ID W9T2P6_9ROSA Unreviewed; 1421 AA.
AC W9T2P6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=SMARCA3-like protein 2 {ECO:0000313|EMBL:EXC53897.1};
GN ORFNames=L484_002467 {ECO:0000313|EMBL:EXC53897.1};
OS Morus notabilis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC53897.1, ECO:0000313|Proteomes:UP000030645};
RN [1] {ECO:0000313|Proteomes:UP000030645}
RP NUCLEOTIDE SEQUENCE.
RA He N., Zhao S.;
RT "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; KE625670; EXC53897.1; -; Genomic_DNA.
DR RefSeq; XP_010107056.1; XM_010108754.1.
DR STRING; 981085.W9T2P6; -.
DR GeneID; 21386036; -.
DR KEGG; mnt:21386036; -.
DR eggNOG; KOG1001; Eukaryota.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000030645; Unassembled WGS sequence.
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; 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; PF13923; zf-C3HC4_2; 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:UP000030645};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 676..950
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1104..1140
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1257..1416
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 53..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 157182 MW; 619BB2D42F121627 CRC64;
MEDENSIFGM EGNTESLEQS NGFVDEFADH DLFEGGDLSI DLDMLFGIID EERDKKDSDP
SQNCSEFSLK NASQGEAVPS ASHHDSACPE NDLMGPSTLH PSYNSEALDS MKGTPIVAEN
DLVGPSTFHP SYNSEASDSM TGVSGGSFGS AMNQNLIFDS RVQRSPVNAW SASLKDWISL
APSDETYLSE RASFSLPTSG TSSNFPQRDA NNSSDFLDKF NSTLQGVTEI QIRNNGAEIS
RQGALEYPGS KNIGINFCKN ETFGQNIMDI VGPPTDNLHT SAEIPFMGAD MRLGDIACKD
SAICPNTQIM SDYSSTQCNV GIDYHFHNSY NSQFFTINEE LKNSVKDEEG EFPAESTCSS
TKMKLNGHFG ENGKSSLGFS TSNYMDIEGC HYGYEGNDYV PSMGCSWFDA DGCPVDDKAV
MQPWGCAQSY ICSEENVKDE KPEEVVAPSI SMWHSVDVID EAVSREHSYS ADNKSFGEDL
RSSFFGISSS LSGQKTEHQM DDKEDHVTYK KVCRSPDNIN GRLTMYNSNG NLKIDASEQY
MPFAQPFSSI GNQSMCVMGP RISKVSPESS HSNFSEKSVV EDDSDICIIE DISHPAPSNQ
SLVPRNMLVT SQSSAISDNY VNVGGMRFKA KDERLILRLL QDLSQPKSET NPPDGVLAVP
LLRHQRIALS WMVQKETDSA HCSGGILADD QGLGKTVSTI ALILKERPPS FKACHVKQDE
TETLNLDEDD VMLSASNGMK EESDPLQVVS NETPIRSKNS SMLAKGRPAA GTLIVCPTSV
LRQWDEELRN KVTQKANLSV LVYHGSNRTR DPCELAKYDV VLTTYSIVSM EVPKQPCVNE
DDEEKGKSED HGFSMGLSSS KKRKYPLSSN KKRSDKKGLD SALLDNARPL AKVGWFRVVL
DEAQSIKNHR TQVARACWGL RAKRRWCLSG TPIQNAIDDL YSYFRFLKYD PFDAYKLFCT
YIKTPISKNP STGYRKLQTV LKTIMLRRTK GTLLDGEPII SLPPKFIELK RVDFSEQERD
FYSQLEADSR AQFQEYAAAG TVKQNYVNIL LMLLRLRQAC DHPFLVKGID SHSLLSSSVE
MAKKLPQDEK EHLLKCLEGS LAICGICSDP PEDAVVAKCG HVFCNQCICE HLTGDDHQCP
NTNCKARLNR YIVFSKATLS SPLHDQSSHD SSRDCTGLEV IQTGESCHEG HFKSSKIKAA
LDVLQSLCGP HDSSSGNSST LNSSDENASS VENSLATCAV EPLKDVPDNR NLEAEEGTNS
SIKVVGQKAI VFSQWTRMLD LLEGCLKHSC IKYRRLDGTM SVTARDKAVK DFNTLPEVSV
MIMSLKAASL GLNMVAACHV LLLDLWWNPT TEDQAIDRAH RIGQTRPVTV LRLTVRDTVE
DRILSLQQKK REMVASAFGE DEMGGRQTRL TVEDLKYLFM T
//
