ID F0W3F8_9STRA Unreviewed; 610 AA.
AC F0W3F8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Branchpoint-bridging protein {ECO:0000256|RuleBase:RU367126};
GN Name=AlNc14C13G1526 {ECO:0000313|EMBL:CCA15601.1};
GN Synonyms=AlNc14C20G2114 {ECO:0000313|EMBL:CCA16339.1};
GN ORFNames=ALNC14_017440 {ECO:0000313|EMBL:CCA15601.1}, ALNC14_024820
GN {ECO:0000313|EMBL:CCA16339.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA15601.1};
RN [1] {ECO:0000313|EMBL:CCA15601.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA15601.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. Has a role in the
CC recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract
CC and the 3'-splice site at the 3'-end of introns.
CC {ECO:0000256|RuleBase:RU367126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU367126}.
CC -!- SIMILARITY: Belongs to the BBP/SF1 family.
CC {ECO:0000256|ARBA:ARBA00010382, ECO:0000256|RuleBase:RU367126}.
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DR EMBL; FR824058; CCA15601.1; -; Genomic_DNA.
DR EMBL; FR824065; CCA16339.1; -; Genomic_DNA.
DR AlphaFoldDB; F0W3F8; -.
DR EnsemblProtists; CCA15601; CCA15601; ALNC14_017440.
DR EnsemblProtists; CCA16339; CCA16339; ALNC14_024820.
DR HOGENOM; CLU_016864_4_0_1; -.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR CDD; cd02395; KH-I_BBP; 1.
DR Gene3D; 6.10.140.1790; -; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032570; SF1-HH.
DR InterPro; IPR047086; SF1-HH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1.
DR PANTHER; PTHR11208:SF45; SPLICING FACTOR 1; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16275; SF1-HH; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367126};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU367126};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU367126};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367126};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW Spliceosome {ECO:0000256|RuleBase:RU367126};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367126};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 387..402
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 18..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 67977 MW; 5C0EDAD45716DF4C CRC64;
MADESNGFDA FMAFVDGNGK TEDRRNETTT VKYDESHSST QKDVIDEEEA KEREVMMKAY
HPSLKQWFRE NPDLVEKYGE YPVFWQELKE WKPYRDVLKA YLKVTEGGNS RTSDLKVEEQ
DSSKVTSENT STQEASRRRR KSRWGDPIDE SGTTGEETKR KKSRWAPTGV NLGLAALNNN
AHETIKLRAK LDLINQKLTT VAIDAVILEK DPNRSPSPPP QYDSNGKRVN TREVRMRESL
ERARQVVVEE LVRINPLFKP PADYMRQKLN RKIYIPIKQF PNYNFIGLII GPRGNTQKRM
ERETNCKIAI RGRGSIKEGS KGKKLNADDN DDLHVLITGD RDDELDRAAR EIQSLLVPVD
DTKNSHKQKQ LRELALINGT LRDDDFCHIC GEKGHRQWEC PNREQTFKPV SVKCAICGDA
SHPTRDCTQK KKTADEAAAI DKEYMSFMQQ LGEKSVISSA DKTVETAPWL QPVKSANNAQ
SWMTSQTSGA PGTISAPPGT ESTAAPVMNA AGAAFPAPGL TPATAFPPPG STPATAFPPP
VAPTMHDYSQ MQAWNAQQWP GYYYAGWTGA PTAAECQYVA YGGLAAQAAP IPVMDPAQYP
QQPTGTGPNQ
//
