ID A0A067TG86_GALM3 Unreviewed; 493 AA.
AC A0A067TG86;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Branchpoint-bridging protein {ECO:0000256|ARBA:ARBA00017984, ECO:0000256|RuleBase:RU367126};
GN ORFNames=GALMADRAFT_244565 {ECO:0000313|EMBL:KDR78914.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR78914.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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.
CC {ECO:0000256|RuleBase:RU367126}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU367126}.
CC -!- SIMILARITY: Belongs to the BBP/SF1 family.
CC {ECO:0000256|ARBA:ARBA00010382, ECO:0000256|RuleBase:RU367126}.
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DR EMBL; KL142374; KDR78914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067TG86; -.
DR STRING; 685588.A0A067TG86; -.
DR HOGENOM; CLU_016864_3_1_1; -.
DR OrthoDB; 1397at2759; -.
DR Proteomes; UP000027222; Unassembled WGS sequence.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR CDD; cd02395; KH-I_BBP; 1.
DR Gene3D; 6.10.140.1790; -; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR045071; BBP-like.
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; IPR047086; SF1-HH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1.
DR PANTHER; PTHR11208:SF45; SPLICING FACTOR 1; 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; Eukaryotic type KH-domain (KH-domain type I); 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50158; ZF_CCHC; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367126};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU367126};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU367126};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367126};
KW Reference proteome {ECO:0000313|Proteomes:UP000027222};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW Spliceosome {ECO:0000256|RuleBase:RU367126};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367126};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00047}.
FT DOMAIN 317..332
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 342..355
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 54452 MW; 427E9CABD110D9D4 CRC64;
MWKPATRQIT GTNDVPLGQR RRFGPAPTDD APAPQLAQPS PSVYPRSQNQ DESPGKRGRD
ESPVNGDPKV DPNAPRKRRS RWGDAKTEIP GLPTAISAAG VSQAQLDNYA IHLRLEEINR
KLRLNDFIPP ERERSASPPP TYDAHGRRTN TREVRYRKKL EDERIKLVDR AMKNDPNFRP
PVEYHQQKRS QRPSDKVYIP VKEFPEINFF GLLVGPRGNS LKKMERESGA KISIRGKGSV
KEGKARPDQY ADDAEEDLHC LVLGDTDEKV AACVKMINKV IETAASTPEG QNDHKRNQLR
ELAALNGTLR DDENQICQNC GGVGHRKYDC PEQRNFTANI ICRVCGSAGH MARDCTVNKD
PNAQAVSISG PSPSLNRTGF DSEYASLMAE LGENAGSGDG GKTPWDAPNM GHDITAGGSN
IPPWRRPESW QQPVNNNQPQ GYRPPQAGYG AGYGTPTGYG TGGQWAGYPS TGGYQQPQDY
SNYATYYQGQ YAQ
//
