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
//