BBP_CANAL
ID BBP_CANAL Reviewed; 455 AA.
AC Q5AED9; A0A1D8PJM2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Branchpoint-bridging protein;
GN Name=BBP; Synonyms=MSL5; OrderedLocusNames=CAALFM_C303300CA;
GN ORFNames=CaO19.329, CaO19.7961;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}.
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DR EMBL; CP017625; AOW28359.1; -; Genomic_DNA.
DR RefSeq; XP_720024.1; XM_714931.1.
DR AlphaFoldDB; Q5AED9; -.
DR SMR; Q5AED9; -.
DR STRING; 237561.Q5AED9; -.
DR PRIDE; Q5AED9; -.
DR GeneID; 3638361; -.
DR KEGG; cal:CAALFM_C303300CA; -.
DR CGD; CAL0000178990; orf19.7961.
DR VEuPathDB; FungiDB:C3_03300C_A; -.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_016864_1_0_1; -.
DR InParanoid; Q5AED9; -.
DR OrthoDB; 887669at2759; -.
DR PRO; PR:Q5AED9; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0000243; C:commitment complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR031150; BBP/SF1.
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; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR PANTHER; PTHR11208:SF45; PTHR11208:SF45; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16275; SF1-HH; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 3: Inferred from homology;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..455
FT /note="Branchpoint-bridging protein"
FT /id="PRO_0000256145"
FT DOMAIN 153..236
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 292..309
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..372
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 50078 MW; 6905857724197F1B CRC64;
MSNRGRQPSG PPPSRKRETK WSGKPKRYAN FGAQSFDTVI TGHLTQEQLD AYQRYFRIEE
ISNFLSVAKQ QHKSIVDVLP SAKVDETDHY KRDPSPPPKY DKNGNRTNTR ERRVTEALEK
ERHELVELAA SSIKNYMIPS NYRRPSRTVE RLYVPVKDYP DINFVGFLIG PRGNTLKKLQ
EDSGARLQIR GKGSVKEGKS SDGFGSSQTG TDIQDDLHVL ITADSPLKIS KAVKLVNEII
DKLIFSPQGM NFMKRDQLKE LAVLNGTLRE TKPFDPEAHE KKQQQQMDIT KIVCKICGNI
GHIARDCKQN NGKRPLDDNA ENEPTTINKK ARTDVPPPPP PPPPPAPPSS STEISKQVPP
PPPPPPPPAP SAAASGFATT ENYKQGLVPP PPPPPPPPPP PVRSALVNFE NNSKVLLTKE
KEESGSSELK NTGESSSSSS GVPPSPPPPS SNVPR
