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Database: UniProt
Entry: A0A1Y1WAS2_9FUNG
LinkDB: A0A1Y1WAS2_9FUNG
Original site: A0A1Y1WAS2_9FUNG 
ID   A0A1Y1WAS2_9FUNG        Unreviewed;       779 AA.
AC   A0A1Y1WAS2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Peptidase S49 domain-containing protein {ECO:0000259|Pfam:PF01343};
GN   ORFNames=DL89DRAFT_321962 {ECO:0000313|EMBL:ORX70475.1};
OS   Linderina pennispora.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC   Kickxellomycetes; Kickxellales; Kickxellaceae; Linderina.
OX   NCBI_TaxID=61395 {ECO:0000313|EMBL:ORX70475.1, ECO:0000313|Proteomes:UP000193922};
RN   [1] {ECO:0000313|EMBL:ORX70475.1, ECO:0000313|Proteomes:UP000193922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12442 {ECO:0000313|EMBL:ORX70475.1,
RC   ECO:0000313|Proteomes:UP000193922};
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 S49 family.
CC       {ECO:0000256|ARBA:ARBA00008683}.
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:ORX70475.1}.
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DR   EMBL; MCFD01000005; ORX70475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1WAS2; -.
DR   STRING; 61395.A0A1Y1WAS2; -.
DR   OrthoDB; 9717at2759; -.
DR   Proteomes; UP000193922; Unassembled WGS sequence.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07018; S49_SppA_67K_type; 1.
DR   CDD; cd07023; S49_Sppa_N_C; 1.
DR   Gene3D; 6.20.330.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR002142; Peptidase_S49.
DR   InterPro; IPR047217; S49_SppA_67K_type_N.
DR   InterPro; IPR047272; S49_SppA_C.
DR   PANTHER; PTHR33209; PROTEASE 4; 1.
DR   PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR   Pfam; PF01343; Peptidase_S49; 2.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193922};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          180..280
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
FT   DOMAIN          458..601
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
SQ   SEQUENCE   779 AA;  84669 MW;  E10358B696BE00D5 CRC64;
     MNQEQQQQQA SSPNSTKAGL LKRSARIMWR YKKTTLFAAG LAYFVYRRQQ RQRNRLDRAP
     IIDGTMLAWR IHEGSIIEAP EPMSFELSWL SRFLRKLSGK NDEMSMLRAL MALEMAADDP
     RIKGLVVKLG PAPDSNEQTN STGTGLGVAQ VQELRQALEQ FRAKKEQQLG AGSGRTYFYT
     DSFDDQLTYY LASAFSDIIV QPTGQLPLTG LSGTQMYFKD LLDKIGLKMH VEARKEYKSV
     VAPYSQSSMP EKHRENMMDL LNSLNDTIID DIATSRGSSI LSQCKDTHIK AQDIVRKAME
     EGPIIAPDAL GSGLVSALGY TYDVASIVGP RKLTLINTYA DARRLEIETN EMSGGAYDES
     GSTKELAKSM LISSDKAAMA SALKLLESDQ PVTVGVVYLL GGIERFGPRG AKAVCQSLLD
     AAKDPTVSAI VLRIDSGGGD VIASDTIGAY VDYVQDKFGK PVVASYGNVS ASGAYYASTS
     CKRIFASPGT ITGSIGVASM RPVVTKKLLE FIGTNVEELY TVDNKSDSIF REPEGAALER
     YRRTIDIIYD DFKSRVAKGR GYSSDQVEDV ARGRVFTGVQ ALQNGLVDEL GSFTRAIEAS
     AQMGFEARTD IATKLAEFYS QRLINSVRHK AVAAGLFDSV DKAQEESPVD IKVVASGTDP
     DAETIKDGVL KGAVYKKGAF TADLLKNVKV KVFPEEASVA RRLISKARNL GGDGDGDDSA
     EDVQLAAGDT SSSFFGTFAK TAVRSALAEE IERILSNPSS AFKGNKAGAR FESDDINFK
//
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