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Database: UniProt
Entry: A0A1E4RXG3_CYBJN
LinkDB: A0A1E4RXG3_CYBJN
Original site: A0A1E4RXG3_CYBJN 
ID   A0A1E4RXG3_CYBJN        Unreviewed;       742 AA.
AC   A0A1E4RXG3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Zn-dependent exopeptidase {ECO:0000313|EMBL:ODV71963.1};
GN   ORFNames=CYBJADRAFT_186221 {ECO:0000313|EMBL:ODV71963.1};
OS   Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS   / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX   NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV71963.1, ECO:0000313|Proteomes:UP000094389};
RN   [1] {ECO:0000313|EMBL:ODV71963.1, ECO:0000313|Proteomes:UP000094389}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC   NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
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; KV453937; ODV71963.1; -; Genomic_DNA.
DR   RefSeq; XP_020069002.1; XM_020217205.1.
DR   AlphaFoldDB; A0A1E4RXG3; -.
DR   STRING; 983966.A0A1E4RXG3; -.
DR   GeneID; 30991601; -.
DR   OMA; NVVIASW; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000094389; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000094389};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..742
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009162503"
FT   DOMAIN          159..228
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          336..524
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          620..741
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          219..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  81640 MW;  EC93426885937864 CRC64;
     MGVSDKSASS GGVTTSLVKL LCIASSVLAL PTYDETSEKL SIDEITKIYQ DVLTSSNNAG
     DWLKTYTQEQ HLAGQNYHLA EFTAQRFEEF GFKAKFENFS VYINYPVENS IKVLEPNEDG
     SYELTYQPTL VEDELEEDPT TSGEGLVPAF HGYSANGNVT AELVFANYGT KEDFALLAEN
     NIDLEGKIVI VRYGGIFRGL KVKFAQEAGA LGVITYSDPA DDYSPPDAEP YPKGPGRNPS
     SIQRGSVQFL SSLPGDPSRF TDRSPEALSN LTTIPRIPSL PISYKEAIPI LETLNGYGSD
     LGFKGGVSTF NYTTGPSSAK INLYNNVEYD FTNITNVYGL IEGQEADKVV IIGNHRDAWV
     KGGAGDPNSG SAVLLELARG LNELFKQGYK PRYSILLASW DGEEYALLGS TSYAEKYAAK
     LDKQAVGYIN VDVAVGGTHL ELAGSPLFNQ LLLDQGSLVT HPDTNVSLTE RFLNESEILI
     LGSGSDYTTF YEHLGIPSID LGFNPGLGDP VYHYHSNYDS YHWISTFADP GFKYHNALAQ
     YLGLLTLKLT EEKLLKSYST SDYASAVAGY FSTLVSTIPQ DWLNQTVVLD DDIIAPYSYS
     EDNLTSTDVT VLRDLITATN DTLSILEEVA KHHDEEKEYL QSQWDESVST SSSPITKTLF
     DKRVATINDK SRNFEKQFLY EGGLKSREWF KHIVYASGRY TGYAGQSLPG LTEALEDDSF
     DEAARWIHIL QVAAQRAIAS LV
//
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