ID A0A200QAD0_9MAGN Unreviewed; 1086 AA.
AC A0A200QAD0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=SNF2-related {ECO:0000313|EMBL:OVA07399.1};
GN ORFNames=BVC80_8825g6 {ECO:0000313|EMBL:OVA07399.1};
OS Macleaya cordata.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Papaveraceae; Papaveroideae;
OC Macleaya.
OX NCBI_TaxID=56857 {ECO:0000313|EMBL:OVA07399.1, ECO:0000313|Proteomes:UP000195402};
RN [1] {ECO:0000313|EMBL:OVA07399.1, ECO:0000313|Proteomes:UP000195402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BLH2017 {ECO:0000313|Proteomes:UP000195402};
RC TISSUE=Root {ECO:0000313|EMBL:OVA07399.1};
RX PubMed=28552780; DOI=.1016/j.molp.2017.05.007;
RA Liu X., Liu Y., Huang P., Ma Y., Qing Z., Tang Q., Cao H., Cheng P.,
RA Zheng Y., Yuan Z., Zhou Y., Liu J., Tang Z., Zhuo Y., Zhang Y., Yu L.,
RA Huang J., Yang P., Peng Q., Zhang J., Jiang W., Zhang Z., Lin K., Ro D.K.,
RA Chen X., Xiong X., Shang Y., Huang S., Zeng J.;
RT "The Genome of Medicinal Plant Macleaya cordata Provides New Insights into
RT Benzylisoquinoline Alkaloids Metabolism.";
RL Mol. Plant 10:975-989(2017).
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:OVA07399.1}.
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DR EMBL; MVGT01002562; OVA07399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A200QAD0; -.
DR STRING; 56857.A0A200QAD0; -.
DR InParanoid; A0A200QAD0; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000195402; 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; 2.
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:SF24; ATP-DEPENDENT HELICASE ULS1; 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 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:UP000195402};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 352..629
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 783..819
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 911..1081
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 188..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1086 AA; 119280 MW; 0D3B3F9C53A3D682 CRC64;
MGFALHVTHI LSVDITLNHG FNFTDIKILI PMGNYLFKFL ADGEIHSAAM ASMDPIDITS
SDSESEIETK TSAPIRSIPP TYRHLPSWAS TSTLNSKSYG GLSQNLLLPN RASASTERLA
DHNHHSQVKP QLHPSYVDKE KTLNQHTALT DDAKHSTSNW LMGQPGNGLG TKNLDGMIDF
QYANMPGTDS SKVSYQQPSR TLPPSFHSTA STSKLKASFE NGSSSQIPIT HGKSYHSVGA
NITDHQVYGK DHLGRQDNDD VVMYEPSGSR VLPSSLMHGK AHTNSQSAIS SESAHRSGVE
ERPAENDERL IFQAALQHLS QPKVEATLPD GLLAVPLLRH QKIGLAWMFQ KETNSLHCLG
GILADDQGLG KTVSMIALIQ MQKHLHSKST PEDVQAIKTE ALNLDDDDDD GVSELEKVKK
IPESDDLKKV PEVSTAVPSF HSGRPAAGTL VVCPASILRQ WARELDDKVT ESAKLSVLIY
HGSNRTKDPV ELAKYDVVLT TYSIVTNEVP KQPLVDDDDE DTKNGEKYGL SSEFSVNKKR
KKMANAGKKG KKGRNGINGS SFDCNSGTLA RVGWFRVILD EAQTIKNHRT QVARACCGLR
AKRRWCLSGT PIQNSVDDLF SYFRFLKYDP YAVYKSFVSS IKYPISRNSG NGYKKLQAVL
KAIMLRRTKG TLIDGEPIIN LPPKTINLTK VEFSSEERAF YSKLESDSRS QFKAYAAAGT
VNQNYANILL MLLRLRQACD HPFLVKGYHS DSVGAASLEM ARKLPKDTLV NLLNSLEASL
PLCGVCNDSP EDGVVTICRH VFCYQCVSEY LTGDDNLCPA SGCKEQLSAD VVFSKSTLIS
CISDELNGTA TSVSEVAENS LALPCMYGSS KIRAAIEFLE KHCKLTSSST ALISEGCNGS
GTSHSSEANN DVNTTATHLM ENNMDSQTKG PEKAIVFSQW TSMLDLVETA LNHSLIQYRR
LDGTMTLSAR DKAVKDFNSD PEVTVMLMSL KAGNLGLNMV AACHVILLDL WWNPTTEDQA
VDRAHRIGQT RPVTVTRLTV KDTVEDRILA LQEEKRKMVA SAFGEDHMGG PATRLTVEDL
RYLFMV
//
