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Database: UniProt
Entry: A0A221SZB9_9DEIO
LinkDB: A0A221SZB9_9DEIO
Original site: A0A221SZB9_9DEIO 
ID   A0A221SZB9_9DEIO        Unreviewed;      1024 AA.
AC   A0A221SZB9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:ASN81960.1};
GN   ORFNames=DFI_02360 {ECO:0000313|EMBL:ASN81960.1};
OS   Deinococcus ficus.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=317577 {ECO:0000313|EMBL:ASN81960.1, ECO:0000313|Proteomes:UP000259030};
RN   [1] {ECO:0000313|EMBL:ASN81960.1, ECO:0000313|Proteomes:UP000259030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-FR2-10 {ECO:0000313|EMBL:ASN81960.1,
RC   ECO:0000313|Proteomes:UP000259030};
RA   Wu K.-M., Liao T.-L., Liu Y.-M., Young C.-C., Tsai S.-F.;
RT   "The complete genome sequence of Deinococcus ficus isolated from the
RT   rhizosphere of the Ficus religiosa L. in Taiwan.";
RL   Submitted (MAY-2017) 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, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP021081; ASN81960.1; -; Genomic_DNA.
DR   RefSeq; WP_027463319.1; NZ_CP021081.1.
DR   AlphaFoldDB; A0A221SZB9; -.
DR   STRING; 317577.GCA_000419625_00669; -.
DR   KEGG; dfc:DFI_02360; -.
DR   Proteomes; UP000259030; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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; PF00041; fn3; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000259030};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..1024
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011296203"
FT   DOMAIN          542..637
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          52..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1024 AA;  107598 MW;  409B656655D9BB79 CRC64;
     MKRFQSVARP GLLALLTLSL AACAPAPTPD PDGPLARDWR DETIYFAMTD RFANGTPAND
     NGPNRDAGDV ADRSNPLAWH GGDFAGLKAK IEEGYFKRMG FTALWVTPVV LQVPAITAGD
     GLNQGKAFAG YHGYWAENFF KVDPHLGTLD EYKALIQAAH RNGIRVIQDI VVNHAGYGAT
     LTKTNPGWFH TDAECAASTS PVTDCPLAGL PDFKQELPEV TAYLNSFVKY WRDTTGIDGL
     RLDTMKHVPD SYWTQFFAAG GVGDPAKLWS VGEVFDGNPA YLARFMDELG SPSVFDFALY
     FAMKDHLSSA GGNLDRVADV FAQDGAYRDP TRLTTFVDNH DVRRFVNEVT SRGGTRAQAV
     ERLDLALSTM YFSRGTPSVW QGTEIAQPGE GDPYNQTTEN SNRQDMDFSQ LGASALDERL
     GALARARWTF RALTRGAQQE LWRPNGGAPV LAYRRVVSGV TGAAGQPVVF VVNGGDAAVD
     LASLPGGGIP LLGTFAGTAL TEVTGRTHGL KVEGGKLVGT VPARTALAVT APAGSGSVGT
     VNPALPEVQN LAAQPGDSAA RLSWTPSTDA AVTGYRIYAS TAGGTERLLN FAPLGREQGS
     YLVRGLPNGA ATTFRVVTVD AQGAESRGAA VTATPGAQYT AKVTFTVDAR SQGNGPVELR
     RFDTGSQVEY PMTQVSRGVW KTDIDLPLFR EVKFKFGNDA AGARNSGYEG PGQPDRSLIV
     GAPDTTYAGT YDFITVPVPA ATIEGTVTGA GQPLANALVE ATTADPNLNY ALTFSDGTYT
     LLSPAGEQTL RASAASFADA GRTVTAPATG VDFALTRPVT ASRYVIDGQL GDWTAPKVNV
     QSPAAGVFGD NNNWLTLQAD SDATYLYLAY TYRVDGNSAI LYLDTGAGGA TAADGFNAWP
     RAATFTGGIP GVDAFIARYG GEQAQLWTVQ STAAVSQVDG AAYQFAATGS LPAQTVELAI
     PWTALGLSGP PAGGVGVVGG IFGGDNYGAG DIIPDAGSTP AGANTIGADT QQRRATFTEP
     VRVP
//
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