ID E3RSZ7_PYRTT Unreviewed; 533 AA.
AC E3RSZ7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Branchpoint-bridging protein {ECO:0000256|ARBA:ARBA00017984, ECO:0000256|RuleBase:RU367126};
DE Flags: Fragment;
GN ORFNames=PTT_12092 {ECO:0000313|EMBL:EFQ91162.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ91162.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91162.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL534918; EFQ91162.1; -; Genomic_DNA.
DR RefSeq; XP_003300752.1; XM_003300704.1.
DR AlphaFoldDB; E3RSZ7; -.
DR STRING; 861557.E3RSZ7; -.
DR EnsemblFungi; EFQ91162; EFQ91162; PTT_12092.
DR KEGG; pte:PTT_12092; -.
DR eggNOG; KOG0119; Eukaryota.
DR HOGENOM; CLU_016864_3_0_1; -.
DR OrthoDB; 1397at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0000243; C:commitment complex; IEA:EnsemblFungi.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0071004; C:U2-type prespliceosome; IEA:EnsemblFungi.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000001067};
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 303..318
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 328..343
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 249..301
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 533
FT /evidence="ECO:0000313|EMBL:EFQ91162.1"
SQ SEQUENCE 533 AA; 57162 MW; 36E11A8B9AEA8A90 CRC64;
MSWRNQGITG SNNIPLGTRR RFGGENDDGG YNPAAPAEGL SELKRGRSPE RTSSTDGPRQ
RKKRNRWGDV KDNKAAGLMG LPTHIQAPMT TEQLDAYTLY LRIEEISQKL KINDVVPADG
DRSPSPPPQY DNFGRRVNTR EFRYRKRLED ERHKLVEKAM KTLPNYHPPA DYRRPTKTQE
KVYVPVNDYP EINFIGLLIG PRGNTLKKME TESQAKIAIR GKGSVKEGKG RSDAAHTSNQ
EEDLHCLIMA DTEEKVNKAK KLIHNVIETA ASIPEGQNEL KRNQLRELAA LNGTLRDDEN
QACQNCGEIG HRKYDCPQKQ NFTASIICRV CGQAGHMARD CPERKVGQPW RNDNRFGDRG
QPGQGRIGGA PENELDAFMA EMGGTAGAPR AAIEYSGNGG AGGDNYGAGE RTVKPWERGP
TGGAAPWARN DDDRGRGDSN SAAPPPWAGG GGGRGGQSYD QGYGAGNGAA PWASAAPAAP
AAAGYGYGGY GYDQSASAGA PGAYAGAPGY GAPPPPAGPP PGLGPLFQSY GAA
//
