ID A0A0E0MF95_ORYPU Unreviewed; 722 AA.
AC A0A0E0MF95;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Morc S5 domain-containing protein {ECO:0000259|Pfam:PF17942};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC11G10830.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC11G10830.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC11G10830.1}
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; A0A0E0MF95; -.
DR EnsemblPlants; OPUNC11G10830.1; OPUNC11G10830.1; OPUNC11G10830.
DR Gramene; OPUNC11G10830.1; OPUNC11G10830.1; OPUNC11G10830.
DR eggNOG; KOG1845; Eukaryota.
DR HOGENOM; CLU_011516_4_1_1; -.
DR OMA; TINLHGF; -.
DR Proteomes; UP000026962; Chromosome 11.
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:SF44; PROTEIN MICRORCHIDIA 6; 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:UP000026962}.
FT DOMAIN 380..515
FT /note="Morc S5"
FT /evidence="ECO:0000259|Pfam:PF17942"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 683..710
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 79207 MW; 80A6F5535D7BBA69 CRC64;
MNSMAADEQD TKPFLSPTTT IPRAHPGYFS ACHHRQMTAA APPLDQHSSG AGVAAAGQQH
ATAACVLNQA SDELPEEDGA DGNFIVRRLQ GETSCSAPVR RISRSFWSAG EYDTATSGSS
SVQPPRNVQN RMCVHPKFLH SNATSHKWPF GAVAELLDNA IDEIKTGATR IIVDKVNGCN
GSPALLVQDD GGGMDPDSLR RCMSFGFSEK QSGSSIGQYG NGFKTGTMRL GADVIVFSRC
MKTSEPTQSI GLLSYTFLAE TNQKDVVVPV VDYKYNLLTG DAKPHQRLGP DQFSLNLSVL
LKWSPFATEE QLIQNFSDIG PHGTKIVVFN LWSNDNGDLE LDFDTDEKDI LISGAPKAAE
TTNAAKRMNE SHLANQLHCS FRVYASVLYL KLPAYFKIIL RGEEVKHHYI ASDLRYTQCI
RYRPQAFGKK EDEVDTTIGF LDGAPTINLH GFSIYHKNRL ILPFHRVLSS ASSKGRGVAG
VLEADFIKPT HDKQDFEKSQ LYQKLINRLK EMTNEDLYSH LVGYHKLPRA ASGSHASALV
PTLSGTTATA SSERIPVTRD NPTNAIPIAF APHLASAPVG TSAVATGAQA VFSQSSLQIS
GPPTLTTGTD LLVDTRKRKM ETLDQMDGPS KRLSIHDLAA NNSVDSSNQV CQHMGERELK
EFSYLKLENT LLRQECAEFE SSEKDLLLKE QQLRLELEQT EAQYKSLLNE YISVAAVRIV
KQ
//
