ID A0A059A9B5_EUCGR Unreviewed; 1589 AA.
AC A0A059A9B5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EUGRSUZ_J00103 {ECO:0000313|EMBL:KCW50329.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW50329.1};
RN [1] {ECO:0000313|EMBL:KCW50329.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW50329.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; KK198762; KCW50329.1; -; Genomic_DNA.
DR EnsemblPlants; KCW50329; KCW50329; EUGRSUZ_J00103.
DR Gramene; KCW50329; KCW50329; EUGRSUZ_J00103.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd15517; PHD_TCF19_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR048686; SHPRH_helical_1st.
DR InterPro; IPR048695; SHPRH_helical_2nd.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF21324; SHPRH_helical-2nd; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 509..662
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1356..1406
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1454..1589
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1589 AA; 179478 MW; E4491C2A5196280D CRC64;
MGRKKQARPR RSGVIITDGN GEGGSKSDWA EENVGANQKV QKDELDVSDP PFFVDVECNC
WALDEHFDIS ELVLTDLNIG GGFSGFRVEN GFYQSSDYSF RFRVCNVNEF VARIKLGHWP
LLSAKDVHLE LVEKHSAENR ENQKVVLSGS FDGPNEGVSG LVHLASLKFM SVRPLEGIAF
SEDVTTLRVR VEILKRAFDA CESLQDNMRQ LWKKSMINVM AWLRPEVMTS EARYGICQSR
AVGNDLHPDD RDTTTVNRKD IKFDVSGFYE AIKPSKTDPM LDENIPNLIP KLRPYQRRAA
YWMVQNEKGA LGSFGTQGTS QLVSPLCMTV GFVDSGLKMF YNPFSGNVAM RSEVFSERVS
GGILADEMGL GKTVELLACI LSHRWSASKS GACINEESQL RKESQIHIKR LKRERVECIC
GAVTESYRYT GLWVQCDVCD AWQHSDCVGY SARGKKVKDG SGQQKREDIE KSRRKKNVPT
IVEREGKYVC QLCLELMSVT ESPVPSGATL IVCPAPILHQ WQTEIIRHTN TDSVKVLVYE
GVKNTSFSEE PAVEVDELVS YDIVLTTYDV LKEDLSHDSD RHEGDRRLMR YQKRYPVIPT
PLTRIFWWRL CLDEAQMVES NAAAATEMAL RLHSKHRWCI TGTPIQRRLD DLYGLLKFLK
LSPFDVPRWW NEVIRDPYEK RDAGAMEFTH NLFKQIMWRS SKRHVADELH LPPQEECLSW
LSFSAIEEHF YQRQHETCVD YARELVESIK ADILKREAPG SASSAPSDIL ITHVEAAKLL
NSLLKLRQAC CHPQVGSSGL RSLQHSPMSM EEVLTVLISK TKIEGEEALR RSVVALNGLA
GIAIIEENPS HAVSLYKEAL DLAMEHSEDF SLDPLLNIHI HHNLTEIVFK ASNGSPQLQL
NDGQTSGSPG NKTSKRPYFG ECNDEYATKR QKLNGIEDDG SISNTPKPPT STFDMSADAL
NETNECNAKP SFASNYFSYD HLKTVCETFK QKFLSTFNSK LIIAQLEFKK SYEQVCDTFS
EVKNHRSVWW LDVLHHIEQS RDSTNELIRK IGEAVLGSTN NSRSSKIGSS FRSIHGLKYY
IQTGLDSLEV SRRAVLDRLL EIDETMDKPR DEDIERVGHC QNCQLNGNGP VCILCELDEL
FQIYEARLFR LSNARGGIIM SAEEALDLQK KKSALNQFYR TLSQANKNLS STSRDEEIAG
KRDTGEKVVV SKSPSELEVV LGVMRGYSKV HLGKEGKSAA TKQLRLLEDM RKEYASARSL
CIAQAQVLRA HDEIKMSTSR LRLREDENDK SLDALSLEEL PANNVHYSNE KFVSLALLLR
IKGKLRYLKG LVQAKQKVSP MEQKSEHSVN AYQEACPICQ EKLSIQKMVF QCGHVICCKC
LFELSEHKQA QAGESQRRWV MCPTCRQHTE FANIAYADDR QNKLPNSSGL HESQDSRNEA
SITVQGSYGT KIEAVTRRIL WIKSTEPNAK VLVFSSWKDV LDVLEHAFKA NSISYARMKG
GRKAHTAVDQ FRGQNPSVKV NTREHCQDIQ VLLLLVQHGA NGLNLLEARH VILVEPLLNP
AAEAQAISRV HRIGQENKTL VHRFIVSEK
//
