ID A0A397HQA5_9EURO Unreviewed; 920 AA.
AC A0A397HQA5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=CDV56_109197 {ECO:0000313|EMBL:RHZ65351.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ65351.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ65351.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ65351.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) 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:RHZ65351.1}.
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DR EMBL; NKHU02000018; RHZ65351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397HQA5; -.
DR STRING; 41047.A0A397HQA5; -.
DR VEuPathDB; FungiDB:CDV56_109197; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000215305; 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: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:UP000215305};
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 93..113
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..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 103374 MW; 4F067824565DC768 CRC64;
MRPSDDHGET SEFLPMTRPR SASSASQTSS DSSLSTESIL PREQKHFPSP NETMGFADED
RYRDLEDGEA EPTEPFLASS KKAATGGGRA RRIFWILALL CLGGWLLAFV LFLTGGRANY
QTASDALKAH EPDSASGSTS TSSGKPVTLE QVLSGQWLPR YHAIGWVAGP NDEDGLLVEK
GGDEKEGYLR VDDIRRRKGD ATGQESKVLM RKPIVRVDGK AIVPSNVWPS PDLKKVLLIS
EQEKNWRHSF TGKYWVLDVD SQTAQPLDPR APDGRVQLAL WSPASDAVVF VRDNNLYLRR
LSSDSAIAIT KDGGENLFYG VPDWVYEEEV ISGNSVTWWS NDAKYIAFFR TNESSVPEFP
VQYYISRPSG KKPLPGLENY PDVREIKYPK SGAPNPVVDL QFYDVEKNEV FSVEVADDFA
DDDRIIIEVL WASEGKVLVR STNRESDILK VYLIDTKSRA GKLVRSEDIA SLDGGWVEPS
QSTRFIPADP NNGRPHDGYI DTVPYNGYDH LAYFTPLDSP NAVMLTSGEW EVVDAPAAVD
LQRGLVYFVA TREAPTQRHV YRVQLDGSNL RPLTDTSKPG YYDVSFSHGT GYALLTYRGP
SVPWQAIINT QGDAITYEDR IEENPQLTSM IQTHALPTEI YQNVTVDGYT LQLVERRPPH
FNPAKKYPVL FYLYAGPGSQ TVDRKFAVDF QSYVASSLGY IVVTVDGRGT GYIGRKARCI
VRGNLGFYEA RDQIATAKMW AAKPYVDETR MAIWGWSFGG FMTLKTLEQD AGQTFQYGMA
VAPVTDWRFY DSIYTERYMH TPQHNPHGYD NSSITDMAAL SENVRFLVMH GASDDNVHLQ
NTLVLIDKLD LSNVENYDLQ FYPDSDHSIY FHNAHTMVYE RLSSWLVNAF NGEWHRIANP
VPDKSMWERV RRSLPLPCIL
//
