ID   BBP_ASHGO               Reviewed;         507 AA.
AC   Q750X2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Branchpoint-bridging protein;
GN   Name=BBP; OrderedLocusNames=AGL183C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 235; 245 AND 252.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(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; AE016820; AAS54308.2; -; Genomic_DNA.
DR   RefSeq; NP_986484.2; NM_211546.2.
DR   AlphaFoldDB; Q750X2; -.
DR   SMR; Q750X2; -.
DR   STRING; 33169.AAS54308; -.
DR   EnsemblFungi; AAS54308; AAS54308; AGOS_AGL183C.
DR   GeneID; 4622777; -.
DR   KEGG; ago:AGOS_AGL183C; -.
DR   eggNOG; KOG0119; Eukaryota.
DR   HOGENOM; CLU_016864_5_1_1; -.
DR   InParanoid; Q750X2; -.
DR   OMA; HYNSNTH; -.
DR   Proteomes; UP000000591; Chromosome VII.
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; 2.
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   Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..507
FT                   /note="Branchpoint-bridging protein"
FT                   /id="PRO_0000256143"
FT   DOMAIN          154..220
FT                   /note="KH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   ZN_FING         272..289
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   ZN_FING         297..314
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          84..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..426
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..507
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  54384 MW;  AFF8486AC26E6A6F CRC64;
     MTRLVWFCMQ VAYCLHGWDW DIMDRGRSSN SYDSLWGGKA RDNPIVSQLP LQYRIRSALT
     QEQQTAYQVM YRIQEITIKL RTNDLNPPTS RYRSLSPPPV YDSQGKRTNT REHRYRKKLE
     EERHRLVEIA LKMIPHFIAP DDYRRPSKFQ DKYYIPINDY PEINFVGLLL GPRGNTLKQL
     QQQSGCKIVI RGRGSVKEGK AATDLPKGAM NMNEPLHCVI SADTEEKIPL GINAVESIII
     KAITSPEGQN DLKRGQLREL AVLNGTLRED NRPCPLCGEQ GHKKWECSSN PSLSMTVICQ
     RCNQPGHAAR DCTSPLNEFG KRTSDGPEFR ETKKLQQDAP PPSGPVGSHP SAPGSGSANS
     GVAPASLHPP GTMAPPGALP PPGSLAAPGT LPPPAALPAP AAPGTLPPPV ALPAPATLPQ
     AGVPPAPDAS PAVKTAVPIE GPPAPPQTAP PLRQTAATAS SAGSSQSAQE EPENARNGVE
     KAAPGPPAAV LPPPPPPPPP PPPPPSS