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Database: UniProt
Entry: A0A2S7NS32_9HELO
LinkDB: A0A2S7NS32_9HELO
Original site: A0A2S7NS32_9HELO 
ID   A0A2S7NS32_9HELO        Unreviewed;       772 AA.
AC   A0A2S7NS32;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   13-SEP-2023, entry version 20.
DE   SubName: Full=Adam family of metalloprotease adm-b protein {ECO:0000313|EMBL:PQE04837.1};
GN   ORFNames=CJF30_00004635 {ECO:0000313|EMBL:PQE04837.1};
OS   Rutstroemia sp. NJR-2017a BBW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Rutstroemiaceae; Rutstroemia.
OX   NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE04837.1, ECO:0000313|Proteomes:UP000238072};
RN   [1] {ECO:0000313|EMBL:PQE04837.1, ECO:0000313|Proteomes:UP000238072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE04837.1,
RC   ECO:0000313|Proteomes:UP000238072};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PQE04837.1}.
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DR   EMBL; NJPT01000092; PQE04837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7NS32; -.
DR   STRING; 2070414.A0A2S7NS32; -.
DR   Proteomes; UP000238072; 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; 3.40.390.10; 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:SF159; ADAM METALLOPROTEASE; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF13688; Reprolysin_5; 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:PQE04837.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Metalloprotease {ECO:0000313|EMBL:PQE04837.1};
KW   Protease {ECO:0000313|EMBL:PQE04837.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238072};
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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..772
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015436871"
FT   TRANSMEM        702..725
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          267..484
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          509..599
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REGION          738..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         421
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   772 AA;  81443 MW;  C69DC56D32CEDEC3 CRC64;
     MYILKTVVAL TALFAELISA HSNERNPLTY ISLVDAPNIR TPTHRVHALS KFDVEFGLHG
     GNQRVKLTLS PNHDVIADGA TIQYLGADGT LRSQETFDRA AYRVFKGSTW LQHYEGAEWT
     NVGWARIMVK KDGAEPIFEG AFRVDGDHHH IQTRTHFVST KHALDPELPD TGKEYMVVWR
     DSDIGSGYLR RSAREEPSCS ADGLTFNAVN NPINSFVPME KRQENFWGSI STRAIFGRQI
     DTQSGGNSAG VNLTSTIGST SGCPTTRKVA LVGIATDCTY TAAFNSTEAA RENVISVLNS
     ASVQYEDSFN ITLGLQNLTV SDALCPATAA SSAPWNVGCS DSVTIQDRLN LFSAWRGERQ
     DTNAYWTLLS TCGTGSAVGL AWLGQACVTN SQVATSSSGN ETVSGANVVV RTSTEWQVLA
     HETGHTFGAV HDCTSQTCGD GTTVAAQQCC PLSANTCDAG GAFIMNPSTG SSISKFSACS
     IGNICSAIGR NSVKTTCLTA NKDITTITGS QCGNGIVESG EDCDCGGESG CGSNSCCDAK
     TCKFTTNSVC DPSNEDCCTH SCQFASGGTV CRASTGVCDP QEVCSGTSAV CPEDTTSPDG
     TSCGSSSSLS CASGQCTSRD LQCKTIMGSY TQGNDTYACS DSGCQISCAS PEFGSNVCYS
     MQQNFLDGTS CQGGGKCSNG DCKGSSVAKE ITSWITHNKP TVIAIAAVAG GLLILAILSC
     CCARARKKKR MAKMEYAAGP PGWPQMQGGA PPPMRGNWDD GRWRPGPSVR YA
//
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