ID   A0A1Z5JGI9_FISSO        Unreviewed;      1122 AA.
AC   A0A1Z5JGI9;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Protease III {ECO:0000313|EMBL:GAX13114.1};
DE            EC=3.4.24.55 {ECO:0000313|EMBL:GAX13114.1};
GN   ORFNames=FisN_17Hh043 {ECO:0000313|EMBL:GAX13114.1};
OS   Fistulifera solaris (Oleaginous diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC   Fistulifera.
OX   NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX13114.1, ECO:0000313|Proteomes:UP000198406};
RN   [1] {ECO:0000313|EMBL:GAX13114.1, ECO:0000313|Proteomes:UP000198406}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX13114.1,
RC   ECO:0000313|Proteomes:UP000198406};
RX   PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA   Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA   Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA   Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT   "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT   by the genome and transcriptome.";
RL   Plant Cell 27:162-176(2015).
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:GAX13114.1}.
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DR   EMBL; BDSP01000061; GAX13114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5JGI9; -.
DR   InParanoid; A0A1Z5JGI9; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000198406; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:GAX13114.1};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:GAX13114.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198406};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1122
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011989483"
FT   DOMAIN          112..239
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          267..447
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          467..770
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   REGION          37..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1122 AA;  127322 MW;  AB62C8B34B2FABDA CRC64;
     MRQTTAAMFL SSLTFCLCLA SSDSFAFHRS AQKASARHVS FTSPETTQSP AVNDGPLRKN
     DSGKTIILAS EEEFIKPDRD RYNYRMILLP NNLQVLLVSN GMKEGDVGVE AASVHVQAGH
     FDDSLSGLAH FHEHMLFLGT KRYPDEDEYE RFLNTHSGFS NAYTDMEDTN YYFSVTTEAG
     SPNEPSEALT GALDRFAQFF IAPLFSPDAV DRELKAIDSE YSMSKTSDSW RNFQLMKSAC
     NRDHRFSKFG CGNYETLSER GSDFLLSELK RFWDTYYQSF NLRLAVVGHA SLDTLQKTVE
     DTFGNLPQSE GFHRYAKSLP GQIFSREHVS GVVAFGPDQL GLVRKVIPYA ETRVIKLYFA
     TPPLDDPAVK KSRPDRVLAH ILGHESPGSL YHLLNGEGFI QSLSAGSAID TSDFSLFAVT
     VSLTPKGMQE REKVLDYVFQ WIALFKRSQE KLPYYHNELR QISEVNFKFR ENGDPTDFAS
     SAAELLFDDL LEPKMLIKGS SAVSDYDPDI ANAFFDRISP TNCMITITSS DFDSSQGEWE
     TEKWYGAKYQ TERIAEASIA VWTNPTIDER LHLPAMNKYI PTDFSLKCDS AKDKDEVDSA
     DTESVPPELI INQPYLRLWH KMDRFWRVPK TYVRFALNSP HIYSSPRSMT LNRLFQRVLN
     DDLNSFVYDA SLAGCGYRVS CAPRGYRISV SGYSEKVPFL LETLTSRIIS LIEEMKTGNA
     VLERRFKKAK ESLLRETKNY RLDTPHEVNN YNSRLLIEES VWYLDDYLNE LEGEWGMRDP
     LTMEECAKSA EQCFTGRLRC EALCMGSIDE DGARAVAKVV EDRFLNRVRP MSEAENPVFR
     SFKLPTRDEA VKIFGAGVSE RQFPLVHQNL AFSATEENHA VEIILQVGSE FDLGYEGMAM
     LDLMTHMSYL SAFNQLRTKE QLGYYVSSFA RKTAGGSWSM VVLVQSAAYL PEKLEERCEA
     WLVQFRKELD EMDPKDIVQE ASSVAAQLLE VETKLSQEVS RVWGEILNTE GLADASRTPA
     FDRLEKLADI LTVDEDEGES YMTGEELKRR LLDLYDRSIS ANSPTRRALS ARVYGHKAKA
     EYEASLKQPG VLSTYSDMIH LKQHLSTWPI IPYWTRNEVS SD
//