ID C5X9Y6_SORBI Unreviewed; 857 AA.
AC C5X9Y6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EER97282.1};
GN ORFNames=SORBI_3002G315100 {ECO:0000313|EMBL:EER97282.1};
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:EER97282.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER97282.1, 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).
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; CM000761; EER97282.1; -; Genomic_DNA.
DR RefSeq; XP_002460761.1; XM_002460716.1.
DR AlphaFoldDB; C5X9Y6; -.
DR STRING; 4558.C5X9Y6; -.
DR EnsemblPlants; EER97282; EER97282; SORBI_3002G315100.
DR GeneID; 8077499; -.
DR Gramene; EER97282; EER97282; SORBI_3002G315100.
DR KEGG; sbi:8077499; -.
DR eggNOG; KOG1002; Eukaryota.
DR HOGENOM; CLU_000315_2_10_1; -.
DR InParanoid; C5X9Y6; -.
DR OMA; YFCKQCD; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000000768; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
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:SF12; DNA REPAIR PROTEIN RAD16; 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:UP000000768};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 168..433
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 604..644
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 687..847
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 95887 MW; 4222D52AF7CAF135 CRC64;
MPRRGSSSGR RRRRDEEDED DLPSDDTSDA DFVVDSGDEA EEDDDDGSDG EGFVPDDDAP
PAPAVPEMAM APPVPAMAPP VPIRIRNQAP GRRRGKKARD HEPPLPWEEW EVANESWLDA
LDAAEGDRDG DGEATEAAPA AVPTADPAPE VVLSLLRFQK EWLAWALAQE ASVSRGGILA
DEMGMGKTIQ AISLVVTARR LRPPDNHAAS SSTSSVGRPK VGCTLVVCPV VAVIQWTEEI
ERHTESGSVR VLIYHGAKRG AQKLDFNSYD FVITTYSTIE VDYRKHIMPP KIRCQYCSRL
FYPNKMKVHL KYHCGPNAIR TEAQAKQQSK KRDSSKGKVR RNRRVHKKGD ESNMDSQELP
DESGSQSRGQ SPLHSVRWER IILDEAHFIK DRRSNTARAV FELESEYKWA LSGTPLQNRV
GELYSLIRFL QIFPYSNYFC KDCSCEILDT SMKKQCDCGH SSVRHFCWWN KYISTPIQYG
STTFEGKRAM TLLKEKVLKG IVLRRTKKGR AADLALPPKI VTLRRDSFDK NEMEFYEALY
TQSVTQFDAY VVAGTLMNNF AHIFDLLTRL RQAVDHPYLV AYSKTAEHPE GMKNEGNDTM
ESQCGICHNL AEDVVVTSCD HAFCKTCLID YSAALGNVSC PSCSIPLTVD LTAQNSAGKV
TQSVKGRKCS GILSRLPSLV DFKTSTKIDA LREEIRNMIE HDGSAKGIVF SQFTSFLDLI
QFSLEKSGIK CVQLNGAMNI TEKGRAIDTF TRDPDCRIFL MSLKAGGVAL NLTVASHVFL
MDPWWNPAVE SQAQDRIHRI GQFKPIKSTR FVIGDTVEER ILQLQEKKHL VFEGTVGDSP
DAMSKLTEED LKFLFQI
//
