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Database: UniProt
Entry: V5I5B8_IXORI
LinkDB: V5I5B8_IXORI
Original site: V5I5B8_IXORI 
ID   V5I5B8_IXORI            Unreviewed;       498 AA.
AC   V5I5B8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Branchpoint-bridging protein {ECO:0000256|RuleBase:RU367126};
DE   Flags: Fragment;
OS   Ixodes ricinus (Common tick) (Acarus ricinus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB83953.1};
RN   [1] {ECO:0000313|EMBL:JAB83953.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB83953.1};
RX   PubMed=25765539;
RA   Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT   "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT   and midguts when blood feeding on the vertebrate host.";
RL   Sci. Rep. 5:9103-9103(2015).
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; GANP01000515; JAB83953.1; -; mRNA.
DR   AlphaFoldDB; V5I5B8; -.
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   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   CDD; cd22382; KH-I_SF1; 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; 1.
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   2: Evidence at transcript level;
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   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          369..385
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          395..410
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          1..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..115
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        460..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:JAB83953.1"
SQ   SEQUENCE   498 AA;  56051 MW;  00FB41B10825A343 CRC64;
     GKDRSRNRSR SRDRNRSRDK SRDKSRDKSR DKSRDRRDRD RDRDKDRERD RDRDKDRDRD
     KDRDRDKDRD RDKDRDREKE REPALPAMTA APPVVSMLPS WASQDENSNT SLGSQENSER
     RRKRRSRWCC DEKEKVFIPG MPTVLPTNLD PNQERAYLLQ LQIEELSRRL RTEDLGIPYN
     PEERSPSPEP IYNSAGKRLN TREYRVRKRL EDERHMHITE MFTINPDYKP PSDYKPPLIR
     VSEKVMIPQE EHPDINFVGL LIGPRGNTLK SLEKETGAKI IIRGKGSVKE GKVGRKDGQP
     LPGEDEPLHA FVTASNQDNV RKAVDRIKEI IRQGVEVPEG QNDLRRMQLR ELALLNGTLR
     ENDLLGGPRC SNCGAPGHKA WQCPDRPNIT NNVICACCGG TGHIARDCRE RGKGGGGGGG
     GRSREDKRDK SREEKRDKSP KPQRESGGET KPAAEKAAST PSGGATSSEA SSNGTAAASA
     PSASLDSSSS AVEGTVSA
//
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