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Database: UniProt
Entry: C0HII5_MAIZE
LinkDB: C0HII5_MAIZE
Original site: C0HII5_MAIZE 
ID   C0HII5_MAIZE            Unreviewed;       771 AA.
AC   C0HII5;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=Morc S5 domain-containing protein {ECO:0000259|Pfam:PF17942};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACN26838.1};
RN   [1] {ECO:0000313|EMBL:ACN26838.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACN26838.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the MORC ATPase protein family.
CC       {ECO:0000256|ARBA:ARBA00007845}.
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DR   EMBL; BT062141; ACN26838.1; -; mRNA.
DR   RefSeq; NP_001296836.1; NM_001309907.1.
DR   AlphaFoldDB; C0HII5; -.
DR   GeneID; 100216876; -.
DR   KEGG; zma:100216876; -.
DR   OrthoDB; 1221114at2759; -.
DR   ExpressionAtlas; C0HII5; baseline and differential.
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   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}.
FT   DOMAIN          366..509
FT                   /note="Morc S5"
FT                   /evidence="ECO:0000259|Pfam:PF17942"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          670..768
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        596..635
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  86148 MW;  DD3E95B4D5849D3F CRC64;
     MAGGGDGGDG QMEVVFNVSS SDTDSDDLGA GGGKRSRPVA GQGGGRDRED KKARILAAAA
     TVPAGFLEPL SPVRLLPPPA PGRSVTKQFW KAGDYVGKPD HLLAVVAAQH SDSGMDHVRV
     HPKFLHSNAT SHKWALGAFA ELLDNSLDEV VHGATYVNID MIESKKDGTP MLLVQDNGGG
     MNPDKMRHCM SLGYSAKSKV KNTIGQYGNG FKTSTMRLGA DVLVFSCSRG IEGTRPTQSV
     GMLSYTFLRS TNRDDIIVPM IDYEKENEWK RKARTTLTDW CMSLETIIQW SPYSTEAELI
     QEFGSIGEQG TRIIIYNLWE DDEGELELDF DADANDIQIR GVNRDQNKIK KANQFPNSKH
     FFTYRHSLRS YASILYLMLP DNFQMILRGK KIDHHNIIND LMLKKQLTYN PTVGDGLPKD
     MHVAAKVTIG FVKDARQHID IQGFNVYHKN RLIKPFWRVW TSAGVAGRGI IGVLEVNFVE
     PAHDKQDFER TNCLARLEAR LNRMQKKYWS DNRHRIGYGT NDASTDSVKR KTGSWKSGYL
     QTIRSDGRSC SNTTNNIMNA SMSSPETSKL SGPNREFSST TVCQHRAEKS ANTIRSERSV
     LHGLSNTDGG KTETANAPSK STSPILRTSL PPTPNEGKRS ERIAAKYQSK QVNATTNGDR
     ESIVDPEAII KKLKEENSSL KERILMVQES LSRELQIERD KNKSLTERFE DVERQLELAI
     KEQEATVELF AEERKCHDQE VENLKRKLTE ASSTIQDLME QLNAARNCCK R
//
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