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Database: UniProt
Entry: A0A0D2TRD9_GOSRA
LinkDB: A0A0D2TRD9_GOSRA
Original site: A0A0D2TRD9_GOSRA 
ID   A0A0D2TRD9_GOSRA        Unreviewed;      1391 AA.
AC   A0A0D2TRD9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Helicase-like transcription factor CHR28 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_009G171000 {ECO:0000313|EMBL:KJB57576.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB57576.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB57576.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008438}.
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DR   EMBL; CM001748; KJB57576.1; -; Genomic_DNA.
DR   STRING; 29730.A0A0D2TRD9; -.
DR   EnsemblPlants; KJB57576; KJB57576; B456_009G171000.
DR   Gramene; KJB57576; KJB57576; B456_009G171000.
DR   eggNOG; KOG1001; Eukaryota.
DR   Proteomes; UP000032304; Chromosome 9.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; cd18008; DEXDc_SHPRH-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; 3.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF16; SNF2 DOMAIN-CONTAINING PROTEIN _ HELICASE DOMAIN-CONTAINING PROTEIN _ ZINC FINGER PROTEIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 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; 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:UP000032304};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          731..913
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1066..1105
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1199..1381
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          43..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          680..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1180..1199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..725
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1391 AA;  153373 MW;  F7571AE10631AF0E CRC64;
     MMMTGEDNYN GSSGFLSTGY PSADFEFDGL SIDLDDFNRI LEETPGSLQS NPEDPSFRNM
     SQGESAPETN QFQSELLSSE FAFGDLLRYP SEASVARAGS LGGLFDYHRE LEPPAHDSLV
     QTSSASFQDF FSTGKGTSCM ERGQMSVLQI SSCSTESSFA EIDHNLVLDH GDNLNFDLVD
     NRNGTESKNI AEEFDNKNAL HDLSVENMNF VFDNCGAILT NTLETPEAPE NEVAMPMEFS
     SVDANLTSHN VTSNESSFCH GSDIVSDVSD PCSVLPNCMN GDVGYFAHSS MHCWYNSSNF
     MFKESKEGEV IEFPTESACS SSRMIFHDQG RTNNGSVPQL SLTDFSDVKQ QHFDVKGNGH
     ILSACGKLSY TANDRLFDDN GSVQPFNRIA FCAKNEYDKF VTPGNIFCNS TEGFDRAGWS
     KSISRVDSLE ESKQFLSDVP PISKKVLMVN GKDAHHSHQD INLTVSSQTS LGGVHLEQYL
     PSSHPITSSM VHFGCFEHEK RSTLIPSRSI GLSKVSPESI HSTSSDCRSH VDNDPDICIL
     EDISQPARSH QSLVLVKKTP SLPNVAFSNP HQNSGMGGIR LKGNDERLIF RVALQGLSQP
     KSEASPPDGV LTVPLLRHQR IALSWMTQKE KAGSHCWGGI LADDQGLGKT VSTIALILNE
     RPPSSRASSQ DMTKVGMEML NLDDDDDDDK DDVGDEEGRK QESDSSQVMS NGASNKSSSP
     SGQAKGRPAA GTLIVCPTSV LRQWAEELHN KVTSKANLSV LVYHGSNRTK DPFELAKYDV
     VITTYSIVSM EVPKQPPACG DDDEKGKWES ENASSNDFPE SRKRKCPSSS NKKGVKHKKG
     ADELLLDSVS RPLAKVGWFR IVLDEAQSIK NHRTQVARAC WGLRAKRRWC LSGTPIQNAI
     DDLYSYFRFL RYDPYAVYKS FCSAIKIPIS KNPAKGYPKL QAILQTIMLR RTKATLLDGK
     PIINLPPKVI ELKKVEFTEE ERDFYSRLES DSRAQFKEYA AAGTVKQNYV NILLMLLRLR
     QACDHPLLVR GFDSNSSQRL SIETAKKLPQ ERLTFLLSCL SSLSLCGICN DPPEDAVAAV
     CGHVFCNQCI SEHLTGDDYQ CPTANCKVRL GASSVFSNAT LNSSLTELPS RETSLNSSGS
     KVAEVIGPYS EDSLYGSSKI KAALDVLKSL AKPQDDRLKI SGCPEGSSGL QSGDSPNGYH
     EEKIPVTGES LNGSSKVLGE KAIVFSQWTR MLDLFEACLK SSSIQYRRLD GTMSVASRDK
     AVKDFNTLPE VLMASYFVLC FFFFYHEVSV MIMSLKAASL GLNMVAACHV LLLDLWWNPT
     TEDQAIDRAH RIGQTRPVTV LRLTVKDTVE DRILALQHKK REMVASAFGE DETGVRQSRL
     TVEDLEYLFM A
//
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