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
//