ID A0A0S3RM84_PHAAN Unreviewed; 1669 AA.
AC A0A0S3RM84;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=Vigan.03G138100 {ECO:0000313|EMBL:BAT81617.1};
GN ORFNames=VIGAN_03138100 {ECO:0000313|EMBL:BAT81617.1};
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:BAT81617.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT81617.1, 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 SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; AP015036; BAT81617.1; -; Genomic_DNA.
DR Proteomes; UP000291084; Chromosome 3.
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:UP000291084};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1356..1404
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1453..1624
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1669 AA; 187773 MW; 021BDC697D0C4828 CRC64;
MGRRKSKPHR AGGIILDPDA SAETELNKQN AVEGGEEAKG SSGGIDKPYF VEVARLDWLS
GEHLDISEVV LRDLKLSEGF SGFELAEDFC RDQQYLLRFR VCNVSNVLGR IKLGHWPVLP
YTDIHLEFAR RVTVDHEETY TVLLSGVFDG PDEGVTGLLH LASLKFVTLR PVLGVGLSEE
ISSLRVRVEV LKNGFNACES LLDTSRQLWK KSMVNVMSWL RPEIMTSEVR YGFYSCMKMD
GDPQTEMVDD TCRSRKHARF DPAGLYEAIK PSKAEPMIED DIPELLPKLR PYQRRAAFWM
VEREKAVEES QGERERNQFH SPLCIPVDFL DTSSQMFFNP FSGNISLYPE TSSPYVFGGI
LADEMGLGKT VELLACIFTH RRSASGSDIL FDLEPQINAD QKVTLKRVKR DRVECICGAV
SESLKYEGLW VQCDICDAWQ HADCVGYSPK GKSLKSKQGC ESKTYKTTVA VRDGKYVCHM
CSELIQATES PIASGATLIV CPAPILPQWH DEIIRHTHQG SLKTCVYEGV RETSFSNASV
MDISDLASAD IVLTTYDVLK EDLSHDSDRH EGDRHFLRFQ KRYPVIPTLL TRIYWWRVCL
DEAQMVESST TASTEMALRL HSKYRWCITG TPIQRKLDDL YGLLRFLVAS PFDTYRWWTD
VIRDPYEKGD VGAMEFTHKV FKQIMWRSSK QHVADELYLP SQEECLSWLT LSPVEEHFYQ
RQHETCVRDA HEVIESLRND ILNRKGQDSI SLQSSSDPLI THTEAGKLLN ALLKLRQACC
HPQVGSSGLR SLQQTPMTME EILMVLISKT KIEGEEALRK LVIALNALAA IAAIQNDFCQ
ATSLYGEALA LAGEHAEDFR LDPLLNIHIH HNLAEILPLA SNFSLTLASK GKQLSESSEF
KMTKRHLILK VDSCHVKRQR ISGCDDINAT VPSSEPSNVS LLENDTKEDQ EFDNLSASSV
ESLIAECEDS KQKFLSVFSS KLSVAQQEFQ SSYVQVSNAY RDSRTHQNSF WWLEALHHVE
QSKEFSSELI RKIEEAMSGT SSNSKSSRIT ARFRSISALK YQIQTGLDQL EASRKTLLDR
LLEIDQTMEK PKEEDIERVG KCRNCQPNSD GPPCVLCELD ELFQDYEARL FVLKNERGGI
ISSAEEAVDF QKKNFALNHF LSKLSQSSNS STTSDIGHEE SKKRNVGQRV VVSRSASELE
LILGVIKNYC KARLGKDSVS AATKDLHVFE GMRKEFGHAR SLALAQAQYL RAHDEIKMAV
SRLHLRTSED DKSLDALGEN ELVAASSNFS HEKFMSLTML SQTKGKLRYL KGLVQSKQKK
QFESPNGSSI SVERTAMSNY TEEKAVLIAK TDDETCPVCQ EKLGNQKMVF QCGHVTCCKC
LFAMTEKRLQ NSKLHNWVMC PTCRQHTDFG NIAYAVDSQN ESSNLSVLHT INSSEKCEAS
ISVKGSYGTK IEAVTRRILW VKANDHKAKV LVFSSWNDVL DVLEHSFTAN NITFIRMKGG
RKAHVAISQF RGKQNDTKGC EGSTPESIQV LLLLIQHGAN GLNLLEAQHV VLVEPLLNPA
AEAQAISRVH RIGQKNKTLI HRFLVKDTVE ESLYKLNRSR SNHSFISGNT KNQDQPVLTL
KDVEALLSRA PLTMPESEEN PSTNTNLRHL PPSVAAAIAA EKRLNEQMT
//
