ID   A0A0V0ZN51_9BILA        Unreviewed;       928 AA.
AC   A0A0V0ZN51;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Mitochondrial intermediate peptidase {ECO:0000313|EMBL:KRY13899.1};
GN   Name=MIPEP {ECO:0000313|EMBL:KRY13899.1};
GN   ORFNames=T12_14515 {ECO:0000313|EMBL:KRY13899.1};
OS   Trichinella patagoniensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY13899.1, ECO:0000313|Proteomes:UP000054783};
RN   [1] {ECO:0000313|EMBL:KRY13899.1, ECO:0000313|Proteomes:UP000054783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS2496 {ECO:0000313|EMBL:KRY13899.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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:KRY13899.1}.
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DR   EMBL; JYDQ01000129; KRY13899.1; -; Genomic_DNA.
DR   EMBL; JYDQ01000129; KRY13900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0ZN51; -.
DR   Proteomes; UP000054783; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06457; M3A_MIP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024969; EIF3F/CSN6-like_C.
DR   InterPro; IPR000555; JAMM/MPN+_dom.
DR   InterPro; IPR033851; M3A_MIP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01398; JAB; 1.
DR   Pfam; PF13012; MitMem_reg; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SMART; SM00232; JAB_MPN; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          23..159
FT                   /note="JAB1/MPN/MOV34 metalloenzyme"
FT                   /evidence="ECO:0000259|SMART:SM00232"
SQ   SEQUENCE   928 AA;  106670 MW;  510F5F2868AB9D50 CRC64;
     MDSADTEHSL IKNNVINNGA SVEITLRPEV ILHLSDHFTR ERVNGRNEHF QVYGALMGKQ
     SGRFIEVIRS FPVTSVKMHG LFPNYDYLMD TMKSFGSIYK DEIFVGWYVI TGLNYFNELD
     HQMHNVSMIV NENPIILRFN PFDNLTRVLP IEFYESNPAM TEFVLLSYSI VYQKNEMICI
     AHVSEQAVEK SNLTANNTLT RLNSQLNAVR LLMMRQKLVI DYLQAVASGT FPINHSILRK
     ISAHINSLLS VKMEYIENDL YASEDDKNLL LSLQAMAKLS LETSSGLFNV ENLNCSDGFS
     QLANDVHAEC NRLCAEAQST NRKRKMVEIF DDMSNKICSA ECVRLLHPDP KIVNAADEAV
     YQLGVLIERL NTSAELYNIF RRSVEEGDIL PLDEVDLRVG ELLLADFEMS GVHLPELSRR
     KFVSFTEDLF RLGSEFMRCC DSPVRILTSD IAEPFAKYLT DVGDGFSELY TALLNYNDHR
     VRKFGYLTYF QPSKYQETKL KNLLHYRDAI ATLVGYRSFA DRAVQKLLLN NSSKVESFLK
     CTLDTVYDQA MKERSELAKF QDGRQPYVWD LPYLCYTAKD NLTQLSFSEL VPFLNRQQVI
     NNLSIMLNYL YGVQIVEAEI NPGEVWHDSV TKWLVQNEQG STLGVIYCDW IDRRGKVSDS
     HFTIQCGKQL SDGSYQQPVV VLSFRCRDRC SDKAYFTLSQ LENFLHEMGH ALHSIFGRTR
     YQHVSGRAEH FLNLHFFRTR CATDFAEVPS NLMENFMYNP KTLLMLTKQA DGSSMPDETI
     EKICRSRNIF GALELVQQIL MSLCDLKLHE QGAEIENTVE FCRSLYSDVG FECLMPEQTA
     WQHRFSHFIP YGSKYHIYLV AKAASLLLWR QSFEKDPLNR QQGDRWRRLQ SFGGERSVAD
     LLEEALGYCV SPSQLAHALR HQLDDTFS
//