ID A0A1Q8S711_9PEZI Unreviewed; 933 AA.
AC A0A1Q8S711;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B {ECO:0000256|ARBA:ARBA00014118};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=CCHL11_02055 {ECO:0000313|EMBL:OLN97225.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN97225.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN97225.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN97225.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-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:OLN97225.1}.
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DR EMBL; MPGH01000011; OLN97225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8S711; -.
DR STRING; 708187.A0A1Q8S711; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000186583; 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 ECO:0000313|EMBL:OLN97225.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:OLN97225.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:OLN97225.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186583};
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 109..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..616
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 700..904
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 105243 MW; 8C3E8A4C3EFF62B5 CRC64;
MDVPTASTAG RQSTSEEPRM SHESSLSSVS TTSLVFDRLH EQNEKNYTSS SNRRRTPSTS
RVAYADHPDD DDEGDEYKES DANDLETGPF LASAGVTRRV GMDRGLKKGL LILGAAFVFA
WGAALFVFLS SKSYRHGSQV DHDPSATHRG SGKPVTLDQV MSGFWSPYSH SIRWIEGPNG
EDGLLLEQGA RGKDYLVVED VRSAKQEARQ ISADVAQSRT LMKNPWIDYN GRQLTPHGSV
PSKDMKKVLV YTDREHNWRH SFTALYWILD VETQTVEPLD PQNADKRVQL ATWSPQSNAI
VFTRDNNLYL RKLDGDKKVT QITTDGGPEY FYGIPDWVYE EEVFAGNSAT WYSQDGKFVA
FLRTNETGVP EYPLQYFLSR PSGGAKPPGE ETYPEERRIK YPRAGSHNPV VDLLFYDVER
GDVFSVDISG GFTDDDRLIN MVLWANDKVL IKETNRVSDI MRVVLVDVVA RTGKTVNTID
VGKIDGGWFE ISHETLFIPA DPANGRPEDG YVDTVVHDNG DHLAYFSPMD NPEPVYLTGG
NWEVVDSPSA VDLKNNLVYF VSTKESSIQR HVYSVYLNGT DLKPFTDTSF ESYYGISFSS
GAGFSLLSYQ GPKVPWQKVI STPSNPTKYE LVIEKNEQLA ENAKKYELPI LKYGTIKVDD
VELNYIERRP PHFSDKKKYP VLFQQYSGPG SQSVNKRFTV DFQSYVASAL GYVVVTVDGR
GTGYIGRKAR VLIREKLGHW EAHDQIAAAK IWSAKKYVDS SRIAIWGWSY GGFNTLKTLE
MDAGQTFSYG MAVAPVTDWR FYDSIYTERY MRTPQLNPDG YDQTAISNVT ALAGNVRWLM
MHGVSDDNVH YQNTLTLLDK LDLEGIENYD VHVFPDSDHG IYFHNANKIV YDKLSNWLIN
AFNGEWLKIS GAKPKAESKE KERRRRSTQV YDV
//
