ID J7RDU0_KAZNA Unreviewed; 859 AA.
AC J7RDU0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Dipeptidyl-peptidase IV {ECO:0008006|Google:ProtNLM};
GN Name=KNAG0M01470 {ECO:0000313|EMBL:CCK73000.1};
GN OrderedLocusNames=KNAG_0M01470 {ECO:0000313|EMBL:CCK73000.1};
OS Kazachstania naganishii (strain ATCC MYA-139 / BCRC 22969 / CBS 8797 / KCTC
OS 17520 / NBRC 10181 / NCYC 3082 / Yp74L-3) (Yeast) (Saccharomyces
OS naganishii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071383 {ECO:0000313|EMBL:CCK73000.1, ECO:0000313|Proteomes:UP000006310};
RN [1] {ECO:0000313|EMBL:CCK73000.1, ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2] {ECO:0000313|Proteomes:UP000006310}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-139 / BCRC 22969 / CBS 8797 / CCRC 22969 / KCTC 17520
RC / NBRC 10181 / NCYC 3082 {ECO:0000313|Proteomes:UP000006310};
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Kazachstania naganishii.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
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; HE978326; CCK73000.1; -; Genomic_DNA.
DR AlphaFoldDB; J7RDU0; -.
DR STRING; 1071383.J7RDU0; -.
DR MEROPS; S09.006; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; MRTPQEN; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000006310; Chromosome 13.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IPR002471; Pept_S9_AS.
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.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000006310};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Vacuole {ECO:0000256|ARBA:ARBA00022554}.
FT DOMAIN 189..550
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 650..852
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 859 AA; 97190 MW; A3781026E9633F6F CRC64;
MSSGEILDGP ATRDGGSANG PLAQSIPDLE VERIPDSHFQ QARRPLWSHV VRLALLSLLI
IWGSVLVLKS INQLMGHGGK SGGNTGDGGD DKGHDRYRLP NPNVTDDGLL KVSLEHMRNS
TFKPKFQTLQ WVHVMDHQGK GDNGLYFTSV NHTYLVKSVV DHDYSKVLFE GETFVYEGYN
LTVDNIVASP DLKSLLIRCN TVKNWRHSNF ASYFVFDERS STFHAIGDNI AIAQWSPTSD
RISYVQDNNI YIYSLEDLAT VVQVTDDGSS QVFNGRPDWV YEEEVFEDDK ALWWSPQGDY
LAFLKIDETD VLEYTIPYFV QDLKDTYPEM KSIKYPKSGT PNPQVELYVY NCEEDSLYES
HMNTLHDLES ILLTEVVWVA NNSVLAKITD RSSDLLKVVK IDALEEDTTV IRSETQANNG
WWEITHNTMY IPRDVKNGRP HDGYIDVLPI DGYNHLVYFT PVNSTTPKVL TRGKWEVVNG
PISFDAELNR VFFVAKKKSS MENHVYYINL SNPEEVVAVS DTSAPGVYDI SFSGSCKYAL
LTYKGPKVPY QKIISLQGGD ESIEGSRIGR TLFYLEDNEL LKTVMADYEI PAKRFRELDL
GLDENGQKIL VNSFEILPSG FNEKLRDYYP VFFYAYGGPN SQQVVQTFSV TFNEVVSAQL
DAIVVVVDGR GTGFKGTKFR TLVHDHLGSV ETEDQIAAAK MYAKKPYVDS NKISLFGWSY
GGYLTLKTLE RDAGKYFKYG MAVAPVTDWR LYDSVYTERY MHTPQDNPEG YSESSVNNVE
SLAQAKRVLL MHGTGDDNVH FQNSLILMDK LNLASITNYD VHVFPDSDHS ISYHNANAIV
YDRLLQWAKR AYTGQFLEE
//
