ID   A0A0D9UYR0_9ORYZ        Unreviewed;       891 AA.
AC   A0A0D9UYR0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=K Homology domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G08060.1, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR01G08060.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR01G08060.1, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR01G08060.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0D9UYR0; -.
DR   EnsemblPlants; LPERR01G08060.1; LPERR01G08060.1; LPERR01G08060.
DR   Gramene; LPERR01G08060.1; LPERR01G08060.1; LPERR01G08060.
DR   Proteomes; UP000032180; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:InterPro.
DR   Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR019510; AKAP7-like_phosphoesterase.
DR   InterPro; IPR009210; ASCC1.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR013666; PH_pln.
DR   InterPro; IPR008546; VAN3-bd-like_auxin_canal.
DR   PANTHER; PTHR13360; ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX SUBUNIT 1; 1.
DR   PANTHER; PTHR13360:SF1; ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX SUBUNIT 1; 1.
DR   Pfam; PF10469; AKAP7_NLS; 1.
DR   Pfam; PF05703; Auxin_canalis; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF08458; PH_2; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF55144; LigT-like; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        155..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          299..408
FT                   /note="PH"
FT                   /evidence="ECO:0000259|SMART:SM00233"
FT   DOMAIN          542..610
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          652..676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   891 AA;  97145 MW;  D369A60265B3C8A3 CRC64;
     MEQCDHHHQQ QQQQKQQRLE GIEEEDGSAA EKWPPPTTVR PPETPTETME FLARSWSLSA
     AEISKALKLL SGKPVSDDAP AAMDGRRSRH EHERDAAAIS PPISPRANLD TKLLRSAAAA
     AGGRGGGKST TTTTMGNWIK EQKERKRAEA RSRNAQAYAA TSVAGVAAAV AALVAGAVFS
     PAPDRPSSNG GGAGATGGGG AKTAAAIASA AALVASHCVE MAQAIGAGHD QILAAIQSAV
     NAQTTGDIMA LTAGAATALR GAAMLRARLH KEIQAAALPA SAAGGGGEPE RDTSPFVFVS
     RGGELLKRTR QGILHWKLVT VYMNSSLQVI IKMRSAHMAG TFIKTKKFVV LDICSEIPAW
     AGREVEDGSH KRGYFGIKTV ERVIEFECRS KYEQHKWVQG ITEMLNRRDS MKNASIRLAR
     PLCAAGSAPR FLQGSISQNS IHSLVMEQGT SSNVAKHNKR KSSVQRWRPI STEAATPKAN
     LNGMSNFVSK QVVENLASDG TTNVFIEVST DNASLPENKV SVEGTMETNS LNKDPDGSDL
     SEKYSSSVQV DAPLMRFLKG KGGTMQKQIE EETGVKIIFP SSKEETRVVL EAKTSENIRK
     ASEKIAKVLE EAVKSPMLDY SHFISLPLAI HPDLVEKLNH FQCSILGTSS NVDSDKDEDL
     SEGSIDEMDH EHKKVESPSV SIKMEIQVEE SVGVKKDNKG SRPDFGINKS IFIKPKTFHL
     TVLMLKLWNK DRVTKASDVL QSISSHVMEA LEDRPISIQL RGLTCMKGSP ARARVVYAPV
     LEVGEEGRLQ QVITDAFVKS GLVPERDARQ ELKLHATIMN VRHRKSKKRN QRNDSFDARN
     IFKKYGEHDW GEYLIPEIHL SQRFKFGENG YYYCCSSIPL PEEMQTECLS K
//