ID M3K1G6_CANMX Unreviewed; 930 AA.
AC M3K1G6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Dipeptidyl aminopeptidase A {ECO:0008006|Google:ProtNLM};
GN ORFNames=G210_0862 {ECO:0000313|EMBL:EMG48554.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG48554.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG48554.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S9B family.
CC {ECO:0000256|ARBA:ARBA00006150}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG48554.1}.
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DR EMBL; AOGT01001058; EMG48554.1; -; Genomic_DNA.
DR AlphaFoldDB; M3K1G6; -.
DR STRING; 1245528.M3K1G6; -.
DR MEROPS; S09.005; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OMA; WHCQEIQ; -.
DR OrthoDB; 2042604at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF160; DIPEPTIDYL AMINOPEPTIDASE A; 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|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 86..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 233..616
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 724..923
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 106949 MW; 9AB770CA9D0FF017 CRC64;
MFTRKPSHHE EYEMVDQTTS SQNSVSTPTS LESSTRDSTD SQSSSVFEDL ESYSFRSGSK
IEDFNDNPLF QTILMRYRKQ GINAKVCGFI SILTVLLWIG SLILYSHLNS SKYISSLRWK
TGMVSLNGEN ITINQYSPSF KNVSLSDWRS GRYYSFEEQI RWLTPKQYPK MKSGSGYYAV
NEHGKVVIKQ INSDVHDVLI SNKKFAYGNN FFEIEDYILN PSNPVEELDN FHILITDQLP
QWRQSSFALY WLYNPLTMIY QPIQPPGNKD FWDHQSDPLG TKVLQKLHFA DFSPDGKYVY
FGFEHNLYIQ DLTGDNINQI TTDGSPNIFN GKADWTYEEE VSPSDKMIWW TQNAEKFIFA
KIDDTKVKEV ELDYYVKENT DVGTTYQQSD VPKKEGVNQY PIKTSLKYPK TGSPNPSISL
YIYDVKEKKA EKIVEDDPGN ESILYYAKWL DNDNFLMKKT DRTSSILSKK LYQLSTNQVK
TINSINVTAE YNGWVEKMSP ITVLEDGKYI DNIVVNKQNS LALFDSPESS QPSKVITKNT
NWEVIGGATY DKQEKFIYLL TTIKSSMDSH LIGIDLANDY KVVNITNTLT DGYYEVDFSI
DGQFANLKYQ GPDVPWQRLI NMGDVHDFSA SEESKEQSIE EGVLLKQPII NKPADLENIN
FPTTRFKEIT IGKAKNNVSV NVMEILPPNF NPQKHKYSLF VHVYGGPGSQ NVFKKFDIGF
LQIISANLNC IVLVIDPRGT GGKGWNFRSF ANRNLGYWEP RDLTLVTSEY ITRNKDIINK
ENVAIWGWSY GGFTVLKTLE YDKGETFKYG MAVAPVTNWL FYDSIYTERY MGLPSENPKY
ETTGRINEIN NFKLAKRLLI MHGTGDDNVH IQNSMWLLNE FNSHNVENYD VQFFPDSDHA
IMYNNAGIIV FDKLFNWLQD AFTGKFDSFM
//
