ID A0A061DDL9_BABBI Unreviewed; 239 AA.
AC A0A061DDL9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=U2 splicing factor subunit, putative {ECO:0000313|EMBL:CDR97534.1};
GN ORFNames=BBBOND_0400260 {ECO:0000313|EMBL:CDR97534.1};
OS Babesia bigemina.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Babesiidae; Babesia.
OX NCBI_TaxID=5866 {ECO:0000313|EMBL:CDR97534.1, ECO:0000313|Proteomes:UP000033188};
RN [1] {ECO:0000313|Proteomes:UP000033188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bond {ECO:0000313|Proteomes:UP000033188};
RX PubMed=24799432; DOI=10.1093/nar/gku322;
RA Jackson A.P., Otto T.D., Darby A., Ramaprasad A., Xia D., Echaide I.E.,
RA Farber M., Gahlot S., Gamble J., Gupta D., Gupta Y., Jackson L.,
RA Malandrin L., Malas T.B., Moussa E., Nair M., Reid AJ., Sanders M.,
RA Sharma J., Tracey A., Quail M.A., Weir W., Wastling J.M., Hall N.,
RA Willadsen P., Lingelbach K., Shiels B., Tait A., Berriman M., Allred D.R.,
RA Pain A.;
RT "The evolutionary dynamics of variant antigen genes in Babesia reveal a
RT history of genomic innovation underlying host-parasite interaction.";
RL Nucleic Acids Res. 42:7113-7131(2014).
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DR EMBL; LK391710; CDR97534.1; -; Genomic_DNA.
DR RefSeq; XP_012769720.1; XM_012914266.1.
DR AlphaFoldDB; A0A061DDL9; -.
DR STRING; 5866.A0A061DDL9; -.
DR EnsemblProtists; CDR97534; CDR97534; BBBOND_0400260.
DR GeneID; 24566075; -.
DR KEGG; bbig:BBBOND_0400260; -.
DR VEuPathDB; PiroplasmaDB:BBBOND_0400260; -.
DR OMA; GGWEPTK; -.
DR OrthoDB; 1967949at2759; -.
DR Proteomes; UP000033188; Chromosome 4.
DR GO; GO:0089701; C:U2AF complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR CDD; cd12287; RRM_U2AF35_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR12620:SF8; U2 SMALL NUCLEAR RNA AUXILIARY FACTOR SMALL SUBUNIT; 1.
DR PANTHER; PTHR12620; U2 SNRNP AUXILIARY FACTOR, SMALL SUBUNIT; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 2.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000033188};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 12..40
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 72..147
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 149..176
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 12..40
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 149..176
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 192..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 28059 MW; 872EDF52A86CC5BA CRC64;
MAENLARIIG TEEDRVNCPF YWKIGACRHG DQCSRAHYKP SAAQTLVIRH MYQNPPVAIA
IAEGQMISDE LLDKAADHFE EFYEEVFLEL MKYGEIEDMV VCDNIGDHII GNVYVKYRDE
NSAAHAISML SGRFYGGKPI QCEYTPVTDF REARCRQFVE GQCRRGGYCN FMHIKHVPRS
VRRKLNERMY TEYPEYKRRS PRRSDGSASR DRPRRQSSQE RRNMIEMWNR EREAREAAK
//
