ID J4DPU0_THEOR Unreviewed; 242 AA.
AC J4DPU0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=U2 snRNP auxiliary factor {ECO:0000313|EMBL:BAM41289.1};
GN ORFNames=TOT_030000552 {ECO:0000313|EMBL:BAM41289.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM41289.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM41289.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM41289.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
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DR EMBL; AP011948; BAM41289.1; -; Genomic_DNA.
DR RefSeq; XP_009691590.1; XM_009693295.1.
DR AlphaFoldDB; J4DPU0; -.
DR STRING; 869250.J4DPU0; -.
DR EnsemblProtists; BAM41289; BAM41289; TOT_030000552.
DR GeneID; 20715722; -.
DR KEGG; tot:TOT_030000552; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000552; -.
DR eggNOG; KOG2202; Eukaryota.
DR OrthoDB; 1967949at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
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; 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:UP000003786};
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 194..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 28436 MW; 60513EC8EB609EFE CRC64;
MAEHLARIIG TEEDRVNCPF FWKIGACRHG DQCSRTHYKP SAAQTLVIRH MYQNPPVAIA
IAEGQMISDE LLDKAADHFE EFFEEVFLEL MKYGEIEDMV VCDNIGDHII GNVYIKYTDE
SAACRAVTSL SGRYYGGRPI QCEYTPVTDF REARCRQFVE GQCRRGGYCN FMHIKHVPRS
LRRKLMKRMY EEFPEYKRRS PRGSHRNRSR SPQRPKRQTS EERRDMIEQW NREREAKTAG
DN
//
