ID B8M4I7_TALSN Unreviewed; 898 AA.
AC B8M4I7;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Glutamate carboxypeptidase Tre2, putative {ECO:0000313|EMBL:EED19182.1};
DE EC=3.4.17.21 {ECO:0000313|EMBL:EED19182.1};
GN ORFNames=TSTA_025040 {ECO:0000313|EMBL:EED19182.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED19182.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC {ECO:0000256|ARBA:ARBA00005634}.
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DR EMBL; EQ962654; EED19182.1; -; Genomic_DNA.
DR RefSeq; XP_002479616.1; XM_002479571.1.
DR AlphaFoldDB; B8M4I7; -.
DR STRING; 441959.B8M4I7; -.
DR GeneID; 8106721; -.
DR VEuPathDB; FungiDB:TSTA_025040; -.
DR eggNOG; KOG2195; Eukaryota.
DR HOGENOM; CLU_005688_1_0_1; -.
DR InParanoid; B8M4I7; -.
DR OMA; YPRKDGR; -.
DR OrthoDB; 67337at2759; -.
DR PhylomeDB; B8M4I7; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-EC.
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:EED19182.1};
KW Hydrolase {ECO:0000313|EMBL:EED19182.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:EED19182.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 168..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..410
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 512..695
FT /note="Peptidase M28"
FT /evidence="ECO:0000259|Pfam:PF04389"
FT DOMAIN 771..896
FT /note="Transferrin receptor-like dimerisation"
FT /evidence="ECO:0000259|Pfam:PF04253"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 100379 MW; 9A08FBBA81AA96B5 CRC64;
MGDKKYRYEE LPIPTYEEAT ASQSGSSHLG PEHSSDDLER QGLLQHEDTN DNFNTGRPHA
TTRNGGYQPP TVESARSSID YLASSASGSA RQSEEELRRE IHQMDVDDSG TSSQTRRPLL
SRRFSKHFSN PFSSLTKTLS SLQLPFRNSF PRFQMRWRFW RLQINEDGVA CMLFLRLFGL
LILVFLVYLV FVSDVFSVGS RFSMGQSYTA ASVESFVQSH INETNIANNL QKATQFAHIA
GTEGSYVLAE WIEQEFINAG LEDVEMEEFQ VYLNYPRTDG RRVAIVDPPE LAWEAAIDEP
QVYSDPRRQQ TLVFHGHSKS GNVTGPLVYA NYGSQEDFKR LADSGISVKG AIVLVRYYGT
QNDRALKIKA AELAGAAGCI IYSDPAEDGF IRGPAYPDGR YMPSAGVQRG GVSLMSWVVG
DVLSPGFAST PNEKKRLSPE KSPGLVQIPS IPLAWRDAQR LLQVLRGHGS KVPVDWVGGV
PDIAEWWTGD SSSPKVNLMN LQDEIERQPI YNVLGRITGL EQPEKKIIVG NHRDSWCFGG
VDPGSGTATF LEIVRIFGEM RSVGWRPLRT IEFASWDGEE YNLIGSTEHV ENEMERLRSN
GFAYLNVDVG VSGSSFEAAG SPLFQRLLNT AMGRVGDESA NKTLKQIWDE QGKRLEGLGA
GSDYVAFQDM AGTSSLDFGF GGEPFPYHSC YENFEWMSKF GDPDFRYHRL LGELWGLLLL
ELADSPILPF DLEAYAAQFR GYVDNLQLYA KNKGVPLKPT SDAPQERSEM VDVTPLYDAA
EVFRTNAVNF QAWEQVWYSA VYGSGGFESN LMGVRRIEHN NRLARFETDL LDLSQDGGVP
NRTQFKHVLF APQAWSGYDE SFFPAIRDAI DIGDWNATQS WINRVAEIVT QASLNLNI
//
