ID   DAPB_PODAN              Reviewed;         927 AA.
AC   B2A951; A0A090C995;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=Probable dipeptidyl-aminopeptidase B;
DE            Short=DPAP B;
DE            EC=3.4.14.5;
GN   Name=DAPB; OrderedLocusNames=Pa_1_8430; ORFNames=PODANS_1_8430;
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; CU633438; CAP60552.1; -; Genomic_DNA.
DR   EMBL; FO904936; CDP23195.1; -; Genomic_DNA.
DR   RefSeq; XP_001913070.1; XM_001913035.1.
DR   AlphaFoldDB; B2A951; -.
DR   SMR; B2A951; -.
DR   STRING; 515849.B2A951; -.
DR   ESTHER; podan-dapb; DPP4N_Peptidase_S9.
DR   GlyCosmos; B2A951; 3 sites, No reported glycans.
DR   GeneID; 6197654; -.
DR   KEGG; pan:PODANSg10119; -.
DR   VEuPathDB; FungiDB:PODANS_1_8430; -.
DR   eggNOG; KOG2100; Eukaryota.
DR   HOGENOM; CLU_006105_0_1_1; -.
DR   InParanoid; B2A951; -.
DR   OrthoDB; 2876738at2759; -.
DR   Proteomes; UP000001197; Chromosome 1.
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..927
FT                   /note="Probable dipeptidyl-aminopeptidase B"
FT                   /id="PRO_0000412159"
FT   TOPO_DOM        1..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..927
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        769
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        846
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        879
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        365
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        828
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   927 AA;  104169 MW;  288D2A5A7DD9AC52 CRC64;
     MAPAPGMAPY SDEPTGPFHR PEHNDESTGR MSHESESSVS TTSIVFDRIE ERLAAKEGHF
     ELDDHDPMKE ADDDDNDLET GRFLGGRSST QEEDFPAKND GMNRGMRRTL IIVAGLLISA
     WVVGLFFYVS HKSYKPASQI EHDPQATVVQ GTGKQVTLDQ VMGSYWRAES HSISWIESPD
     GEDGLLLLKD GPGKDFLVVE DVRTQNSAGV NAAVDVASSR TLIKERHFDF GGQTHTPGRV
     WPSKDLKKVL IATNLEANWR HSFYASYWVF DVDMQIAEPL IPGEPNVRVQ LAQWSPTSDA
     IAYVRDNNLF LRSLKHDKVV QITKDGGAEV FNGVPDWVYE EEVFSGNSAT WWSEDGNYIA
     YLRTNETGVP EYPVQYFLSR PSGTEPAPGE ESYPEVRQIK YPKAGAHNPV VNLKFYDVAR
     DESFTVEISG RFADDDRLIT EVVWAGGQVI VKETNRVSDV LRVVLVDVAA RTGKAVRELD
     VKAIDGGWFE ITHKTKYIPA DPSKGREQDG YIDMVIHDDN DHLAYFTPLN NSEPIMLTSG
     HWEVVDAPST VDLDNNIVYF VATKESSIQR HVYQVDLSGN NLKAVTDTGS EGYYDISFSA
     GTGYALLSYR GPNIPWQKVI STPANAHKYE HMVEENKELA KSAREYELPI KIYGTIKVDG
     VELNYVERRP PHFDKNKKYP VLFQQYSGPG SQSVNKRFTV DYQSYVAAGL GYVCVTVDGR
     GTGFIGRKNR VIIRGDLGKW EAHDQIAAAK IWASKSYVDE ERLAIWGWSF GGFNTLKTLE
     QDGGRTFKYG MAVAPVTDWR FYDSIYTERY MLTPQTNGHG YDTSAINNVT ALKQSVRFLM
     MHGVADDNVH MQNSLTLLDK LNMVGVENYD VHVFPDSDHG IYFHNANRIV YDKLTNWLIN
     AFNGEWIKVA NAKPQKKRSI QPILPIL
//