BBP_YARLI
ID BBP_YARLI Reviewed; 605 AA.
AC Q6C187;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Branchpoint-bridging protein;
GN Name=BBP; OrderedLocusNames=YALI0F18370g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382132; CAG78384.1; -; Genomic_DNA.
DR RefSeq; XP_505575.1; XM_505575.1.
DR AlphaFoldDB; Q6C187; -.
DR SMR; Q6C187; -.
DR STRING; 4952.CAG78384; -.
DR EnsemblFungi; CAG78384; CAG78384; YALI0_F18370g.
DR GeneID; 2907809; -.
DR KEGG; yli:YALI0F18370g; -.
DR VEuPathDB; FungiDB:YALI0_F18370g; -.
DR HOGENOM; CLU_016864_1_1_1; -.
DR InParanoid; Q6C187; -.
DR OMA; ENADREY; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
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..605
FT /note="Branchpoint-bridging protein"
FT /id="PRO_0000256152"
FT DOMAIN 184..264
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 328..345
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 67189 MW; 81609D2CF2EDFC59 CRC64;
MSSTYSSIQR HRKDTSSSGS NTTPLARRRR FDEGPADPGS APHLDSFVVP PTRHDDGTKR
QPGRRKQRWS HGENKVADLL QMPTALTGHL TPEQAEAYAI YYRIEEISQQ LRLGDIVPPE
DERSPSPPPQ YDSMGKRTNT RDARYTRQLE EERHRLIERA QRLIPNYRPP VDYHKPAKTQ
EVVYIPVNEY PDINFIGQLL GARGKTLKKM EQESGAKICI RGRGSVKQGK GRTDIPFQST
AEDDLHCLII SEDEEKIARA VQLVQQVIDT AASVPEGQNE LKRSQLRELA ALNGTLRDDE
NYGGAPQSSS GDEMDDRNKR RNNFMSSIVC HICGSKGHFA RDCLEKGTNA GTSENADREY
DALMRELQGE GVIDTASQQQ SIAQNPNTNN VSKLPPAVTG SNAAPINMRK PMSERGGSFD
RFDRGGFNQS NQREPQQQSH QQNMHNTNGN NYDRYDRNFN NSSNSSPELP PWHRPTPPSQ
PAAPPWLRRD NYKKHDKVSV QQSMQQSPWN RDTRQHQHQH QPPVHHQSMF NNNQSPIGPP
GMSSSGFGGY GGAPAGVPGM SVPPGPPGLS KVPPPPPPPG VPGMDGDQPI RHPPPPPPGV
IGPPK
