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Database: UniProt
Entry: A0A1B8EN48_9PEZI
LinkDB: A0A1B8EN48_9PEZI
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ID   A0A1B8EN48_9PEZI        Unreviewed;      1034 AA.
AC   A0A1B8EN48;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Insulysin {ECO:0000313|EMBL:OBT72754.1};
GN   ORFNames=VF21_08992 {ECO:0000313|EMBL:OBT72754.1};
OS   Pseudogymnoascus sp. 05NY08.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT72754.1, ECO:0000313|Proteomes:UP000092096};
RN   [1] {ECO:0000313|EMBL:OBT72754.1, ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|EMBL:OBT72754.1,
RC   ECO:0000313|Proteomes:UP000092096};
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT   white-nose syndrome of bats.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX   PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA   Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT   "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT   white-nose syndrome of bats.";
RL   Nat. Commun. 9:35-35(2018).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; KV458879; OBT72754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B8EN48; -.
DR   STRING; 1622149.A0A1B8EN48; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000092096; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092096};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          54..202
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          228..407
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          414..702
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          707..888
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1011..1034
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1034 AA;  118087 MW;  554995836A104729 CRC64;
     MPTPSQPQTP TTLDSPLREH RQRPVERLTD KLETPSLDDR QYRVIKIASN QLEVLLVHDA
     DTDKASAAMD VNVGNFSDPE DTPGMGHAVE HLLFMGTKKY PVENAYSQYL SAHSGSSNAY
     TAATSTNYYF EVAAKAAESA EETDRSPLYG ALDRFAQFFI EPLFLPSTLD RELRAVDSEN
     KKNLQSDQWR LHQLDKSLSN PKHPYCHFST GSLETLKIQP EAKGIDVRQE FINFHDKHYS
     ANRMKLVILG REPLDVLEEW AVDLFAGVKN KDLEQNRWED EQPLGKDELL TQIFAKPVMD
     SRLLELTFPF LNEEDLYESQ PSRYISHLIG HEGPGSIMSY IKGKGWANGL SAGGYAVCPG
     SLGLFNCQIR LTEEGLKNYK EIVKVFFQYI SLLNESPPQE WIFEEQKGLA EVDFKFKQKS
     PASKFTSKIS AVMQLPLPRE WLLSGHSRLR KFDPKAIEAG LAYLRPDNFR MSVVSQTFPG
     GWDKKEKWYE TEYKYEKIPQ EFIAEIESAA SSTKASRLSQ LHLPHKNQFI PTNLDVEKKE
     VKEPTRAPTL IRNDDMVRAW FKKDDTFWVP KANLFIQCKN PLPSATAENT IKSRVYAELV
     RDALEEYAYD AELAGLDYSV SSYSGGLDIQ ISGYNDKLPV LLEKVLLTMR DLEVKPDRFA
     IVKERLLRGM RNWDYQQPYN QVGDFTRWLN IEKGFISDQL LTELPRLEAE DIKLYFPQLL
     RQVHIETLVH GNLYKEDALR LTNMVETTLK ARALPQAQWP VFRSLVFPPG ANFVYHKTLK
     DPANVNHCIE YLLYVGDKAD RALRAKCLML DQITHEPAFD QLRTKEQLGY VVFSGARTTS
     TTIGYRFIVQ SERTPEYLEG RIDSFLANYL TTLKNMSDSE FEGHQRSLIT KRMEKLKNLD
     QESSRLWTHV ASDYFDFDLS YEDAAHVKAL TKKEMIEFYE HYISPSSPSR AKLAVHLRAQ
     GTSKKSSTGN IADDVKGLKL TSEDKTAQET PVEGNGTKPW AIDDVRAFKS KLGVTPGPQP
     VRDLSEFEET DSKL
//
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