ID A0A165A0K6_XYLHT Unreviewed; 887 AA.
AC A0A165A0K6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Glutamate carboxypeptidase Tre2 {ECO:0000313|EMBL:KZF19781.1};
GN ORFNames=L228DRAFT_214568 {ECO:0000313|EMBL:KZF19781.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF19781.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF19781.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF19781.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KV407465; KZF19781.1; -; Genomic_DNA.
DR RefSeq; XP_018185336.1; XM_018330036.1.
DR AlphaFoldDB; A0A165A0K6; -.
DR STRING; 1328760.A0A165A0K6; -.
DR GeneID; 28895173; -.
DR InParanoid; A0A165A0K6; -.
DR OMA; YPRKDGR; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000076632; 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:KZF19781.1};
KW Hydrolase {ECO:0000313|EMBL:KZF19781.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:KZF19781.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..413
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 514..699
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 760..885
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 99194 MW; CA997CCE963F94CB CRC64;
MSDKKTADVD YAHLPIPTYE EATSSRPTSS QSYHQGTQEI NDNAEREGLL GQSGRAGERG
ESRHGGYRPP MVGSERSSID SEFSFESLER DNRNAEDEEL RREMFEMEVL DAESGQASSQ
TSPMRHRFSK RLNSITNTLS SIHLPFRMRM PSFSFDIWSR MPPWMVEYSV RVRVLARFLG
LILVMLVVYA LFVTEIFPFR NAAMGGQMYD PESVRSFVQG NVDEHQIRKY LSNLTGYDRM
AGTEGSYASA LYVEELFRAG NLEGVGLDRY QVYLNFPRKD GRRVAIIEPP ELAWEAVIEE
ESVYEHPTPQ QQQTMVFHGH SRAGNVTGPL VYANYGSRED FETLKENGVD LKGTIVLVRY
YGTQGDRALK VRAAELAGAA GCIIYSDPAE DGFRKGAAWP DGRWRPSDGV QRGAVSLMSW
VVGDVLTPGY GSLPDADRIS KNNNPGLVNI PSIPLAWRDA QKLLQVLKGH GHKVTDDWVG
GVPDIKEWWS GDQSSPIIHL MNEQDEIDKQ PIYNVVGKIT GLEQPSKTVY VGNHRDSWCF
GATDPGSGTA VMLEVIRIFG ELRDLGWRPM RSIVFNSWDA EEYNLIGSTE FVESNLEYLH
RDGIAYLNVD VAVAGSDFEA AGSPVFRKSL GHVLDRTSDP FKNKTLRAIW EETGRDLGGL
GAGSDYVAFQ DIAGTSSIDI RFSGPGFPYH SCYDSFEWMD KFGDPGFQYH KILAQVWALL
ILEIADTPVL PFDMFGYAVA VGKYIEDVQV YAYSNMGGGL NFAPLREAAE VMAKNTETFE
AWEMAWVQEV YGSGGFESNV IAIQRMSRNT RMAQFETDLL DLLPGGGLPG REQFKHVIFA
PQAWSGYDEA FFPGIRDAVD ARDWPLAQKQ IQKAADLIRS ASEKLIL
//
