ID A0A2U1PVZ3_ARTAN Unreviewed; 1094 AA.
AC A0A2U1PVZ3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=SNF2-related, N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CTI12_AA106850 {ECO:0000313|EMBL:PWA89877.1};
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608 {ECO:0000313|EMBL:PWA89877.1, ECO:0000313|Proteomes:UP000245207};
RN [1] {ECO:0000313|EMBL:PWA89877.1, ECO:0000313|Proteomes:UP000245207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Huhao1 {ECO:0000313|Proteomes:UP000245207};
RC TISSUE=Leaf {ECO:0000313|EMBL:PWA89877.1};
RX PubMed=29703587; DOI=10.1016/j.molp.2018.03.015;
RA Shen Q., Zhang L., Liao Z., Wang S., Yan T., Shi P., Liu M., Fu X., Pan Q.,
RA Wang Y., Lv Z., Lu X., Zhang F., Jiang W., Ma Y., Chen M., Hao X., Li L.,
RA Tang Y., Lv G., Zhou Y., Sun X., Brodelius P.E., Rose J.K.C., Tang K.;
RT "The genome of Artemisia annua provides insight into the evolution of
RT Asteraceae family and artemisinin biosynthesis.";
RL Mol. Plant 11:776-788(2018).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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:PWA89877.1}.
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DR EMBL; PKPP01000676; PWA89877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1PVZ3; -.
DR STRING; 35608.A0A2U1PVZ3; -.
DR Proteomes; UP000245207; 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; 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; 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:UP000245207};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 370..627
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 781..817
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 916..1083
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 164..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 123574 MW; B5EA8421AD84F5A0 CRC64;
MDGLVRLLEL AYSAGSVSVI DIMRLGFERE VQEERDWFSF LYGWCVHVAD RVAYLDAIIR
ELEFCSNDVS VAQLVVELRS GDGLVFADSI MYFKTIRDFE AEKLANMQLF LQASGAHLRQ
RMQFLARFNA MCCISVVAWK KQENCRIRYC FLDEVVDLSS LWSGSKTSPH GASTSRTVSS
GGSFDSERKR KMENFGRYPH TLYNSHDRFP TPFNKHCLDK ESPKKASLSY DDTSLKNIKD
EIEREHKVLN NMGPLPPKIS QPEVPITINL DDDDPDICIL EDMSQPPPKK PCQVDKKPNI
SGQWSSPSAP TTPNVSNHTR FEKKDEQSVY RAALQDLAQP TSEATLPDGA LAVPLMKHQR
IALSWMVQKE TKNTHCIGGI LADDQGLGKT ISTIALILKE RPPTSSYVGA TEVKMEKAET
FNLYDVDHDD VTKHDKSNLK VETLIKGAKS RPNAGTLIVC PKSVIRQWYD ELHYKVSAKS
RLSVLIYHGT KKTKDPDELS KYDVVLTTYS IVSNEVPIKA LTEEDYDEDD YESFYRPASS
SNKKRKLSKK LKKGAEKYIL ESSVSPLVKV RWFRVVLDEA HIIKNHRTKV SRACWGLKAK
RRWCLSGTPI QNKIDDLYSY FRFLRYDPYD EIRTFRSTIK NLIKMDPEKG YKKLQAILTT
MLLRRTKGTF IDGKPIISLP TKTVHMKKLH FTDEERNFYT ALEERSRAEF QAFSNAGTVE
QNYASILVML LRLRQACGHP LLVIGSSSAS ELESSLEKAK QLSPEKRNSL LNCLKASLAI
CGICGDPPED AVVTTCEHVF CNQCVLERLS SDDCECPSAG CEALLDPSLV FSRSALGLSD
SDQNMYESSA EPLDHCSSNV TVKAEPVDHY SSNVSVKSEP LDYYISNDGI NSSKFEAARA
LKSSKIKFAM EYIQSIVKPR GITMETSSSS FVGGSVVGEK AIVFSQWTKM LDFLEACLTD
SSIGFRRLDG TMSIPERDKA VKDFNRRPEV SVMIMSLKAA SLGLNMVAAN HVILLDLWWN
PTTEEQAIDR AHRIGQTRPV EVMRLTVEET IEDRILELQK EKRQIVASAF GEDEVGRRQT
RLTVNDLRYL FGFE
//
