ID A0A091D7M7_FUKDA Unreviewed; 802 AA.
AC A0A091D7M7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Fragile X mental retardation syndrome-related protein 2 {ECO:0000313|EMBL:KFO18841.1};
GN ORFNames=H920_19745 {ECO:0000313|EMBL:KFO18841.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18841.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18841.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18841.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule
CC {ECO:0000256|ARBA:ARBA00004331}. Postsynapse
CC {ECO:0000256|ARBA:ARBA00034110}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- SIMILARITY: Belongs to the FMR1 family.
CC {ECO:0000256|ARBA:ARBA00006633}.
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DR EMBL; KN125302; KFO18841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091D7M7; -.
DR STRING; 885580.ENSFDAP00000004091; -.
DR eggNOG; ENOG502QPKJ; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0006417; P:regulation of translation; IEA:InterPro.
DR CDD; cd22505; KH_I_FXR2_rpt1; 1.
DR CDD; cd22508; KH_I_FXR2_rpt2; 1.
DR CDD; cd22511; KH_I_FXR2_rpt3; 1.
DR CDD; cd04301; NAT_SF; 1.
DR CDD; cd20476; Tudor_Agenet_FXR2_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR022034; FMR1-like_C_core.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR032172; FXR1_C1.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR047422; KH_I_FXR2_rpt1.
DR InterPro; IPR047424; KH_I_FXR2_rpt2.
DR InterPro; IPR047420; Tudor_Agenet_FXR2_rpt2.
DR InterPro; IPR041560; Tudor_FRM1.
DR PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1.
DR PANTHER; PTHR10603:SF3; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN 2; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF05641; Agenet; 1.
DR Pfam; PF12235; FXMRP1_C_core; 1.
DR Pfam; PF16096; FXR_C1; 1.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF17904; KH_9; 1.
DR Pfam; PF18336; Tudor_FRX1; 1.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR PROSITE; PS51641; AGENET_LIKE; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 19..174
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT DOMAIN 203..255
FT /note="Agenet-like"
FT /evidence="ECO:0000259|PROSITE:PS51641"
FT REGION 519..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89521 MW; 09D2B46BC2E7B875 CRC64;
MAFVHIRAAK EGDCGDLMRL IRVKKTSELA EFEKLSDEVK ISEEDLRAHG FGENPSYHCL
VAEILPAPGE RQGPRIVGYG LYFFIYSTWK GRNVYLEDIY VMPEYRGQGI GSKIIKKVAE
VALDQGCSHF RLAVLEWNTR AIDFYKTLGA QDLTQAEGWH AFRFEEEAMR KLAGSWQSER
QIPFGDVRLP PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD FYVIEYAACD
ATYNEIVTLE RLRPVNPSPL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF
LNITNSELFI LSTTEGPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ
EEFTVREDLM GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE
FSEDSVQVPR NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT
RENISNAQAL LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG GGNDKTGYTT
DESSSSSLHT TRTYGGSYGG RGRGRRTGGS AYGPNSDPST ASETESEKRE EPNRAGPGDR
DPPTRGEESR RRLIGGRGRG PPPTTRPTSR YNSSSISSVL KDPDSNPYSL LDTSEPEPPV
DSEPGEPPPA SARRRRSRRR RTDEDRTIMD GGLESDGPNM TENGLEEESR PQRRNRSRRR
RNRGNRTDGS VSTDRQPVTV ADYISRAESQ SRQRPPLERA KPSEDSLSVQ KGDSVSKLPK
GPSENGELST PLELGSLVNG VS
//
