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Database: UniProt
Entry: A0A0D9YS38_9ORYZ
LinkDB: A0A0D9YS38_9ORYZ
Original site: A0A0D9YS38_9ORYZ 
ID   A0A0D9YS38_9ORYZ        Unreviewed;       793 AA.
AC   A0A0D9YS38;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Morc S5 domain-containing protein {ECO:0000259|Pfam:PF17942};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G16390.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM02G16390.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM02G16390.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the MORC ATPase protein family.
CC       {ECO:0000256|ARBA:ARBA00007845}.
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DR   AlphaFoldDB; A0A0D9YS38; -.
DR   EnsemblPlants; OGLUM02G16390.1; OGLUM02G16390.1; OGLUM02G16390.
DR   Gramene; OGLUM02G16390.1; OGLUM02G16390.1; OGLUM02G16390.
DR   eggNOG; KOG1845; Eukaryota.
DR   HOGENOM; CLU_011516_6_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0031349; P:positive regulation of defense response; IEA:UniProt.
DR   GO; GO:0002833; P:positive regulation of response to biotic stimulus; IEA:UniProt.
DR   GO; GO:0032103; P:positive regulation of response to external stimulus; IEA:UniProt.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR045261; MORC_ATPase.
DR   InterPro; IPR041006; Morc_S5.
DR   PANTHER; PTHR23336:SF54; OS02G0469300 PROTEIN; 1.
DR   PANTHER; PTHR23336; ZINC FINGER CW-TYPE COILED-COIL DOMAIN PROTEIN 3; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF17942; Morc6_S5; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT   DOMAIN          378..512
FT                   /note="Morc S5"
FT                   /evidence="ECO:0000259|Pfam:PF17942"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          692..783
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        75..94
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..576
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  88861 MW;  EE8A6E16236A4060 CRC64;
     MAPAAGEPSA AAGGGEGDTE AHAVIDVSSS ETDSDPDPGF GGAGKRPRRV VATAGSGREA
     EKRARILAAA VPPGFLDPLP RPSAPPPPPP PRGRRRVTRQ FWNAGDYDGK PDLLGGDPSL
     RSDSGMDHIR VHPRFLHSNA TSHKWALGAF AELLDNSLDE VANGATYVNI DMLENKKDGT
     RMVSVEDDGG GMDPDKMWHC MSLGYSAKSK VKDTIGQYGN GFKTSTMRLG ADVLVLSRSC
     GNGGRRRTQS IGMLSYTFLR ETRKDDIIVP MIDYEKGQQY WKRMMRTTSI DWQTSLATII
     EWSPYSTEAE LLQEFSSIKE QGTRIIIYNL WENEQGELEL DFDTDVNDIQ IRGGNRDQKN
     IQLAKQFPNS RHFFTYRHSL RSYASILYLQ VPSVFQMILR GKEIEHHNII GDMMMKNHVI
     YKPVMTDGFP RDIDMMTDVT IGFVKDAKHH IPIQGFNVYH KNRLIKPFWR LWALPGIQGR
     GVIGVLEVNF VEPAHDKQDF ERTNSLARLE ARSDNCHRIG YGGNSANRKS GREYKGPTSD
     QSPEGCRSSN YLQRKRSFGS PYSGSSNNNS KTGITSLNTS KISLPESRFS LRTTAQQTVE
     KTKRTLRYTR PLLHGLSHTS NDSDAQTSGT PSRSTSHILK TPEKSCHNEN TLPLIPSSEA
     IRSEGTTRYQ SEERNVTNNG DGQTVDNPET VIKLLTDENS SLKESIMKME ESLSRELHIE
     RDKNKSLIER LENVQKQLET ANKEQEALVD IFTEERARRD QEVENQRTKL KEASSTIQNL
     LDQLNAARSC RKN
//
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