ID A0A420I0D6_9PEZI Unreviewed; 873 AA.
AC A0A420I0D6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Putative glutamate carboxypeptidase {ECO:0000313|EMBL:RKF63156.1};
GN ORFNames=GcM3_141002 {ECO:0000313|EMBL:RKF63156.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF63156.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF63156.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF63156.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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:RKF63156.1}.
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DR EMBL; MCBQ01014157; RKF63156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420I0D6; -.
DR STRING; 62708.A0A420I0D6; -.
DR Proteomes; UP000283383; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08022; M28_PSMA_like; 1.
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 Carboxypeptidase {ECO:0000313|EMBL:RKF63156.1};
KW Hydrolase {ECO:0000313|EMBL:RKF63156.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:RKF63156.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..391
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 493..665
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 745..869
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 98184 MW; 13619D95EB667D5B CRC64;
MMNQKDPEES IPILSHEEAI ESSSRRHLSN FRSQRPEISS HDLEPGISTY RQRAEDLPST
VDDHNEENEH DTFLGQDLSN WRQRQTEEND IRREIEELEL DESTSNMARS ALGKRITSLS
QRFNIQFKIP FSLKWKLQSP EGIRWPQINV NMCILFARCA SILFVLAVLY VLFMSDLFTV
GMQRMAGQVF DPESVKIHVQ SLVDENQIRE NLRLLTTTDH IAGTKGDYVL AQYLNEYFKK
NSLDDVRMEE YGVYLNYPKK EGRKIEILKE DGSISWSAKI DEDPIYTNPP RQPIPVFHGH
SKTGDVTGHL MYANYGSLDD FKVFHDRGID TKGAIALVRQ FGDQNDDALK IKAAELSGFA
GCLIYSDPAD DGFVKGQVAP TGRYMPEGGV HRGGVSLVSW TVGDVLTPGW ASIPGAERIP
KENNSALVNI PSIPISWGNA RQLLSAIEGY GAASPQGWKG GIPNLEYWTG NLSSPKVRLL
NDQDEVEQQP IWNVLGKING VEQKEKSIIV GNHRDAWHYG AADPGSGTAV MMEVIRIFGD
LVHRGWRPLR TIEFASWDGG EYNLIGSTEW VEDNMEKLRK DAYAYLNVGS AVSGSDFRVS
GSPMFTKSLV EVLKRTSDPL KNKTIAQLWR EHGGNLATLG VSSDYVAFQD MAGTSSLDIG
FSGDSFPRNS AFDNFEWMDS VGDPGFVYHK ILAQIWALLI LEYADKLILP FDLSAYSSSL
TQWVISLNQW SEDKGVNKDG NTKWDIEPLR EAVLQFASDS RRFTKWEEEW NTVVYGGGGY
ETAIMAEHRK SHNNRMANFE THLLDLEEGG GIPNRTLFKH VLFGPQQWSL DSENIFPSIR
DAVIAQDWDL AKKQVEKAAN VIKKASRKLV GNT
//
