ID E6ZWG5_SPORE Unreviewed; 617 AA.
AC E6ZWG5;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Branchpoint-bridging protein {ECO:0000256|ARBA:ARBA00017984, ECO:0000256|RuleBase:RU367126};
GN ORFNames=sr16829 {ECO:0000313|EMBL:CBQ71572.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ71572.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ71572.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311445; CBQ71572.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZWG5; -.
DR EnsemblFungi; CBQ71572; CBQ71572; sr16829.
DR VEuPathDB; FungiDB:sr16829; -.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_016864_3_1_1; -.
DR OrthoDB; 1397at2759; -.
DR Proteomes; UP000008867; Chromosome 23.
DR GO; GO:0000243; C:commitment complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
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 Pfam; PF00098; zf-CCHC; 2.
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; 2.
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 365..380
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 390..405
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 617 AA; 65255 MW; 1B213ABF60BA9169 CRC64;
MSWRSNAQRT GMNAQPLQGA RRWGGGGGGD GPNDAPSGYA PPSDNYQPPR PYQSSYHQQQ
QQPSHPYSAA PPSSSNPRDA ALAAAAAVAA SIRIKRDRDA AGPPSTSYAG ASSSSSAALD
TSGADGGPRK RKSRWGDAND KLTIPTAIGA NVSAHELDKY AIQVRLDEIS RKLRSGDFIP
PDRERSPSPP PTYDNQGRRT NTREVRYRKK LEDERVALVD RQLKLDPNFR PPSDYHAIKR
NQRPTEKVYL PIKEFPEINF FGLLVGPRGN TLKTMERQSG AKISIRGKGS VKDGKGKGGD
EDEEEMHCVV AADDEAAVKK CIKLINQVIE TAASTPEGEN DHKRNQLREL AALNGTLRDD
ENQLCKNCGN KGHRAFECPE QRNWTAHIIC HRCGGQGHLA RDCTQGRGGS FGAGPSGPGA
PAGGGTGNRQ FDSEYASLMA ELGEPAAAGA AAGGASAVDG ANVPAVGADG KKIPPWRNPD
VWTQPGFGGP RGADPGRGGW GRGGYSNRGD RPNGGYNAPH QPYPHPNQAY AGYDQSAPAP
AGEQGAEAQQ DYSAEWAAYY AAQAAAGEAS AATATAAGGD GAAAGQVDYT KEWEEYYRMQ
AAAAAQDGSA YGAARAQ
//
