ID A0A103XVZ0_CYNCS Unreviewed; 867 AA.
AC A0A103XVZ0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Histidine kinase-like ATPase, ATP-binding domain-containing protein {ECO:0000313|EMBL:KVH97875.1};
GN ORFNames=Ccrd_000011 {ECO:0000313|EMBL:KVH97875.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH97875.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH97875.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH97875.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family.
CC {ECO:0000256|ARBA:ARBA00007845}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVH97875.1}.
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DR EMBL; LEKV01003816; KVH97875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XVZ0; -.
DR EnsemblPlants; KVH97875; KVH97875; Ccrd_000011.
DR Gramene; KVH97875; KVH97875; Ccrd_000011.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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:SF83; HISTIDINE KINASE-LIKE ATPASE, C-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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 ATP-binding {ECO:0000313|EMBL:KVH97875.1};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|EMBL:KVH97875.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KVH97875.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW Transferase {ECO:0000313|EMBL:KVH97875.1}.
FT DOMAIN 450..596
FT /note="Morc S5"
FT /evidence="ECO:0000259|Pfam:PF17942"
FT REGION 691..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 720..762
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 691..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 98032 MW; C19A2CA503088746 CRC64;
MDVRMNPEST VVDLIEPTIG EGIQTVSKND VQASDRSSLC FSDTDVIEES NGRPSKKPKI
EEKTLTCALP QGFLDPMNHD ERSQSILEYG DSAKAAVPSM SKQFWKAGDY EGSPNNTESI
SHPDGMDHVR VHPRFLHSNA TSHKWALGAF AELLDNSLDE VRTGATYVHV DVLNNERVTH
NKMLLVKDLL DSLFFYPRVF ISYMMTDNGG GMTPEKMRAC MSLGYSVKSK LANTIDGNGF
KTSTMRLGAD VLVYTRCPGQ DGRRCVFISW HLIIGLVSIG YPRLSLSHSH ALCISNQIPL
LSIFSSTQSI GMLSYTFLME TGKEDIVVPM VRHLTLFLYP CKLVDFEKRG EEWGMMARSS
PADWKRNMET LVRWSPYSSE EGLLQQFDFL NDQGTHIIIY NLWEDEEGQL ELDFDTDLHD
IQIRGVNRDP KKIEMAKDYP NSRHFLTHRH SLRSYASILY LSIPNGFRII LRGEDVIHHK
IVDDMMLTEK VMYKPTQPNA DGTRKDQNLM VAVVTIGFVK DAKDHIDVQG FNVYHKNRLI
KPFWRVWNAA GSDGRGVIGV LEADFIEPAH DKQGFERTTV LSRLENRLVA IQKKYWFDSL
SLDLIWPTIN FDRSTNCQEI GYAKRCKSVS DTKCRPSMKD ESDRHIAPTG IDTIDARVKL
RPIRKLEASK FLECAQNDEI PEAYACTSRE KQASTRRLPS EVATTNGDGH ASTDYNGDTV
AKLREENLVL RQRLEGSERV MINNLLSDLQ YERDKVVSLE NQNDVMLHGQ VLKAQEKIEE
LDREQISLID IFSEERQRRD HQEETLRKRW KEAMDTIEDL RGQIKVLESS RVLGSPGLNA
GGLEKGGKFG GGYGKDGGCG KGDGGGN
//
