BBP_DEBHA
ID BBP_DEBHA Reviewed; 518 AA.
AC Q6BSP4; B5RTE6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Branchpoint-bridging protein;
GN Name=BBP; OrderedLocusNames=DEHA2D07238g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAR65631.1; -; Genomic_DNA.
DR RefSeq; XP_002770275.1; XM_002770229.1.
DR AlphaFoldDB; Q6BSP4; -.
DR SMR; Q6BSP4; -.
DR STRING; 4959.XP_002770275.1; -.
DR PRIDE; Q6BSP4; -.
DR EnsemblFungi; CAR65631; CAR65631; DEHA2D07238g.
DR GeneID; 8998483; -.
DR KEGG; dha:DEHA2D07238g; -.
DR VEuPathDB; FungiDB:DEHA2D07238g; -.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_016864_1_1_1; -.
DR InParanoid; Q6BSP4; -.
DR OMA; HYNSNTH; -.
DR OrthoDB; 887669at2759; -.
DR Proteomes; UP000000599; Chromosome D.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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 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..518
FT /note="Branchpoint-bridging protein"
FT /id="PRO_0000256148"
FT DOMAIN 167..233
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 319..336
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..518
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 56119 MW; F5832BCD6FEBB80B CRC64;
MSAYSRRYTD GPSNYGQDVR GRSEKKVEAS HTTKWSGTPS RHKKIGKEDF DTIVTGHLTQ
EQMDAYQQYF RIEEISDILR MASESQSEVL SLLPSGNIAN NPNYEREPSP PPKYDAAGNR
SNTREARTKL ALEKERHYLV EVAAGSIKNY MSPIDYRKPV KTYEKIYIPV KDYPDINFVG
LLLGPRGNTL RQLQEDSGAR LAIRGKGSVK DGKSTSSNND DDDSNSSLSF SNPNLNSSGN
DDLHVVITSD SQSKIAKAIK LTNQVIEKAI SSPVGQNDLK RGQLRELAIL NGTLRETKPY
NPETQQSRRS RPGLDVSQLV CKSCGKVGHF ARDCKFRGTS DGNNNPIVQD QADSYQQTAP
YSDSRRQREE EDPRNNGREE ILPPWKKKKP NVPLPPWQKP QQPLPSTDAP PPPVGLAPPP
SSLAPPPPPP SSLAPPPPPP PSSLAPPPPP SSDIAPPPPS SDRAPPPPPS GIAPPPPPSG
IAPPPPKSPN GVAPPPPPAN DAPPAPSSTK NPPPPPPA
