ID A0A2T1DSA9_9CYAN Unreviewed; 646 AA.
AC A0A2T1DSA9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Cyclomaltodextrin glucanotransferase {ECO:0000313|EMBL:PSB23274.1};
GN ORFNames=C7B76_00845 {ECO:0000313|EMBL:PSB23274.1};
OS filamentous cyanobacterium CCP2.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107700 {ECO:0000313|EMBL:PSB23274.1, ECO:0000313|Proteomes:UP000239512};
RN [1] {ECO:0000313|EMBL:PSB23274.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB23274.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB23274.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB23274.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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:PSB23274.1}.
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DR EMBL; PVWD01000002; PSB23274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1DSA9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000239512; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05467; CBM20; 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; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02806; Alpha-amylase_C; 1.
DR Pfam; PF00686; CBM_20; 1.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000239512};
KW Transferase {ECO:0000313|EMBL:PSB23274.1}.
FT DOMAIN 538..642
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 74341 MW; 6684FA29BEA8E467 CRC64;
MPTDQHKIAP AQATSEQYDV TDPQAKVETL VEEQPPDTDI DLEFLYTRDI EFRQETIYFL
VVDRFYDGDP SNNEGPNPEL YDPTKQDWGK YWGGDLQGVI DKLDYLKNLG VTAVWLTPLF
EQTEELFCGN AAIHGYWTKD FKRLNPRFLG VGENNSLNKT QDSRDTIFDR LIEELHKRNM
KLILDVVCNH STPETMGGKG ELYDDGVKIA DFNEDEKHWY HHYGEVVDWE DDWQIQNCEL
AGLATFNENN TEYRNYIKGA IKQWLDRGVD ALRVDTVKHM PIWFWQEFNA DIQTHRPDVF
VFGEWIYNHP ADERSVEFAN NSGMTILDFG LCVAIRAALG QGAEDGFYLI KDVLALDHHY
SGALELITFI DNHDMPRFQS LNPDPDMLKV AVSLIMTTRG IPCIYYGTEQ YLHDDTDGGN
DPYNRPMLES WDTDTDVYRA IRLLSGLRRL NPAVSMGSQW QKYITPDVYC YVRRYRDSRC
FVALNRGEAI TLEEVDTELP DGEHTCVITH NKYEVKDGKI QDFHIDTRGV VVLSHVGERV
KAQTIVRAQL NGVRTLPGEQ VVVTGDCPEL GNWDISKAYP LEYINSNTWF AEIPFDESAG
KLISYKYAMW REGQAPLREN LVARRWVIAS EGTVKWRDTW ASGPES
//
