ID A0A3B6LVK1_WHEAT Unreviewed; 683 AA.
AC A0A3B6LVK1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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};
GN ORFNames=CFC21_074207 {ECO:0000313|EMBL:KAF7068443.1}, CFC21_074208
GN {ECO:0000313|EMBL:KAF7068448.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5B02G462500.3};
RN [1] {ECO:0000313|EMBL:KAF7068443.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7068443.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5B02G462500.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5B02G462500.3};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5B02G462500.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7068443.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7068443.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM022224; KAF7068443.1; -; Genomic_DNA.
DR EMBL; CM022224; KAF7068448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6LVK1; -.
DR EnsemblPlants; TraesCS5B02G462500.3; TraesCS5B02G462500.3; TraesCS5B02G462500.
DR Gramene; TraesCS5B02G462500.3; TraesCS5B02G462500.3; TraesCS5B02G462500.
DR Gramene; TraesCS5B03G1135000.2; TraesCS5B03G1135000.2.CDS; TraesCS5B03G1135000.
DR Proteomes; UP000019116; Chromosome 5B.
DR Proteomes; UP000815260; Chromosome 5B.
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 InterPro; IPR011108; RMMBL.
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 Pfam; PF07521; RMMBL; 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:UP000019116};
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 415..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 75671 MW; 8CA7D7F1C3EFF480 CRC64;
MGTSVQVMPL SGAYGEGPLC YLLAVDGFRF LLDCGWTDHC DPALLQPLAR VAPTIDAVLL
SHPDMMHLGA LPYAIKHLGL SAPVYATEPV FRLGLLTMYD YFLSRWQVAD FDLFSLDDID
AAFQNVVRLK YSQNHLLNDK GEGIVIAPHV SGHLLGGTVW KITKDGEDVV YAVDFNHRKE
RHLNGTTLGS FVRPAVLITD AYNALNNQVY KRQQDQDFID SMLKVLSSGG SVLLPVDTAG
RVLELLLIME QYWAQRHLDY PIYFLTNVST STVDFVKSFL EWMSDSISKS FEHTRDNAFL
LRHVSLIINK EELEKLGDAP KVVLASMSSL EVGFSHDIFV EMANEAKNLV LFTEKGQFGT
LARMLQVDPP PKAVKVTMSK RVPLVGDELK AYEEEQERIK KEEVLKASIS KEKELKASHE
SNAKASDPMV VDASSSRKSS NAGSHVGGSV DILIDGFVSP VTSIAPMFPF FENTADWDDF
GEVINPDDYM MKQDEMDSNM MLGAGDGMDG KLDESSARLL LDSAPSKVIS NEMTVQVKCS
LAYMDFEGRS DGRSVKSVIA HVAPLKLVLV HGSAEATEHL KMHCAKNSDL HVYAPQIEET
IDVTSDLCAY KVQLSEKLMS NVISKKVEFA GGALRCGEYI TVRKIGDSNQ KGSTGSQQIV
VEGPLCEDYY KIRELLYSQF FLL
//
