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Database: UniProt
Entry: A0A0D2STC1_GOSRA
LinkDB: A0A0D2STC1_GOSRA
Original site: A0A0D2STC1_GOSRA 
ID   A0A0D2STC1_GOSRA        Unreviewed;      1325 AA.
AC   A0A0D2STC1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Helicase-like transcription factor CHR28 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=B456_010G151100 {ECO:0000313|EMBL:KJB66663.1};
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:KJB66663.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB66663.1, 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; CM001749; KJB66663.1; -; Genomic_DNA.
DR   RefSeq; XP_012449724.1; XM_012594270.1.
DR   STRING; 29730.A0A0D2STC1; -.
DR   EnsemblPlants; KJB66663; KJB66663; B456_010G151100.
DR   GeneID; 105772812; -.
DR   Gramene; KJB66663; KJB66663; B456_010G151100.
DR   KEGG; gra:105772812; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   OrthoDB; 11932at2759; -.
DR   Proteomes; UP000032304; Chromosome 10.
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; 2.
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          593..864
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1017..1056
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1152..1320
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          47..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..789
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1126..1168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..677
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..771
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1126..1146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1325 AA;  146145 MW;  EC150EF99D014512 CRC64;
     MLMMGEDNRN DSFGILSSGD LSADYKFDDF VGDGMCIDLD SINRILEENS DPPQINPEDP
     SLRNMSQGDS DLESIQFQSE SPCSGFTFAD CLRNNSDDSD ARAGSTGGSF YYHGNLELSA
     HDCSPVQTSS ASFKEWSAIC QGTSYRERVE IPSCSTASSF SEIDGNHALD HGDNLRFDLV
     DDKTSSLFMN TKEEFGYKNA LHSPVDENTN LIFDQYDPCS VISCYVNGDD AYFADSSMQH
     SPGSLNFMFE ESKEGEVVEF PTESACSSSR IIFNSQGEID NRSVSQLSMN GFSDVKKLHF
     EGEGNGHVAY GKFSYTANDG LFDDKGSLQP FTHSKPCILN NKQAVYGKNE DNELITSGNI
     FSHSAESLDE ASWRKSTNRV AESLSLDEAS KQSSDIYPSV SNQDFMVNGK DAHHYNHDIN
     LNVSSQSFFS EGHLNLTSPE NYFSSAYPIS STKMQLGCFQ DERENKFIPS RSMGLSKVSP
     ESIHSNSSDC RSYVDDDPDI CILEDISQPA RSNQSLVLVK KTSSLPNTAS STQLHNPGIG
     GIRLKGNDEQ LIFRVALQGL SQPKSEASPP DGVLAVPLLR HQRIALSWMT QKEKTGLHCM
     GGILADDQGL GKTVSTIALI LNERPSSSKA SSQDVRKVEL ETLNLDDDEE MKQDSDNSHV
     MSNGASKKSS SPSGQAKGRP AAGTLIVCPT SVLRQWADEL HNKVTKEANL SFLVYHGSNR
     TRDPLELAKY DVVLTTYSIV SMEVPKQPPV QGDDDEKGKL EGDRASSLDF PPSRKRKYPP
     SSNKKGAKHK EVDDLLLDSA ARPLAKVGWF RIVLDEAQSI KNHKTQVARA CWGLRAKRRW
     CLSGTPIQNA IDDLYSYFRF LRYDPYAAYK YFCSSIKIPI AKNPAKGYPK LQAILQTIML
     RRTKATLLDG EPIINLPPKV IELRKVEFTK AERDFYSRLE SDSRAQFKEY AAAGTVKQNY
     VNILLMLLRL RQACDHPLLV RGFDSNSSWK LSIETARKLP QEKLTFLLSC LSSLELCGIC
     NDPPEDAVVT ICGHVFCNQC ISEHLTGDDK QCPTKNCKGQ LSASSVFSNT SLNSSLSEQP
     GEDKSLDCSG SKVVEVIGPC SEDSLNDSSK IKAALDVLKS LAKPQDNRLR TSGCPEGSSD
     LQSPDSLNGL PDGKDLVMGA SSNDSSKAPG EKAIVFSQWT RMLDLFEACL KSSSIQYRRL
     DGTMSVAARD KAVKDFNTLP EVSVMIMSLK AASLGLNMVA ACHVLLLDLW WNPTTEDQAI
     DRAHRIGQTR PVTVLRLTVK DTVEDRILAL QQKKRKMVAS AFGEDETGGR QTRLTVEDLE
     YLFMA
//
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