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Database: UniProt
Entry: A0A1D2NBZ4_ORCCI
LinkDB: A0A1D2NBZ4_ORCCI
Original site: A0A1D2NBZ4_ORCCI 
ID   A0A1D2NBZ4_ORCCI        Unreviewed;      1256 AA.
AC   A0A1D2NBZ4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Nardilysin {ECO:0000313|EMBL:ODN02783.1};
GN   ORFNames=Ocin01_03937 {ECO:0000313|EMBL:ODN02783.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN02783.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODN02783.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODN02783.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN02783.1}.
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DR   EMBL; LJIJ01000096; ODN02783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D2NBZ4; -.
DR   STRING; 48709.A0A1D2NBZ4; -.
DR   OMA; ICHFINE; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000094527; 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; 1.
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:UP000094527};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          298..401
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          444..629
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          634..903
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1154..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1206..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1154..1197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1256 AA;  143420 MW;  5892FB376A71DF36 CRC64;
     MSQNRQPVKS FQPCMKCCRP RRCPESSDHS KSKKSSTPVP IPSTNTESCQ DIIKSPLDQR
     LYKAITLGNG VRVMLISTFN VERQDGETDA TKTPCQVPEL ADFNKTYLGY NNPAAKVKCA
     CPCDERKPCC GKGSKEEEAK RSILKDIVAN IKHTCCSANQ NQPRQSEEKK VSFDDNLNQF
     RNAIERPSNP DDLITYQNTI FNELQKRADR FKHISEAKSR SRFEQSSVKL HEDKDRAAVD
     SLAGEMHKLD SNGEADIIIE NRSSTHFETC DGDFIDETAP RSNRPQLTSP YNSDLDGTVY
     LVIGTGYFDD PEDQPGLAHF CEHAVFLGSN KFPEPNQLFK LVLPYEGYVN AYTSGMMTTF
     VTSASFRLFP LAVEILGDMV GFPLFPNSLV AAELEALDSE YSLRQDDTPK YFQLVGSLAK
     NGHVMRKMDS GNMSTLTVPN FYRKLVEWRR IYYNPSRMTV ALEAPFPLDY LERLAISSFG
     KIASAALPHI NKHLLISSPF EMNRFHQIYH VPSVYHSEFL SLHWAVEAKA WKNLRVKPLE
     YLGAIIAHKS EGGLFRYLTT QGLATNVEAG CWESDVTKNH FTSVFSISVD MTEKGFKRQD
     NILQAIFGYI QMLINNGPQK SFFQELQKQQ LDSFHYQAAE TSFNVGESCA RWMQYIPPKW
     CLISPGLTAE FDDKTIQRYT ESLKVETANV IIFSKNYRAV EYLRNNNMEE FYNTTFAAFH
     FPTELEEKMR RTKDEYATKF TLPVPNSLLL GTKCSRSREE DMLKKGTMLK IKGKLVVQYV
     GRKMRVARGV LPQAKYTFWI GSPIASYVGA PEGNATKMII WSRLFNEIFK TKFYHASNAD
     LQLETEISQG ELHIMLAGPH TMLPSLVEQV LELFNNFENI LDPIQFEVVR TAFIESLDNT
     ILDNRFLAWD LFYYLWTNNH ELIFDHKRHA ERGLTFNSFI TFVSSFKIKM YIQGHLYGYV
     TKSQGEKVAN ALTKLDYSPI DIRQYIVFRC LRLPLGERVI RVHTQNPHIH TSVVINSYQF
     GQLTPVEETV VKFFTQTMSD AAFYQLRTEQ QLGYIIIIYA EVTFGVSSII VELVTQPKNF
     TTEYCNECID KFLIDFFVTN LADQESFEEF SLGKPKLELP FPVIQNLFAS NLLQNPFTYR
     KLSIQVVGTV DHTSPQTKTH EKAESPTQII PPSTKESRMD ETANSKVYRS QSLGGRTTID
     RMRAAKKSLK MRDDSSVSSR GRKTSSGITT KVVNDIAKFK SSLMYYPKLY NNNNKN
//
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