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Database: UniProt
Entry: A0A0C7N6C4_9SACH
LinkDB: A0A0C7N6C4_9SACH
Original site: A0A0C7N6C4_9SACH 
ID   A0A0C7N6C4_9SACH        Unreviewed;       775 AA.
AC   A0A0C7N6C4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   03-MAY-2023, entry version 34.
DE   RecName: Full=Mitochondrial intermediate peptidase {ECO:0000256|ARBA:ARBA00018046};
DE            EC=3.4.24.59 {ECO:0000256|ARBA:ARBA00012441};
GN   ORFNames=LALA0_S02e03510g {ECO:0000313|EMBL:CEP60956.1};
OS   Lachancea lanzarotensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP60956.1, ECO:0000313|Proteomes:UP000054304};
RN   [1] {ECO:0000313|EMBL:CEP60956.1, ECO:0000313|Proteomes:UP000054304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP60956.1,
RC   ECO:0000313|Proteomes:UP000054304};
RA   Neuveglise Cecile;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of an N-terminal octapeptide as second stage of
CC         processing of some proteins imported into the mitochondrion.;
CC         EC=3.4.24.59; Evidence={ECO:0000256|ARBA:ARBA00000436};
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; LN736361; CEP60956.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C7N6C4; -.
DR   STRING; 1245769.A0A0C7N6C4; -.
DR   MEROPS; M03.006; -.
DR   HOGENOM; CLU_001805_0_0_1; -.
DR   OrthoDB; 735202at2759; -.
DR   Proteomes; UP000054304; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:UP000054304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          292..767
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   775 AA;  88206 MW;  4A0AFD7E98086BFA CRC64;
     MILRRTGALK VYRSPFQTHL RFLATVPISK AKHDIKKVFD DQRYWRDINN QTYRTAESNN
     TNIFGRLKNA TKVADKLETG LFQNPYLTSS QGLRKFSLRT LEEAQQLVDT MRSDHSPHGL
     LTYVQRLDRL SDMLCRVIDL CEFVRASHPD PHFVQAAQLC HEEMFEFMNV LNTDTSLCEV
     LKAVLADKSL VSQLSVEELR VGKILLEDFE KSGIDMAPEI GEQFITLSQQ ISLVGQEFIN
     NTDYAKNQSV SIPCSDLEKS GTSKILLDQL SRDARGRSYK IPTHGYIPFA ILRGCPDEKI
     RMKVWTAMHS CSDQQIVRLK QLVKLRGYLA HIMGKESYAQ YQLEGKMAKS PVYVRGFVQS
     LVDTTKPLAV QELRVLANLK SEHRGLKKPE SDLEVLDLVR PWDRDFYSAL NALQQQRKTL
     ENEQIKSYFS LGTVVQGLSN LFQSIYGIHL EPVVSVPGET WSPEVRRLNV VSDTEGIIGV
     VYCDLFERQG KTTNPAHFTV CCSRQIYPEE TDFSTIQTGQ LQTTGEKFQL PVISLVCSFA
     HETESDESAC LLQLSDVETL FHEMGHAMHS MLGRTSLQNI SGTRCATDFV ELPSILMEHF
     ARDPRVLSSI GQHYITNEPV PLELLKLNQN ELNYLQHTET YSQAKMAMLD QGLHSSIMLT
     DQPINVVEMY HDLEKRLGVL SDDKSNWCGR FGHLFGYGAT YYSYLFDRAI ASKVWSHLFA
     RDPFSRQNGD KFKNAVLKWG GSRDPWECIA DALDNKTLSN GDENAMRFIG RTEDI
//
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