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Database: UniProt
Entry: A0A1E3QEX7_LIPST
LinkDB: A0A1E3QEX7_LIPST
Original site: A0A1E3QEX7_LIPST 
ID   A0A1E3QEX7_LIPST        Unreviewed;       909 AA.
AC   A0A1E3QEX7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ODQ76253.1};
GN   ORFNames=LIPSTDRAFT_67134 {ECO:0000313|EMBL:ODQ76253.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ76253.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ76253.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ76253.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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DR   EMBL; KV454289; ODQ76253.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3QEX7; -.
DR   STRING; 675824.A0A1E3QEX7; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000094385; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        141..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          296..365
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          483..673
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          781..906
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   909 AA;  101625 MW;  CA35F5D5EAA4B7D8 CRC64;
     MPVPTDSHPL QSSDSPDEPH ENLELSDAPG SPIIADFHDA LGANNNEISG AESSAAIDLL
     EYDEDGDENQ SLLHPQPRLA HGRHLFRNSI LTNSKHSTER ASSPTYTEDS LDSATEADLL
     LPSPSSASSI REYFKKRWGT FFTRLLAYAL FGIVFIIGWK LVFLPRTTLR RDLARLRHFQ
     VSLSDLERTL FGVPETSKVR EWSHYYTSGA HLAGTNYSQV QWTADKFKEY GFTAEIVSYE
     TYLNYPRDHS LKLLDVHGTI RYEAPLKEDM LTQDPTTNDP NSVPTFHGYS ANGNVTAAYV
     YVNYGRQEDY DLLEERGIDI SGKIVIARYG GLFRGLIVKG AQERGAVGAL LYTDPGDDGD
     ITLVNKYRAY PDGPARNPSS VQRGSVLFLS SAPGDPTTPG FASKPGAERV DPHERIPSIP
     SLPISYRDVL PLLIELNGMG LNPNDLGESW RGGLREYDYS TGPSTMDVNL YNAQDYKTTP
     IWNAIGRIDG VIKDEVVILG NHRDAWIVGG AGDPNSGSAV LIELARAFGE LKSHGWKPLR
     SIVLASWDGE EYGLLGSTEW GEDMARYLDA NALVYLNVDG AVTGSHFHAA ASPLLNTVLQ
     EVMKRVPDPK GGYVYDHWLE ETEGRIGNLG SGSDYTVFQD HLGIPSIDFG FSEGSNAVYQ
     YHSNYDSFHW MDKYGDPTWE YHVAMVKIWG LVALQLSEIE VISFDVVEYA RSLLSYFNDV
     KTKISHIVSE DELSVDIYDG FYDCPEIPGS LIRECRYIDA SAIVDVDLPD LKLGWWYISS
     SLRNCSDALD KLLSTATTFD AKSSYINKQY LTDYPWFKGY KKMRVYFQIQ GLNSQYRQFE
     RKFLYEGGLD GREWFKHVVF APGVWTGYAG VTFPGLNEAL DARNISNTKR WLDIITERIS
     QAVDLLSAN
//
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