ID A0A162J8W4_9HYPO Unreviewed; 857 AA.
AC A0A162J8W4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE SubName: Full=Peptidase aspartic, catalytic {ECO:0000313|EMBL:OAA41078.1};
GN ORFNames=BBO_05614 {ECO:0000313|EMBL:OAA41078.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41078.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41078.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41078.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA41078.1}.
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DR EMBL; AZHA01000017; OAA41078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162J8W4; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..376
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 392..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 93416 MW; 266A8FDA65EE2B66 CRC64;
MRSSRMAAAA SAAATAVFVN AYDPAAVSIP YGDWLGIDGN WSTVRFLLEE QHCMTARGGI
YTPGDSKRWT SWGQYFLGLE YLGYGGNGAY GIDNINTWSP FTNIAFGMSN VLVAAYNTTD
YFNGLFGLGI SQGRFKGNIG ESALTQAVKT FGWIPSYSYG YTAGASYKNM PGSLTLGGFD
SARLVDHDTL FTITQSDNSP RVNVRSINVF NDRKPNGWDS SINKLSSYND TFMALVDSTT
PYLWLPESIC ESFASALNLT YNDTYKLYTL TNTQYQDYST SNAYSFTFSL ASIDNNDNFG
LPLSAPGVVN ITVPIKAFVG SLQYPFAKEA IKYGQPAVPY FMLRKATNGS SIIIGRSFLQ
EAYIRTKFDS GVFSLHQAAF PRDPDTDIKL NLIKQPSNSP YPRPPPTKDH HGLTTPQMIG
IAVGVVAFCT LLLAALCFWN RRRRQKKHGE TAAKEAESQD SSSTISPDSP MTPVSRILSK
IVRRKRSRRA TTTTRTSAPT EAPASEIYEL PAPLPPAELA AHNEDDDSVL GGTVAGTDDS
QNLSAYELAR RKLARQLAGP VPAYAPPENG IVPAEKDMHI DTNVVRTTTI PHPQPTYHFH
NVSPVRSHEG LGTNSLPGTL PSPVSPRTDW NTNELPSPIT ASLHPNSASS QSGSTGRRRA
GSNTMNGTSS ESGSARRSDS NSSSNSNGHE QSRERKVAFP LPQASFQRTP IEPSKVVCLG
PLPENVPLFK QQMLPSVSAT REQSWTGPAH HSHHRPSTGS LGSNYTDEED AMVEELTRQS
TSVSRSLGSQ SVTRPPALVD PLIRTVLPER TEEEENVSPT SEKSGAESHK SGGRIGGDDL
IHVPQMAEKR YSWEEER
//