ID A0A1R3GWQ2_COCAP Unreviewed; 654 AA.
AC A0A1R3GWQ2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Splicing factor YJU2 {ECO:0000256|HAMAP-Rule:MF_03226};
GN ORFNames=CCACVL1_22794 {ECO:0000313|EMBL:OMO62477.1};
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:OMO62477.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO62477.1, 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:OMO62477.1};
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 -!- FUNCTION: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA. Plays a role in stabilizing the structure of the
CC spliceosome catalytic core and docking of the branch helix into the
CC active site, producing 5'-exon and lariat intron-3'-intermediates.
CC {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SUBUNIT: Component of the spliceosome. Present in the activated B
CC complex, the catalytically activated B* complex which catalyzes the
CC branching, the catalytic step 1 C complex catalyzing the exon ligation,
CC and the postcatalytic P complex containing the ligated exons (mRNA) and
CC the excised lariat intron. {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03226}.
CC -!- SIMILARITY: Belongs to the amidase family.
CC {ECO:0000256|ARBA:ARBA00009199}.
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:OMO62477.1}.
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DR EMBL; AWWV01013239; OMO62477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GWQ2; -.
DR STRING; 210143.A0A1R3GWQ2; -.
DR EnsemblPlants; OMO62477; OMO62477; CCACVL1_22794.
DR Gramene; OMO62477; OMO62477; CCACVL1_22794.
DR OrthoDB; 4001253at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IEA:UniProtKB-UniRule.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR46310; AMIDASE 1; 1.
DR PANTHER; PTHR46310:SF7; AMIDASE 1; 1.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
DR SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03226};
KW mRNA processing {ECO:0000256|HAMAP-Rule:MF_03226};
KW mRNA splicing {ECO:0000256|HAMAP-Rule:MF_03226};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03226};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Spliceosome {ECO:0000256|HAMAP-Rule:MF_03226};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03226}.
FT DOMAIN 259..398
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03226"
SQ SEQUENCE 654 AA; 72460 MW; 06632C99418EE253 CRC64;
MGERKVVQKY YPPDFDPAKL PRVGRRKNQQ MKIRDMMPMK VRCNSCGNFI TGGTKLNSRK
EVVSGKTYLG IKIYRFYYKC NNPKCSSEII ITTDPQNSDY AVESGARRCF EPWRAADEEA
GKRKLKREFE EKGNSMKALE NRTLDSRREM DKLAALDYLK SMKARHATVS ANDMLEKLHS
SDVEKKKKLE EEDEELTKLN FPRPKEDFVK RISDEVFEEH GGDFLKRPKV YEDVSSNPTD
ALVKTSFHRT HRVKAPSKFD VDGYVTGFGN PDWKRTHSAA VSTAPSVLDV LRAGATCVGK
TVMDEMAYSI NGENVHYGTP TNPCAPDRVP GGSSSGSAVA VGASLVDFSL GTDTGGSVRV
PASYCGILGF RPSHDAISTS GVTPMAQSFD TVGWFARDPV LLNQVGRVLL HSPNMDPVRP
SQIIIPEDCF SLSSIPNHRT TQVLVKSVEK LFGGQILKQI VLGDYVKEKV PSLQHFMSNG
NEEQAYNIPS LAALSSAMRL LQRYEFKKNH AEWVTTVNPT LGPGLHERVW DAVRTPEENI
DVCHSVKTEL RAALTFLLED HGVLALPTVP GDPPKLQSNP ASLEVFRARA FSLLSVAGVS
GFCQVSIPLG MHNNLPVSIS LLAKHGSDAF LLNLVETLYD TIKKEAEISE KMSS
//
