ID A0A0E0JK33_ORYPU Unreviewed; 709 AA.
AC A0A0E0JK33;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 2 {ECO:0000256|RuleBase:RU365006};
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit {ECO:0000256|RuleBase:RU365006};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC01G19840.3};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC01G19840.3}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC01G19840.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365006}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000256|RuleBase:RU365006}.
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DR AlphaFoldDB; A0A0E0JK33; -.
DR EnsemblPlants; OPUNC01G19840.3; OPUNC01G19840.3; OPUNC01G19840.
DR Gramene; OPUNC01G19840.3; OPUNC01G19840.3; OPUNC01G19840.
DR HOGENOM; CLU_002227_1_1_1; -.
DR Proteomes; UP000026962; Chromosome 1.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR45922; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR PANTHER; PTHR45922:SF1; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR SUBUNIT 2; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 17..222
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 242..365
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
FT REGION 403..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 78191 MW; CA9704D302328C8B CRC64;
MGTSVQVTPL SGAYGEGPLC YLLAVDGFRF LLDCGWTDLC DPSHLQPLAK VAPTIDAVLL
SHADIMHLGA LPYAMKHLGL SAPVYATEPV FRLGILTLYD YFISRRQVSD FDLFTLDDID
AAFQNVVRLK YSQNHLLNDK GEGIVIAPHV AGHDLGGTVW KITKDGEDVV YAVDFNHRKE
RHLNGTALGS FVRPAVLITD AYNALNNHVY KRQQDQDFID ALVKILAGGG SVLLPIDTAG
RVLEILLILE QYWSQRHLIY PIYFLTNVST STVDYVKSFL EWMNDSISKS FEHTRDNAFL
LKCVTQIINK DELEKLGDAP KVVLASMASL EVGFSHDIFV DMANEAKNLV LFTEKGQFGT
LARMLQVDPP PKAVKVTMSK RIPLVGDELK AYEEEQERIK KEEALKASQN KEEEMKASLG
SNAKASDPMV IDASTSRKPS NAGSQFGGNV DILIDGFVPP SSSVAPMFPF FENTSEWDDF
GEVINPEDYL MKQEEMDNTL MPGAGDGMDS MLDEGSARLL LDSTPSKVIS NEMTVQVKCS
LAYMDFEGRS DGRSVKSVIA HVAPLKLIEE TIDVTSDLCA YKVQLSEKLM SNVISKKLGE
HEIAWVDAEV GKADDKLTLL PPSSTPAAHK SVLVGDLKLA DFKQFLANKG LQVEFAGGAL
RCGEYITLRK IGDAGQKGST GSQQIVIEGP LCEDYYKIRE LLYSQFYLL
//
