ID A0A1L9SWU6_9EURO Unreviewed; 893 AA.
AC A0A1L9SWU6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Glutamate carboxypeptidase Tre2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASPZODRAFT_2107315 {ECO:0000313|EMBL:OJJ51523.1};
OS Penicilliopsis zonata CBS 506.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicilliopsis.
OX NCBI_TaxID=1073090 {ECO:0000313|EMBL:OJJ51523.1, ECO:0000313|Proteomes:UP000184188};
RN [1] {ECO:0000313|Proteomes:UP000184188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 506.65 {ECO:0000313|Proteomes:UP000184188};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; KV878336; OJJ51523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9SWU6; -.
DR STRING; 1073090.A0A1L9SWU6; -.
DR VEuPathDB; FungiDB:ASPZODRAFT_2107315; -.
DR OrthoDB; 67337at2759; -.
DR Proteomes; UP000184188; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184188};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 175..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..406
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 508..691
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 767..891
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 893 AA; 98859 MW; 0855D21F88E7D1FB CRC64;
MGDDKHHYES LPIPTYEEAT SSRSRRSVEE AGDDAERQGL LGRSEVSGSG GIHGGTRDRE
EGGGGGGGGD GYQPPTVESA RSSLDYLGSS APNSARGSME QLRREIDEMD IEDMGQGGAR
RGRSQLGHRF SKRLNDFTRT LSAIHLPLRQ YLPTVRFTID LGRARTHVQK NACMLVLRLF
AVILVVILVY LFFFSDLFSF GNRLNMAQAY SPASVENYVQ GHINGTRIAE NLKKLTNFPH
MAGTEGSFVL GEWIEQEFKI AGLDEVVSEE FQVYLNYPTA DGRRVAIVDP PDLAWEATLE
EDDAQAPVFH GHSKSGNVTG PLVYANYGSR QDFKMLADLG ISLDGAIALV RYYGTETDRA
LKVKAAELAG AAGCIIYSDP AQDGFVQGPA YPDGRFMPAD GVQRGAVSLM SWVVGDVLTP
GFASTPEQKK QRLKPEESPG LVQIPSLPIA WRDAQRLLNA LRGHGLLVPQ DWVGGVPEVD
QWWTGDAQSP QVNLMNLQDE VEKQPIYNVL GRIIGLEQPE KKIIIGNHRD SWCTGSADPG
SGTAVFLEIV HIFGELLTYG WRPLRTIEFA SWDGEEYNLI GSTEHVEDRV DALRADAYAY
LNVDVGVSGP DFRVAASPLY ESVVLQLLNR ISDPARNATL KEIWERKGLR IEGLGAGSDY
VAFQDIAGTS SIDFGFTGAP YPYHSCYENW DWMVRFGDPG FQYHTMLGQF WALLLLELAE
NPILPFNMEA YANYVSSYVA ELETYARNQH VPILDPLDAA GSDGGVRFNA LYNAAAEFRE
NAVLFHGWDQ MWHDTVWGAG GYESSVMTVQ RLSHNSRMAN FETHLLDLDE GGGIPNRTQF
KHILFGPQAW SGYDEAFFPA IRDSIDARDW TATQAWIDRT AHILSKASRK LLY
//
