCACVL1_11364 {ECO:0000313|EMBL:OMO83532.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO83532.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO83532.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO83532.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a
CC primary hydroxy group in a similar glucan chain.; EC=2.4.1.18;
CC Evidence={ECO:0000256|ARBA:ARBA00000826};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC {ECO:0000256|ARBA:ARBA00004602}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. GlgB
CC subfamily. {ECO:0000256|ARBA:ARBA00009000}.
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:OMO83532.1}.
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DR EMBL; AWWV01009857; OMO83532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3ILT2; -.
DR STRING; 210143.A0A1R3ILT2; -.
DR EnsemblPlants; OMO83532; OMO83532; CCACVL1_11364.
DR Gramene; OMO83532; OMO83532; CCACVL1_11364.
DR OMA; AYWTETR; -.
DR OrthoDB; 349883at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0102752; F:1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis); IEA:UniProtKB-EC.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00593; RIBOc; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF4; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME 3, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF14709; DND1_DSRM; 1.
DR Pfam; PF00636; Ribonuclease_3; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00358; DSRM; 2.
DR SMART; SM00535; RIBOc; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 1.
PE 3: Inferred from homology;
KW Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW Plastid {ECO:0000256|ARBA:ARBA00023234};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 874..1016
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1127..1200
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 42..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1204 AA; 137519 MW; C840205C382A6BC5 CRC64;
MTSLSLQPKI SLYPNNPILH FRPQNKPQII FFPRKIKVKT RCSSMDPQRQ KQQESYSKKK
SSVAETEKGV DPVGFLTKLG ITHKAFAQFL RERHKSMKDL KATIFTRHLN LQELASGFEI
LGMHRHKEHR VDFMDWAPGA RYCALVGSFN GWSPTENAAR EGHFGHDDYG YWFIVLEDKL
REGEKPDELY FQQYNYVDDY DKGDSGVTIE EVFKRANDEY WEPGEDRFIK NRFELPAKLY
ERLFGPNGPQ TLEEFEEIAD PETRYKAWKE QHKNDPPSNL PPFDVIDNGK EYDVFNIVAS
PEWQEKFRAK KPPLPYWIET RKGRKAWLKK YHPAIPHGSK YRVYFNTPDG PLERVPAWAT
FVEPDAEGNQ AYAVHWEPPP ELTYKWKNKA PKVPKSLRIY ECHVGISGSE PKIASFNDFT
EKVLPHIKEA GYNAIQLIGT IEHKDYFTVG YRVTNLFAVS SRYGTPEDFK RLVDEAHGLG
LLVLLDIVHS YSAADEMVGL ARFDGSNDCY FHSGKRGYHK CWGTRMFKYG DLDVLHFLLS
NLNWWISEYK IDGFQFHSLA SMLYTHNGFA SFTGDLEEYC NQYVDKDALM YLILANEILH
VLHPNIITIA EDATFYPGLC EPTSQGGLGF DYYVNLSASE MWSSLLESTP DHEWSMSKII
SVLLGNRQYA NKMIIYAENH NQSISGGWSL AEILLGQGND QAPLSDELLR RGSSLIKDLM
NLDENERLLS RRLPTIHHVN DSNMVISYIR GPFLFIFNFH PSNSYQGYCV GVDEAGEYQV
ILNTDEIKYG GQGFIKEEQY LQRTISRRVD GQQNCLEVPL PSRTAQVDSN FTSPMNQFFP
KVDADRYTYF HAPPISYNHV NNCPSPSPSM VASIAAVERI LNYSFRNKRL LEEALTHPSY
SDSASYQRLE FLGDAVLGLA FTNHVFLVYP KLEPGQLSLI RAANISTEKL ARVAIKHRLF
QFVRQNATGL HDKVREFAEA VSQEEDAISY GGSIKAPKVL ADIVESLAAA VYVDINFDLI
KLWEIIGGLL EPIATLEDLQ QQPQPVTVLF EHCQKLGKHV DIKHWKKGLT NITSVYVDGE
FVASGSSEQK QISKLNAVKG ALHKLSQSMS AKIDADDGIN EPFEIEGAKQ KLHELCFKKK
WERPIYELEK DEGLPHEKKF VSSVKVPTVD GILYITGEEK ARVKEAENSA ASFMIRALQE
SNYL
//
