ID A0A1S3M6X1_SALSA Unreviewed; 1239 AA.
AC A0A1S3M6X1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE RecName: Full=RNA-binding protein 47 {ECO:0000256|ARBA:ARBA00015191};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE AltName: Full=RNA-binding motif protein 47 {ECO:0000256|ARBA:ARBA00030579};
GN Name=LOC106570794 {ECO:0000313|RefSeq:XP_013998805.1,
GN ECO:0000313|RefSeq:XP_013998806.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013998805.1};
RN [1] {ECO:0000313|Proteomes:UP000087266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=double haploid {ECO:0000313|Proteomes:UP000087266};
RX PubMed=20887641;
RA Davidson W.S., Koop B.F., Jones S.J., Iturra P., Vidal R., Maass A.,
RA Jonassen I., Lien S., Omholt S.W.;
RT "Sequencing the genome of the Atlantic salmon (Salmo salar).";
RL Genome Biol. 11:403-403(2010).
RN [2] {ECO:0000313|RefSeq:XP_013998805.1, ECO:0000313|RefSeq:XP_013998806.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RBR family. RNF19 subfamily.
CC {ECO:0000256|ARBA:ARBA00061087}.
CC -!- SIMILARITY: Belongs to the RRM RBM47 family.
CC {ECO:0000256|ARBA:ARBA00005319}.
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DR RefSeq; XP_013998805.1; XM_014143330.1.
DR RefSeq; XP_013998806.1; XM_014143331.1.
DR KEGG; sasa:106570794; -.
DR Proteomes; UP000087266; Chromosome ssa14.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd20362; BRcat_RBR_RNF19A; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16775; RING-HC_RBR_RNF19A; 1.
DR CDD; cd12485; RRM1_RBM47; 1.
DR CDD; cd12491; RRM2_RBM47; 1.
DR FunFam; 3.30.70.330:FF:000022; APOBEC1 complementation factor isoform X1; 1.
DR FunFam; 3.30.70.330:FF:000026; APOBEC1 complementation factor isoform X1; 1.
DR FunFam; 1.20.120.1750:FF:000001; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 2.20.25.20:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.40.10:FF:000052; RBR-type E3 ubiquitin transferase; 1.
DR FunFam; 3.30.70.330:FF:000146; RNA-binding protein 47 isoform X1; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR047044; RBM47_RRM1.
DR InterPro; IPR034440; RBM47_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR NCBIfam; TIGR01648; hnRNP-R-Q; 1.
DR PANTHER; PTHR21245; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR PROSITE; PS50102; RRM; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 334..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..420
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..324
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 105..153
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 714..787
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 794..876
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 889..961
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..59
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..468
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..664
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1239 AA; 134084 MW; 8FE28DB3373228D6 CRC64;
MSLQQLRGDR GGSGSERDLH SAASSISLPS VRKAPKKRRL SLRSLFSRRH RGDRDHKRKS
QDLQGVGVDG IASVESIHSE ICHGDKTSTL SAPVAASSSS EFLECPLCLL RHSRDRFPDI
MTCHHRSCAD CLRQYLRIEI SESRVNISCP ECSERFNPHD IRIILGDQPL MEKYEEFMLR
RWLVADPDCR WCPAPDCGYA VIAFGCASCP KITCGREGCG TEFCYHCKQL WHPNQTCDAA
RQQRAQSLRL RTFRSSSLNY SQESGAAADD IKPCPRCAAY IIKMNDGSCN HMTCAVCGCE
FCWLCMKEIS DLHYLSPSGC TFWGKKPWSR KKKILWQLGT LVGAPVGIAL IAGIAIPAMI
IGIPVYVGRK IHNRYEGKDI SKHKRNLVIA GGVTLSVIVS PVVAAVTVGI GVPIMLAYVY
GVVPISLCRS GGCGVSAGNG KGVRIEFDDE NEMNVGSAAA ATDATSVAET RHNPSIGEGS
VGGMTGSLSA SGSHVDRMGA MRDNLSENAS TTALAGASIT GSLSGSTMGN FLNRLEVQAD
VQKERCSLSG ESATFSLGTV SDNASTKAMA GSILNYRDGT SMEVQVDIEP CKSGGQLHYH
SGISSTDDGR DAGRCSWSCP SGCPSEGQDG TASSSSSSSA MSNIPAPSGS IAPGPSHHSP
HGPITVPEGV SGAPNEAALV SLMGRTGYGM VQENGQRKYG PPPGWDSASP PRGCEIFVGK
IPRDVYEDEL VPVFESVGQI YEMRLMMDFD GKNRGYAFVM YTQKHQAKRA VRELNNYEVR
PGRLLGVCCS VDNCRLFIGG IPKTKKREEI LEEVSKVTEG VLDVIVYASA ADKMKNRGFA
FVEYESHRAA AMARRKLMPG RIQLWGHQIA VDWAEPEIDV DEDVMETVKI LYVRNLMMET
SEETLRQVFG QWNQGCVERV KKIRDYAFVH FSSRDDAVVA MDHLNGTEVE GSCIEVTLAK
PVDKEQYTRY QKASKGGATA ATAAPEPVQQ NYVYQCDPYT LTYYGYPYNT LIGPNRDYFI
KGGPMIQTNA GAVRGRGRAV TGSRAPGPRG SYLGGYSAGR GIYSRYHEGK AKGPDNKAYE
LLPSMELSAS VNPLGIKPCT MGLQALGGQY PVFQGAKLME EGKMHPAVEH LINPLTLQHD
HTAQTTVLPA VSTPPPYQGR PITPVYTMTH NMQRIPAAGG LYGGGYMPIT NYNAAALAAL
QKNAAAAAAA YGGYASYAVP QAFPGAAFQV PIHDVYQTY
//
