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Database: UniProt
Entry: A0A091SDC3_PELCR
LinkDB: A0A091SDC3_PELCR
Original site: A0A091SDC3_PELCR 
ID   A0A091SDC3_PELCR        Unreviewed;      1055 AA.
AC   A0A091SDC3;
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:KFQ56637.1};
DE   Flags: Fragment;
GN   ORFNames=N334_11575 {ECO:0000313|EMBL:KFQ56637.1};
OS   Pelecanus crispus (Dalmatian pelican).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Pelecanidae; Pelecanus.
OX   NCBI_TaxID=36300 {ECO:0000313|EMBL:KFQ56637.1, ECO:0000313|Proteomes:UP000054150};
RN   [1] {ECO:0000313|EMBL:KFQ56637.1, ECO:0000313|Proteomes:UP000054150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N334 {ECO:0000313|EMBL:KFQ56637.1};
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; KK469480; KFQ56637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091SDC3; -.
DR   MEROPS; M16.987; -.
DR   Proteomes; UP000054150; 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:UP000054150};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          108..237
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          263..441
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          457..737
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          743..924
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          25..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..96
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ56637.1"
FT   NON_TER         1055
FT                   /evidence="ECO:0000313|EMBL:KFQ56637.1"
SQ   SEQUENCE   1055 AA;  121390 MW;  EBA644EF085B0C0B CRC64;
     FRYIRLQNGL CALLISDLNY LDGAPAALSS EEEEEEDNDD DESEEESDED DDSGAEIEDG
     REGFDDEDCD EGDEDEDNDG DNDDFNDPDD SELEELAEKE ETRKRGCTEK QSAAALCVAV
     GSFSDPEDLP GLAHFLEHMV FMGSLKYPDE NGFDAFLKKH GGSDNASTDC ERTVFQFDVQ
     RKYFKEALDR WAQFFIHPLM IRDAIDREVE AVDSEYQLAR PSDANRKEML FGSLARPGHP
     MKKFFWGNAD TLKHEPKMNN IDTYTRLRDF WQRHYSAHYM TLVVQSKETL DTLEKWVTEI
     FSEIPNNGLP KPSFGHLTQP FDTPEFHKLY RVVPIRKVHS LSITWALPPQ EQYYRVKPLH
     YISWLVGHEG KGSVLSFLRK KFWALALYGG NGETGFEQNS TYSIFSISVT LTDEGYKHFY
     EVAHVVFQYV KMLQKRGPDK RQVLIWEEIQ KIEANEFHYQ EQTDPVDYVE SLCENMQLFQ
     KEDFLTGDQL LFEYKPEIIA DALNQLSPQR ANLVLLSAAN EGQCHLKERW FGTQYSVEDI
     DKYWSDLWAS DFELNPDLHL PEENKYIATD FALKVADCPE TEYPVKTLST QQGCLWYRKD
     DKFKIPKGYV RFHLISPLIQ QSAENIVLFD TFVNILSHNL GEPAYEADVA QLEYKLVAGE
     HGLVIRVKGF NHKLPLLFQL IIDYLSDFSF TPAVFEMITE QLKKTYFNIL IKPETLAKDV
     RLLILEHGRW SMIDKYQTLM NGLSIESLSS FVKAFKSQLF VEGLVQGNFT SREAKDFLNY
     VVQKLQFAPL AHPCPVQFRV VDLPNTHLLC KVKTLNKGDA NSEVTVYYQS GARNLREYTL
     MELLVMHMEE PCFDFLRTKQ TLGYHVYPTC RNTSGILGFS VTVATQATKY NSELVDKKIE
     EFLSCFEEKI KHLTEDAFST QVTALIKLKE CEDSHLGEEV DRNWNEVVTQ QYLFDRLARE
     IEALKSVTKS DLVTWFQAHR SNKKKVLSVH VVGYGKHEGD SEVTAVPEVQ NSSSGEIPHL
     IFLPPSSLMT NVTSIKDIKA YTSTLNVLPY HKILK
//
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