ID A0A078IJD1_BRANA Unreviewed; 1521 AA.
AC A0A078IJD1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=BnaC05g03160D protein {ECO:0000313|EMBL:CDY49504.1};
GN Name=BnaC05g03160D {ECO:0000313|EMBL:CDY49504.1};
GN ORFNames=GSBRNA2T00093190001 {ECO:0000313|EMBL:CDY49504.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY49504.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY49504.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; LK032838; CDY49504.1; -; Genomic_DNA.
DR STRING; 3708.A0A078IJD1; -.
DR PaxDb; 3708-A0A078IJD1; -.
DR EnsemblPlants; CDY49504; CDY49504; GSBRNA2T00093190001.
DR Gramene; CDY49504; CDY49504; GSBRNA2T00093190001.
DR OMA; WIDEHET; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45081; EF HAND FAMILY PROTEIN, PUTATIVE, EXPRESSED-RELATED; 1.
DR PANTHER; PTHR45081:SF1; EF HAND FAMILY PROTEIN, PUTATIVE, EXPRESSED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13432; TPR_16; 2.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
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:UP000028999};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 6..41
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REPEAT 236..269
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 346..379
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 380..413
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 414..447
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 925..1099
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1266..1306
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1347..1511
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 166..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1521 AA; 171527 MW; CDCDBA64765B1C99 CRC64;
MATRGSRSEK VKRIFQQFDG NRDGGLNREE MAALVVAVNP RVKFSDEQIN AILDEVFRTY
AEFIDPAKGL TYDGLLRTYD DGAGDVDRDF DALGLELNPE ETIIAKGGSE AASSSSIADE
RAVEAQKKQR TAAWAVSPNH GIVFDDTWKL VDDLEILIKR LKSKQEKVNN NSNNSNNNNA
DAFSDAGWSR ELGPSTELSD KRIYWEESSH DYNVFVKELG VLRSKADGAR SREEAFDGHM
AIGRVLYEHQ LFKEALVSFK RACELQPTDV RPHFKAGNCL YVLGKCKESK EEFLLALEAA
ESGGNQWAYL LPQIYVNLGI SLEGEGMVLS ACEYYREAAI LCPTHYRALK LLGSALFGVG
EYRAAVKALE EAIYLKPDYA DAHCDLASSL HSMGEDERAI EVFQRAIDLK PGHVDALYNL
GGLYMDLGRF QRASEMYTRV LAVWPNHWRA QLNKAVSLLG AGETEEAKRA LKEALKLTNR
VELHDAVSHL KHLQKKKKGK KNGNGNGGEG GPFIVVEASK FKTVGEKTTL RPDLATALQV
RAFQKVTRLG KCDVEGLRKE MRDNDVPVSY SGSGGPTKSI RKPNLEEILR RLLISLKPET
FQGAIKAINE RILSVLDDSG SGRVDMGMFY AVIAPLCGGH SDKRKRVAFE ALLWRPVNEG
SSQITKTDAD KYIKLLRAIY IPSHGMSEML EVHGEEGGDS SVTVTFNQFL AMFDDPDWGF
GIMSTILKLE GNDRNRHGNH VCSVCRYPVI GSRFKEVKAR FSLCNQCYSE GKVPPSFKQE
EYKFREYGSE AEAMKAKCDC DVKQKSELSP LDVLRATILI NPNSPIAYRQ FSGRGMKIQP
GKKAIHPFNE VDNVEEDGDD ESSSDGKRLW EIREKEDQKW IDEHETEDGD LDHLNNVITE
TAEPPPDLII PLLRYQKEFL AWATKQEQSA VRGGILADEM GMGKTIQAIS LVLARREAAR
ALFRETMGLT LVICPLVAVS QWSDEIERCT SPGSAKVLVY HGAKKVKNAE EFKKYDFVLT
TYSTLESGYR GCIVEKPIFH SIRWNRIILD EAHNIKERRS KTARAVFALE AKYRWALSGT
PFQNNIGELY SLVRFLQIRP YSYYLCKDCD CELLDFPTNS RCQCSDNAWR HFCWWNKNFV
NMIKGNAERI KRAMIFLKHK ILKDILIRRT KLGRSADLAL PPRIITLRRD ALDIKEFDYY
ESLYKQSQAQ FNTYVEAGTL MTNYAHIFDL LTRLRQAVDH PYLVVYSQSS GANANLNDEN
KKESECGLCH EPAEDSVVTS CAHVFCKACL IDFSASLGKV SCPTCSKLLT MDLTTNADTE
QQAESKTTLK GLRASSIMNQ LKLDDFQTST KIEALREEIR LMVERDRSAK AIVFSQFTSF
LELIDYTLGK CGVSCVQLVG TMSKAARDVA INKFREDPDC KVFLMSMKVG VVALNLTVAS
HVFIMEPWWN PAVERQAQDR IHRIGQYKPI RVMKFIIENT VEERILKLQK KKELLFETTV
DGSQRGIGKW TSEDYKFLFT T
//
