ID S8E1A8_9LAMI Unreviewed; 1173 AA.
AC S8E1A8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Chromatin remodeling complex subunit {ECO:0000313|EMBL:EPS69408.1};
GN ORFNames=M569_05357 {ECO:0000313|EMBL:EPS69408.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS69408.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS69408.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPS69408.1}.
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DR EMBL; AUSU01002133; EPS69408.1; -; Genomic_DNA.
DR AlphaFoldDB; S8E1A8; -.
DR OrthoDB; 8175at2759; -.
DR Proteomes; UP000015453; 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; cd18070; DEXQc_SHPRH; 1.
DR CDD; cd15517; PHD_TCF19_like; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR048686; SHPRH_helical_1st.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45865:SF1; E3 UBIQUITIN-PROTEIN LIGASE SHPRH; 1.
DR PANTHER; PTHR45865; E3 UBIQUITIN-PROTEIN LIGASE SHPRH FAMILY MEMBER; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21325; SHPRH_helical-1st; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 451..644
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1173 AA; 133462 MW; A77920C4C29590F2 CRC64;
MGRRKQVRPR RSGGIAVERQ VPETELKEED NDGDPKLGKF FNPEEPFYVE IDKSLMVSEE
HHLDISEILL LNVNVNQEFV GCKLTEELFM DPNLFLRFKS INVNAHLGRM KLGHWPALSE
KNTCLEFLMR SNVEGVLKNL VMLSGIIDGT GEGVTGLVHL CSLKYFALRP IFAVELSDSL
LSVRIRVEIL SNLFDQCESL LDNTRHPWKK SVVNVMTWLR PEVVTSETRY GCSSVDGDSF
PTEQVRFEVS RFYEAIKPSK QAPMLEDELP DMVPELRPYQ RRAAYWMVQR EKAGDEVFNG
NATTCAVSPL CVPICLIDTP RRIYYNPFSG NVSLDAKCSS AYVSGGILAD EMGLGKTIEL
LACVLANQMP SSEVPVYLQT EKIPRKSFSR LKRERVECLC GAVAESFKYE GLWVQCDVCD
AWQHADCVGY APERRNRRSV DRDKWQIGNS SRKRKSRKKE IELVEMDGEF TCQTCTALIQ
ATEPAVATGA TLIVCPTPIL SQWHSEILRH TKKGALKTCV YEGVRSTSFS DVPAVSIDDL
LNADIVLTTY DVLKEDLPHD SERHEGDRRF MRFMKRYPVI PTLLTRVLWW RVCLDEAQMV
EGSAAAATEL ALRLHAKNRW CITGTPIQRE LDDLYGLLRF LQSSPFDVFR WWSDVISGPY
ERGDAAAIRF THDFFKQLMW RSSKSHVWDE LELPPQEECI SWLSFSPVEQ HFYRRQHETC
VDDARMVLES FNKEKNSDVA KSDSSVQPFI TASEAAKLFN SLLKLRQACC HPQVGSSGLR
SWQKSPMTME EILSMLIGKT KLEGEDALRK IVVALNGLAG IAMIKKDTSE AVSLYREALN
LVEENADDFR LDPLLDIHIH HNLAEASSIF PEACDAVEME KAHRNSPEEL NSSAHIERLK
TSCEDLKQKY LTVYNSKLSV ARQEFRKLYE QVCDGFLKRK IQQATWWLDA LHRIDEAEDL
SRSLFQKIGE ALSSGNLNNK RSRASAGSFG SITSLKYYIQ TGLDALYESR STLLDRLLEL
DETMENPTEA DIVLVRYCRN CNSDSDGPVC THCELDEVFR VYEARLFRLN KSNNGETVMS
AEEAVNLQKK KSALNQFYWS LSRENDRIPD FSSSEDHKDD GKKRDAAEKV MTSKSPSDLE
IMLTIIRNVS KGFFSGRETI STSRNHLDLL QVM
//
