ID A0A0R3PJB2_ANGCS Unreviewed; 655 AA.
AC A0A0R3PJB2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Branchpoint-bridging protein {ECO:0000256|RuleBase:RU367126};
GN ORFNames=ACOC_LOCUS4529 {ECO:0000313|EMBL:VDM56114.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000452801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000452801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM56114.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM56114.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UYYA01003819; VDM56114.1; -; Genomic_DNA.
DR STRING; 334426.A0A0R3PJB2; -.
DR WBParaSite; ACOC_0000452801-mRNA-1; ACOC_0000452801-mRNA-1; ACOC_0000452801.
DR OMA; TANTMDN; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
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; 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; 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:UP000267027};
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 456..471
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 504..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..99
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..634
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 71449 MW; 163B024C5F2AA5A0 CRC64;
MGSKTGGNTE PMPFVRKWGA AAAASGSDDN ATPTIVTTEP VSTSDHDNYS HSHRDRSRSR
SRDRKDRRRR RSRSGDRDRH KRRRSRSRRR SRSRERKRSR TRSRDRERDR VSPVAAPAHP
IGPPMIKEPL INPLMRPEVA LSGTDPVVGQ ETALMEAGRK RERKSRWSAT KSFVPGMPTI
LPSNLSDDQR TAYLLQLEIE DATRKLRLGD FLGSTDPAQR LVVKNGKALC SSVSGTNHTF
SAMHIWSPSP EPIYDSNGKR LNTREVRKRQ ELEQLRHEKI QALLKINPNF KPPADYRAPN
IRLHDKVWIP QDNHPELNFV GLLIGPRGNT LKSLEAETGA KIIIRGKGSV KEGKLGSRLG
PMPGENEPLH AYVTGTDQAT IKKACDKIRS IIAEATAIPD GQNELRKLQL RELALLNGTL
RPEDLVSGAR CSNCGSDEHK TWECPDAPNV TAKVVCMACG SAGHIARDCK NPRPGGADAT
GTADGGMDDE YSALMEELGE RPTRQADGSL RGRGGTVPFR GTRGTFFPRG ALNNQQPVIR
VNLGTAAQQQ NAMMNAGMVP PPPGTRPPYG MGPLPDPYQP HGFFSSPGAR GRGSFRGGWY
GSPSAMPLPV PPPPPPPIGG FPPPPPPPPP APQADLSRIL SAPAPPPPPP PPPQS
//
