ID A0A074VM28_9PEZI Unreviewed; 897 AA.
AC A0A074VM28;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=M437DRAFT_75954 {ECO:0000313|EMBL:KEQ61775.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ61775.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ61775.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ61775.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal
CC dipeptides sequentially from polypeptides having unsubstituted N-
CC termini provided that the penultimate residue is proline.
CC {ECO:0000256|ARBA:ARBA00002218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a
CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither
CC Pro nor hydroxyproline.; EC=3.4.14.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001257};
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; KL584836; KEQ61775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VM28; -.
DR STRING; 1043003.A0A074VM28; -.
DR HOGENOM; CLU_006105_0_1_1; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000030672; 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:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
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:UP000030672};
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 87..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..593
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 676..881
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 897 AA; 101448 MW; E4C65DD5DDFF8F75 CRC64;
MAFRDDEEAL PLTRHDANHT DDIDQPRPSA SSISTTSLVL EHLSGHPNSI QAKEALYSQP
RSEEFDFDDR AAWKHKSHGF DFKARRILYI VASIAAAGWL AALVLFLSSG SHKSLASRPH
DPHATKTAGH GQKITLEQVL QGKFYPKSHG ISWIEGAEGE DGLLLQWGGE GGRDYLVVEE
VRYMQDAQAS KQHSKTLMKN GAFYHNGEAI SPSNVWPSAD HKRVLIQSHI QKNWRHSHTG
RYWIFHVDSQ TAEPLDPAEP NKRIQYASWS PNSDAVVFTR DNNMYIRNLS DNKVKSITTD
GGAQLFYGVP DWVYEEEVFS SNKATWWSGD GKYLAFLRTD EAAVPEYPVQ YFFSRPSGKQ
PKPGEENYPE VRKIKYPKAG APMSVVTIQL YDIAKGQVFT VPIQGDFEDK DRLITEVTWA
GRSGKVIVRE TNRESDVLKV VLIDAERREG KTIREVDVNA LDGGWFEVSQ TTTYVPSDPA
KGREHEGYID TVIHDGYDHL AYFTPLDSPE PIMLTKGKWE VVDAPSALDL KNNLVYFVAT
KKSSIERHIY SVKLDASDLK SITDDSEVGY YSGSFSKGGG YLLLTNKGPG IPWQKVLNTP
SNSDKLEMTI EENKPLRELV TKTELPIQIY QTINVDGFDL NLVERRPPHF DERKKYPVLF
FLYNGPASQQ VDRTFHLDFQ SYVASSLGYI VVTLDGRGTG HLGRATRCIV RGNLGHYEAH
DQIAAAKMWA AKKYVDADRI AIWGWSYGGF MTLKTLEQDA GRTFKYGMAV APVTDWRYYD
SIYTERYMHT PQHNPVGYAN STITDVDALS KNVRFLVMHG VADDNVHFQN TLSLLDKLDL
ANVQNYDVHF FPDSDHSIYF HNANRVVYEK LSNWLINAFN GEWLRTPNPT PLAQIEK
//
