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Database: UniProt
Entry: V4ABY4_LOTGI
LinkDB: V4ABY4_LOTGI
Original site: V4ABY4_LOTGI 
ID   V4ABY4_LOTGI            Unreviewed;      1072 AA.
AC   V4ABY4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Nardilysin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=LOTGIDRAFT_233049 {ECO:0000313|EMBL:ESO92600.1};
OS   Lottia gigantea (Giant owl limpet).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX   NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO92600.1, ECO:0000313|Proteomes:UP000030746};
RN   [1] {ECO:0000313|EMBL:ESO92600.1, ECO:0000313|Proteomes:UP000030746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23254933; DOI=10.1038/nature11696;
RA   Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA   Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA   Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA   Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA   Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT   "Insights into bilaterian evolution from three spiralian genomes.";
RL   Nature 493:526-531(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; KB202050; ESO92600.1; -; Genomic_DNA.
DR   RefSeq; XP_009056741.1; XM_009058493.1.
DR   AlphaFoldDB; V4ABY4; -.
DR   STRING; 225164.V4ABY4; -.
DR   MEROPS; M16.005; -.
DR   EnsemblMetazoa; LotgiT233049; LotgiP233049; LotgiG233049.
DR   GeneID; 20249131; -.
DR   KEGG; lgi:LOTGIDRAFT_233049; -.
DR   CTD; 20249131; -.
DR   HOGENOM; CLU_004639_1_0_1; -.
DR   OMA; INQVMEH; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000030746; 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:UP000030746};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          137..251
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          295..478
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          485..762
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          769..948
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          86..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..128
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  124272 MW;  237DBDD16E727907 CRC64;
     MIGIKLLRHF RKYTPRVHLT VRLFSPTHHQ PHLRVKTFKC QHISIRQRSA LPSTQKKMNI
     IKSLNDKREY RVINLENGLT AVLISDPSGA EECHAASQED ESEEESDEED EEMSGSEEDE
     EMEEEAVERD EDDKKKKSGE RKSAAALCIG NGSFCDPDDI PGFAHFLEHM VFMGSEKYPA
     ENELDDYLGK HGGYSNAWTD CERTLFYFEV QKKNFQKSLD MFANFFISPL LREDCVDREV
     QAVDSEFQMS VPDDDDRVNQ IISLRAKKGH PMDKFLCGNL KTLKTLPEER GVNIYANLRG
     FYEKMYSAQY MTLAVESKDS LDTLEQYVRE SFSSLPNNGQ PKPSFHHLKD PFKTAEFGRF
     YTVSSVENIH SLDIVWYLPP LSQQYRCKPL EYLSTLITHE GKGSILSYLK NRTLALGLSG
     GSSYNGLDNN STCSGFTINI TLTDQGLQRI QEVLMVIFQY IRLLQTVGPQ KRIFDELKII
     EENKFRWKEM GESIDYVEEM SENMQMFPVE HYITGRHLLY DWNEKLIEDC TMNLKPDEAC
     IILRTKAFDN DCIYDKEEKW FGTKYHVQDI DPEWIKQWKD PPDNKGLFLP EDNKYIASDF
     SISSETATQH PEVILEDDGC KVWFKKDCKF DVPKGCIYLR LTSHVIFDTI QNAVLCDLFI
     NLLLQNLTET VYPAVIAGYE YSIEGFPTGV LITLSGFNHK LLLFLEALLN HIEQFSCTSE
     LFDAVKIQLK KAYYNEMIKP YELAKMLEMS VLEANYNPVP DRYQNLSSVT QSMLDTFMLQ
     LRQNLYIDSF IYGNFHKEEV KSMGDLLKNK LQSAVPAKHL KPKRCYREID KRSIYCCVEG
     VNKDDNNSCV IAYYQSVPGS IYHSVLNELL AYRMKEPCFD FLRTKHQLGY SVGANSRLNN
     GILGLQVSVE SQADKFSLST IDDHINNFLQ DFQQILTDMT VDEFNGLVKS VITNKLIDEV
     TLEDEGNRLW REISREYYLF DRRDREISVL EKITHQELLD WYKQYVNKEQ KKLCLQVEGK
     KGKDMCINNE IEKSSDDCLI FQSIEDPART YITNIEEYKQ TLTILPYHII DS
//
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