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Database: UniProt
Entry: A0A0J7L1L9_LASNI
LinkDB: A0A0J7L1L9_LASNI
Original site: A0A0J7L1L9_LASNI 
ID   A0A0J7L1L9_LASNI        Unreviewed;       932 AA.
AC   A0A0J7L1L9;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Far upstream element-binding protein 1 {ECO:0000313|EMBL:KMQ96498.1};
GN   ORFNames=RF55_3211 {ECO:0000313|EMBL:KMQ96498.1};
OS   Lasius niger (Black garden ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Lasius; Lasius.
OX   NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ96498.1, ECO:0000313|Proteomes:UP000036403};
RN   [1] {ECO:0000313|EMBL:KMQ96498.1, ECO:0000313|Proteomes:UP000036403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:KMQ96498.1};
RA   Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT   "Lasius niger genome sequencing.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMQ96498.1}.
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DR   EMBL; LBMM01001331; KMQ96498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J7L1L9; -.
DR   STRING; 67767.A0A0J7L1L9; -.
DR   PaxDb; 67767-A0A0J7L1L9; -.
DR   OrthoDB; 1662at2759; -.
DR   Proteomes; UP000036403; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd22396; KH-I_FUBP_rpt1; 1.
DR   CDD; cd22397; KH-I_FUBP_rpt2; 1.
DR   CDD; cd22398; KH-I_FUBP_rpt3; 1.
DR   CDD; cd22399; KH-I_FUBP_rpt4; 1.
DR   CDD; cd07987; LPLAT_MGAT-like; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 4.
DR   InterPro; IPR015096; FUBP_C.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF09005; DUF1897; 2.
DR   Pfam; PF00013; KH_1; 4.
DR   SMART; SM00322; KH; 4.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 4.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000036403};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT   DOMAIN          294..364
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          393..464
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          496..567
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          612..683
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   REGION          272..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          708..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          760..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          851..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..292
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..815
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..887
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        898..932
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  101349 MW;  414471551384F461 CRC64;
     MHDIFILRML YLKVEEMRGI CSVLMDLNPN DSDDSRGYEI VGLENIPQDK PVLFIYYHGA
     IPIDLYYFTS KVFLFNSKLV HTVADRFLFN FPGFSIISDV LKVIPGTVQT CSAILKEGNM
     LSISPGGVYE AQFGDSYYEL MWKKRMGFAK VALDAKVSII PLFTRNIREA FRTVSWGRRM
     WLRIYTWIKF PLAPVYGGFP VKLVTYVGKP IPYDGNLTPE ELQLKIAAKI NPAGANNQDS
     KLKRPLEDSS EPEAKKMASL VADPLIGIRG GPTGSSIGDS GSQGSRPVSS SVGGICNEDI
     RVPDKMVGLI IGRGGEQITR LQSETGCKIQ MAPESGGLPE RVCTLTGSRE AVNRAKELVL
     SIVNQRSRSE GIGDMNMSSS SASTGSGGGM MGHPGFVEIM IPGPKVGLII GKGGETIKQL
     QEKSGAKMVV IQEGPSQEQE KPLRITGDPQ KVEYAKQLVY ELIAEKEMQM FHRGGRSTDR
     TGNYSNDSGF NHGPATSDGV EVLVPRAAVG VVIGKGGDMI KKIQAESGAK VQFQQGREDG
     PGDRKCLLSG KHQAVEQARQ RIQELIDSVM RRDDGRNNMG GRGGLRGNGF GGNRNPNEYG
     NWDRRQGGPM QDKIETTFTV PSSKCGIIIG KGGETIKQIN QQTGAHCELD RRNQSNENEK
     IFIIRGNPEQ VEHAKRIFSE KLGMGPAGSS YAGAQGAVGY NPNWNTGYQA WPSQPQSNDG
     SNANQAPVQV NPQTGQPDYS AQWAEYYRSL GMHREADMIE QQAKQGKQDH NQQGGNSQNQ
     SNPATTGSAG PSQQQQQQQQ TQQQQQAGAA QNGGQADYSV QWAEYYRSIG KIKEAEAIEA
     QMKAGKLGLQ GNQMAQQQMQ TLQGQSAGPP GTTPNAFPQT YGSYPTMNAG SAPGGYYAAN
     AGSNSQPQTG QQNPSFPTGY QNYPYSQTTS EN
//
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