ID C1L5T7_SCHJA Unreviewed; 351 AA.
AC C1L5T7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative Mitochondrial processing peptidase beta subunit, mitochondrial {ECO:0000313|EMBL:CAX70065.1};
DE EC=3.4.24.64 {ECO:0000313|EMBL:CAX70065.1};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:CAX70065.1};
RN [1] {ECO:0000313|EMBL:CAX70065.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX70065.1};
RX DOI=10.1038/nature08140;
RA Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., McManus D.P.,
RA Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., Chen Z.;
RT "The Schistosoma japonicum genome reveals features of host-parasite
RT interplay.";
RL Nature 460:345-351(2009).
RN [2] {ECO:0000313|EMBL:CAX70065.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX70065.1};
RA Gang L.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
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DR EMBL; FN314332; CAX70065.1; -; mRNA.
DR AlphaFoldDB; C1L5T7; -.
DR MEROPS; M16.973; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
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:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
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; PTHR11851:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
DR PROSITE; PS00143; INSULINASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000313|EMBL:CAX70065.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..197
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..308
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 351 AA; 39718 MW; 4DC3559476118603 CRC64;
MALRLISRRL TPLVSSICHR RIGAATVYFP SFETVHMPET EVTTLKSNGF RIASENWNTP
TCTVGIWVDV GSRYESEFNN GVAHFLEHMA FKGTEKRSQQ SLELEVENKG AHLNAYTSRE
MTVYYAKCFV EDLPWAVELL SDILKNSKFE VSQVERERGV ILREMEEIES NYQEVVFDYL
HATAYQGTPL GRTILGPVEN VKSLKADDMR DFIKQNYKAP RMVLSAAGGI DHKQLCDLAE
EYFGDFQASY KEGEVVPSLL HCRFTGSEIR DRDDAMPLAH AAIAFEGPGW QVRTRWRLWL
LVVCTVLGIE VMVGDLMLPV NSPPSSSKKV RYTVSNISLL AIMILLFGVF T
//
