ID A0A1S3UFQ6_VIGRR Unreviewed; 1419 AA.
AC A0A1S3UFQ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=E3 ubiquitin-protein ligase SHPRH isoform X4 {ECO:0000313|RefSeq:XP_014504794.1};
GN Name=LOC106764879 {ECO:0000313|RefSeq:XP_014504794.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014504794.1};
RN [1] {ECO:0000313|RefSeq:XP_014504794.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014504794.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014504794.1; XM_014649308.2.
DR GeneID; 106764879; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000087766; Chromosome 6.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF21324; SHPRH_helical-2nd; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 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; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_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 Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1106..1154
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1203..1374
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1419 AA; 159351 MW; FBFB3020C1AB5E58 CRC64;
MTLAGQGNMQ GLILQVYMKP LSLQKPMIED DIPELLPKLR PYQRRAAFWM VEREKAVEES
QGERERNQFH SPLCIPVDFL DTSSQMFFNP FSGNISLYPE TSSPYVFGGI LADEMGLGKT
VELLACIFTH RRSASGSDIL FDLEPQINGD QKVTLKRVKR DRVECICGAV SESIKYEGLW
VQCDICDAWQ HADCVGYSPK GKSLKSKQGC ESKTYKTTVA VRDGEYVCHM CSELIQATES
PIASGATLIV CPAPILPQWH DEIIRHTHQG SLKTCVYEGV RETSFSNASV MDISDLASAD
IVLTTYDVLK EDLSHDSDRH EGDRHFLRFQ KRYPVIPTLL TRIYWWRVCL DEAQMVESST
TASTEMALRL HSKYRWCITG TPIQRKLDDL YGLLRFLVAS PFDTYRWWTD VIRDPYEKGD
VGAMEFAHNV FKQIMWRSSK KHVADELDLP SQEECLSWLT LSPVEEHFYQ RQHETCVRDA
HEVIESLRND ILNRKGQDSI SLQSSSDPLI THTEAGKLLN ALLKLRQACC HPQVGSSGLR
SLQQTPMTME EILMVLISKT KIEGEEALRK LVIALNALAA IAAIQNDFSQ ATSLYGEALA
LAREHAEDFR LDPLLNIHIH HNLAEILPLA SNFALTLASK GKQLSESSEF KMTKRHLILK
ADSCHVKRQR ISGCDDINAT VPSAEPSNGS LLENDIKEDQ EFDNLAASSV KSLIAECEDS
KQKFLSVFSS KLSAAQQEFE SSYVQVGNAY RDSRTYQNTF WWLEALHHAE QSKDFSSELI
RKIEEAISGT SSNSKSSRIT ARFRSISALK YQIQTGLDQL EASRKTLLDR LLEIDQTMEK
PKEEDIERVG KCRNCQPNSD GPPCVLCELD ELFQDYEARL FVLKNERGGI ISSAEEAVDF
QKKNFALNHF LSKLSQSSNS SATSDIGHEE SKKRNVGQRV VVSRSASELE LILGVIKNYC
KARLGRDSVS AATKDLHVFE GMRKEFGHAR SLALAQAQYL RAHDEIKMAV SRLHLRTSED
DKSLDALGEN ELVAASSNFS HEKFMSLTML SQTKGKLRYL KGLVQSKQKK QFESPNGSSI
SGERTAMSNY TEEKAVLIAK TDDETCPVCQ EKLGNQKMVF QCGHVTCCKC LFAMTEKRLQ
NSKLHNWVMC PTCRQHTDFG NIAYAVDSQN EASNLSVLHA IDSSEKCEAS ISVKGSYGTK
IEAVTRRILW VKANDHKAKV LVFSSWNDVL DVLEHSFTAN NITFIRMKGG RKAHVAISQF
RGKQNDTKGC EGSTPESIQV LLLLIQHGAN GLNLLEAQHV VLVEPLLNPA AEAQAISRVH
RIGQKNKTLI HRFIVKDTVE ESLYKLNRSR SNHSFISGNT KNQDQPVLTL KDVEALLSRA
PLTVPESEEN PSTNTNLRHL PPSVAAAIAA EKRLNEQRT
//
