ID   SLU7_CHICK              Reviewed;         564 AA.
AC   Q5ZIG2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Pre-mRNA-splicing factor SLU7;
GN   Name=SLU7; ORFNames=RCJMB04_26j3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC       spliceosome. Participates in the second catalytic step of pre-mRNA
CC       splicing, when the free hydroxyl group of exon I attacks the 3'-splice
CC       site to generate spliced mRNA and the excised lariat intron. Required
CC       for holding exon 1 properly in the spliceosome and for correct AG
CC       identification when more than one possible AG exists in 3'-splicing
CC       site region. May be involved in the activation of proximal AG. Probably
CC       also involved in alternative splicing regulation.
CC       {ECO:0000250|UniProtKB:O95391}.
CC   -!- SUBUNIT: Component of pre-catalytic, catalytic and post-catalytic
CC       spliceosomes. Associates with the spliceosome prior to recognition of
CC       the 3'-splice site for step II, probably during catalysis of step I.
CC       {ECO:0000250|UniProtKB:O95391}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95391}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:O95391}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O95391}. Note=Predominantly nuclear.
CC       {ECO:0000250|UniProtKB:O95391}.
CC   -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
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DR   EMBL; AJ720822; CAG32481.1; -; mRNA.
DR   RefSeq; NP_001006146.1; NM_001006146.1.
DR   AlphaFoldDB; Q5ZIG2; -.
DR   SMR; Q5ZIG2; -.
DR   STRING; 9031.ENSGALP00000002277; -.
DR   PaxDb; Q5ZIG2; -.
DR   PRIDE; Q5ZIG2; -.
DR   GeneID; 416157; -.
DR   KEGG; gga:416157; -.
DR   CTD; 10569; -.
DR   VEuPathDB; HostDB:geneid_416157; -.
DR   eggNOG; KOG2560; Eukaryota.
DR   InParanoid; Q5ZIG2; -.
DR   OrthoDB; 816947at2759; -.
DR   PhylomeDB; Q5ZIG2; -.
DR   PRO; PR:Q5ZIG2; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR   InterPro; IPR021715; Slu7_dom.
DR   InterPro; IPR039974; Splicing_factor_SLU7.
DR   PANTHER; PTHR12942; PTHR12942; 1.
DR   Pfam; PF11708; Slu7; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Reference proteome; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN           1..564
FT                   /note="Pre-mRNA-splicing factor SLU7"
FT                   /id="PRO_0000289198"
FT   ZN_FING         116..133
FT                   /note="CCHC-type"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..219
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..507
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  65364 MW;  E0131594AB8C2CAA CRC64;
     MASGTAVNAA PSGGPGDVSL EEPKKMTRED WRKKKELEEQ RKLGNAPAEV DEEGKDINPH
     IPQYISSVPW YIDPSKRPTL KHQRPQPEKQ KQYSSSGDWY KRGVKEHSIA TRYRKGACEN
     CGALTHKKKD CMERPRKVGA KYTGMNIAPD EHVQPQLMFD YDGKRDRWNG YNPEEHMKIV
     EEYAKVDLAK RTLKAQKLQE ELASGKLEQV ERDHNSEDED EDKYADDIDM PGQNFDSKRR
     ITVRNLRIRE DIAKYLRNLD PNSAYYDPKT RAMRENPYAN TGKNPDEVGY AGDNFVRYTG
     DTISMAQTQL FAWEAYDKGS EVHLQADPTK LELLYKSFKV KKEDFKAQQK ESILEKYGGQ
     EHLDAPPAEL LLAQTEDYVE YSRHGTVIKG QEKAIACSKN EEDVKINNHT CIWGSYWKEG
     KWGYKCCHSF VKFSYCTGEA GKEIANAEAN LLEEQPREEE HMTKPKTLME IHQEKQKEKK
     KKKHKKSSNS DSEGEEKKKQ EKLKKALNAE EARLLQVKEI MQLDERKRPY NSVYETREPT
     EEEMEAYRMK RQRPDDPMAS FLGQ