ID A0A1R3IH17_COCAP Unreviewed; 1454 AA.
AC A0A1R3IH17;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pectinesterase, catalytic {ECO:0000313|EMBL:OMO81882.1};
GN ORFNames=CCACVL1_12155 {ECO:0000313|EMBL:OMO81882.1};
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:OMO81882.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO81882.1, 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:OMO81882.1};
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 -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC gluconate from pectin: step 1/5. {ECO:0000256|ARBA:ARBA00005184}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OMO81882.1}.
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DR EMBL; AWWV01010067; OMO81882.1; -; Genomic_DNA.
DR STRING; 210143.A0A1R3IH17; -.
DR EnsemblPlants; OMO81882; OMO81882; CCACVL1_12155.
DR Gramene; OMO81882; OMO81882; CCACVL1_12155.
DR OrthoDB; 35225at2759; -.
DR UniPathway; UPA00545; UER00823.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd15539; PHD1_AIRE; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR033131; Pectinesterase_Asp_AS.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR032308; TDBD.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47025:SF27; ACYL-COA N-ACYLTRANSFERASE WITH RING_FYVE_PHD-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47025; AUTOIMMUNE REGULATOR; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF16135; TDBD; 2.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS00503; PECTINESTERASE_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 702..747
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 793..851
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 493..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1307
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10040"
SQ SEQUENCE 1454 AA; 160693 MW; ED6AA321EFFD6C7E CRC64;
MKRELEIPLE SSLSPTRESV AVCKSQASSS TSCKRVKVTQ VNGYIVYTRV KKKRSNCRDE
FSENLEITKL ENFNKPINGV KESLVEDQKN KASAEASHVN NSVIGARLGS EKVARKKEAV
ANVVGESLVV RDIGGGGGLV EALIQESRAI GENAIVGNLV VEEIGLDGRS IVQAALGEGS
SSHLATVMSR KELTDELETC LVEKGRFRGA SVQIGDSCEG NDDILLKSLR RSKRSLLRPL
KVEPVDNLEC EQQPAEDVSV SDIGGQEAAE GSDLTTPWKN LELKMSKKIA LNKCPMTVKE
LFDTGLLDGV PVVYMGTISS KTAGLRGIIM DGGILCSCSL CKGHRVVPPS QFEIHACKQY
KRAAQYICFE NGKSLLEVLR ACRRRPLHTL EATIQNILSA LPEQKCFTCR RCKGSFPVMH
VGQIGPLCNS CVELKKSQSS TTSAPIARAR SEEPLLISRS AGSASVGIFP PSTSQWKTMR
KLQEPVLMSQ SYGSASSSIS PQSKSQWKKP RKSSELDATS NSPQNASLCI SSENRSPWKT
TRKLTKPRLF TKSLKSASVN LSSQDKGHWK TKKKSVKSVL LSKTIKGAPS SPLYSPDGSQ
WKMTTKDQRL HKLVFEEDGL PDGTEVAYYA RGQRLLEGYK KGFGIICRCC NCEVSPSQFE
AHAGWASRRK PYAYIYTSNG VSLHELAISL SKGRRYSAKD NDDACIICAD GGNLLLCDGC
PRAFHKECAS LPTVPRGRWY CQYCQNLFMR ENFGEHSANA VAAGRILGVD AIEQINSRCI
RIVKNIEAEL SGCALCRACD FSKSGFGPRT ILLCDQCEKE YHIGCLRTHK MADLREIPKG
KWFCCSDCSR IHSILQKLLL RGAEKLPDVF LDIIKKKYVE KGLDADINID VRWRLLSGRF
ASPETRLLLS QAVGIFHECF DPIVDTTTGR DLIPCMVYGR NLKGQEYGGM YCAVLTINSF
VVSAGIIRVF GQEIAELPLV ATSKANHGKG YFQLLFSCIE KLLAFLNVKN LLLPAAEEAE
SIWTDRFGFK KLTPEQLVQY KRSCCQMVVF QGTSMLQKEV PPCRVVNTIP PFSKTSTIDI
NDNNYDHSLE VSLVRKVVSQ CGEFLSVITR MVARHYHHHH HHHHHQRRPS KHKCDHTKES
STFISQYKAV SLVLTVDWKG CANFSSVQQA IDNVPDSSPS KTLIVIHSGT YREKVVVHAN
KSNLILQGEG FLKTAIEWND TANSTGGTVY SSSVSIFAPN FTAYNISFRN SAPEPSPGES
GKQAVALRIA GDQAAFYNCG FFGAQDTLLD ERGRHYYKGC FIQGSIDFIF GNAKSLYVGC
VIHSIAKEGT PGVSGCITAH ARNSPNEQTG FSFVNCIIRG TGSVWLGRAW GAYATVVFSR
TYMTDVVSPD GWNDWRDPSR DQTVFFGEYE CLGPGANYTF RVAYGKQLME YEAAPYWNIS
YIDGEEWLQD QAFL
//
