ID A0A0A2IA93_PENEN Unreviewed; 906 AA.
AC A0A0A2IA93;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=PEX2_085980 {ECO:0000313|EMBL:KGO61523.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO61523.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO61523.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO61523.1,
RC ECO:0000313|Proteomes:UP000030143};
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 -!- FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline.
CC {ECO:0000256|ARBA:ARBA00002218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC Pro nor hydroxyproline.; EC=3.4.14.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001257};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}. Vacuole
CC membrane {ECO:0000256|ARBA:ARBA00004576}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004576}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family.
CC {ECO:0000256|ARBA:ARBA00006150}.
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:KGO61523.1}.
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DR EMBL; JQFZ01000034; KGO61523.1; -; Genomic_DNA.
DR RefSeq; XP_016602315.1; XM_016745868.1.
DR AlphaFoldDB; A0A0A2IA93; -.
DR STRING; 27334.A0A0A2IA93; -.
DR GeneID; 27681288; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OrthoDB; 2876738at2759; -.
DR PhylomeDB; A0A0A2IA93; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF200; DIPEPTIDYL PEPTIDASE FAMILY MEMBER 2; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 230..604
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 688..892
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 101121 MW; 8F96297B2DEAB1EA CRC64;
MGKFEDEGNS ESVPLNRQRS ESLTSQTSTD SGLSIASESF MKSHKGGNTM PMEEGEGERY
RDIEDGGEIG SDEPLISSGK KAGSSSRLRQ IVWLLVLLCV GGWVLAFVLF LTQKRPDIAA
LSSAATTSTA VIHEPDSATG HATHGKPVTL EQVLSGTWSP KSHAISWIAG PDGEDGLLVE
QGEKQDAFLR VKDIRSSKNG VDALETRVLM KKAYIWFDGE ALPPAKTWPS PDMNKVLIMT
DSQSNWRHSY FGKYWILDVA TQKAEPLDPG NLSGRVQLAA WSPTSDAVVF VRENNLYLRK
LASLEVTPIT KDGNENLFYG VPDWVYEEEV FAGNTGTWWS GDGKFVAFLR TNESAVPEYP
IQYFLSRPSG KEPPPGLENY PEVRQIKYPK PGSPNPIVNL QFYDVEKNEV FSFEMPEDFV
DDERIIIEIV WASGGKVLVR ETNRESDVVK IFVMDTKART GKLVRSDDIA ALDGGWVEPS
QSTRVIPADP ENGRPHDGYI NTVIYEGYDH LAYFTPFDNP EPVMLTKGNW EVVKAPSAVD
LKKGLVYFVA TKEAPTQRHV YSVKLDGSDL RPLTDVSAPG FFEVSFSHGA GYGLLSYKGP
EVPWQAVINT QGDEIDFINL IEENVKLAKM VEDFALPTEV YTNVTIDGYT LQVLERRPPN
FDPAKKYPVL FYLYGGPGSQ TVDRKFTIDF QTYVASSLGY IVVTVDGRGT GFIGREARCV
VRGNIGHYEA LDQIETAKIW ASKSYVDESR MAVWGWSYGG YMTLKVLEQD AGETFQYGMA
VAPVTDWRFY DSIYTERYMH TPEHNPSGYA NASISDVTAL GQSVRFLIMH GVADDNVHLQ
NTLVLIDKLD LKNIDNYDMQ VFPDSDHSIQ FHMAHALVYE RLSSWLINAF NGEWHRITSP
KPQEST
//
