ID A0A1R3JKW0_COCAP Unreviewed; 802 AA.
AC A0A1R3JKW0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 03-MAY-2023, entry version 22.
DE SubName: Full=Lipase, GDSL {ECO:0000313|EMBL:OMO95509.1};
GN ORFNames=CCACVL1_05389 {ECO:0000313|EMBL:OMO95509.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO95509.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO95509.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO95509.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00008668}.
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:OMO95509.1}.
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DR EMBL; AWWV01007644; OMO95509.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JKW0; -.
DR STRING; 210143.A0A1R3JKW0; -.
DR EnsemblPlants; OMO95509; OMO95509; CCACVL1_05389.
DR Gramene; OMO95509; OMO95509; CCACVL1_05389.
DR OMA; CCETEYG; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR48102:SF16; CLP PROTEASE REGULATORY SUBUNIT CLPX2, MITOCHONDRIAL-LIKE ISOFORM X1; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT DOMAIN 199..363
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 412..484
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
SQ SEQUENCE 802 AA; 89184 MW; C369ABED69429345 CRC64;
MLSLVKHTAR ALTSAALRCR RTTVPVFGLT SPWSTISRQI SDGTEYDHIL AEVNCPRCSN
QMPVTFSNRP LSITAPEPGL YHALNFCRNC NTAFYFRPLK LVPLQGSFVE LGRIREDFDG
VPEKEPGRIG KLKDDSVDED DMAGRSMRRK LPTPKEICGR LDEFVIGQQK AKKTESLHLN
ARSLGDNNEN DADDSVELDK SNVLLIGPTG SGKTLLAKTL ARIVNVPFVI ADATTLTQAG
YVGEDVESVL YKLLVEAQFD VEAAQHGIVY IDEVDKITKK AESSNIGRDV SGEGVQQSLL
KMLEGTLVNV PIPDKGARRY PHGDSFQIDT KDILFICGGA FIDLEKTISE RRQDSSIGFG
APVRANMRSS GFTTAAVTTS LLESVESDDL VAYGLIPEFI GRFPILISLS ALDEDQLVEV
KLHFTENALR LISKKAMAKN TGARGLRAIL ENILTEAMFE IPDTKMESHG VHAVVVDEEA
VGSVDETGCG AKILYNEDEL DQFLNKKTLK DFVILCLTEF ISTKEPLEAE SFGILQLIPP
FAKAQNNESI NVIQGVNYAS GWAGIRDETG QRMGQRIPLN EQLRNHKTII SRISKKIGDS
AAKKHLSECI YSLQIGGNDY TDNFYQYEHY NSSHIYNEEQ YATLLVQQYS QQIKSLHEDG
ARMFAVFGLE PIGCSPNSIE IYGRNFSGCV LKLNQAAELF NGKLEAVVNE LNKNLSYAKL
RYLNHTPPGS FESIGIKELE KTCCETEYGS KTSGRMLCRK NSETCIHPEQ YLYWDGHHHT
ELWNKLSARV AYEILRTLVP KK
//