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Database: UniProt
Entry: A0A166J3A2_9AGAM
LinkDB: A0A166J3A2_9AGAM
Original site: A0A166J3A2_9AGAM 
ID   A0A166J3A2_9AGAM        Unreviewed;      1062 AA.
AC   A0A166J3A2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Presequence protease, mitochondrial {ECO:0000256|ARBA:ARBA00020167};
DE   AltName: Full=Pitrilysin metalloproteinase {ECO:0000256|ARBA:ARBA00034552};
GN   ORFNames=SISSUDRAFT_1038822 {ECO:0000313|EMBL:KZT44320.1};
OS   Sistotremastrum suecicum HHB10207 ss-3.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Trechisporales; Trechisporales incertae sedis; Sistotremastrum.
OX   NCBI_TaxID=1314776 {ECO:0000313|EMBL:KZT44320.1, ECO:0000313|Proteomes:UP000076798};
RN   [1] {ECO:0000313|EMBL:KZT44320.1, ECO:0000313|Proteomes:UP000076798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB10207 ss-3 {ECO:0000313|EMBL:KZT44320.1,
RC   ECO:0000313|Proteomes:UP000076798};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV428004; KZT44320.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166J3A2; -.
DR   STRING; 1314776.A0A166J3A2; -.
DR   Proteomes; UP000076798; 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:UP000076798}.
FT   DOMAIN          484..753
FT                   /note="Peptidase M16C associated"
FT                   /evidence="ECO:0000259|SMART:SM01264"
FT   REGION          1041..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1062 AA;  117468 MW;  5113046ACF4DC00A CRC64;
     MAPGIDVPPK ANGVTTKQTV AKLGNFDLVK SIKVDYTDLT VSKWISSKTG LTLIHLDYEA
     PIVKGYFVVR TEIFDDTGRP HTLEHLVFMG SKKYPYKGIL DHFANRGFSN GTNAWTDIDH
     TAYTVATAGS QGFLQILPVY LDHILNPTLL KSGFVTEVHH IDGAGEDSGV VYSEMQGREN
     TSGDLMALRM QRLLNPDGSG YRSEIGGLME VLREITVEDI RTYHSQYYVP HNLAIVVAGK
     IDPAAILETL ETHVEPGLIE NGFDKGPNPP GWKRPFVETE SANRPGIPKT IQSIVEFPEK
     DESTGEIAFS FVGPSPTNYL EDSALDLLGT YLTSSATAPL NKEFIETANP LCTYIYFDAN
     TRVKYSDLQI IVGSVPVQHL EVFDQKLISA LTRIANEGIN MDRMSRVISR DRRKFFSALE
     SAQGDAFSTN IISDYLYGDA NGKTLQPLLD DLAYYDALSH WTSDQWVELL RRYFLDSPRV
     VILGKPSAGL ADRLQETEKA RIQRQIQDLG PAGLENARKE LEKAKTEHDA PIPQDILSQF
     KVPDVRSISW IPVKSYQNAV PSERSAPRVI SRSDELAKHI EADGNDLPFF VQFDHVKSDF
     IKIHAFLSLR SLPDHLRPYL TIYQGSFFSL PVKRASGVLS HTEVVDQLEN ETVGYSIGLG
     QDGSFEEALK ISMEVETTRY SEAISWLRDL LFNSQFDEER LRVTVAKVQQ SLPELKRDGS
     AVASSFSGDL LYNRNSTSQA NTLLQQIETI PKLARELEED PARVIQSFTE LRNWITKPAG
     LRFSVSGNVL AVKEPRSSWA KYFTVERTPL EPIRLACETL SDLGKAPSQK AVVVSLPTIE
     SSFSVHTAKS IQGWGHPEWP ALRIAVECLN ALESFLWRYI RGSGLAYGAY IGADLESGLV
     SFTLYRSPNA YKAFEEGAKV VRGLADGSIP LDQTVVDAAK SSIVYGVTKA VSTPGRAAMN
     SFANQALKGV SHDFNVQLLD KYQEVTIDDV RTAIKRRFLP LFDPSSSIAV VVSAPGKVEE
     ISSSLTEAGF TVDNRVLEVA EDEAMEVDDG SSSDDSSGSS ER
//
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