ID A0A316U2U1_9BASI Unreviewed; 1082 AA.
AC A0A316U2U1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Dipeptidyl aminopeptidase B {ECO:0008006|Google:ProtNLM};
GN ORFNames=BCV69DRAFT_290909 {ECO:0000313|EMBL:PWN19168.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN19168.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN19168.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN19168.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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}.
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DR EMBL; KZ819332; PWN19168.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316U2U1; -.
DR STRING; 1684307.A0A316U2U1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000245942; 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: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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022438};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000245942};
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 97..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..722
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 811..1009
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 120703 MW; 57C839B91F4BCBEE CRC64;
MVRASFQSDS TASDATLDEK DPSEPYRGHE ERDDAGHVTS SNYRFRDSVE FIGQEEEEEQ
VGLMQLDRRR QRSSQRIPLS SRKPERKLRR LLREHEALII IIFSSILALP LLVALYAWLV
SASHLPIAAS TDVIVSPPSG FLPDNKVSIS AARKYAASSD DAEGHYGLRQ APGFAFNEAV
PGWATPEEAD QVLRLAKGTT KKALESQGWT TLKPKSMDVI FNGTLDTVSI DLAWSAEDKD
DGVFMRKDPA TSDIIFQDVT HARLQMTGQG SVAPGGGQVT FVRGKDVQDK TGKQLAWDTF
VVSPDLSHVM FFSDTMRVYR HSRQSNVWIH NVEEKRTWPI GDGPSKPPAI AHAAWIPSTS
FSLAYVKDNN LYVALDPDRG EATRITSDGT ATIFNAVTDW VYEEEVFESN HALWFSPGGT
KLAYLRFDET EVPVYDFPIY NPDPSTAGAT TPYLNSIKLK YPKPGFKNPI VSAHLLDLKK
LADLTAQSTS INIEVAKYHL KSPLPVSEIA DEKKVDEALF AAEDAKDRLV TEVAWLDDDS
LFIRETDRGS DHLRGIVFDT AKVGGGQEMV GTVVRRIDAK DKSWVPFGQD IAALGVKDLA
AKSTAYLDLI ENSQGFKHLA YYPNATSSAP IFLTFGTWEA DKLLHADVKR NKAYISAAYP
LPHHRHIFAV DLPDIKQGKS ALSSFRPHFK DINAAHPEAS FDATFDPKGA YYLLREAGPR
VPTARVIGVD DASFDWIVED NAAAVKTSAQ YTQAHYVYYN VTLPNGVTTS VKEIRPYDFD
ASGETRYPVL LNVYGGPDSQ QVTHTYSPQE WHQSLVNELG YVVAIVDGRG TGYRGAAYRD
GVAKQLGSIE IDDLLATADK IRRLPYVDEK RLGLWGWSYG GYFTNKVLER DSGLITLGIS
VAPVTKWTFY DSIYTERYMK TLESNQAGYE KSDVHVTDGF KHAHYLLAQG SGDENVHFEN
SAHLLDLLTA QKVRGFWFRM FTDSAHGIST RGAYRELHEY LTDFLKTKWG AGGKRRFEGK
GGRKGLVAEH VQRRGVEERE EEDGGQLGER DWESEAKRIF RQAQDEALVR RLARRGRKGA
DL
//
