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Database: UniProt
Entry: A0A484FLF4_COLOR
LinkDB: A0A484FLF4_COLOR
Original site: A0A484FLF4_COLOR 
ID   A0A484FLF4_COLOR        Unreviewed;       927 AA.
AC   A0A484FLF4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:TDZ18606.1};
GN   Name=MAL2-2 {ECO:0000313|EMBL:TDZ18606.1};
GN   ORFNames=Cob_v008588 {ECO:0000313|EMBL:TDZ18606.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ18606.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|ARBA:ARBA00000548};
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:TDZ18606.1}.
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DR   EMBL; AMCV02000023; TDZ18606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A484FLF4; -.
DR   STRING; 1213857.A0A484FLF4; -.
DR   Proteomes; UP000014480; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   GO; GO:0000023; P:maltose metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF222; MALTASE MALT (AFU_ORTHOLOGUE AFUA_8G07070); 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Maltose metabolism {ECO:0000256|ARBA:ARBA00026248};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        837..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..442
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          798..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   927 AA;  104452 MW;  4719E52318485135 CRC64;
     MGSVTVEKGD RAWWKDAVIY QIYPASFKDS NGDGLGDVPG IISKVDYLKD LGVDVVWVSP
     MYASPQVDMG YDISDYQDVH RPYGTVQDME VLIDECHKRG MKLILDLVVN HTSDQHAWFK
     ESRSSKTNPK RDWYIWKPPR YAEDGTRLPP TNWRSFFSGS TWEWDEATGE YYLHLFAVEQ
     PDLNWENPET REAIYESAMR FWLDKGVDGF RVDTVNMYSK GVEWRDAPVV DESAYEQPAY
     NIFCNGPRIH EFLREMNQKV LSHYDTVTVG ELPHTPDPQH VLRYVGAGDR QLDMVFQFDI
     VDLGQGKICK YTAVDWTLPE LKRVVAKWQQ FVEGTDGWTT AFLENHDQGR SVSRYGSDAP
     PWREPSAKML SLMNCAMTGT LFVYQGQEIG MVNVPRSWPI EDYKDIECRN FYSDFRREHG
     EGSEFLEYVM DSINKLGRDN ARVPMQWDDS PYAGFTDCKT GAWMRVHELY PEINVARQER
     EPKSVLNFWR AMLRLRKEEG ELLTHGAFEL FDEDNEKTFV FKKSRGGRAA VIALNFTSEE
     QAVDVPGEGL VIRVGNYDDV KERVAQEGEK RVLRPWEGRL YLQDWSYVAN KLIWEFFLAC
     TIVINIDTAT VIVAVLITIT ITITEPTTEP DLKRSLEFNP EFDLKHRSLG VGPLPRSICG
     YYTLSGDPDI KTRSCEFGTT CGIASPNFSG LLACHTTVYT ECVVKKIFDP CPSVANPSET
     AHPLCCQEKD GAIPVCRTYI GPRSNNPIAL KMYACEPTSL GHETNVFLYQ ETGYLLPQTR
     SSGQTTGLTA NNLSSMTVSD ASTSGMTSTT GPLSTPTSTA TPAATSDVPS AQAQTPVIVG
     GVIGGLVILG FVVCFVVWVR TRKPPAVSGP AELPGDQPVE HAGCELDAGG HRGRRREEEF
     LMPESPVIRH FGNDDFHSVR QRSDLSP
//
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