ID A0A1Y1ZA16_9FUNG Unreviewed; 827 AA.
AC A0A1Y1ZA16;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:ORY06954.1};
GN ORFNames=K493DRAFT_332912 {ECO:0000313|EMBL:ORY06954.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY06954.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORY06954.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY06954.1,
RC ECO:0000313|Proteomes:UP000193498};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY06954.1}.
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DR EMBL; MCFE01000012; ORY06954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1ZA16; -.
DR STRING; 1314790.A0A1Y1ZA16; -.
DR InParanoid; A0A1Y1ZA16; -.
DR OrthoDB; 170111at2759; -.
DR Proteomes; UP000193498; Unassembled WGS sequence.
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:SF193; DIPEPTIDYL PEPTIDASE 9; 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 Hydrolase {ECO:0000313|EMBL:ORY06954.1};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000193498};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 144..518
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 622..827
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 827 AA; 96000 MW; C640D3D68D1674C0 CRC64;
MTSWESIRQE IRAFRSSIPQ PSLSTMKDFI FDDTNDCVYF IGTDPSKNFR TTTLFTVALP
LGSVAYSYFD EQTVPCEHAC SDDPFSSTLE WKHMLADLYL RDKLHENLSR EEILAKERRR
ISIEGITWYL YEESSGLLVF PHSNNFYIGS VGKNKKFQPT PMFQHRSHSP RMDPKIGGRD
RDLIAYVKQR DIWVSTLDGQ EVQLTFCGNS DDSSISCGSP EFVMQEEFDR FTGFFWAPSN
GVPSTDAFER ILYLQVSESN VDQVCFAHGT KTEEFRYPRT GTPNAMSDIQ IVEFAHPNEV
SEQDITHKRL WGKATLNEMF PWMEYIVRLG WLPHGKSIWV QILDRRQQHM AVVKIPLSNF
TTVYGYNSNV KYEQCVKDVE ILYEEEIKTG WINHTIAYHF LETSNENTTE FIWSSERTGF
RHLYYIKKHR LDIHWTIRPL THGEWPVVDL PISVDLRRKA VYFIAKRDTP LENHLYVASF
REDASPHHVV LLTPKGYFHN VTMNSNCTRF VTFYSSINES PKSSIYYLTW EDKSPFPKSN
LWSKIRPLGI TKDNLPIGNF FSFTNRNAEP FVYVFLGNQI HGCYYKPDNY VEGHKYPTLL
HVYGGPKGQV VTNDYKCPRF LRMFLATKMG FVVIMIDGRG SSERGLAFET QIRWRMGTVE
LDDQVDGLRH LIENSPSHIS TMIDTDKIAI SGWSYGGYLS LLALAHYPDI FKIAIAGAPV
TDWMLYDTAY TERYMGMPEE NPDGYRNASV LSHVDKFPDS EHRLLLAHGL IDENVHFTHV
ELLVSALTKN NKPHQLQLYP NERHGIRHPA TNEHFETLMF YWLKNYL
//