ID D8PQN4_SCHCM Unreviewed; 1048 AA.
AC D8PQN4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN ORFNames=SCHCODRAFT_46713 {ECO:0000313|EMBL:EFJ02419.1};
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN [1] {ECO:0000313|EMBL:EFJ02419.1, ECO:0000313|Proteomes:UP000007431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(2010).
CC -!- SUBUNIT: Monomer and homodimer; homodimerization is induced by binding
CC of the substrate. {ECO:0000256|ARBA:ARBA00011853}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000256|ARBA:ARBA00004569}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. PreP subfamily.
CC {ECO:0000256|ARBA:ARBA00007575}.
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DR EMBL; GL377302; EFJ02419.1; -; Genomic_DNA.
DR RefSeq; XP_003037321.1; XM_003037275.1.
DR AlphaFoldDB; D8PQN4; -.
DR STRING; 578458.D8PQN4; -.
DR GeneID; 9584953; -.
DR KEGG; scm:SCHCO_02611317; -.
DR VEuPathDB; FungiDB:SCHCODRAFT_02611317; -.
DR eggNOG; KOG0961; Eukaryota.
DR HOGENOM; CLU_006065_0_0_1; -.
DR InParanoid; D8PQN4; -.
DR OMA; YITEVHH; -.
DR OrthoDB; 227593at2759; -.
DR Proteomes; UP000007431; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR013578; Peptidase_M16C_assoc.
DR PANTHER; PTHR43016:SF16; METALLOPROTEASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G07610)-RELATED; 1.
DR PANTHER; PTHR43016; PRESEQUENCE PROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SMART; SM01264; M16C_associated; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007431}.
FT DOMAIN 470..730
FT /note="Peptidase M16C associated"
FT /evidence="ECO:0000259|SMART:SM01264"
FT REGION 1023..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1048
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 116174 MW; 5C95A475966F2746 CRC64;
MATSESFGNF DLVKRVKLDY TAVEVSKWRS RDSGLSIVHI DYEAPIVKGY FVVATEIFDD
SGCPHTLEHL VFMGSEKYPY KGIIDHFANR GFSNGTNAWT DDDHTAYTAS TAGAQGFLQL
LPIYVDHILY PTLTKSGFVT EVHHIDPQGK DSGVVYSEMQ GRENTSGDLM ALRLNQLSEP
EGSAYRSETG GLMAALRKLT VEKIRDYHHK YYVPHNLSLI VAGKLTGGTE SLLRVAQEQI
EPSIVAHGQN KGIKPTGWKR PFLETPSAPR PPFEKTIKDT IEFPEKDESV GELVINFLGP
PPNEFVERKA LDILGTYLTS STVAPLNKEY IEIESPMCTY IYMGQDTRAT KIFLPVYIGS
VPTELLDTFD EKLKASFQNI VKTGIDMDRM RMVIDRDERQ FRSKLESSKG DAFSDSLITD
FLYGAEDGSD IKRTLEEDTW YAQLRAWDSK QWTDLLSKYY IDQHSIVLRG KPSASLVDKL
EKDEKERIAK QVEALGPEGL KKAEQELNEA KAEHDKPIPT EVLNTFPVPD VKSIAWIPVQ
SVVQKGKGRQ SPAPAQNAAA LSTHINADGS ELPFFVEYDH VESDFVTIHA FFDLKKLPDH
LRPYATLYAS AFFSLPIKRA SGETLTHEEV VNRLDDETVS YEVSQGVSSG FAESFRLSIK
AETAQYETAI AWMHDLLYGP IYDRERLQVT IAKVQSALPE LKRDGSTVLS AVWSDAMYSE
RSTARAGTVL QQTEFIPKVA EQLQQQPDEV AKIMAEVRDT VAQPSGVRFS VTGNILALSK
PRSTFEKHFG TKLPSVELEP VTFTSDVLSD LGRNPAKKAI VMSLPTIESS FVTHTSRGIQ
GFGDAEYPAM RVALEVMNAT ESYLWRYIRG SGLAYGAYMS IDLEAGLTSF SLYRSSNSVG
AFEQAKKVVE GLCDGTIPLD TTTMDAAKSS IVYGVTKTVS TASRAALTSF VNQSLKGVSQ
NYQSEILAKT QTVTIDDVLQ SIRKYFLPLF DAKQSMVVAV TAPGKADEVA AGLAKEGFEV
ERRSMHIDES EMEGSESESG SDDSDESQ
//
