ID F2SK21_TRIRC Unreviewed; 796 AA.
AC F2SK21;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Mitochondrial intermediate peptidase {ECO:0000256|ARBA:ARBA00018046};
DE EC=3.4.24.59 {ECO:0000256|ARBA:ARBA00012441};
DE AltName: Full=Octapeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032470};
GN ORFNames=TERG_03374 {ECO:0000313|EMBL:EGD87124.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD87124.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; GG700650; EGD87124.1; -; Genomic_DNA.
DR RefSeq; XP_003236329.1; XM_003236281.1.
DR AlphaFoldDB; F2SK21; -.
DR STRING; 559305.F2SK21; -.
DR GeneID; 10373142; -.
DR VEuPathDB; FungiDB:TERG_03374; -.
DR eggNOG; KOG2090; Eukaryota.
DR HOGENOM; CLU_001805_0_0_1; -.
DR InParanoid; F2SK21; -.
DR OMA; ALMFEYM; -.
DR OrthoDB; 735202at2759; -.
DR Proteomes; UP000008864; 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:UniProtKB-EC.
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:UP000008864};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 288..762
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
FT REGION 766..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 796 AA; 89353 MW; BA8DDC6BFA80A3B1 CRC64;
MLRALQPRSW TCSRCLLRIT AGISRCYSVA VPERTKLDPA IAGLSGANRH DDTNLRLVFD
SNSFWREFSQ RQLASSRRTG LLQNQYLTNP EGFRKFAHIS LHKCQKIVGK VLAASTLEDF
RRMAKDLDRL SDLLCRVIDM AEFMKTNHPD PAIQEAATEA FAFIFEYMNI LNTTPGLHEQ
LKRAIENPEV TSHWSEEENV AATAFLRDFA KSAIHLPPED RHRFVTLSNE ISQLGPAFVR
NMNPETSQLS FNKNQLQGMD PDLLRKLKRW SKVTIPMYGS TPKAALSTVE DAEVRRQIHL
AYRTSSREQI GRLETLLQRR AELAKLSGYQ SYAHMTLSDK MARTPEAVVN FLSSLNASNR
GQLDDELSKL IALKQIESPL ASNLQPWDYS YYIEKYYVKH GRERRSRSAD LLPSFFSLGT
VMQGLSRLFT RLYGVRFVPS ETLPGETWNP DVRRLDVWDE DDNHIAVVYC DLFSRPGKSP
NPAHFTLRSS REISPTEIAE CASLPDSPHP NDGMTTGLKP GTNRLYQLPT IALICDFDTP
TSSTPSAQPS LLSEHSVRTL FHEMGHAIHS VLGRTDLQSI SGTRCVTDFA ELPSVLMESF
AMDPQVLRLY ARHWSTDDPL PEDMVQNIHL NRQNRDSIHG GMDNETQIIM ALMDQAYHTI
SAGCHIDSTA ILHAVSSNHS SIPDPADSKT AWQGYFTHLF GYGATYYSYL FDRAIANKIW
SDVFGGGDLS VDRNAGERFK NEVLRWGGGR DGWSCVAGVL GTSNPANSNG RLSEGGEEAM
REVGRWGLGK TGSSEP
//
