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Database: UniProt
Entry: A0A094DA39_9PEZI
LinkDB: A0A094DA39_9PEZI
Original site: A0A094DA39_9PEZI 
ID   A0A094DA39_9PEZI        Unreviewed;      1081 AA.
AC   A0A094DA39;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN   ORFNames=V497_06396 {ECO:0000313|EMBL:KFY56325.1};
OS   Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY56325.1, ECO:0000313|Proteomes:UP000029268};
RN   [1] {ECO:0000313|EMBL:KFY56325.1, ECO:0000313|Proteomes:UP000029268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFY56325.1}.
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DR   EMBL; JPJZ01001103; KFY56325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094DA39; -.
DR   STRING; 1420910.A0A094DA39; -.
DR   HOGENOM; CLU_009402_0_0_1; -.
DR   OrthoDB; 2165012at2759; -.
DR   Proteomes; UP000029268; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR   CDD; cd11319; AmyAc_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR015340; A_amylase_C_dom.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23501; MAJOR FACILITATOR SUPERFAMILY; 1.
DR   PANTHER; PTHR23501:SF107; TRANSPORTER, PUTATIVE (AFU_ORTHOLOGUE AFUA_7G04730)-RELATED; 1.
DR   Pfam; PF09260; A_amylase_dom_C; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        86..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        324..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        433..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        458..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          626..978
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          29..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1081 AA;  116977 MW;  B1BA51FBB9874284 CRC64;
     MSDSCIVRMK LAIFSRVMGE RAVAPTVLSP DEMNCETTAS SGKAEKELVP TEEGEPSSDE
     EAPSETAAEG IKKVEAIAIV WSRSELYAAY ACVFLVYFVN SLQQQIISNL LPYVMSDFAS
     HSLIPVTGIV SQILGGVLKL PIAQLINIWG RPQGLIVMTT LCTIGLILMA VCNNVQTYAA
     AQCFYWVGYN GIGFVLDVFI ADTSNLRNRA LAFAFASTPY IVTTWAGPKA AESFYAHSGW
     RWAFGCFSIL TPIVILPLLY ILFSNQRKAA RLGFIQKRES GRTVKESLWY YFIEFDVVGI
     LLISAGFALF LLPFALAGSQ TDKWAAASTI IMLVLGVALL AAFGLYEKYL APRSFIPFHL
     VTDRTVLGSC GLSAVSFASF YLWDNYYLSY LQVVHQLSIT TAGYVFNIFS IGCSFWAVVV
     AAAIHYTGRI KPLALYFGAP LNLLGVGLMI HFRQPSHSIG YVVMCQIFIA FAGGILVICE
     QMAAMAAVKH ADVAAILAVL GLSAAVGGAI GSSMAGAIWT NTLPDALTAA LPEAEKARAG
     EIYGSLKEQL AFKWGSEARM GIVQAYGIAQ RRMTIASTSV IVLMFIKVMF FNRPALVARY
     LAVAAALFTS TSAKTAAEWR ESSIYQLLTD RFATTEGSAP DCSIRSYCGG TWKGIENKLD
     YIQGMGFDAI WISPVIHNIE DNTQYGNAFH GYWGDDPFTL NPHFGTGDDL KSLSDALHGR
     GMSLMIDVVI NHLAANQPST SVDYSVFPAP FNSASAFHTP CAIDYTNQGS IENCWLVTDT
     PSLPDIDSEN GDVYTAMVNS VADIVKTYGV DGIRLDTARH VPKEFLTQFQ EAVGVFVTGE
     VLDGNPDFVA GYQGPLSSTL NYPLWYPLVD SFMGGDFSAL ATTMGTVGSV FTDVNALANF
     LDNHDQPRFA SREGNDVVRD RNAATFLMFT SGIPVVYYGF EHRFGGASDP DNREALWGSG
     YNVDAELYKH IALLHQIRDL ASGIGEKAAY FSTSAEVIGT STQYMAIKRG AVVVVVSNVG
     AQGATDGFNV SGSQFDSGDQ IVDLFSCTTA TVGDGGAFDS TANNGEARIW IRSRDKGSFC
     P
//
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