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
//