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Database: UniProt
Entry: A0A3B3QYS6_9TELE
LinkDB: A0A3B3QYS6_9TELE
Original site: A0A3B3QYS6_9TELE 
ID   A0A3B3QYS6_9TELE        Unreviewed;       403 AA.
AC   A0A3B3QYS6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Splicing factor 45 {ECO:0000256|PIRNR:PIRNR031066};
DE   AltName: Full=RNA-binding motif protein 17 {ECO:0000256|PIRNR:PIRNR031066};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000011069.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000011069.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Splice factor that binds to the single-stranded 3'AG at the
CC       exon/intron border and promotes its utilization in the second catalytic
CC       step. Involved in the regulation of alternative splicing and the
CC       utilization of cryptic splice sites. {ECO:0000256|PIRNR:PIRNR031066}.
CC   -!- SUBUNIT: Associates with the spliceosome.
CC       {ECO:0000256|PIRNR:PIRNR031066}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR031066}.
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DR   AlphaFoldDB; A0A3B3QYS6; -.
DR   Ensembl; ENSPKIT00000035209.1; ENSPKIP00000011069.1; ENSPKIG00000025526.1.
DR   GeneTree; ENSGT00790000123099; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR   CDD; cd12647; RRM_UHM_SPF45; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR040052; RBM17.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   InterPro; IPR034653; SPF45_RRM.
DR   PANTHER; PTHR13288:SF8; SPLICING FACTOR 45; 1.
DR   PANTHER; PTHR13288; SPLICING FACTOR 45 SPF45; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF031066; Splicing_factor_SPF45; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00361; RRM_1; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   4: Predicted;
KW   mRNA processing {ECO:0000256|PIRNR:PIRNR031066};
KW   mRNA splicing {ECO:0000256|PIRNR:PIRNR031066};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR031066};
KW   RNA-binding {ECO:0000256|PIRNR:PIRNR031066};
KW   Spliceosome {ECO:0000256|PIRNR:PIRNR031066}.
FT   DOMAIN          239..279
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   REGION          38..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..144
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   403 AA;  45268 MW;  2C3432DD30E2D804 CRC64;
     MSLYDDLGVA TSDAKTEGWS KNFKLLQSQL QVKKAALTQA KSQRSKQATV LAPVIDLKRG
     NTSDDRQISD TPPHAATGLK DPAPGGFSSG DVLIPLADEY DPMFPNEYDK VVKRQREERQ
     RQREQERQKE IEEREKKRKD RQEGGVPSGF SSFPADGESD EEEDYEKERR KRAQMCTTTF
     NYVKDFFLVA EFATTYPYDD DGRPRTHSSK AAIPPPMYED SDRPRSPPGP TSSFLANMGG
     TVAHKIMQKY GFREGQGLGK HEQGLSTALS VEKTSKRGGK IIIGDLTEKG DSGKKPESNP
     LTEILKCPTK VVLLERDMTV DEDLEAETKE ECEKYGKVTK CVIFEISDTT DDEAVRIFLE
     FERVESAIKA VVDLNGRYFG GRVVKACFYT LDKFRVLDLG EQV
//
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