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Database: UniProt
Entry: A0A1L7XMI0_9HELO
LinkDB: A0A1L7XMI0_9HELO
Original site: A0A1L7XMI0_9HELO 
ID   A0A1L7XMI0_9HELO        Unreviewed;       623 AA.
AC   A0A1L7XMI0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Branchpoint-bridging protein {ECO:0000256|ARBA:ARBA00017984, ECO:0000256|RuleBase:RU367126};
GN   ORFNames=PAC_16129 {ECO:0000313|EMBL:CZR66228.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR66228.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR66228.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR66228.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJOG01000035; CZR66228.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7XMI0; -.
DR   STRING; 576137.A0A1L7XMI0; -.
DR   OrthoDB; 1397at2759; -.
DR   Proteomes; UP000184330; 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:UP000184330};
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          322..337
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          347..362
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          381..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..623
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  67067 MW;  516CC94B4F048A40 CRC64;
     MAWRQQGSTG SNNIPLGNKR RFGGGDTESP RGENDYQVAF SDGPVKRGRS PIKEERLDDG
     SRRRKKRNRW GDATDNKAAG LMGLPTAIMA NMTSEQLEAY TLHLRIEEIS QKLRIDDVVP
     ADGDRSPSPP PQYDNFGRRV NTREYRYRKR LEDERHKLIE KAMKVIPNYH PPQDYRRPTK
     TQEKVYVPVN DYPEINFIGL LIGPRGNTLK KMETESGAKI AIRGKGSVKE GKGRSDAAHT
     SNQEEDLHCL IMADTEEKVN KAKKLIHNII ETVRNPFQPV YRILLTYQAA SIPEGQNELK
     RNQLRELAAL NGTLRDDENQ ACQNCGQIGH RKYDCPEQRN FTANIICRVC GNAGHMARDC
     PDRYENYQYS RGRMLMFGRQ RGANWRNDGP GGPPGPAAGR IGAGDAVDRE YEQLMQELSG
     GGPANGEAPR RIESGPAGGF DQGAGEDVKP WQRGPTGAAA PWQKRGDDRG FDSRDSAPSG
     GAAPWARDRR GGDNRGGDSY GGYGAQNGGF NAPSGPSGGN AAPWAQQPPA YPAAAAGAGA
     AGYGGYAAPG YTGGYPAQQA MGAPPGLAAP PGLSGAGLSA LLQQFAGSPP PPPPTSSIPP
     PPPGSAPPPP PPSDQPPPPP PGN
//
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