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Database: UniProt
Entry: A0A2U1QJ10_ARTAN
LinkDB: A0A2U1QJ10_ARTAN
Original site: A0A2U1QJ10_ARTAN 
ID   A0A2U1QJ10_ARTAN        Unreviewed;      1620 AA.
AC   A0A2U1QJ10;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=IQ motif, EF-hand binding site {ECO:0000313|EMBL:PWA97996.1};
GN   ORFNames=CTI12_AA024570 {ECO:0000313|EMBL:PWA97996.1};
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:PWA97996.1, ECO:0000313|Proteomes:UP000245207};
RN   [1] {ECO:0000313|EMBL:PWA97996.1, 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:PWA97996.1};
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 TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class XI subfamily.
CC       {ECO:0000256|ARBA:ARBA00008049}.
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:PWA97996.1}.
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DR   EMBL; PKPP01000090; PWA97996.1; -; Genomic_DNA.
DR   STRING; 35608.A0A2U1QJ10; -.
DR   Proteomes; UP000245207; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR   CDD; cd15475; MyosinXI_CBD; 1.
DR   CDD; cd01384; MYSc_Myo11; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   InterPro; IPR002710; Dilute_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR037975; MyosinXI_CBD.
DR   InterPro; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF792; MYOSIN-9; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000245207}.
FT   DOMAIN          98..147
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          152..826
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1250..1562
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          707..729
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1087..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1156..1182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1620 AA;  183935 MW;  3445E23BAB1EAAF2 CRC64;
     MRKSKAWEIV VEGMKNLASK CQISSIIRRY IVSWLQRLKI AQGLFSAKLV VVSLEAVLKA
     SQVIIDPFEK VPSMQLHHLS CYSQHFCKAK LAAPVNIILG TQVWVEDPNV CWIEGVVTKI
     TGQEVEVETT DGKKVVTNLS KTYPKDVDAP AGGVDDMTKL SYLHEPGVLQ NLSTRFQLNE
     IYTYTGNILI AINPFQRLTH LYETHMMEQY KGAPLGELSP HVFAIADVAF RAMIREGKSN
     SILVSGESGA GKTETTKMLM RYLAYLGGRK GTEGRTVEQQ VLESNPVLEA FGNAKTVRNN
     NSSRFGKFVE IQFDKHGRIS GAAIRTYLLE RSRVCQISDP ERNYHCFYLL CAAPPEEIEK
     YKLGDPKSFH YLNQSNCYQL VGINEAQDYL ATRRAMDVVG ISDKEQEAIF RLVAAILHLG
     NVEFIKGKEV DSSLLKDEKS KFHLKMTAEL LTCDRAALED ALLKRVMVTP EEVIKRSLNP
     EAATISRDGL AKTLYSRLFD WLVNKINMSI GQDPNSKSLI GVLDIYGFES FKLNSFEQFC
     INFTNEKLQQ HFNQHVFKME QEEYTKEQID WSYIEFVDNK DVLELIEKKP GGIIALLDEA
     CMFPKSTHET FSQKLYQTFK SHARFVKPKL SRSDFIISHY AGEVQYQSEL FLDKNKDYVV
     PEHQDLLMAS KCSFVAGLFP PIPEETNKSS SKSAKFSSIG SRFKLQLQSL METLNSTEPH
     YIRCVKPNNL LKPSIFENAN IMQQLRCGGV LEAIRISMAG YPTRKSFFDF LNRFSLLAPE
     VLGGNLDAKD ACKKIIDKMG LQGSQIGKTK VFLRAGQMAE LDARRAQKLN TAAKKIQRKI
     RTHITRNRFL ALRKASISMQ SLCRGKLGTK LFEHMKRQAA SLKIQKNYRR HSFWMWYKKL
     KLSVIVLQTG MRAMAAHSAF RHKKTTKAAL LVQANWHRHR DFKYYKNLMR SALVTQKRWR
     GRAARKELRK LKMAAKETGA LQEAKDKLQK QVEDLTWRLQ LEKRLKTDLE EAKGHEIQKL
     QNSLQAMQAK VDETTELLTK ERESAQKAIQ EASAIVEETA PIHVEDTEKI DKLSAEVEQL
     KNLLESEKKR ADESEKKCTE ALESSESKQL KLDETVNRAN QLQESMNRLE EKLSNIESEN
     KVLRQQALDM AESAKLQATR SKSTRLQRSE SQKIQSVDLH SPSMQMRDAD VEERPQKSLN
     EKQQEYQDLL IRCIAQNLGF AKGRPVAACI IYKCLRQWRS FEAEKTSIFD RIIQTIGQAI
     ETQDNNETLA YWLSNASTLL LLLQRTLKAS GSAGAQQHRR PTSASLFGRM TQSFRGTPQD
     VNISLIDGGT AGASDTLQQV EAKYPALLFK QQLTAYVEKI YGMIRDNLKK DISPLLGLCI
     QAPRISRANL LKGTAVALAS AASQDILIAH WQGIVNNIGC SLNMLKSNNV PPFLVRKIFT
     QIFSFINVQL FNSLLLRREC CSFSNGEYVK AGLSELEHWC YKATEEYAGS AWDELKHIRQ
     AIGFLVIHQK PKKTLDEISH DLCPVLSIQQ LYRISTMYWD DKYGTYSLSH DVISNMRVLM
     TEDSNNAVSS SFLLDDDSSI PFSVDDLSKS KDQINIADIE PPPLIRDNSG FSFLLLRAET
//
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