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Database: UniProt
Entry: A0A091HTS0_BUCRH
LinkDB: A0A091HTS0_BUCRH
Original site: A0A091HTS0_BUCRH 
ID   A0A091HTS0_BUCRH        Unreviewed;      1051 AA.
AC   A0A091HTS0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Nardilysin {ECO:0000313|EMBL:KFO90678.1};
DE   Flags: Fragment;
GN   ORFNames=N320_04944 {ECO:0000313|EMBL:KFO90678.1};
OS   Buceros rhinoceros silvestris.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX   NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO90678.1, ECO:0000313|Proteomes:UP000054064};
RN   [1] {ECO:0000313|EMBL:KFO90678.1, ECO:0000313|Proteomes:UP000054064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO90678.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KL524392; KFO90678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091HTS0; -.
DR   Proteomes; UP000054064; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
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.
DR   PROSITE; PS00143; INSULINASE; 1.
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:UP000054064};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          105..234
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          260..438
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          453..733
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          739..920
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          24..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..93
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO90678.1"
FT   NON_TER         1051
FT                   /evidence="ECO:0000313|EMBL:KFO90678.1"
SQ   SEQUENCE   1051 AA;  120872 MW;  98B97D3E2D2D1CE4 CRC64;
     RYIKLQNGLC ALLISDLNYL DGAPAALSSE EEEGEDSDDD DSEEESDQDD DSGAEIEDGR
     EGFDDEDCDE EDESEDNDGD NEDFNDPDDS ELEELAEETR KRGCTEKQSA AALCIAVGSF
     SDPEDLPGLA HFLEHMVFMG SLKYPDENGF DAFLKKHGGS DNASTDCERT VFQFDVQRKY
     FKEALDRWAQ FFIHPLMIRD AIDREVEAVD SEYQLARPSD ANRKEMLFGS LARPGHPMKK
     FFWGNADTLK HEPKMNNIDT YTRLRDFWQR HYSAHYMTLV VQCKETLDTL EKWVTEIFSE
     IPNNGLPKPS FGHLTQPFDT PEFHKLYRVV PVRKVHSLSI TWALPPQEQH YRVKPLHYIS
     WLVGHEGKGS VLSFLRKKFW ALALYGGNGE TGFEQNSTYS IFSISVTLTD EGYRHFYEVA
     HVVFQYVKML QKRGPDKRQV IWEEIQKIEA NEFHYQEQTD PVDYVESLCE NMQLFQKEDF
     LTGDQLLFEY KPEIIADALN QLSPQRANLV LLSAANEGQC HLKERWFGTQ YSVEDIDKNW
     TDLWASDFEL NQDLHLPEEN KYIATDFALK VADCPETEYP VKIVSTQQGC LWYRKDDKFK
     IPKGYVRFHL ISPLIQQSAE NIVLFDTFVN ILAHNLGEPA YEADVAQLEY KLVAGEHGLV
     IRVKGFNHKL PLLFQLIIDY LSDFSFTPAV FEMITEQLKK TYFNILIKPE TLAKDVRLLI
     LEHGRWSMID KYQTLMNGLS IESLSSFVKA FKSQLFVEGL VQGNFTSREA KDFLNYVVQK
     LQFAPLAQSC PVQFQVVDLP NRHLLCKVKT LNKGDANSEV TVYYQSGARN LREYTLMELL
     VMHMEEPCFD FLRTKQTLGY HVYPTCRNTS GILGFSVTVT TQATKYNSEL VDEKIEEFLS
     CFEEKIKHLP EDAFSTQVTA LIKLKECEDS HLGEEVDRNW NEVVTQQYLF DRLAREIEAL
     KSLTKSDLVT WFQDHRSNKR KMLSVHVVGY GKHEGDSEVT AVSEAQNSSS GEIPHLVFLP
     PSSLMTNVTS IKDIKAYTST LTVLPYHKIL K
//
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