ID A0A2C5WRS1_9PEZI Unreviewed; 912 AA.
AC A0A2C5WRS1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Probable dipeptidyl-aminopeptidase B {ECO:0000256|ARBA:ARBA00014118};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN Name=DAPB {ECO:0000313|EMBL:PHH51939.1};
GN ORFNames=CFIMG_006060RA {ECO:0000313|EMBL:PHH51939.1};
OS Ceratocystis fimbriata CBS 114723.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=1035309 {ECO:0000313|EMBL:PHH51939.1, ECO:0000313|Proteomes:UP000222788};
RN [1] {ECO:0000313|EMBL:PHH51939.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH51939.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=23931120; DOI=10.1016/j.funbio.2013.06.004;
RA Simpson M.C., Wilken P.M., Coetzee M.P., Wingfield M.J., Wingfield B.D.;
RT "Analysis of microsatellite markers in the genome of the plant pathogen
RT Ceratocystis fimbriata.";
RL Fungal Biol. 117:545-555(2013).
RN [2] {ECO:0000313|EMBL:PHH51939.1, ECO:0000313|Proteomes:UP000222788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114723 {ECO:0000313|EMBL:PHH51939.1,
RC ECO:0000313|Proteomes:UP000222788};
RX PubMed=24563841; DOI=10.5598/imafungus.2013.04.02.14;
RA Wilken P.M., Steenkamp E.T., Wingfield M.J., de Beer Z.W., Wingfield B.D.;
RT "IMA Genome-F 1: Ceratocystis fimbriata: Draft nuclear genome sequence for
RT the plant pathogen, Ceratocystis fimbriata.";
RL IMA Fungus 4:357-358(2013).
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:PHH51939.1}.
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DR EMBL; APWK03000081; PHH51939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C5WRS1; -.
DR STRING; 1035309.A0A2C5WRS1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000222788; 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:PHH51939.1}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:PHH51939.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438, ECO:0000313|EMBL:PHH51939.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000222788};
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 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 222..594
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 677..882
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 889..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 102015 MW; D66AD2B17F4B7B27 CRC64;
MASFTDDDYD HGPRDSLSSA STTSLVFDHI DDQNNLKAAR MQFQTSGHHH AEKSPFVDST
DLETARFLPS SNHDDGGELM LPSVQRGMDR SLRKYGIVGF CILTALWVVT MLSFLSSGSP
SSTSPQRHLV GNPVTLDSVL QGQWRANSHD ISWISGPDGE DGLLMERDAK GKDFLVVEDV
RSIDSQITGK NTGSSRTLIQ KAKLSYNDTD ITPQETYPNT ALTKVLIASN VERNWRRSFS
AVYWILDVES QSVQPLIPGE PSSMVQLASW SPTGDAIAFT RDNNIYIRSL ESDDKEAVTQ
ITKDGGREYF YGIPDWVYEE EVFGGNSATW WSDDGKFIAF LRTNESGVPE YPIDYYVSRP
NGDAEDGEEA YPDVRQIKYP KAGAHNPVVD LLFFSVEKGD VFSIEIEGEF ANDDRLITTV
LWAGDKVLVK ETNRVSDIMR VVLIDVETRT GKAIQTINVK DIDGGWFEIS TKTKFIPADP
KNGRPHDGYI DSVIYENRDH LAYFSPMDNP EPIMLTKGDW EVEDAPSAVD LKNNLVYFVS
TKESSIQRHV YSVKLDGSDL KPLTNVSTEG YYDVSFSDGA GFALLSYRGP DIPWQKITST
PGNPSSYSRM IEENADLAKE VSKTDLPTLV YGTIMVEGVN LNYVERRPAN FNPSKKYPVL
FQQYSGPGSQ SVSKRFSVDF QSYVASSLGY LCVTVDGRGT GFIGRKARVV VRGQLGVVES
HDQIAAAQHW SSFPYVDASR LAIWGWSFGG FNTLKTLEVD AGKTFSYGMA VAPVTDWRYY
DSIYTERYML TPQENPDGYN RSAVRNATAL GESVRFLVMH GTGDDNVHMQ NTLTLLDKLD
MSSVENYDLH LFPDSNHGIY FHNANRIVYD KLSNWLINAF NGEWLKVNDP SPKPEKKKRD
VKLRETGTKS DF
//
