ID   A0A2V0P5C1_9CHLO        Unreviewed;      1072 AA.
AC   A0A2V0P5C1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Chloroplast processing enzyme {ECO:0000313|EMBL:GBF93050.1};
GN   ORFNames=Rsub_05661 {ECO:0000313|EMBL:GBF93050.1};
OS   Raphidocelis subcapitata.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Sphaeropleales; Selenastraceae; Raphidocelis.
OX   NCBI_TaxID=307507 {ECO:0000313|EMBL:GBF93050.1, ECO:0000313|Proteomes:UP000247498};
RN   [1] {ECO:0000313|EMBL:GBF93050.1, ECO:0000313|Proteomes:UP000247498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-35 {ECO:0000313|EMBL:GBF93050.1,
RC   ECO:0000313|Proteomes:UP000247498};
RX   PubMed=29795299; DOI=10.1038/s41598-018-26331-6;
RA   Suzuki S., Yamaguchi H., Nakajima N., Kawachi M.;
RT   "Raphidocelis subcapitata (=Pseudokirchneriella subcapitata) provides an
RT   insight into genome evolution and environmental adaptations in the
RT   Sphaeropleales.";
RL   Sci. Rep. 8:8058-8058(2018).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:GBF93050.1}.
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DR   EMBL; BDRX01000037; GBF93050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V0P5C1; -.
DR   STRING; 307507.A0A2V0P5C1; -.
DR   InParanoid; A0A2V0P5C1; -.
DR   Proteomes; UP000247498; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF34; ZINC PROTEASE PQQL-LIKE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247498};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        1036..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..144
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          186..249
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          228..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..249
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..813
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1072 AA;  112569 MW;  F5AA7863CCCBEC2C CRC64;
     MGAVYRGLEP AEISDYDAAL PLGPSELLHG HLSNGLTYYV RPCKKPAQRA AIALAVRVGS
     VCEEEGERGV AHILEHLAFN ATENYSNHEI NAYTSADETV YQLTVPTGEW RLLERAISVL
     GEWAGRIRCA PADLAKERGP VLEEWRMGRT GGGRMQEAHW ELLLAGSKYA SRLPIGLQSV
     ITSCPPDAVR GFYEKWYTPE RMAVVVVGDF GDPGRVVECI AAHLGTLGPR PGVPPAAPQP
     QPPRQPPPEL KSKGKGGGGG RGGKPAGSSG GAAACGAVCA SCAPAAAAPW APHSEPRCKA
     FVDREAQGAL VYASFKVPRR PCGTPAEFKR VITDQLFITA LNNRLFRASR ALDPPFFDAQ
     ASDEGLCSAV DAYVLSAAAP DGGTLRALEA LLTELARLRL HGLSDGEFRR AAAAIEAQVE
     TTYLERHQCH SEDARDEYVR HFTGGEFVTG QEFEARLYRA LLPQITRAEV EAVAARLGPA
     DSAVFKTVEH RRRHSDADVA AVVARVARAE QRGEVARWRQ DEVPDSILPS EPEPGGVVFE
     RRLALLQGHE LICGNGLRVV LLPRSSLDDE LLITALAVGG LSELPPSLLG VGRMAHLLAG
     ELGVYGHRPQ ALNDALAGKR IDLSLSAGAY TRSLRGSASP VDAAELLQLV HALFTARLEV
     VEAELHTAVV QLSQSIEAQR RSPTFVFESR LRQMNYGGCY YFEPLTLAEV DKADPHAAVA
     LHSEMFGDPS EFTVALPLVE RYLASIPKRP PPPPGPAAAA VAAAAGMLGG GGARGAAAGA
     GAEGSGGGGG GSGGGAKTDG KRKAGKKSGG GGKRGADDAA AEPPLSPRRS PHRGRDARAL
     TPLPFEFPEA PVVEDVAVDM VYAVAASPFF GAESPSREGL LRGEVSIAFS CAPDDREGLV
     AAALEVVAAL QAEGPTAEEV ETVRNLERLE WETGQEDNAW WHEHAVAALQ GRGMAETGDV
     DAVFGRMRAA HESVLSALAP EAMRAALQRL LPSPPTRRYT VVTMTPRPPG LLLSAALRAR
     AAWAAASDAA GGEGRAAAAA AVVAVGAAAA VAFAVAAWRR RGAGGGGAGG AA
//