ID A0A061DD95_BABBI Unreviewed; 968 AA.
AC A0A061DD95;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Trehalose-6-phosphate synthase domain containing protein, putative {ECO:0000313|EMBL:CDR96075.1};
GN ORFNames=BBBOND_0212170 {ECO:0000313|EMBL:CDR96075.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR96075.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RA Aslett M., De Silva N.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR EMBL; LK391708; CDR96075.1; -; Genomic_DNA.
DR RefSeq; XP_012768261.1; XM_012912807.1.
DR AlphaFoldDB; A0A061DD95; -.
DR SMR; A0A061DD95; -.
DR STRING; 5866.A0A061DD95; -.
DR EnsemblProtists; CDR96075; CDR96075; BBBOND_0212170.
DR GeneID; 24564616; -.
DR KEGG; bbig:BBBOND_0212170; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0212170; -.
DR OMA; PRSDDWE; -.
DR OrthoDB; 1023at2759; -.
DR Proteomes; UP000033188; Chromosome 2.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR CDD; cd05467; CBM20; 1.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003337; Trehalose_PPase.
DR NCBIfam; TIGR00685; T6PP; 1.
DR PANTHER; PTHR10788:SF113; TREHALOSE 6-PHOSPHATE PHOSPHATASE; 1.
DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033188}.
FT DOMAIN 1..107
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 208..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 968 AA; 110641 MW; B7729C61DB2B2F08 CRC64;
MVFFTGVHFR CRAGLEFGQR LVVVGDHSAL GDWDFGACHE LLQSATVDDV WNSRAPAHLP
LNKRREYRYA VLNDLGEFLR WHEESARFVN PTGNEMLVED DDGYYRDQCA KLITSGDEQG
APVAVENNID SKNPLQVIEA LRGLDVDPNL TVYFVTSRLP IQIKRGADGS FSIRQSNTPL
TTTLWKTRNR CRNKMRFIGA CLITPESAGD DGDGVDPPPA SERREPDKDA GGDHFTDDEK
EEIRMLLLEH DCIPVFVPPA ELNESLRFCK EHLWNLFYNI GLWDVNKQRE FRWDLWKSYV
SVNRQYATAA AINASEGDFF WIHDYKLLMV PHFITRRIKR ANIGIFMHAM FPPCSLFICL
AVREIILRSM LCADLIGFQF YDYARHFLTC CKRLLGLDHS SKPGGMLDIE YNGREVMILL
SHSHIQPDLL ATMLEERNGV PALVESFREQ WPDRFVFGSL DRDIRLSGLY LKLKAFRLFL
EQCPSARNKA LLVQYVCAKD TLWECRRDTT ERLQSIVDSI NADFGGTHVV LEFNVSIERK
YALFVSADCF LDASIRGGIN MRALEYIYCR QGKPACAILS EFVGFSKMLL SAMRVNPWHI
ESVVDAMRTA MSSKSEERVE VCRRDFEYIV SSDTVSWADQ FIRELFFARK RQDMLHLTWG
FGKTLKTYSV ANTFQHLSID YVLNSYDAAR RRLIFLDCEG TLSASLWDTP PRSPQDCERS
IRMGISPLEC NVKSIRTLAE DPLNIIVVIS GRGRECMEKL WFPDQPKLGL CAGYGLYYKV
PCLTGNEWCC MLETFNEEWK ELVVQIMEQY AHRTPGSYVE VMDAVVVFQY HHSDPEFGAT
QSGELYTVLK CAMSKYPVEV QLCKWNVMVR LKGVCKGSAL LNVAKRYSAL HGDLDFVLCI
GDHRSDEDTF KALETMSQWS KKGDGSPTSD DKSRSFISVT VGMKPSKAKY YVNDHTEVSE
LLTALTKH
//
