ID A0A0D2JSQ4_9EURO Unreviewed; 1009 AA.
AC A0A0D2JSQ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=dipeptidyl-peptidase IV {ECO:0000256|ARBA:ARBA00012062};
DE EC=3.4.14.5 {ECO:0000256|ARBA:ARBA00012062};
GN ORFNames=Z520_07763 {ECO:0000313|EMBL:KIX96497.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX96497.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX96497.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX96497.1,
RC ECO:0000313|Proteomes:UP000053411};
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 Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN848077; KIX96497.1; -; Genomic_DNA.
DR RefSeq; XP_016630620.1; XM_016778260.1.
DR AlphaFoldDB; A0A0D2JSQ4; -.
DR STRING; 1442371.A0A0D2JSQ4; -.
DR GeneID; 27713509; -.
DR VEuPathDB; FungiDB:Z520_07763; -.
DR OrthoDB; 2876738at2759; -.
DR Proteomes; UP000053411; 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: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: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.
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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022438};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
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 203..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..706
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 789..994
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1009 AA; 113018 MW; 4FF29F7520A4249E CRC64;
MDAASAAQLE TRHRIAPQPP PPPPPSSSRI SEKSQTLRII TDLGAEGPLV SPRKRISRKD
PASAVTPCAY QPLSCTDNPN HTQSRSTSLA VNFDVFNWSP RRQPPTSIMG TASQSLQEEQ
ETLIKGSRQS SEDPYPRPSE ESVTTASTVS LVLESLNSAD AVKEPLQQPS SYRDDDSDPE
LPRFNDKNFT IGGQRMSKGL RRAIWIVSVV GIIGWILAVV IFVAGGRYKH ASTLDYDHET
PIKSSAKKVT LEQIQSGQWS PRYANIEWTP GPNGEDGLLL EINQPNQDYL VVEDIRSGTP
SEVNAFKRTA LVKSGWIKYG GQQFWTSEFW VSPDMKHVLL MANPEKVFRH SFLGLYFILD
VETQNAQPLD PALPDAKIQL AQWSPRSDSV VFTRDNNLFL RHLSSPQVTT ITTDGGPEYF
YGIPDWAYEE EVFGTNTATW WARDGQYLAF LRTNETTVPE YPVQYFLSRP SGKKPIEGLE
NYPEVKEIKY PKAGAPNPVV DMLFYDIKKG EVFSVDIEGG FPDEDRIIFN IVWADEGKAL
VSESNRESDR VRIVLVDVPS QSGHTVRIVD LKDVDGGWIE PSQQAKYIPA DPANDRPEDG
YVDIIISDNG NHLAYFSPLN SSIPVMLTRG NWEVDGGPAA VDLKNNLVYF VAAKEAPTQR
HLYSVKLDGT SMDSLVPTNE AAYWESSFSS GAGYVSLKYT GPGIPYQKVV STPANPEKIE
EVLEDNQDLA KMASSHELPH QVFQNVTIDG YTLQVVERRP PHFDPKKKYP VLFYLYGGPG
SQMVNRRFHV DFQSYIASSL GYIVVTVDGR GTGFIGRKAR TIVRNELGTY EAHDQIATAK
LWAEKPYVDA DRMAIWGWSY GGFMTLKVLE TDAGETFKYG MSVAPVTDWR FYDSIYTERY
MRTPQDNPLG YSKSAISNVT AISQNVRFLI MHGVADDNVH MQNTLTLLDK LDLAGIENYD
VHFFPDSDHS ILFHNANHIV YDKLANWLVN AFNGEWYRTE DPKPIDLGT
//
