ID C5MH75_CANTT Unreviewed; 836 AA.
AC C5MH75;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Dipeptidyl aminopeptidase B {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTRG_05429 {ECO:0000313|EMBL:EER30977.1};
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747 {ECO:0000313|EMBL:EER30977.1, ECO:0000313|Proteomes:UP000002037};
RN [1] {ECO:0000313|EMBL:EER30977.1, ECO:0000313|Proteomes:UP000002037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; GG692402; EER30977.1; -; Genomic_DNA.
DR RefSeq; XP_002551131.1; XM_002551085.1.
DR AlphaFoldDB; C5MH75; -.
DR STRING; 294747.C5MH75; -.
DR ESTHER; cantt-c5mh75; DPP4N_Peptidase_S9.
DR MEROPS; S09.006; -.
DR EnsemblFungi; CTRG_05429-t43_1; CTRG_05429-t43_1-p1; CTRG_05429.
DR GeneID; 8300486; -.
DR KEGG; ctp:CTRG_05429; -.
DR VEuPathDB; FungiDB:CTRG_05429; -.
DR eggNOG; KOG2100; Eukaryota.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:EnsemblFungi.
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, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000002037};
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 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..534
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 621..831
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 836 AA; 95826 MW; 15F375D58179389C CRC64;
MYGISSEYLK ETGGTTPRRS MSSYKRYIYY GTLLAVLLYG TSFLLITIER FSTTFELQSI
SAFSNNNDEL PEFASPSTRS TDFKGKIPLS KKIYDDHVLA PKLHSIQWIK TPESIYDDQG
TYVIKEEEKD KDSGFRVVVK SLADESYEKV LIESSKFKYK GREHEITDYI ASPDLSKVIL
KTDVTSLWRY SSVSLYWVLD IESKTIEPIY NEIDKISTVS WSPDSNKIAF IFDNNLYYKS
LQSNEIVQIT SDGSPSIFNG KPDWVYEEEV YGSDKVFWWS HNSDKIAFLR SNNTEVPEFT
LPFYAQEEHL DYPEIVKIKY PKAGYPNPIV DVLTYDLEKD KVHEHDLKSK TIDIHNRLIT
EVVWIGESLK VKTSNRHSDL LEIFLISRNE KVSLIRTLHA EDSWFEASAS TVHIPANETL
GRKYDGYLDI VVEGGYNHLA YFSPPDSPDY ELLTKGNWEV TDGVVFDDAS NTVYFTSTAK
SPIERHVHAI ELLDRTNNGL PYIKDITTKE GWYSASFSSG ARFLFLSDLG PGVPTQRVND
LKMNKNVKTI EDNAELVAKL RDYIIPEVKY SQVELTDEEG GKFLATAMET LPLNFDKKRK
YPVLFFIYGG PGSQTVTKKW AVSFSSLIAA ELDAIVVTVD GRGTGFNNLN YKLGSKFKFI
VRDKLGKYEP LDVIAAANKW AEKSYVDPER IAVWGWSYGG FLTLKTLETD VKNPIFNYGV
AIAPVTRWRL YDSIYTERYL NTPAENPYGY ETGSIQNVTN FKHVKKFFIG HGSGDDNVHV
QHTLQLLDEF NLAEVENYEF MIFPDSNHAM NYHNGQKVVY DRILSFFRRA FDWEFV
//
