ID   C5K875_PERM5            Unreviewed;       699 AA.
AC   C5K875;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN   ORFNames=Pmar_PMAR015823 {ECO:0000313|EMBL:EER19263.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER19263.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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}.
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DR   EMBL; GG671101; EER19263.1; -; Genomic_DNA.
DR   RefSeq; XP_002787467.1; XM_002787421.1.
DR   AlphaFoldDB; C5K875; -.
DR   EnsemblProtists; EER19263; EER19263; Pmar_PMAR015823.
DR   GeneID; 9039517; -.
DR   InParanoid; C5K875; -.
DR   OMA; ALMFEYM; -.
DR   OrthoDB; 276723at2759; -.
DR   Proteomes; UP000007800; 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; 1.10.1370.10; Neurolysin, domain 3; 1.
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; PF01432; Peptidase_M3; 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:UP000007800};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          240..656
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   699 AA;  77675 MW;  B3FACF9F323AF88D CRC64;
     MMLRRDIPKT AAASLWRRLA WPKATLSTAV DYLGVPGLRK PKDFPRLATT AVADARATLG
     AWNIDDSPHK VVNMIDGVSN SLCRIADAAE LTRNVHSDDH WVNEASEAVN IIAQYMSEAN
     VDSTLYDKCV PAAKRAVAED GGCSREEQDV IKAMREAMEN EGVHLDEQRK KELIALQEED
     AVKSFEIVSQ GDNDDPSDDG QWLNVPQQWM SILRLLPKRT VHKDVTEVFL PKDHAAIGYL
     LKACEDPTVR QKVWKMNHRG EPKKEAALKD LVSIRQQLAR IRGYNTWNEY VMRESVLSGS
     DAVKDFLSEL WTALLPGLAR ELSVLESTKR DHTNDPNATL QPWDIDFYVS MWKQMNQPSS
     LQELGVNLSI NALIEGSQRV SSTVLGVDMK ENNIKGETWS DNDVRRFEFH DAATSDPYGI
     LYLDPCERAW KKVQSAQFTI AGSCVLPDGS RQLPRTAMVL SLPEIQGALG QGAATTYMHE
     FGHAAHSILS QTTLQHFSGS RGCIDYVEFP SHLFEYFALD PNTLSSLLLP NLSSKAVEDY
     GNFRMAFGHI EAAQQLIYAL VDQVFYAHGS VPEDLAHFLP HSHAMSNERL IELLSPPGQA
     QFSHLVHYGG NYYCYLLCKA VAADVWSRGG FADGDPMAGQ RLRHFLEAGS VTQTLDKIYE
     LVPSGRLESA SSAAGHVPLD AMLSLLNTCT SIHGNGHHH
//