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Database: UniProt
Entry: A0A2A3EE38_APICC
LinkDB: A0A2A3EE38_APICC
Original site: A0A2A3EE38_APICC 
ID   A0A2A3EE38_APICC        Unreviewed;       459 AA.
AC   A0A2A3EE38;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Tudor and KH domain-containing protein {ECO:0000313|EMBL:PBC29489.1};
GN   ORFNames=APICC_06607 {ECO:0000313|EMBL:PBC29489.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC29489.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC29489.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC29489.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KZ288285; PBC29489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EE38; -.
DR   STRING; 94128.A0A2A3EE38; -.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR   CDD; cd22398; KH-I_FUBP_rpt3; 1.
DR   Gene3D; 2.40.50.90; -; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 2.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   PANTHER; PTHR22948:SF75; FI20010P1; 1.
DR   PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00322; KH; 2.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
DR   PROSITE; PS50304; TUDOR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242457};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          293..352
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          199..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   459 AA;  51532 MW;  9BC3CE404D2FC84B CRC64;
     MRWMTRQFSL PILLGISLTS VSIAILYVLY KKDEEDIKSR KNHVEISKRF TAECKVPRQF
     VPAVIGRGGS MIKDIQNKTG TQIHFKEDNI DCPDRICIIK GSYEGVHLAE EMIKSVIQNQ
     PIIETYEMYV PQKACGRIIG RGGEVIHQIQ ATSSAKIIIE SSYTPYDPNA ERRIIIKGTA
     EQIATALLQI EDKVREEKEA RTKLEASSAS RLPRGKLSPR NTKNNIQSEQ VQTTELLPVS
     DGGMEVYISA METPSQFWVQ VVGPGTTALD KLVSDMTVYY NDEKNHELHK LRNITLGQIV
     AAKFSFNEQW YRAEVISAPE DGQCEVYFVD YGDREMVQLD CILELRTDFL SLRLQAIECS
     LANIKPRCQL LNSLSSMLLD LELPIPASQT SLNNSGFVCS IIFHAKFFLS TVKFSSQYAK
     LAFLSASHPN SSAIKSLLAI FSGVIVSIRF LSQSSFNPK
//
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