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
//