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Database: UniProt
Entry: A0A094HYW6_9PEZI
LinkDB: A0A094HYW6_9PEZI
Original site: A0A094HYW6_9PEZI 
ID   A0A094HYW6_9PEZI        Unreviewed;       650 AA.
AC   A0A094HYW6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0000259|PROSITE:PS50215};
GN   ORFNames=V500_05655 {ECO:0000313|EMBL:KFY89457.1};
OS   Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY89457.1, ECO:0000313|Proteomes:UP000029284};
RN   [1] {ECO:0000313|EMBL:KFY89457.1, ECO:0000313|Proteomes:UP000029284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFY89457.1}.
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DR   EMBL; JPKC01001889; KFY89457.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094HYW6; -.
DR   STRING; 1420913.A0A094HYW6; -.
DR   HOGENOM; CLU_012383_0_1_1; -.
DR   Proteomes; UP000029284; Unassembled WGS sequence.
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:InterPro.
DR   CDD; cd04271; ZnMc_ADAM_fungal; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
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; PF13688; Reprolysin_5; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..650
FT                   /note="Peptidase M12B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001904740"
FT   DOMAIN          280..497
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   REGION          529..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..592
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        435
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         438
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         444
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ   SEQUENCE   650 AA;  69974 MW;  DF616E80238D7823 CRC64;
     MRLLRCVAAA LVSASFSHIA QAHSVKRAPL SYLSIVDEPV IHTPSHHVHA YSSFDLSFHL
     HDRQQYIKLT LAPNDDVIAE GATVNYVGAD GQVREVELIE RSDHRVFKGH AWVRTHEGTQ
     WTHAGWARVV IHRDGVDPLF EGAFRIDGNH HHIHPRNSYI ATKHELDPYV EDDREDLMIV
     WRDSDITPDE PNRGELKRDL NTGSCLSDDL TFNLMPEHPV YSQVYSQSTI LRKGESFWGS
     ISSGSIFGRD IDATGNLPGN GAAVNLLNSI GNPAGCPTSR KVALVGIATD CTYTAFFNST
     SSVRSNIITQ MNSASVLYEE SFNISLGIQN LTITDAACPG VSQVNTPWNR DCNSGLEIQD
     RLNLFSAWRG ASPDTNAYWT LLTTCNTGSA VGLAWLGQAC VNTAQASTQS GSNDTVSGAN
     VVVKTDTEWL VIAHEVGHTF GAVHDCDSTT CADGKTVAAQ QCCPLSADTC PAGGKYIMNP
     STSPGITNFS PCSIGNICSA IGGHAETASS RWAKTAIVAV CPGAATIHAA TPQPANSRPR
     TTPSATPRTR TAVSQPANSP PPAQSAAPQP APAIRRKRAR EPRRRVQRTR TRTKARAAVP
     PARASLAQAD SARREINSVR PLWGRSTTSA ATTGASSSAR RTRRSIIVRG
//
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