ID A0A0S3T464_PHAAN Unreviewed; 672 AA.
AC A0A0S3T464;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=CW-type domain-containing protein {ECO:0000259|PROSITE:PS51050};
GN Name=Vigan.10G138700 {ECO:0000313|EMBL:BAT99851.1};
GN ORFNames=VIGAN_10138700 {ECO:0000313|EMBL:BAT99851.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT99851.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT99851.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family.
CC {ECO:0000256|ARBA:ARBA00007845}.
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DR EMBL; AP015043; BAT99851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3T464; -.
DR Proteomes; UP000291084; Chromosome 10.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 3.30.40.100; -; 1.
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 InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR23336:SF11; OS06G0622000 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 Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 563..613
FT /note="CW-type"
FT /evidence="ECO:0000259|PROSITE:PS51050"
FT REGION 113..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 76491 MW; C1F686DB9079D701 CRC64;
MVMFLVLKKD KKMICTTRCL DPPIDLPQEL SLTCEISKNK IHSLSEFPQF SLTPVPNNLH
EMSEWGNFLN YLCKKDKVAL INFEQYQFYI LPPALVSTSS SVNVAYNIDN TGSVDTRPRD
SESGSQLEEC GGPNTAEGLK FSRAEETCNE YQSRVPLKNF IRADPSYLKT LGQAHSGWIF
GAIAELVDNS KDAKATKMDI FVDIIQLKKS RKDVPMLCLI DDGQGMNHDE VMKMVSFGHK
QSHKVDTDRI GKFGVGFKTG AMRLGRDVLV LTQTTTSRSL AFLSQSLNEG KDNIEIPIVS
YCRQGQLMEI DLSMQSEALA KYNLKAIKDF SPFNKYLIGE KAALFGTGTG TQIYIWNLDE
WGSKYCLEWH DGLKGGSSFH QGDILIRSKR TRSRPGQISQ KVPLDYSLRA YLEIIFLVPR
MKISVQRTLV KSRPLSKFLT QTIVETGDIL RRPVELILGF SQLEWERANC GMFLYWHGRL
IEAYKRVGGM THSADVGRGV IGVVDVTNLM DDEDGRVWVH NNKQGFQDSE QYACLEQWLS
RKVDEYWDNN FDALELNKDN CVFKPDHEWV QCDKCRKWRI LPTDFDSRKL PLEWFCYMKP
FKGHCSDSEQ KMAPGIVNVS TKRSGYACLL KDSNDKKVEG VGKTSGADDK SIKYEDAKFP
ALKRLRKGQW KQ
//
