ID A0A0D2BLZ7_9EURO Unreviewed; 731 AA.
AC A0A0D2BLZ7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Dipeptidyl-peptidase V {ECO:0000256|ARBA:ARBA00032829};
GN ORFNames=PV08_00178 {ECO:0000313|EMBL:KIW19605.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW19605.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW19605.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW19605.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S9C family.
CC {ECO:0000256|ARBA:ARBA00010040}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN847492; KIW19605.1; -; Genomic_DNA.
DR RefSeq; XP_016239821.1; XM_016374545.1.
DR AlphaFoldDB; A0A0D2BLZ7; -.
DR STRING; 91928.A0A0D2BLZ7; -.
DR GeneID; 27327261; -.
DR VEuPathDB; FungiDB:PV08_00178; -.
DR HOGENOM; CLU_008615_0_1_1; -.
DR OrthoDB; 5471261at2759; -.
DR Proteomes; UP000053328; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053328}.
FT DOMAIN 487..695
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 731 AA; 80607 MW; 5407C640E04B958F CRC64;
MTVRKLYTPE VLLSAPRRSA AIPSPDGKLA VYTQSTYSFD SHSRTNEICV LDLTTAQSVC
ISKDPKASEP RWTGTGHELV WLKECDNGNT SFVITDATLP GKCYTAGTVP GLVSSLKVFV
IEPGKVAVAV AGKANPDGSL HNPKDVQKPR SSARVYDSLF VRHWDTYISE QRNSIFTALL
QKSQPVVTSR QGRYSLLGFK NALQGSKLEC PIPTFGGTDH FDIGPTGLII VAKDPDLNPA
THTKCQCYFF PQRDLTDVSK PQFRKIGVPG LHGAATSPVF SPSGESAAFL KMATDGYESD
KNCTVLVHGL SDDHELTAAE LMHTSDGKGG WDRSPSSLKW TADGKTILME AEDNGRGCLF
ALDLDQAPGP GWRPRQITHS GYIIDFAPLS SDSALYLVSS NSLVDSSTYS IVDSSGKHAT
TIISSISNGG ARFGLSPEQV SSLWWEGANS HPVHAWMMRP SFFRADHKYP LAYLIHGGPQ
GAWNDQWSTR WNPAVFAEQG YIVVCPNPTG STGYGQAFTD AIRNEWGGLP YEDLVKGFEH
IEANLDFVDT SRAVALGASY GGFMMNWIQG HDLGRKFKAL VCHDGVFSMT GQLASEEQYF
PVHDLGGPIW ERQEIYDKWD PSRFTKNWST PMLVIHNELD YRLTIAEGLS AFNVLQMRGI
ESRFLSFPDE NHWVLKPENS LVWHLVVINW INKFVGLPKL VDRDGRDGST FSKQNEPRGI
VRRIAAAHLQ Q
//