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Database: UniProt
Entry: G7X824_ASPKW
LinkDB: G7X824_ASPKW
Original site: G7X824_ASPKW 
ID   G7X824_ASPKW            Unreviewed;       789 AA.
AC   G7X824;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=ADAM family of metalloprotease ADM-B {ECO:0000313|EMBL:GAA82952.1};
GN   ORFNames=AKAW_01067 {ECO:0000313|EMBL:GAA82952.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA82952.1};
RN   [1] {ECO:0000313|EMBL:GAA82952.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA82952.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   EMBL; DF126448; GAA82952.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7X824; -.
DR   STRING; 1033177.G7X824; -.
DR   VEuPathDB; FungiDB:AKAW_01067; -.
DR   eggNOG; KOG3607; Eukaryota.
DR   InParanoid; G7X824; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR   Gene3D; 3.40.1620.60; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR041645; ADAMTS_CR_2.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR034028; ZnMc_ADAM_fungal.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF159; MIND-MELD, ISOFORM J; 1.
DR   Pfam; PF17771; ADAMTS_CR_2; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF13688; Reprolysin_5; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023049, ECO:0000313|EMBL:GAA82952.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:GAA82952.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:GAA82952.1};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..789
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003505234"
FT   TRANSMEM        700..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          275..487
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          512..601
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          738..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..756
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         435
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   789 AA;  84142 MW;  4AF365632E42550B CRC64;
     MRFLTYSLPF IASAISLFGA SVQARSQAPS AIRHVSTLDQ PTIKTPSQRV DHLDHFDITF
     DIHDTHQRIK LELEPNHDIL AEDASVQYLD ADGNVRRHEP IARHEHKVFK GRSLLGRGKG
     MWDPVGWARI YLKQDGSEPL FEGVFSVDGD NHHVQLKSAY MEKKRPVDVD LPDSAKDYMI
     FYRDSDMVRL HTELKRSSLG STSCQADQLG FNTNPNHPVL QPYVQAETDA WGAMSLNSLF
     GLNKRQSDIG SVSGNAGGVN LASTIGDTSG CPSTKQVALI GVATDCSFTG SFNNETAAKE
     WVISTVNSAS NVYEKSFNIT IGLRNLTITD SSCPDNPPAA TAWNMPCSSG NLTSRLDLFS
     KWRGEQSDDN AYWTLMSDCA TGNEVGLSWL GQLCNSDASS DGSSTVSGTN VVVRSSGSDW
     QIFAHESGHT FGAVHDCDSQ TCAQDLEASS QCCPLTSSTC DANAKYIMNP TTGTDITSFS
     QCTIGNICAA LGRNSVKSSC LSANRDVTTY TGSQCGNGIV ESGEDCDCGG EDGCGDNNCC
     DAKTCKFKSG AVCDDSNDSC CSSCQFSSAG TVCRASRGDC DVAETCSGNS STCPTDSFKK
     DGTSCGSSGS GLACASGQCT SRDYQCRSVM GSLLHSNDTY ACSSFSSSCE LVCTSPKIGT
     CYSVNQNFLD GTPCGSGGYC SNGDCKGQNV ESWIKNHKGI VIGVACAVGA LILLALMTCI
     VNRCRQARAP KPVPRPVPYG PWPGARPPPP PPMNQWPARG YQGLGNEPPP PYPGVAGQPQ
     YMSPQGRYA
//
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