DAPB_PODAN
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 03-AUG-2022, entry version 67.
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; 5145.XP_001913070.1; -.
DR ESTHER; podan-dapb; DPP4N_Peptidase_S9.
DR EnsemblFungi; CAP60552; CAP60552; PODANS_1_8430.
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 OrthoDB; 269253at2759; -.
DR Proteomes; UP000001197; Chromosome 1.
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..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
