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Database: UniProt
Entry: A0A093G185_TYTAL
LinkDB: A0A093G185_TYTAL
Original site: A0A093G185_TYTAL 
ID   A0A093G185_TYTAL        Unreviewed;      1049 AA.
AC   A0A093G185;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Nardilysin {ECO:0000313|EMBL:KFV60426.1};
DE   Flags: Fragment;
GN   ORFNames=N341_03863 {ECO:0000313|EMBL:KFV60426.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV60426.1, ECO:0000313|Proteomes:UP000054190};
RN   [1] {ECO:0000313|EMBL:KFV60426.1, ECO:0000313|Proteomes:UP000054190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV60426.1};
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; KK401843; KFV60426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093G185; -.
DR   MEROPS; M16.987; -.
DR   Proteomes; UP000054190; 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:UP000054190};
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..445
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          451..731
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          737..918
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          25..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:KFV60426.1"
FT   NON_TER         1049
FT                   /evidence="ECO:0000313|EMBL:KFV60426.1"
SQ   SEQUENCE   1049 AA;  120710 MW;  FF76AC915A673DE7 CRC64;
     FRYIKLQNGL RALLISDLNY LDGAPATLSS EEEEDDDDES EEESDEDDDS GAEIEDGREG
     FEDEDCDEGD ESEDDNGDNE DFNDPDDSEL EELAEKEETR KRGCTEKQSA AALCVAVGSF
     SDPEDLPGLA HFLEHMVFMG SLKYPDENGF DAFLKKHGGS DNASTDCERT VFQFDVQRKY
     FKEALDRWAQ FFIHPLMIRD AIDREVEAVD SEYQLARPSD ANRKEMLFGS LARPGHPMKK
     FFWGNADTLK HEPKMNNIDT YTRLRDFWQH HYSAHYMTLV VQSKETLDTL EKWVTEIFSE
     IPNNGLPKPS FGHLTQPFDT PEFHKLYRVV PIRKVHSLSI TWALPPQEQY YRVKPLHYIS
     WLVGHEGKGS VLSFLRKKFW ALALYGGNGE TGFEQNSTYS IFSISVTLTD EGYKHFYEVA
     HVVFQYVKML QKRGPDKRIW EEIQKIEANE FHYQEQTDPV DYVESLCENM QLFQKEDFLT
     GDQLLFEYKP EIIADALNQL SPQRANLVLL SAANEGQCHL KERWFGTQYS MEDIDKYWSD
     LWASDFELNQ DLHLPEENKY IATDFALKVA DCPETEYPAK TLSTQQGCLW YRKDDKFKIP
     KGYVRFHLIS PLIQQSAENI VLFDTFVNIL SHNLGEPAYE ADVAQLEYKL VAGEHGLVIR
     VKGFNHKLPL LFQLIIDYLS DFSFTPAVFE MITEQLKKTY FNILIKPETL AKDVRLLILE
     HGRWSMIDKY QTLMNGLSIE SLSSFVKAFK SQLFVEGLVQ GNFTSREAKD FLNYVVQKLQ
     FAPLAHPCPV QFRVVDLPNT HLLCKVKTLN KGDANSEVTV YYQSGARNLR EYTLMELLVM
     HMEEPCFDFL RTKQTLGYHV YPTCRNTSGI LGFSVTVATQ ASKYNSELVD KKIEEFLSCF
     EEKIKHLTED AFSTQVTALI KLKECEDSHL GEEVDRNWNE VVTQQYLFDR LAREIEALRS
     VTKLDLVTWF QAHRSSKKKV LSVHVVGYGK HEGDSEVTAV SEAQTSSSGE IPHLIFLPPS
     SLMTNVTSIK DIKAYTSTLN VLPYHKILK
//
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