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Database: UniProt
Entry: A0A0A2LB28_PENIT
LinkDB: A0A0A2LB28_PENIT
Original site: A0A0A2LB28_PENIT 
ID   A0A0A2LB28_PENIT        Unreviewed;       861 AA.
AC   A0A0A2LB28;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Peptidase M28 {ECO:0000313|EMBL:KGO76408.1};
GN   ORFNames=PITC_072900 {ECO:0000313|EMBL:KGO76408.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO76408.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO76408.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO76408.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO76408.1}.
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DR   EMBL; JQGA01000261; KGO76408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2LB28; -.
DR   STRING; 40296.A0A0A2LB28; -.
DR   HOGENOM; CLU_005688_2_0_1; -.
DR   OMA; LWNVIGT; -.
DR   OrthoDB; 67337at2759; -.
DR   PhylomeDB; A0A0A2LB28; -.
DR   Proteomes; UP000030104; 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   InterPro; IPR005349; TMEM14.
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   Pfam; PF03647; Tmemb_14; 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:UP000030104};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        836..856
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..280
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          396..583
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
FT   DOMAIN          647..756
FT                   /note="Transferrin receptor-like dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF04253"
SQ   SEQUENCE   861 AA;  94213 MW;  EC992F9E74F40235 CRC64;
     MREKDMRYSE TTPLLEVNVA PPRHRYPHHA IRRACTISLA ALLSVATLLF LLPTAILPRE
     GGSIWSYLPG AHPIPHEAWP ESYGLPYEQL QQILLNVPSA AKAREWSQYY TAGPHLAGKN
     LSQALWTLEK WKEFGVEDTG LATYDIYINY PLEHRLALLK TSGDKTEVTF EATLEEDILE
     EDPTSGLPDR VPSFHGYSAT GNVTAQFVYV NFGTYKDFED LVNANITLEG KIAIAKYGGI
     FRGLKVKRAQ ELGMVGVVIY SDPQEDGEIT EENGYEAYPN GPARNPSAIQ RGSTQFLSIL
     PGDPTTPGYA SKPGCERQDP HNSIPSIPSL PVSYKEVLPF LKALNGHGPK ASDFNESWQG
     GGLGYKGVEY NIGPSPEDVV INLHNLQEYV TTPLWNVIGT IKGHISDEVV VLGNHRDAWI
     AGGAGDPNSG SAALNEVVRS FGEALKAGWK PLRTVVFASW DGEEYGLLGS TEWVEEHLPW
     LSKANIAYLN VDVAAAGTNF EPRASPLLNK VINDVTALVQ SPNQTVRGQT IRDVWDGKIS
     TMGSGSDFTA FQDFAGIASL DFGFGRGKND PVYHYHSNYD SFAWMEKYGD KEFLYHQACT
     KLWALAAAQL VESPLLALNA TDYSLGLGSY LDHIKPAADN LPEGTHFDFA PLDRAIFEFQ
     ESAKAFDAHA ADLKSQLGDD VPWYHWWKKV RLLFQIRITN AKYKGIERAF LYQPGLDGRE
     WFKHVVFAPG IWTGYSGATY PGLVESFEAG DVENAEAPTT SALALSLLTS IGGIIGYART
     GSLPSIIAGV SVGLVYLLSF LRLRAGQSYG EELGLLASAV LGGSSVPRVI KTGGKPVPLV
     LSVLATYGLF VFGIAFREKR A
//
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