ID A0A1Q5UG70_9EURO Unreviewed; 924 AA.
AC A0A1Q5UG70;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=PENSUB_2939 {ECO:0000313|EMBL:OKP11453.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP11453.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP11453.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP11453.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKP11453.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNBE01000277; OKP11453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5UG70; -.
DR STRING; 1316194.A0A1Q5UG70; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000186955; 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:UP000186955};
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 92..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 232..606
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 691..894
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 103478 MW; 7EF032582865B907 CRC64;
MGKLDNEGVP EAVPLTRQRS ASAASNASSD SGLSVASAAF LDAYKHEFAA GEDGDGDGEG
QRYRDLEDGK ESGVDEPFLP SKKTKSSSGR RWCLFGVLVC VVMASGWIVA FVFFLVQGRS
NAAAISSPSA VEVHEPDSAT GGTSYGKPVT LEQVLTGYWS PQSHAIAWTA GSNGEDGLLI
EQGEHGGGYL RIEDIRNRKA GGAKVSDAKV LMKESHFWVG TTFVMASKIW VSPNHEKVLV
LSDYASNWRH SYYGNYWIFD VATQTAEALD PDNHTGRIQL AWWSPESDAV VFVWENNVYL
RDLSSSKAIP VTTDGGKEVF NGVPDWVYEE EVLSGNGATW WSLDGKFLAM LRTNETDVPE
YPVQYFLHRP SGTQPEAGLE NYPEVRQIKY PKAGTPNPIV NLRFYDVEKH ELFSIEMPED
FEDDDRIIIE VVWAPEQKVL IRETNRESDV VKIFLVDAKA RTAKLVRSTD IAALDGGWVE
PSQSTWIIPA DPSSGRPEAG YIDTVIHEGY DHLAYFSPLD SSEPVMLTSG KWEVVQAPTS
VDLKNNLVYF VATKEGPTQR HVYQVKLDGS DLRALTDTSK PGYYGVSFSD GAGYALLSYK
GPAVPWQAVV STQDSVMKKE IVIEENKQLA EKVEDFALPA EVYSTVTIDG YELQVVERRP
PHFNPKKKYP VLFHLYGGPG SQTVDRKFLV DFQSYVASSL GYIVVTVDGR GTGFIGREAR
CIVRDNLGYY EARDQIETGK IWAQKPYVDE SRLAIWGWSF GGFMTLKVLE QDAGETFQYG
MAVAPVTDWR FYDSIYTERY MHRPQNNPEG YDNSTISDVA AMGENTRFLI MHGVADDNVH
YQNTLTLLDK LNLQNIDNWD MVMYPDSDHS IFFHNAHRVV YERLSSWLIN AFNGEWHRIA
HPKPVESSWK RAKRFVTRRL SFTL
//
