ID G7J9W2_MEDTR Unreviewed; 1412 AA.
AC G7J9W2; A0A0C3VQB5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=CHD3-type chromatin-remodeling factor pickle protein {ECO:0000313|EMBL:AES73562.2};
GN Name=11436035 {ECO:0000313|EnsemblPlants:AES73562};
GN OrderedLocusNames=MTR_3g106210 {ECO:0000313|EMBL:AES73562.2};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:AES73562.2, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES73562.2, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES73562.2}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES73562,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2] {ECO:0000313|EMBL:AES73562.2, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73562,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3] {ECO:0000313|EnsemblPlants:AES73562}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES73562};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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DR EMBL; CM001219; AES73562.2; -; Genomic_DNA.
DR RefSeq; XP_003603311.2; XM_003603263.2.
DR STRING; 3880.G7J9W2; -.
DR PaxDb; 3880-AES73562; -.
DR EnsemblPlants; AES73562; AES73562; MTR_3g106210.
DR GeneID; 11436035; -.
DR Gramene; AES73562; AES73562; MTR_3g106210.
DR KEGG; mtr:11436035; -.
DR eggNOG; KOG0383; Eukaryota.
DR OrthoDB; 2910821at2759; -.
DR Proteomes; UP000002051; Chromosome 3.
DR ExpressionAtlas; G7J9W2; differential.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45623:SF17; CHD3-TYPE CHROMATIN-REMODELING FACTOR CHR7-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF06461; CHDII_SANT-like; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000002051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 50..97
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 99..185
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 195..244
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 300..486
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 614..775
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 906..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..923
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 161613 MW; A14D358ED680C586 CRC64;
MSSLVERLRV RSDRKPVYNL DESDDEDFLL KKPGASQEKF ERIDRSDAKE DLCQACGESG
DLLSCATCNY AYHSSCLLPP LKGPAPDNWR CPECVTPLID IDKLLDCEMR PTVEGDGDAD
SDAAKSGSKQ IFVKQYLVKW KGLSYLHCAW VPEKEFLKAF KSHPRLKTKV NNFHRQMASS
NTSDEDFVAI RPEWTTVDRI IACRGDNDER EYLVKWKELP YDECYWESES DISAFQPEIE
RFNRFRSRSS KLASIKQQSR VNDDNELKKQ QKEFHQYEHS PEFLSGSLHP YQLEGLNFLR
FSWSKQTHVI LADEMGLGKT IQSIAFLASL FEEGVSAHPH LVVAPLSTLR NWEREFATWA
PQMNVIMYVG SAQARSVIRE YEFYFPKKLK KNKKKKSLVS ESKHDRIKFD VLLTSYEMIN
LDTTSLKPIK WECMIVDEGH RLKNKDSKLF SSLKQYSTRH RVLLTGTPLQ NNLDELFMLM
HFLDAGKFAS LEEFQEEFKD INQEEQISRL HKMLAPHLLR RVKKDVMKEL PPKKELILRV
DLSSKQKEYY KAILTRNYQI LTRRGGAQIS LINVVMELRK LCCHAYMLEG VEPDIDDPKE
AFKQLLESSG KLHLLDKMMV KLKEQGHRVL IYSQFQHMLD LLEDYCSYKK WHYERIDGKV
GGAERQIRID RFNAKNSSRF CFLLSTRAGG LGINLATADT VVIYDSDWNP HADLQAMARA
HRLGQTNKVL IYRLITRGTI EERMMQMTKK KMVLEHLVVG RLKAQNINQE ELDDIIRYGS
KELFADENDE AGKSRQIHYD AAAIDRLLDR DQVVDEETTL DDEDEDGFLK AFKVANFEYV
DEAEAAAEEA AQKRAMETAN SSDRTHYWEE LLKDKFQEHK VEEFNALGKG KRNRKLMVSV
EEDDLAGLED VSSDEDDNYE AELTDGDSNS TGTTTTRRPY KKKARTADST EPLPLMEGEG
KAFRVLGFNQ SQRAAFVQIL MRFGVGDFDW KEFTSRMKQK TYEEIKDYGT LFLSHIAEDI
TDSSTFTDGV PKEGLRIQDV LVRIAVLLLI RDKVRFASEH PQTPLFSDDI LLRYPGLKGI
RKWKEEHDFM LLRAVLKHGY GRWQAIVDDR DLKIQEIICQ ELNLPVINLP GPGQVGSHVQ
NGANVANAEI PSNESRENGG SGIAADGAQG SGDAKNQTQL YQDSSLYHFR DMQRRQVEFV
KKRVLLLEKG LNAEYQKEYF GDPKAGEVTN EELKSEPKST TIPSFISVDT DTQMIDQLPQ
VEIIAPEDVS VVCDSDSNRL ELVRLYNEMC KVVEENPMDL VQSSSAREPA EVNAVKKCPP
LETICEDINR ILTPTAEQPV AETPVLNSDN KSEEISHIEV LGSKSPPNPQ NDLKRDSLAN
DDAKDMVVDS AEKKESNTAM DESSNAELNE DT
//
