ID A0A182EXG5_ONCOC Unreviewed; 151 AA.
AC A0A182EXG5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=NOO_LOCUS12868 {ECO:0000313|EMBL:VDN00193.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t12868-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t12868-RA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t12868-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDN00193.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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}.
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DR EMBL; UYRW01012338; VDN00193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182EXG5; -.
DR STRING; 42157.A0A182EXG5; -.
DR WBParaSite; nOo.2.0.1.t12868-RA; nOo.2.0.1.t12868-RA; nOo.2.0.1.g12868.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; Unassembled WGS sequence.
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 InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
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; PF13299; CPSF100_C; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|RuleBase:RU365006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365006};
KW Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW RNA-binding {ECO:0000256|RuleBase:RU365006}.
FT DOMAIN 1..148
FT /note="Cleavage and polyadenylation specificity factor 2 C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF13299"
FT REGION 17..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 16979 MW; F1FF842C04A75FED CRC64;
VKDAELSWLD ARIVRRKTIT PGQTQNGDEE NPETNGNKEE VEEMEQDIEQ IEGKRLSSLK
VASADTFCLE PMLSANIPPH QAVFVNDPKL SDVKQLLTSN GFRAEFSSGV LYINNIASIR
RNEAGRFHVE GCACEDYYKI RDIVYAQFAV V
//
