ID   M3C1F3_SPHMS            Unreviewed;       676 AA.
AC   M3C1F3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Alpha/beta-hydrolase {ECO:0000313|EMBL:EMF14136.1};
GN   ORFNames=SEPMUDRAFT_162337 {ECO:0000313|EMBL:EMF14136.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF14136.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF14136.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF14136.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- SIMILARITY: Belongs to the peptidase S10 family.
CC       {ECO:0000256|ARBA:ARBA00009431}.
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DR   EMBL; KB456262; EMF14136.1; -; Genomic_DNA.
DR   RefSeq; XP_016762257.1; XM_016907997.1.
DR   AlphaFoldDB; M3C1F3; -.
DR   GeneID; 27905134; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_3_1; -.
DR   OMA; QTWFFEF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR033124; Ser_caboxypep_his_AS.
DR   PANTHER; PTHR11802:SF189; CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00450; Peptidase_S10; 2.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EMF14136.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..676
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013311413"
FT   REGION          546..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          645..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..586
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  75026 MW;  10C45465A40D4B85 CRC64;
     MASIALTLLV SLAAAQFPPK PEGVKVLRSK HHDGVTLSYK EPGLCETTPG VKSYAGYVHL
     PVEALNETFE HNGYPINTFY WFFESRMDPH NAPLAIWLNG GPGGSSLLGA LSENGPCFVS
     NDSKSTYLNP WSWNNEANLL FIDQPNQVGY SYDVLTNVTV NLIPSDSWLP GGDVQPTDFS
     DGVPEQNNTF LVGTSSSQKV SSTANSTQHA ATAIWHFAQT WFEEFPQYKP DDERISLFTE
     SFGGHYGPGF MDYFIRQNDK ITRGEIPRDG AHYMHLSTLG IVNGCIDAPD MFESEIIFAY
     NNTYGIQAIS QDDYEWSMNE FHKPGGVLDD LHKCREAELQ TDPHNHGTVA ATNKICSEAG
     ERAENISDGM YEEGGSRAPF DITHDAQDSF PPSFVLGWLN QVEVQQALGV PVNHSWFSQA
     VSKAFSSTGD IAKGGQLEQL RNVLEHGITV ALLYGDRDFA CNWIGGERYS LNVPWSGQAK
     FRAAGYTPLV LSEPYTQSGG LVRQYGNLSF TRVYQAGHMV PSYQPEAAYR IFMRALNHRD
     IATGTINTHD TFPTTTTTTN TTTSSSSSSD DDDDDDDDDD DEEQYEYYST TGPSDTWWKK
     NDVLPGMPHV CYTLDPLRQC TEEEVEWIRD GTAVVKDWIL VGRKNVSDSD SNSDSGSQVE
     RMISNREGQV PFKVDL
//