ID A0A0V0SIR0_9BILA Unreviewed; 1456 AA.
AC A0A0V0SIR0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=1,4-alpha-glucan branching enzyme {ECO:0000256|ARBA:ARBA00012541};
DE EC=2.4.1.18 {ECO:0000256|ARBA:ARBA00012541};
GN Name=GBE1 {ECO:0000313|EMBL:KRX26339.1};
GN ORFNames=T07_10175 {ECO:0000313|EMBL:KRX26339.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX26339.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX26339.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX26339.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- 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:KRX26339.1}.
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; JYDL01000008; KRX26339.1; -; Genomic_DNA.
DR Proteomes; UP000054630; Unassembled WGS sequence.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11321; AmyAc_bac_euk_BE; 1.
DR CDD; cd02854; E_set_GBE_euk_N; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR025946; CABIT_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 PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF3; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF12736; CABIT; 1.
DR Pfam; PF02922; CBM_48; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1005..1341
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 83..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1456 AA; 163615 MW; 4AA4DACF72DE913D CRC64;
MERNVENNFS TEIIFIFLGF QIFIEKEIKT CQSIRKDKLD PHTMQHAVCS VLINFTILLS
SLQDGDSVDL DFRGSGVKRQ RSDGWLVGRS GGRPSANRNE QPIREQVLPT TGPVDNGRQT
QPPGLVDQSV RFRADRPSVS RLARALSKWE STDDAGKKRK FPSPDSGRVE KRPTSGVIVG
KLAGWSRTMR VTAETPLLTT VKWDVENAPF LNEFVDRYPL PHVALVTKGQ HLGVGLPNVS
NPTLKPYLLA YAKQRSRKLL GTLVKIKDGK RSALSAASVA IPLEYGGYFE ILSEDGHRPP
CFETVGELAA HTAVDQCLVR QRCKAYLPDA DGELKTLRRS RAVLAGEVLT VVGQFRLKRV
WFLRCFDEAG RSLFFKAHHK GRFSALAKAE SVGGVHTAAS LASKRLPLTV RLVHGHCPAE
VAKLAGSAEL IIRLRSVYEE QFLLAYCLQK SEGQLLSIPL NAHLKLAPAV NYPQMVVHPE
FRQLCAYCAK LAPSFSNRLS LLHQPDQLTT RASAFHINDA DENSSGGGSW CRSRSRSGSR
SGSGSWSAAT VDQDEHELQA LYDCIRAAPT RNGDGDRSWS SRLVVERPTM VDDWPDAGRR
QLCYHCHCAD SSGCDSTAPP PPPPQPLPPP PTLPLQPPQP LPLPLLLSAT TATTTAAAAA
AVTPRRRHTA ARPRPKSLFL PDTSRFFYPI APFTSPSTPV YSKPRRPTGC ELTTVAQPYH
SAFTTTYRPP PYPAYAAVYT AYEVLFFCVL TSGSVLMGSV FSSIGDAFSS LCEGFNAIFA
EIGKIPECCG CLRGLSEVEN IDIIMSDRPP FLNNLLQLDG YLKNYENEIC RRYGEFKRLV
MQINKEEGGL DKFSRGYEKF GVVVTPENGV FCQEWAPGAD GLFLIGDFNN WDRTAHPYDR
KDFGKWELYI PPNADGSCPI PHKSVLKIMV AKDGGFCDKI SPWATYVCCP SDSIVYHHVF
YNPPQKYKFL YNKPEKPVAL RIYECHIGIS SPEGKVASYV YFTNNIIPRI VKQGYNAIQV
MAVMEHAYYA SFGYQVTNFF AASSRYGTPC DLKFLVDKAH ELGIFVLLDI VHSHASKNTA
DGLNQRETLR FLLSNLRWWI EEYHFDGFRF DGVTSMIYHS HGLGPGFSGH YDEYFGLSVD
TESLLYLTTA NYMLHKFYPS VVTIAEEVSG MPALCRPVEE GGQGFDYRLA MAIPDKWIKL
LKHYRDEDWN MGDLVFTLEN RRYGEKNIAY AESHDQALVG DKTIAFWLMD KEMYTEMSTL
CPLNSTIDRG IALHKMIRLI THGLGGEGWL NFMGNEFGHP EWLDFPRQGN NSSYHYCRRQ
WNLVDDPLLR YKFLNNWDRA MNLAEEKYHW LSAGPAYTSW KHEQDKVIAF ERANLLFVFN
FHVNKSYTDY KIGVNKSGKY KMILDSDAEE FGGHQRLDSS CEWFTFPHEY ANRANHLCVY
APSRCCFVLA LDSDLS
//
