ID F1CZK5_FLAVE Unreviewed; 776 AA.
AC F1CZK5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=mitochondrial intermediate peptidase {ECO:0000256|ARBA:ARBA00012441};
DE EC=3.4.24.59 {ECO:0000256|ARBA:ARBA00012441};
GN Name=MIP {ECO:0000313|EMBL:ADX23534.1};
OS Flammulina velutipes (Agaricus velutipes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Flammulina.
OX NCBI_TaxID=38945 {ECO:0000313|EMBL:ADX23534.1};
RN [1] {ECO:0000313|EMBL:ADX23534.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KACC 42780 {ECO:0000313|EMBL:ADX23534.1};
RA van Peer A.F., Park S.-Y., Shin P.-G., Jang K.-Y., Yoo Y.-B., Park Y.-J.,
RA Lee B.-M., Kong W.-S.;
RT "Mating type genes in the edible mushroom Flammulina velutipes.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cleaves proteins, imported into the mitochondrion, to their
CC mature size. While most mitochondrial precursor proteins are processed
CC to the mature form in one step by mitochondrial processing peptidase
CC (MPP), the sequential cleavage by MIP of an octapeptide after initial
CC processing by MPP is a required step for a subgroup of nuclear-encoded
CC precursor proteins destined for the matrix or the inner membrane.
CC {ECO:0000256|ARBA:ARBA00025208}.
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; HQ630589; ADX23534.1; -; Genomic_DNA.
DR AlphaFoldDB; F1CZK5; -.
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:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06457; M3A_MIP; 1.
DR Gene3D; 1.10.1370.40; -; 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR033851; M3A_MIP.
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 Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 285..758
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 776 AA; 87116 MW; B77CC81AEB1565CC CRC64;
MIARVSRNVL PKPSAPFRFR GCLFEKDSFH RGSRRFSTET RPTIPASADD RSLVALFDHP
RYTPSGNYSS RTGLFGHTSL AHPRGLISLA NATYVRAQML TNRILNSRAS RDEMFKVVKN
LDRLSDLLCG VIDLAETVRN SHPDRAWVEA ANTAYETLCE FMNVLNTHVG LYEVRAVLAD
PEIVKSLSPE AHTTALIFWH DFEHSAINLR PEQREKFVSL STDILVLGRQ FLADVNAPRP
PASIKPSELS GLKDQGMGVR LKLQARFTQR DLLVYPGSLQ AQMIMHSAPA EEARRRVYMA
SNSSTPEQIE VLEAMLHRRA EVARLVGRES YGHLVLDNKM SKSPENVSHF LNALMDYTRP
YARSAIGALS QRKQAHLKTP PHPTIQAWDR DFYCPPEPPS PPIPLPPMTV GTVFMGLSRL
FRHLYGITFR PAETSPGEVW HPDVHKLEVV DEEKGIIGWV YADLFARRGK GSGAAHYTVR
CSRRTDDDDA EADNELSGLV VNSHDVRQSV EFEAAKKHRL PGQPGVYQLP LVVLICEFRR
PNSSDGATCL EWHEVNTLFH EMGHAMHSML GRTEYHNVAG TRCATDFVEL PSLLMEHFLT
SPDVLCLFDI NSTSTVSQGA NNAQDPCHAI DTYNQILLSA VDQRYHSSIA ISPNFDSTKE
YANLVNTRGL IPYVEGTSYQ TQFGHLYGYG ATYYSYLFDR AIASRVWSHV FAKDPLNRGQ
GEKFKDEVLK YGGGKDPWKM VSTILAKPEL ENGDADAMRE VGQWRIEDEM GLSGLH
//
