ID   W7HSK5_9PEZI            Unreviewed;       916 AA.
AC   W7HSK5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Glutamate carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DRE_04607 {ECO:0000313|EMBL:EWC46229.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46229.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC46229.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC46229.1,
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 M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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DR   EMBL; KI966420; EWC46229.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7HSK5; -.
DR   HOGENOM; CLU_005688_1_0_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02121; PA_GCPII_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 1.20.930.40; Transferrin receptor-like, dimerisation domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   InterPro; IPR039373; Peptidase_M28B.
DR   InterPro; IPR007365; TFR-like_dimer_dom.
DR   InterPro; IPR036757; TFR-like_dimer_dom_sf.
DR   PANTHER; PTHR10404:SF71; CARBOXYPEPTIDASE TRE2, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G10650)-RELATED; 1.
DR   PANTHER; PTHR10404; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   Pfam; PF04253; TFR_dimer; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF47672; Transferrin receptor-like dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        198..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          352..418
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          538..722
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          792..913
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   916 AA;  101776 MW;  DC136954ED4B78C9 CRC64;
     MSEEKEAFRL RERLALPPGY EEATAGSSRA SDVSDNDDEP HENQRLLFSS DGAHDDAAAV
     AGPSTGSTVL SRLRNAASST RPDGYQPPTV QSVRSSFDSN SSFLASSSSS SSDSGDGDGR
     RSTESLRRIL EVMDVEEPEQ DGRSSRIRER ISKPFSIIGG AISSLGSRVG SRFGWFTSRL
     PSMPSLPSYL SFPSDEDGVI NLQRFVGVVI VVIIVYAIFA TDLFTLRMNQ GHQYDPDSVK
     RYLIDNIDPD NIKHMLKYLS SFDHLAGTEG DYQMAQYVAG KFKEAGMRDI RTEEYEVYLN
     YPSKDGTGRH VSIVNPSQMR FEAKLEEEHF DTTKNSGKIT PAFHGYSKSG NVTGHLVYAN
     YGSRQDFAYL KAKGVDVKGA VVLVRYFGTE SDAAVKVKEA ESAGAAGCII YSDPKENGNV
     RGAVWPEGRW AADDYVQRAS VGRTRYQPGD PLTPGVPSTP KSKRIPKDHA ILSKIPSLPL
     AWRDAQQLIK ALKGHGSEVE DSWKGGIPAV EWWTGDKNGP QVNLVNMLVE HDKQKIWNIL
     STFEGYEQPR KAIIIGSRRD SWAYGASAMT GTAIMLEIMR VFGQMYDIGW RPARTIHFAS
     WDGGQYGEVG STEWVEQYAN ELRMDGVAYI NVGTAVSGPE FTAKGSPALQ LALNTALGWF
     LDPSTNTTML ERFGGHPLAG PAINTDSLAF TNFAGMASID IGFETKDGNQ ALPLHSAYDS
     YDWMTKFGDP KWEFVPLLAQ IWGVLTIVMS DNLVIPLNYL DYANALGRHV DELERWVDGK
     RDKRHTDAKN TIDWQPMKDT IKKLQDRSSR FNEFVTQLEN TLLQLDGAEP ASLTVERLEH
     NNKLALFETH MLDMSAVPGR EWFKSTIFAP QVRSELDHLW FPSIVDAVEA GNWDRARFQL
     ERVRQIIDNA SAWIAK
//