ID A0A2G8K142_STIJA Unreviewed; 1058 AA.
AC A0A2G8K142;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE SubName: Full=Putative presequence protease, mitochondrial {ECO:0000313|EMBL:PIK41727.1};
GN ORFNames=BSL78_21427 {ECO:0000313|EMBL:PIK41727.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK41727.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK41727.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK41727.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK41727.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {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:PIK41727.1}.
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DR EMBL; MRZV01000993; PIK41727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8K142; -.
DR STRING; 307972.A0A2G8K142; -.
DR Proteomes; UP000230750; 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; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR PANTHER; PTHR43016:SF13; PRESEQUENCE PROTEASE, MITOCHONDRIAL; 1.
DR Pfam; PF08367; M16C_assoc; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:PIK41727.1};
KW Protease {ECO:0000313|EMBL:PIK41727.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT DOMAIN 487..734
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
SQ SEQUENCE 1058 AA; 118455 MW; 0ECBDD91C2BEA519 CRC64;
MEGRFRSGVV QIVYEGIQHY QKRLCKTTSL ELCSMDIRLR RSPELYLTAI KLSHLQTGAE
HLHIARDDTN NVFSVGFRTT PMDNSGVSHI LEHTVLCGSQ RFPCRDPFFK MLNRSLSTFM
NAFTASDYTM YPFSTQNSKD FQNLLSVYLD AVFFPNLNHL DFLQEGWRLE HDSNEDKGSP
ITFKGVVFNE MKGAMSSPDQ LYAVHCQNML LPSHTYSYNS GGNPNDILNL THEQLREFHA
THYHPSNARF YTYGDLPLES HLEQINSLAL DRFHKIEPGT SIPNETRWTE KLLSIVHCCV
MSPDPDKQTT VSVSYLLPRI TEVHESFEMS FLASLLTSGP TSPFYQSLLD TNIGAGYSPV
CGYDGSTREA SFSVGLQGIL AEDEQKVKEI IRSTLEKVTE EGFEAERIEA VLHSVELAQK
HQTTSFGLGL VMSLMSVWNQ DGDPISSMQL DKLVSSFKQK IADNPRYLQD LVQKYLVNNQ
HQLWLRMTAD ENYNTNQEKA EMDKLNTLVQ ALDENTKEQI YQAGIELAES QNQEVDVSCL
PTVTVGDINP NTRRTDIKTE CLDGSYVQLH EQPTNGVTYF KAVSPLGLAD QELVQYLPLF
CNVVTQMGTK NMSFRELAKE EELRTGGLGV GPHIIQRRED TTSYEVGVAL SSHCLERNLH
EMFGLWQDIF QSVTLSDQER LTTLVRMEAA EMANSVSFMG HAYAMRGAAS SLSPVGQIGE
VTGGMSQVNL MKQIAELDDL SDVVSKLTQL SSVLLNRSNM RFCLNAAPSG MSPAVEALDS
FLTKLPGRRG SRSSLEDAIS VTKDGDFSAV SSCRHFQLPF PVNYVSMGTT AVPYKHEDFA
KLVVLARLLS AKFLHKEIRE KGGAYGSGAT MSNDGTFKFY SYRDPRSMET LDVFHQSLPW
IQSQNFTNQD LDEAKIALFS NVDAPIAPGS RGVSTFLNGV TDDDRQIQRD RLFAVTREDV
VDVAQRKTKL PTHNSVVVKW LRQWTCDLRI TGSSPGQIIA LCPWARHFIS IASLHPGVKW
DLPVTCKYSC MRRFVAAPYG KSQGHVAVVH CGAPGEIV
//