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Database: UniProt
Entry: A0A194YHQ5_SORBI
LinkDB: A0A194YHQ5_SORBI
Original site: A0A194YHQ5_SORBI 
ID   A0A194YHQ5_SORBI        Unreviewed;      1324 AA.
AC   A0A194YHQ5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Homeodomain-like transcription factor superfamily protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SORBI_3010G065300 {ECO:0000313|EMBL:KXG19483.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG19483.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:KXG19483.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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DR   EMBL; CM000769; KXG19483.1; -; Genomic_DNA.
DR   STRING; 4558.A0A194YHQ5; -.
DR   EnsemblPlants; KXG19483; KXG19483; SORBI_3010G065300.
DR   Gramene; KXG19483; KXG19483; SORBI_3010G065300.
DR   eggNOG; KOG0383; Eukaryota.
DR   InParanoid; A0A194YHQ5; -.
DR   OMA; MINMDST; -.
DR   OrthoDB; 2910821at2759; -.
DR   Proteomes; UP000000768; Chromosome 10.
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; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000000768};
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          55..101
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          103..183
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          197..257
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          292..479
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          607..767
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          19..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1287..1324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          161..188
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          830..857
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        875..894
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..912
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1303..1317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1324 AA;  152330 MW;  48A22B9A51AD48F9 CRC64;
     MSSLVERLRV RSERRPRYAL DESDDDLPLR AVAGKGKDRQ NDAPAERIER EDAKEEACQR
     CGKSDNLVSC STCTYAFHRK CLVPCLNITS DKWSCPECIS PLTEMERILD IEVLEAPQED
     SSSTEPRSKK AERYLIKWKG LSYIHCSWVS EKEYSEAANI HPRLRTRLNN FRRQKEAMKK
     EAERSGEDIV AIRPEWTTVD RILSSRKNSG GEREYYVKWN ELTYEECTWE NESDISAFQP
     EIERFNEIQS RRKKSGDKAK ATREPRQFKE SPTFLSCGTL HPYQLEGLNF LRYSWFHNKR
     VILGDEMGLG KTIQSIAFLA SLFEDKFGPH LVVAPLSTLR NWEREFATWA PQMNVVMYFG
     AAASRDIIRK HEFYYPKEKL KKLKKKKSSP SNEEKKQSRI RFDVLLTSYE MINMDSNVLK
     NIEWECLIVD EGHRLKNKDS KLFGQLKDYN TKHRVLLTGT PVQNNLDELF MLMHFLEGES
     FGSITDLQEE FKDINQDKQI EKLHGMLKPH LLRRFKKDVM KELPPKKELI LRVELTSKQK
     EYYKAILTKN YEVLARRNGG HTSLINVVME LRKLCCHGFM IDEPDFEPAN PEEGLRRLLD
     SSGKMQLLDK MMVKLKEQGH RVLIYSQFQH MLDLLEDYLS YRKWSYERID GKISGAERQI
     RIDRFNAKNS TRFCFLLSTR AGGLGINLAT ADTVIIYDSD WNPHADLQAM ARAHRLGQTS
     KVMIYRLVSR GTIEERMMQL TKKKILLEHL VVGRLTKASN VNQEELDDII RYGSKELFDD
     ENDESRQIHY DEAAIERLLD RDQVDGDESV EDEEEDEFLK GFKVANFEYI DEAKAQAERE
     EEARRKAAAE AENSERLNYW DELLKGRYDV QKVEEHTAMG KGKRSRKQMA AADEEDIDLS
     TEDEDYSLED DVSDNDTTLQ GNISGKRGQY SRRKSRNVDS IPLMEGEGRT LRVLGFNHAQ
     RAMFLQTLNR FGFQNYDWKE YLPRLKGKSV EEIQRYAELV MTHLVEDIND SENFSDGVPK
     EMMRVDDVLV RIANITLIEE KVSATGPGKI TSIFPNYLLY EFQGLSGGRI WKAEHDLLLL
     RGILKHGYAR WQYISDDREN GLFEAARREL NLPSANEIIQ SNTEANGNLE GAQEVQVNST
     SMSHYKEIQR KIVEFLRKRY HLLERALNLE YAVIKNKIPV PDDITEQGVP AGHVPLLPDI
     SELLRELPNL EPISTNEVAP EGTAGQSEVP HLYNKMCGVL EESGGSAISS FFGDKSASSS
     LANSLHQFEI VCENVIEALR PQQNGTASAI KEEVVDPATK AAAAPQQDSN GQSSTAKADM
     EIDG
//
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