ID A8P5K3_COPC7 Unreviewed; 780 AA.
AC A8P5K3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN ORFNames=CC1G_05516 {ECO:0000313|EMBL:EAU82894.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU82894.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU82894.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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 ECO:0000256|RuleBase:RU361134};
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, ECO:0000256|RuleBase:RU003615}.
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:EAU82894.1}.
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DR EMBL; AACS02000011; EAU82894.1; -; Genomic_DNA.
DR RefSeq; XP_001838963.1; XM_001838911.1.
DR AlphaFoldDB; A8P5K3; -.
DR SMR; A8P5K3; -.
DR STRING; 240176.A8P5K3; -.
DR GeneID; 6015559; -.
DR KEGG; cci:CC1G_05516; -.
DR VEuPathDB; FungiDB:CC1G_05516; -.
DR eggNOG; KOG2212; Eukaryota.
DR InParanoid; A8P5K3; -.
DR OMA; PVNFVWQ; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 2.60.40.2440; Carbohydrate binding type-21 domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR005036; CBM21_dom.
DR InterPro; IPR038175; CBM21_dom_sf.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF03370; CBM_21; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51159; CBM21; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..780
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002725028"
FT DOMAIN 28..129
FT /note="CBM21"
FT /evidence="ECO:0000259|PROSITE:PS51159"
FT REGION 121..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..169
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 85776 MW; D81546CFF0E73F29 CRC64;
MKLPQLWTVS LSLFGLFLAL TYASPAPQHV KRAPQVSLIN HSYSNAVLSG TINVQNIAYS
KVVEVVWAVG DSWSDSQIIP ATYTSSGSNN FETWAFSGRA SGATQFYIRY TVSGQTYYDP
GNYQNHQVNR PPSNSQPPVV TSSTAVVPPP TSTTAPAPPP TGTVAPGNLP PIIPANIPYE
APATPPTGCN NFNGLDNCQG NSHEMAASSE RRRWQTPPRG DPAHEESFQD YSHLVGYADI
QYNSARNAAV VTVNAAHKEG ATLTYSFNGA EQSSPIFQVT NSLQTALAIT VTSSDGKKLV
LEPINFFWQH QSLSAAQSSF NNGQKGGIVE LFGWPWNDIA KECEFLGKAG YMGVKVWAPN
EHVWGSHYYE PDGQFRPWYF VYQPVSYRLQ SRMGTREELR NMINSCRRAG VRVYADAVIN
HMSGQGTDIQ NHRVGNCELY SGHNATENSP YYTSGNTFLI NPFTGTRPTL EFPAVPYGPT
DFHCERSLNS WTDGIVVTKG WLVGLTDLNT SKPYVQDRIA TYLTDLLSIG FSGFRVDAAK
HIGPQDMAQI LARLKNKMGG SLPDDFITWM EVIIGGEAAL MACSGGEWSW YTNFDNKMRA
AGLSNEDIQK VKIWSSDYPK EMPICGHWIL PPSRFAIQND DHDQQNDGSS SRDMADKGSV
LIKEKNVAAH RNFEVNLFAR RDNDWHIKLI LSSYMFMPNG GSGFPDGLSD CSLHYTGNQN
INGCKGVPKD TAYVANACGY TMQPGKYTRP HRDISIINAM RGWVGLGPTN ANALGIPGCQ
//
