ID   A9U4J0_PHYPA            Unreviewed;       409 AA.
AC   A9U4J0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EDQ49421.1};
GN   ORFNames=PHYPADRAFT_156259 {ECO:0000313|EMBL:EDQ49421.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1] {ECO:0000313|EMBL:EDQ49421.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00008668}.
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DR   EMBL; DS545389; EDQ49421.1; -; Genomic_DNA.
DR   RefSeq; XP_001785775.1; XM_001785723.1.
DR   AlphaFoldDB; A9U4J0; -.
DR   HOGENOM; CLU_015101_2_0_1; -.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   CDD; cd01837; SGNH_plant_lipase_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   InterPro; IPR035669; SGNH_plant_lipase-like.
DR   PANTHER; PTHR22835:SF659; GDSL LIPASE_ACYLHYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G00510)-RELATED; 1.
DR   PANTHER; PTHR22835; ZINC FINGER FYVE DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..409
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002744017"
SQ   SEQUENCE   409 AA;  45347 MW;  D404AC37DB7F1352 CRC64;
     MRAVEAFTLS LAVAFNFFEP AKAELKNCTC SAVYSFGDSL TDNGNGIATF PDQFIDSETN
     PNGFNFPHHA ADRYCDGRLL VDYVAAFGMG RKPNYAILRS IAADFTYGAN FAVAGATARN
     NTEWVQETGF SSPFSLNVQV SWLERYKVRL QFYYAQVASD SLNTSLYFVY AGFQDYFFPM
     YYQTMTPTEA LDIVDAVVDS IVAAIQRIYA FGARSIMIVN LPPMGCLPAL LTLYADEDSE
     KYDTYGCLDS PNKVSNSHNT LLESRVADLR HNYTNATFYY ADYYSVYRDV LKSPTLYGIS
     ESDTLTACCG YGGSYNFNAS LFCTHSGIMN GGMVNLSYPC SNSTSYINWD GIHPTAQMNW
     ITATLFLNGT HITPAGGFNC SADTSNWYLS HDSLQLVSCI DEVLEELSN
//