DAPB_GROCL
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 03-AUG-2022, entry version 39.
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; Grosmannia.
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 PRIDE; F0XS04; -.
DR EnsemblFungi; EFW99394; EFW99394; CMQ_7762.
DR GeneID; 25981342; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR InParanoid; F0XS04; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 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
