ID E9R9I7_ASPFU Unreviewed; 607 AA.
AC E9R9I7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE SubName: Full=ADAM family of metalloprotease ADM-A {ECO:0000313|EMBL:EAL89278.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:EAL89278.1};
GN ORFNames=AFUA_6G14420 {ECO:0000313|EMBL:EAL89278.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL89278.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL89278.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:EAL89278.1}.
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DR EMBL; AAHF01000006; EAL89278.1; -; Genomic_DNA.
DR RefSeq; XP_751316.1; XM_746223.1.
DR AlphaFoldDB; E9R9I7; -.
DR EnsemblFungi; EAL89278; EAL89278; AFUA_6G14420.
DR GeneID; 3508633; -.
DR KEGG; afm:AFUA_6G14420; -.
DR VEuPathDB; FungiDB:Afu6g14420; -.
DR eggNOG; KOG3607; Eukaryota.
DR HOGENOM; CLU_012383_1_0_1; -.
DR InParanoid; E9R9I7; -.
DR OMA; WNADCSA; -.
DR OrthoDB; 2961161at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 4.10.70.10; Disintegrin domain; 1.
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:SF222; ADAM FAMILY OF METALLOPROTEASE ADM-A (AFU_ORTHOLOGUE AFUA_6G14420); 1.
DR Pfam; PF00200; Disintegrin; 1.
DR Pfam; PF13583; Reprolysin_4; 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:0000313|EMBL:EAL89278.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW Metalloprotease {ECO:0000313|EMBL:EAL89278.1};
KW Protease {ECO:0000313|EMBL:EAL89278.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
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..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..607
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003246340"
FT TRANSMEM 555..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 204..408
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 433..520
FT /note="Disintegrin"
FT /evidence="ECO:0000259|PROSITE:PS50214"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 607 AA; 64947 MW; 5D405F447400F7EF CRC64;
MKIFNLVSFI GVIAAVKHVA AHSVRTSAWD SETRLENIII HTASHGVDAY SPFELSFSLP
GQGALKLSLE PNHDILTQGS RVHYIGTDGI VRRAEAVNRA QHKVFKGVVS ARHVGSDATW
NQVGWARIYI HRDGVDPLFD GIFGVAGQQY QVTITSGSGN ASEPQMIAHY HSSYQTWDRL
APRSPQSSGN PFITDDDLPC PSTRRVALVG IATDCTYSAS FTSSDELRRN VINMVNTASE
VYERTFNISL ALHDLTISDR DCPSSPSSPT SWNADCSAGD LNWRLNRFTS WRGSLNDDNA
YWTLMTGCPS GQEVGVSWIG QLCSSNRARQ SAGANVVARS RSEWQVFAHE SGHTFGAVHD
CESTQCASAQ SQCCPLSSST CDANGQYIMN PVSTASQTAF SPCTIRNICS QLSSGRVSTR
CLVSNSNITT ITDSQCGNGI VEVGEECDCG ATCDQNSCCD GSTCRLRAGA LCDDAASPCC
TNCQFASADT VCRPSTGPCD VEEMCTGNST ICPVDRVLSG GQRCGDGEGG SGNPSCSNGE
CRRNETSWVD SHRSLIIGLA AGIGGALVLA ILGCMICSCC RRPSKKASPA VPVISQVYPP
PPPYRYR
//
