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Database: UniProt
Entry: A3LSU5_PICST
LinkDB: A3LSU5_PICST
Original site: A3LSU5_PICST 
ID   A3LSU5_PICST            Unreviewed;       847 AA.
AC   A3LSU5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Glutamated carboxypeptidase {ECO:0000313|EMBL:ABN65956.2};
DE            EC=3.4.17.21 {ECO:0000313|EMBL:ABN65956.2};
GN   Name=GCP1 {ECO:0000313|EMBL:ABN65956.2};
GN   ORFNames=PICST_72031 {ECO:0000313|EMBL:ABN65956.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65956.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN65956.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC       {ECO:0000256|ARBA:ARBA00005634}.
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DR   EMBL; CP000498; ABN65956.2; -; Genomic_DNA.
DR   RefSeq; XP_001383985.2; XM_001383948.1.
DR   AlphaFoldDB; A3LSU5; -.
DR   STRING; 322104.A3LSU5; -.
DR   GeneID; 4838629; -.
DR   KEGG; pic:PICST_72031; -.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_005688_1_1_1; -.
DR   InParanoid; A3LSU5; -.
DR   OMA; RIIDPIY; -.
DR   OrthoDB; 67337at2759; -.
DR   Proteomes; UP000002258; Chromosome 4.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd03874; M28_PMSA_TfR_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; 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; N-ACETYLATED-ALPHA-LINKED ACIDIC DIPEPTIDASE; 1.
DR   PANTHER; PTHR10404:SF72; ZINC METALLOPROTEASE TRE2-RELATED; 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:ABN65956.2};
KW   Hydrolase {ECO:0000313|EMBL:ABN65956.2};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ABN65956.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        123..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          450..579
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          715..844
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   847 AA;  96030 MW;  353B673E61E79806 CRC64;
     MASHMRYTPL TADPSHTLPS FPPSYDDLDD NNDDYTYSSS ATPAIEQFEL DDGIDGIDDG
     ITRRTQREGL LVRASLMTKK FANNFNNSII HPVSQIIDPI YEGYKYFQQK YEQNILKLGN
     PLVVKRLLYV LFIMIVIFFV TKHNVNDGVN GTSGGTFSAG KFYNIDKLSS SVDDFISAKL
     MKENLEYFSS MSHITGSNGD LTLARYIETY MHNNGIRIMD MNQLQSYTNY PVYNEKDTYL
     KLSDNSFSAH LYEMNNKTME HLAYNPNALN TNGPVESHFI YGNYGTQEDY QKLISSGIDL
     TDAILLIKYG GSIPEPNKVS FGQQSKVKAI VFITPKFEFG TGDSKQEFVD VIQKANVGLT
     RVDPGDVLTP GWSSEDGYVT RLPWFRSSTT PKIPTIPISW EDGEKLLSKL EGSGVKFDDG
     YFSGKGKSSS VPTMVLKIAN EERATHQIWN VVGSIQGREQ NEKGIIIGSS RDSTCYGTIS
     SNTGTVVMLE MIKVFTSLQR KYNWSPSRSI YFVSFDATEY NLAGSAEWIE NRKDSLRKEG
     YAYIDLSDAI SGDDLSIKAS PFVEDVIKKA LKQVETDVTK NDNGNEKLSL YDLYLRQQGN
     DGISNDLIES KNYIPFINLV NMPSLELKFS GKKYPKNSCY DNFENFEKSA IDPDMNKHRE
     LVKVLSLIAL RLAESPMIPF DFQKLASKLT HYVDDLEKYS RDIISTLEQE NKPVLHFKSL
     RDSIEILRNA ANSLQSWGDS WKQYVENSAE IEPSMLAMNR WKRNENMVAF NQKFLVRNHM
     KDTRPGFANV LFGVPFMAPE VSDGKYEWNT FPRIRDSLYL HDFNAAQDQI NKLASLVQEA
     CQELDSQ
//
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