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Database: UniProt
Entry: A0A364L639_9EURO
LinkDB: A0A364L639_9EURO
Original site: A0A364L639_9EURO 
ID   A0A364L639_9EURO        Unreviewed;       769 AA.
AC   A0A364L639;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RAO71262.1};
GN   ORFNames=BHQ10_007274 {ECO:0000313|EMBL:RAO71262.1};
OS   Talaromyces amestolkiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO71262.1, ECO:0000313|Proteomes:UP000249363};
RN   [1] {ECO:0000313|EMBL:RAO71262.1, ECO:0000313|Proteomes:UP000249363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:RAO71262.1,
RC   ECO:0000313|Proteomes:UP000249363};
RX   PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA   de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA   Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT   "Differential ?-glucosidase expression as a function of carbon source
RT   availability in Talaromyces amestolkiae: a genomic and proteomic
RT   approach.";
RL   Biotechnol. Biofuels 10:161-161(2017).
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:RAO71262.1}.
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DR   EMBL; MIKG01000015; RAO71262.1; -; Genomic_DNA.
DR   STRING; 1196081.A0A364L639; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000249363; 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:SF46; GLUTAMATE CARBOXYPEPTIDASE 2 HOMOLOG; 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:UP000249363};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..274
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          391..580
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          643..768
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          298..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   769 AA;  84912 MW;  D61BE0A95572844B CRC64;
     MPLSETTPLL VVQTAPRRHR YPHHTLRRTC TAILCLVLLI AVTLFLLPIK LLSREDGAPW
     VYGPWSKPYP QSWPHGNGLS NAELRALLHE TPTAEKIEEW SKYYTAGPHL AGANFSQVLW
     TQEKWKEFGV EDTTIATYDV YINYPLDHRL ALLNKKGEDD YEVAYEASLE EDVLDEDGTS
     GLPDRIPTFH GYSASGNVTA PFVYANFGTF QDYQDLVDAG ISVEGKIVIV KYGGIFRGLK
     VKRAQDLGAV GVIIYSDPQE DGDITELNGY EAYPAGPARN PSAVQRGSVQ FLSIAPGDPT
     TPGYASKPGV ERQPPEHSIP SIPSLPISYT DALPLLKALN GHGPKAADFN DFWQGGGLAH
     KGVDYNIGPT PDDVVINLHN LQDYVTTPLW NVIGVIKGTI LDEVVILGNH RDAWVAGGAG
     DPNSGSAALN EXVRSFGEAL KAGWKPLRTI VFASWDGEEY GLVGSTEWVE EQLPWLTVAN
     AVYLNVDVAS SGPIFDVSGS PLLNKAVHEV TRTVQSPNQT VKGQSVLDAW GGHISSLGSG
     SDYTAFQEFA GVPSVSFGFK GGKTSAVYHY HSNYDSFDWI KRFGDPGWKY HVTTAKIFSL
     LGAYFSEKPV LGFNATDYAI NLQKYVNNIR SHADNLPKKT HFSFGPLERS IADFYDAAVE
     FDAYAAKVES ELDQEEPWYH WWKKLQLWFK VRAINTKYKT LERKFLYEAG LDGRSWFKHV
     VFAPGLWTGY AGATYPGLVE SLDAGNVTNA VRWSEIIQER LGVATKLLE
//
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