ID W7I8P8_9PEZI Unreviewed; 1229 AA.
AC W7I8P8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=PDZ-like domain-containing protein {ECO:0000259|Pfam:PF12812};
GN ORFNames=DRE_01900 {ECO:0000313|EMBL:EWC48678.1};
OS Drechslerella stenobrocha 248.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC Orbiliales; Orbiliaceae; Drechslerella.
OX NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC48678.1, ECO:0000313|Proteomes:UP000024837};
RN [1] {ECO:0000313|EMBL:EWC48678.1, ECO:0000313|Proteomes:UP000024837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=248 {ECO:0000313|EMBL:EWC48678.1,
RC ECO:0000313|Proteomes:UP000024837};
RA Liu X., Zhang W., Liu K.;
RT "Drechslerella stenobrocha genome reveals carnivorous origination and
RT mechanical trapping mechanism of predatory fungi.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; KI966372; EWC48678.1; -; Genomic_DNA.
DR AlphaFoldDB; W7I8P8; -.
DR HOGENOM; CLU_003212_0_0_1; -.
DR Proteomes; UP000024837; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR025926; PDZ-like_dom.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR PANTHER; PTHR46366:SF1; PDZ DOMAIN-CONTAINING PROTEIN C1685.05; 1.
DR PANTHER; PTHR46366; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR Pfam; PF12812; PDZ_1; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000024837}.
FT DOMAIN 494..569
FT /note="PDZ-like"
FT /evidence="ECO:0000259|Pfam:PF12812"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1229 AA; 136352 MW; AB42F45BE1B35AD8 CRC64;
MEEQQESPIS GVKPTVPSAR TITAGQSLIA ERRRSKPDIV LRSEVPRISS GPAEITTPVS
ATFRPRSDSL ISIEHPIPEL PLEESLISLP EIRESRPDPL GPTHEELEGR PAEAPLTKTP
TLELPSLIST IPVKPLPEIV NEPQATISAA DKETWDRTLP RVIRGIVSIK ATTVRPFDTE
TAGDYTATGF VIDAKRGLIL SNRHVVSPAP ITAVAIFFNY EEVKLAPIYR DPVHDFGIFR
YDPAALKHMV ATEIPLRPDL ARVGLDIKVV GNDAGEKLSI LGSTLARLDR PAPVYGSDMY
NDFNTFYFQA ASGTSGGSSG SPVLNVQGEA IALNAGGSRS SQSSFYLPLD RVVRAVELLK
LGKPVPRGTL QTEFYHQSYD ELKRLGLSDE NMMACRERNA DATGLLTVRM VLKGGPAASP
QPTNPANNTE EDPSTPIQGL EPSDILLTCN GQYITNFIGL WQIIDDSVDK EITMEVYRAK
VLRKCTLKVQ DLHSITPDRF LHFGGAVFHD ASYQECRWYN EAIGNGTFCA SSGFMMWSSY
SRDFLVTKVD GKPTPNLEEF MKVIRNVPDY KRIQCMTRAL GKSDDQLLMV DIDWHFYPAS
LFVRDDQEGF WRREDISPPA AIIEKEDQKA VPATEGENDS AIDVESVSSS PPAPESEAAN
YTAAGSQDSS PQPQPQPEVL DDEEVEEDDT PLEVAIEELR CCMAYVRCFL PHTIYGYTSN
MSYSGVGLVL AVDPIPLLFF DRTCVPTDMV DIRLTVANKN IPGRIVYMGD FVLLTFDKTL
LPEGSKILVP EWDTKPLKVR ESVKIFGLTS DQLLSTKETT IGSIGTNSNT WPCNPPRHRL
INTENVSIAE GASCWGGVIA RMEQLKSIQK GEKILVSAWL MTVSSQSNGT DSYWTQGIDL
HRYVFPIVRE IEEKKLTRYD HVTWDLGFEF SDVALPTVST LGLSERRFND FVKQAKKIRG
IARPLIVETR MQPPKAPLTE EEEAKGLKVG DILLEIDLKP VYRVAQLTEF QFEGRDTVPV
LVLRNNEELL LNVPVVRSWP NTGDRVIQIF GAIVHASHAA AIEQVAKSAR NVPLDSEGLY
ISGVSYGSPA LDKMRPTFWI LSIDDHPVST IDDVLSLARE RQWAQGEYVR IKQVNRVGIT
SIASVKVDDR FWPLYQWRMN SDTGKWQMTK ETGLQYNHEL LDNNMALFEE KVVPAITEDV
KTAELETASP GNIDAPSTTP VENPPTLTA
//