ID A0BWK3_PARTE Unreviewed; 1018 AA.
AC A0BWK3;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Chromosome undetermined scaffold_132, whole genome shotgun sequence {ECO:0000313|EMBL:CAK62920.1};
GN ORFNames=GSPATT00032772001 {ECO:0000313|EMBL:CAK62920.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK62920.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK62920.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK62920.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR EMBL; CT868022; CAK62920.1; -; Genomic_DNA.
DR RefSeq; XP_001430318.1; XM_001430281.1.
DR AlphaFoldDB; A0BWK3; -.
DR STRING; 5888.A0BWK3; -.
DR EnsemblProtists; CAK62920; CAK62920; GSPATT00032772001.
DR GeneID; 5016102; -.
DR KEGG; ptm:GSPATT00032772001; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_296559_0_0_1; -.
DR InParanoid; A0BWK3; -.
DR OMA; GVIMNAR; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd05467; CBM20; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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 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:UP000000600}.
FT DOMAIN 1..103
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 162..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1018 AA; 119634 MW; CC0A266A033829B7 CRC64;
MNTECSVLFH VTVRTTLSQV VGVIGNQEEL GSWNEKCLCI LKTDPQIFPK WVAEKPIAFK
QGTKLEFKFV ILDNGTAIWE ELPQNRKYRC RYWKVILTAD WNNYEGKEYI EKRFKSSVCL
DQEILSQYTK PRLSDQFDPF NQANDDSEDS VDGFDSFAKE IANRNDSESS ESEEDKKKPT
VELNKDSEFS SLYQLYTENP KFRQLKNFSQ NDILYEINDD PLIGLSDEDS LLISTYYLPI
VIIKQTDGSY QRSNFQHSFS LHLLFGVQQF KRIWFGLPIV LNELGEKITD QSVELKNYLK
QFGFVPVFVN QECLDYFNKE FCSKLYQAIM NNDVSITKLA ALEYSDYMQE CFKKLNDEFF
QEIKPHINQH SIALIADYRL LYLSQIFVNH KFTRLPLVIF YNRLFPHLDN LKLIPFFHEI
INSFLHANVI CFSNYKTANE FLTVMKDIYK VEYHSFKGNL AFHYYGREIL VKLQNPGIEL
TACGEKRYEI GELHYDKVEN DNEIKIVGVD TYGHQSGVEL KFRHLLKFIK ETDIIQKNPH
IKYIQILLKA FEDHDINEQR VSLLNQIEQI NSYLYPNRDN YFVKLIEEEM DSKHRFKVFE
KAKIYLQCKY SGRHDFYLSE YIHLNKMPIA LISDSSCYHR GFQSIVTFNV FSHIDFKEKF
ADLLIKVINK QYQFTQLHKL KVEKDQLIIR QNQTSQWIEN IFIDAKKAVS MLKFAQISLR
FQDGLMIKVA HNLKFQHLDI QSVAKAYQQS TKPIIIIEFE TIVTDQYFID YKPKHFLQQS
PHLKGNEEAV MIRQVEQELL NRIKELSKTN KVYIVSGGLF NELSSIFSGY NISLFAENGF
LYKSDQLQWN ALFNLDYQCL IQVRKIFNQY AMKTEGALIE SKESSISLKL MNSDEYVQQL
IQDLVENVQM IVDRYPTFQL IIGSHSVEVS PKNLNKGMIL EIIMQKENLQ RGKLDFALII
ARGIQNEDIF SHFKVITQSR KYFSENASLF SVSQGLMPSY ANYYLNNQQE LIQLFKTI
//
