ID I1NEQ9_SOYBN Unreviewed; 1098 AA.
AC I1NEQ9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRG90383.1, ECO:0000313|EnsemblPlants:KRG90383};
GN Name=100806677 {ECO:0000313|EnsemblPlants:KRG90383};
GN ORFNames=GLYMA_20G087900 {ECO:0000313|EMBL:KRG90383.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG90383.1};
RN [1] {ECO:0000313|EMBL:KRG90383.1, ECO:0000313|EnsemblPlants:KRG90383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG90383};
RC TISSUE=Callus {ECO:0000313|EMBL:KRG90383.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRG90383}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG90383};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRG90383.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRG90383.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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; CM000853; KRG90383.1; -; Genomic_DNA.
DR RefSeq; XP_014628545.1; XM_014773059.1.
DR AlphaFoldDB; I1NEQ9; -.
DR PaxDb; 3847-GLYMA20G21940-1; -.
DR EnsemblPlants; KRG90383; KRG90383; GLYMA_20G087900.
DR GeneID; 100806677; -.
DR Gramene; KRG90383; KRG90383; GLYMA_20G087900.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OMA; LTSHCRW; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000008827; Chromosome 20.
DR ExpressionAtlas; I1NEQ9; baseline and differential.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16449; RING-HC; 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; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 471..665
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 862..902
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 938..1094
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 45..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 124565 MW; B6157D12020CCD80 CRC64;
MSMAEEEPSI TSPPARTLHK FLSRSGKTVI AAQPLAVVRA TTSTGGARVL AAPPNSNDDP
TPPQEEEGEG ETGFDASHHH ERILLQRELT VSFDEFLEVT NTKVATEEEA LKSVMAPLEE
ETEEGEEAES SQAQSAQPVQ PVPRGPQLFR PVQKKKAVTG DDVEVVEVRK PVEKKNIPNI
SNLEDGEFPE ESGWFLLGRK VEVAVSTARG VNRLVDNEIV HFNFPIPSYS SKSQWIVRAS
TKRSGEVGRM PMEWAKAVIP VMQSGRVKVR GRCIAVPDKL QMMQEIMFLV SFYVHHSVFA
ERVDTSWRLE ACGKIDDTVY PLLALLKMLE IKPSQKAVFT PEDIDSRKRL LYPKADPDEA
AALPLIKRRK GGEPLPEQNN DEQALSESAL NKLVGAAEIY DLKEKEAPET LVCNLKPYQK
QALHWMTEIE KGMDIESVER NLHPCWSAYT ICKGRTIYLN IFTGEASKKF PKATQMARGG
ILADAMGLGK TVMTIALILS NPGRGNSENN DVENGDDNFI TNKRKNANTL HKFEGGTLIV
CPMALLSQWK DELETHSKEG SISIFVHYGG ARTTDPWMIS GHDVVLTTYG VLQAAYKNDG
ENSIYNKVKW YRVVLDEAHN IKAHRNQTAQ SAFVLSSHSR WCLTGTPLQN SLEDLYSLLR
FMRVEPWCNL AWWQKLIQRP YENGDPRSLK LVKAILRMLM LRRTKETKDK KGRPILFLPP
IDFQLIECEQ SESERDFYEA LFERSKVQFD QYVAQGKVLH HYANILDLLM QLRRCCNHPF
LVMCGSDTQK RADLSRLARK FFQTNTEFPD ESNQNDPRQQ AELNKLASRL LLKSASSLHS
VQPHAYIAEV LENIQKGDII ECSICMESPE DPVFTPCAHK FCRECLFSCW GTSVGGKCPI
CRQLLQKDDL ITYSSESPFK VDIKNNVTES SKVSKLFEFL QRILNTSSEK SIVFSQWTSF
FDLLENPLRR RGIGFLRYDG KLTQKQREKV LDEFNETREK RVLLMSLKAG GVGLNLTAAS
NVFIMDPWWN PAVEEQAIMR IHRIGQNRRV VVRRFIVKDT VEDRLQQVQA RKQRMISGTL
TDDEVRTARI QDLKMLFT
//