BBP_ASPFU
ID BBP_ASPFU Reviewed; 566 AA.
AC Q4WXV6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Branchpoint-bridging protein;
GN Name=bbp; ORFNames=AFUA_3G10840;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000002; EAL92497.1; -; Genomic_DNA.
DR RefSeq; XP_754535.1; XM_749442.1.
DR AlphaFoldDB; Q4WXV6; -.
DR SMR; Q4WXV6; -.
DR STRING; 746128.CADAFUBP00003751; -.
DR EnsemblFungi; EAL92497; EAL92497; AFUA_3G10840.
DR GeneID; 3511814; -.
DR KEGG; afm:AFUA_3G10840; -.
DR VEuPathDB; FungiDB:Afu3g10840; -.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_016864_3_0_1; -.
DR InParanoid; Q4WXV6; -.
DR OMA; GAAPWHQ; -.
DR OrthoDB; 887669at2759; -.
DR Proteomes; UP000002530; 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:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
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; 2.
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; 2.
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..566
FT /note="Branchpoint-bridging protein"
FT /id="PRO_0000256144"
FT DOMAIN 186..266
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 304..321
FT /note="CCHC-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT ZN_FING 329..346
FT /note="CCHC-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 566 AA; 61069 MW; A506A6D018D15F25 CRC64;
MAWRNQGITG SNNIPLGRRR FGGEDGPEEE SRTATPASVG GDNGIKRGRS PVRADPPADG
VKRRKKRNRW GDAQENKAAG LMGLPTMIMA NFTNEQLEAY TLHLRIEEIS QKLRINDVVP
ADGDRSPSPP PQYDNFGRRV NTREYRYRKR LEDERHKLVE KAMKTIPNYH PPSDYRRPTK
TQEKVYVPVN DYPEINFIGL LIGPRGNTLK KMEAESGAKI AIRGKGSVKE GKGRSDAAHA
SNQEEDLHCL IMADTEEKVN KAKKLVHNVI ETAASIPEGQ NELKRNQLRE LAALNGTLRD
DENQACQNCG QIGHRKYDCP EQRNFTANII CRVCGNAGHM ARDCPDRQRG SDWRNGGGYG
GGRRAIGQGD AVDREMEQLM QELSGGAPGP DGQPPRRIEA GPDHGYDDRD VKPWQRGPPP
SDVAPWQQRG RDNRSRDDYG SRDQGSAPPW AAQSRGGDYG YGSHAGGYGA PGAGAATSGA
APWHQQAPPP PPGGASAYGY GAYPGYGAAV PGMGAPGAPP GLSVPPPPPG MPSMYYGSGS
PPPPPPGEGP PPPPPSELPP PPPPSA
