ID V4MSE7_EUTSA Unreviewed; 730 AA.
AC V4MSE7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Branchpoint-bridging protein {ECO:0000256|RuleBase:RU367126};
GN ORFNames=EUTSA_v10024523mg {ECO:0000313|EMBL:ESQ56203.1};
OS Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ56203.1, ECO:0000313|Proteomes:UP000030689};
RN [1] {ECO:0000313|EMBL:ESQ56203.1, ECO:0000313|Proteomes:UP000030689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA Mitchell-Olds T., Schumaker K.S., Wang X.;
RT "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL Front. Plant Sci. 4:46-46(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.
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; KI517384; ESQ56203.1; -; Genomic_DNA.
DR RefSeq; XP_006414750.1; XM_006414687.1.
DR AlphaFoldDB; V4MSE7; -.
DR STRING; 72664.V4MSE7; -.
DR EnsemblPlants; ESQ56203; ESQ56203; EUTSA_v10024523mg.
DR GeneID; 18029260; -.
DR Gramene; ESQ56203; ESQ56203; EUTSA_v10024523mg.
DR KEGG; eus:EUTSA_v10024523mg; -.
DR eggNOG; KOG0119; Eukaryota.
DR OMA; VTTPPWQ; -.
DR OrthoDB; 1397at2759; -.
DR Proteomes; UP000030689; 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; 3.30.70.330; -; 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; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
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; PF00076; RRM_1; 1.
DR Pfam; PF16275; SF1-HH; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00360; RRM; 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 SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
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:UP000030689};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
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 423..501
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..591
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 79866 MW; BBF638F49BBC4FA6 CRC64;
MDSVELNQYN HSSHALDNPP PSSEALDSST ASDQLNPQIP TSEFTRDLVS EKGVSKTMSG
TEKDQSGGEE ENTSRSRKRR SRWDSSPPKR KSRWADDEPK PIIQLPDFME FDPEVQVLNA
RLLEISRILQ SGLPLDDRQE GQRSPSPEPI YDNNGIRVNT REYRAKERLN RERQEIISQI
ISKNPAFKPP ADYRPPKLQK KLFIPKNEFP GYSFIGLIIG PRGNTQKRMQ RETGAKIVIR
GKGSVKEGRH QQKKFDPSEN EDLHVLVEAD TQESLDAAAG MIEKLLQPVD EVLNEHKRQQ
LRELATLNGT VRDEEFCRLC GEQGHRQYAC PSSATTFKSD VLCKICGDGG HPTIDCPVKG
NTGKNMDDEY KNFLAELGGT VPESSLKQSG TTLAIGPGSN PPWGNSAGLG SNPIKPSKEY
DETNLYIGFL PPMLDDDGLI NLFSSFGEIV MAKVIKDRES GLNRGYGFVK YADVQMANAA
IQAMNGYRLE GKTLAVRIAG KPPPPTSPQS RTQAYPPSNH LPGAYPSQQY PSGVRLPNPP
PPPVPSYYPY APPPGCYHPV AGQHMSPYGM HYPPPPPPHM AQAPPPGTAS QNPPSSESQQ
SFPPGVQPDK GAPASSVPPN VYVSSVTGLP GQPPYMSYPY YNAVRPPVPA SSTDLGNMTW
ANNPPVPTVD QSQGLGNAPW ASNPSMPTTD DYSQRMGSVP WAPKPPGQPS AENASAPGDS
EYDKFMAEVM
//
