ID   DAPB_GROCL              Reviewed;         975 AA.
AC   F0XS04;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; ORFNames=CMQ_7762;
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150;
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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:0000250}.
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   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type
CC       II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR   EMBL; GL629990; EFW99394.1; -; Genomic_DNA.
DR   RefSeq; XP_014168877.1; XM_014313402.1.
DR   AlphaFoldDB; F0XS04; -.
DR   SMR; F0XS04; -.
DR   STRING; 655863.F0XS04; -.
DR   ESTHER; grocl-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; F0XS04; 4 sites, No reported glycans.
DR   GeneID; 25981342; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; F0XS04; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000007796; 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:UniProtKB-KW.
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; Glycoprotein; Hydrolase; Membrane; Protease;
KW   Reference proteome; Serine protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Vacuole.
FT   CHAIN           1..975
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412146"
FT   TOPO_DOM        1..125
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..975
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        826
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        903
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        936
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        397
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        885
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   975 AA;  106581 MW;  487AC28233F1D863 CRC64;
     MAEHGHNMWE EEPSKGRDSL DSDSSASTTS LVFDQISERV AAESGTTKGK RMRYGHDEAD
     LGARLSELDD EDPLKDEASG DYDLETGPFL GGHGHNSNHD GLSAASGSAG KTQGGYRMMD
     RGLRRVLIIA SLVFVTAWVG GLFIYISHKS YLHGSEFEHD PQATVSRGSL RKITREQVDN
     GFWRPVKASI AWVAGPAGED GLLLETNASG ASDKAYLTVQ DVRSLQQGLD ASTEAAVAAA
     RRTLVEKSTF TFAGKTYRIG SSKASKDMSK VLLGVDVQSN WRHSSTAAYF ILEVATQTVQ
     PLIPGEVSAR VQLAQWSPQS DAIAFTRDNN LYFRQVVAGS SSSAEDADSV IKQITTDGGP
     ELFYGVPDWV YEEEVLGGAS ATWWSPDGRY IAFLRTNETG VPEYPVQYFL HRPSGAAPAE
     GEENYPEVRQ IKYPKAGAHN PVVDLQFFDV GRGDSFSVAV SGEFADENRL ITTVLWAGAQ
     KVLVKETNRV STVMRVVVVD VAARSGQAVR TVDVGAIDGG WFEISQRTRF IPADPARQRP
     DDGYIDTIVH NNGDHLAYFS PPENPEPIML TAGPDWEVDD APAAVDLERN LVYFLATIQG
     ITQRHLYSVR LLDGGGLSPL TNTSEPGFYG ASFSAGVGAG YVLLEYGGPN IPWQKVMNTP
     AAAAAAAAGS ADVSKQMPFV HVLEDNHELA ERARQYALPL LVRGTFDVKG HDEGVGAGKL
     NYLERRPPHF DPSKKYPVLF QQYSGPGSQE VTHEFSVDFQ SYVAASLGYV VVTVDPRGTG
     FAGRSNRVVV RGRLGVVESH DHIAAAQHWA SLPYIDGDRL AIWGWSYGGF TTLKTLEQDA
     GRTFRYGIAV APVTDWRFYD SVYTERYMDT PQANAVGYDT GAVTNASALA QNVRFLIMHG
     IADDNVHLQN SLALLDRLDI EGVSNYDVHV FPDSDHSIYF HNGRQIVYDK LENWLINAFN
     GEWLKIDNAK PQGKR
//