ID A0A3B6TMU6_WHEAT Unreviewed; 2171 AA.
AC A0A3B6TMU6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CFC21_111826 {ECO:0000313|EMBL:KAF7111869.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7D02G531100.1};
RN [1] {ECO:0000313|EMBL:KAF7111869.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7111869.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS7D02G531100.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS7D02G531100.1};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS7D02G531100.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7111869.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7111869.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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 EMBL; CM022231; KAF7111869.1; -; Genomic_DNA.
DR SMR; A0A3B6TMU6; -.
DR STRING; 4565.A0A3B6TMU6; -.
DR PaxDb; 4565-Traes_7DL_EF64BC4FC-2; -.
DR EnsemblPlants; TraesCS7D02G531100.1; TraesCS7D02G531100.1; TraesCS7D02G531100.
DR Gramene; TraesCS7D02G531100.1; TraesCS7D02G531100.1; TraesCS7D02G531100.
DR Gramene; TraesCS7D03G1250700.2; TraesCS7D03G1250700.2.CDS; TraesCS7D03G1250700.
DR Gramene; TraesKAR7D01G0453700.1; cds.TraesKAR7D01G0453700.1; TraesKAR7D01G0453700.
DR OMA; TEDNIQM; -.
DR Proteomes; UP000019116; Chromosome 7D.
DR Proteomes; UP000815260; Chromosome 7D.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
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 PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT DOMAIN 22..94
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 678..843
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1207..1357
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1623..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2051..2089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 110..137
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1547..1581
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 172..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1426..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1650
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2171 AA; 245912 MW; D31FF509CF40052B CRC64;
MASKGPRSKL DHETRPRRKK ALEAPREPRK PKVHWDHVLG EMVWLSKEFE SERKWKLSMA
KKIAQRANMG VVDQATKDEK KQKEGEHRLR KVALNISKDV KKFWTKIEKL VLYKNQLEVE
ERKKKALDKQ LDFLLGQTER YSTMLAENLV DVPHLQTQEN GLLQTNVLSQ EEVAGPSQTN
QPSQEEVAGP SQTNQPSQEE VAGPSQTNQP LQEDVAEPSQ TNQPLQEDVA EPSHTNQPLQ
EDVAEPSHTN QPVQEEVAEE NINAPTPDDL VADTMETDDD YDSSSLNEEQ EDDERTIDED
EAQITEAERN EELAALQAEA DIPIDDLLKS YLKSQVSRES SPANKDTCSN SDLKNSTKDS
SNQVNGCNHD SGYTSSDEGN FSEEVDDSHH YAEFVKRNHG KSNGGISGEQ EDNDYVCTDE
GKDDEATLSE EEELAKKDGP DPLDEIKLLQ KESEIPLEEL LARYPKDGYA DEVTNELEDS
PTHSSEEVNS DMSLDDLPAD LELNNDTSEN HEIAEVLGTE HVSGNALQLE IVSEPSVQEC
PVKGDELTDA KVMADEEASV QECSVEEVEM TDAKVMADQE TIVQECPVKE DELTDAKVMA
DEETSVQERS VKEDERTDAK VIANEETGDS VMADAAAAAR AAQPTGNTFS TTSVRTKFPF
LLKHSLREYQ HIGLDWLVAM YEKRLNGILA DEMGLGKTIM TISLLAHLAC EKGIWGPHLI
VVPTSVMLNW ETEFLKWCPA FKILTYFGSA KERKQKRQGW MKPNFFHVCI TTYRLVIQDS
KAFKRKKWKY LILDEAHLIK NWKSQRWQTL LNFNSKRRIL LTGTPLQNDL MELWSLMHFL
MPHVFQSHQE FKDWFCNPIS GMVEGQDKVN KEVIDRLHNV LRPFILRRLK RDVEKQLPQK
HEHVIYCRLS RRQRNLYEDF IASSDTQATL SSGNYFGMIS IIMQLRKVCN HPDLFEGRPI
ISSFDMAGID MQISSSVCMV LDKGPFSQAG LSDMNLVFTQ NEFNMTSWEA DEVAAVFLPG
ITSRGSGAEI FCSSKAGQRS NGTNIFEEIQ KALQEERIKE AKERAASIAW WNRLRCEKRP
VYGRNIRELL TIRHPMCDVL EKKNNPSCYM DFSSSLADLV LSSVERFNKM LGFIESFTFA
IPAARAATPI CWCKKRNSPV LLGPAYREQC MNEFSPILSP IRPAIVRRQV YFPDRRLIQF
DCGKLQELAI LLRRLKSEGH RALIFTQMTK MLDTLEEFIN LYGYTYLRLD GSTQPEERQT
LMQRFNTNPK FFLFILSTRS GGVGVNLVGA DTVIFYDSDW NPAMDQQAQD RCHRIGQTRE
VNIYRLISES TIEENILKKA NQKRTLDDLV IQRGCYNTEF FKKLDPMEFF SGHTALNVED
QPRDHSTTAV SSNETGLGLS NADVEAAIRQ AEDEADYMAL KRLEQEEAAD NQEFSEEVAG
RLEDDELVNE EDTKPDDHTS EEHKHQSSDA DKDKNVGLPV NQINEEKALT LAAGDGDMDM
LADVKQMAAA AAAAGQASSS FENHLRPIDR YAMRFLELWD PIIDKAAVNY QVNVEEEEWE
LERIEKLKED LEAEIDEDQE PLSYESWDVD FATTAYRQQV EALAKKQLLE EQERQALEAA
KELEEMNDMA SSHRKKSKKK KRKAGKFKSL KKGRVSSESE AMHDETSVDT MSIDDNAPSP
ELMSDESPHH GSNKRKKMTP RNEEVSSSSR ALKKFKKAPK SNCTPESSSH KHSLEGKQLK
LMDEANDSDP KSVRIKSDGR IAMPSMPAKR VMVIKPERLK KKGLMWPRDC ALDSWTTEED
AVLCGTVHEY GPVWELASDF LHSIPGGAFY RGRYRHPVHC CERFRELFCK YVLSATDNAN
SEKAPSGAGK AVLKVSEDQT RMLLNVISEI PNNELLLQKH FMAILSSVWR SKCTHESRRV
TSVCSSATHK PVSLSENWSM TNDKPSFNLV RTALADAQAQ CPRVAIPTSN QEPRRRHLDL
VLDFRTDRHA YQADFPSVVN VSILEPDPIR RTVVPVEQSL LSGLPHRHAE NRFRIASEAC
FEGEGSHWAS SVHMNDTARH KSGSKSTGKH KAASESGRPP KSKIQRTAEP QDMPALKFDF
LRSPRQLLTS AAEFPITQSL SDFGIDDSEL TYMEDLPLEE TDTEFAPYQY DPVSLAGIEE
LDPLVDLTDI G
//