ID K1WWI1_MARBU Unreviewed; 800 AA.
AC K1WWI1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Eukaryotic aspartyl protease {ECO:0000313|EMBL:EKD17431.1};
GN ORFNames=MBM_04292 {ECO:0000313|EMBL:EKD17431.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD17431.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD17431.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD17431.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; JH921436; EKD17431.1; -; Genomic_DNA.
DR RefSeq; XP_007292181.1; XM_007292119.1.
DR AlphaFoldDB; K1WWI1; -.
DR STRING; 1072389.K1WWI1; -.
DR GeneID; 18760227; -.
DR KEGG; mbe:MBM_04292; -.
DR eggNOG; ENOG502RV5I; Eukaryota.
DR HOGENOM; CLU_009988_1_0_1; -.
DR InParanoid; K1WWI1; -.
DR OMA; WIPSYSY; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF89; SACCHAROPEPSIN; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EKD17431.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EKD17431.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..800
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003853127"
FT TRANSMEM 442..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..401
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 412..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 85394 MW; 255387A002BBA3A8 CRC64;
MMDSRWLRVL GVAASLVRCA EGDGKALSVP PSEKWYGDDG TWSAVSLRVG TPQQWIDVMV
STASSETWVV GDGGCGPGDT QCVFTRGGTF APSKSSTWKD QGLYELGASQ QLGNNGVGLY
GLDTLTFGGS GVTISSAIIG AFNGTGPIHG ASYLLGFFGV GIIPGAFNNI APLSAVSALV
EEVGAIPSYS WGYTAGAHYR QKGTVASLTL GGFDLNRFIN HDTNFNLNAA KQLLTSINKI
TVSSSQASNN WTAPVQLLST TDQVSAVFDS STPFLWLPPS VCERFATALG LSYNTSLNLY
TFDDNPSQHD VLAASQLSFT FTFADMLSAP STVDITLPYD AFDLQLKYPA IPGTGFGDPD
ATKYYFPLRQ AENEAQYTIG RAFLQEAYLI ADYERNTFSI FQALHPSDSV TNTSIHEINP
PSDSPLTGGP GTPKASKLTT GAIIGISAGA FVSVASMAVA IVYLCFRKRQ KQARDSDSEK
SSSSSPSSLP RSGSPLDHEV NHKATPPPIH IHEVDGNTSY PTEVGADATH ERFELPAPLG
PVELDGESCG STQDSSYLSA YECARRKMER QQAEFAATQG AGASPPRVEK SETDISHMGH
YRAPDTENQH FRASTSSETQ GDSPPIYDRI NPANVVYAGR LPDNVQPPGL APPLFGRDGR
VYRPEVSGPP PDMNTNSSLG SELTFDAFYR NLCSESSGSN TDLYGASTGS IGSHLVSPLQ
SAPSESGARI GGTNTVSPLD NSSPDALWSE RAGYAQGGSS RENPVLDQLS SRNRLDGEDL
IHVPQLAERR FSWEHERTRT
//
