ID T1KYH1_TETUR Unreviewed; 2187 AA.
AC T1KYH1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:tetur27g00660.1};
GN Name=107368552 {ECO:0000313|EnsemblMetazoa:tetur27g00660.1};
OS Tetranychus urticae (Two-spotted spider mite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC Tetranychoidea; Tetranychidae; Tetranychus.
OX NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur27g00660.1, ECO:0000313|Proteomes:UP000015104};
RN [1] {ECO:0000313|Proteomes:UP000015104}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA Rombauts S.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:tetur27g00660.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; CAEY01000713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015791886.1; XM_015936400.1.
DR STRING; 32264.T1KYH1; -.
DR EnsemblMetazoa; tetur27g00660.1; tetur27g00660.1; tetur27g00660.
DR GeneID; 107368552; -.
DR KEGG; tut:107368552; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_000192_2_2_1; -.
DR OMA; KYQAANM; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000015104; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd20818; C1_Myosin-IX; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd01779; RA_Myosin-IX; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF5; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 2.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000015104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 4..122
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 155..926
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1441..1497
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1740..1789
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1804..1992
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 808..830
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1043..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1508..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2136..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2158..2187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2187 AA; 248114 MW; 7EC74268D9DEEE5C CRC64;
MSNDRFVLQV YVGAFSRLYE ALSIEASKQT TTEEIIECIA EKLSLRDANS YELAEVILGH
EGEDCKERRI GPSECPVALQ LLWPLNPKCN NNQGIPKDGK NKDIFSGFIG PEYRFCLRRK
IMQQCMNWSF SWTDSNDSQL LKDYFLRFLY QPRDREYPDL CQLPDLTEQT LLENLKARFE
KGHIYTYVGS ILIAVNPFKF YPIYNPKYVQ LYQNRRLGDL PPHIFAIADA AYQAMLRKRC
NQCIVISGES GSGKTESTNL LLHHLTALSQ KGSHGSGVEQ TILGAGPVLE AFGNAKTKHN
NNSSRFGKFI QVNYKENGMV HGAVVQKYLL EKSRIVSQAK NERNYHVFYY LLAGADQADK
EVLHLTKASD YFYLNQSKCY TLEGVDEAYE FSRLKQSLEM VGFSREKQRR LYAVLSAVLH
LGNVEFTKKS TYHSDETVMV QNVQAVSIIS KLLMVKEETL LSALTCKKTK AAKGETIIIN
YKMADAVATR DAMAKCLYGA LFDWIVMQVN QALLTKKEPR DHRGNYIGVL DIFGFEDFGD
QNYFEQFCIN FANEHLHHYF NQHVFKYEQE EYRREGINWK SIDFHDNVGC LNLIEGRPQG
LLCLLDDQCN FPGASNSTVL QKFVNHHQNN PLFEVPPCRQ SAFVIKHYAG KVKYQIKDFR
EKNMDLMRPD IVCLLKSSSS AFVRELVGSN PLAIFRWQIL KAFFKSYFVF TKLREQSKQR
RAMNGAGSMN TTSSKSKTCK IGAFEMKQRK NKFIKPNSFR STGSGIEKSI KSLQTLKLIV
GKTNYLPPLG RTGRKQTPTV TAQFQQSLNQ LMETLNQANP FFVRCIKSNA DKIPYHFDDM
LVLVQLRYTG MLETVTIRQS GYSVRLSFDE FIQHYRILLP KGLLSSQADV RHFLERMNLN
RDNYQIGKTK IFMRESEKLA LDDMLHQEIL RRIITLQRWV RTWITRKRFQ QMRQAVVVLQ
THIRRWLAQQ RLNQLKWIAH LEYLAATIIQ RNWRCYYARQ CFLRLRRATV MFQSYARGFI
VRRKFNQDYL DQKSKNHHQV MSSLYGSGQD SHSSHSDEAF LSKGSSQEEL EADRTLSNVQ
HPHRHAVKSV ARKQHSKDSE DSSGVHEDSE PESFHVHENN YLTSQTSDEP PPPLPPRRQP
PPPLIIPAST ERNSYSERPH HFSCYSNTPT SNQPSSLPPA PTSMNSLSHT SPLLSGSSPQ
SLQPISSSSS QQPLKSLQPH QIPLPADKYS LPSPTEDDDK PRLDRRRTRP FRKVSLKRSK
SNKGPVSSVF SESLGGHEKV AKSPSEADIV IVKKPIKEMV SEPCIPSSPS KINPPDSFLS
SEGGRDQKGA FQKAKKHIRT FITGSSSNKT EKKSKAEGEN HQWETENHSI YSTEESHNNQ
TISSQSKSKK SKPSPLYSSL LPTNNSSSTT TPSPTSNTPT PNTTSTTPSG EPLSHYNSLT
RHSLKSVISF QKSDICALCE QVMYQNSSTL VNSGFRCAEC SLLFHTTCLS NANSVPCIDK
SKLALFSSSK MNSPHNPSRP PRNKTRGKSS KNYSSGGNNL SSKHDTMVST GSSLSGSSQA
NGSSNSSSSW NVTRTTEFID PKDILITDVT ELHYMEIFIN NKIMAMEESK KSHAKESMVD
VVFKIALKEF KSNLLSTYSV AVAQDGQLHI AYKNLIDHFG QVIMNVCQKE NTWKSFPVIM
GVNAFRGFLD EFRNLGSKVP PEDTKAKSKR RKRGGGTSGN NSSGSGKKKE SREEFILKCD
HKFTSMMANI PTVCEVCSTL MWLTEKIWVC QGCKFTCHKK CTSKVTVSCR DKTLLQQGKK
LFGAPLERLV SDEIKMPTVL ENLITAIELR GLYTEGIYRK SGTTSKINEL KAKLEDNIET
VDLDSYSVHV LTAVLKSFFR EMPNPLMTYQ LYDDFLWTTA ISDPSERVQA IYSHIAKLPR
ANYDVLERLI FHLARVAQQE AANRMNANSL AIVFAPCILR TDKLMQMQDK LSDISKQTKC
IETIINDRLK QVKDTLADIE MLDSVYHTTS SRLSSLKMSK SQPIRDNAGQ TSRNSQQDEE
EVLTQQIDIL RHEKAHLTNI LPTFNLVSAG SDDDLLSTGT ELESSLGTSL DEVSLYSNTK
IPVSVRNTNL DFPSLPSQPL NLNHLTKSRV SQVPLNRRLP SRFSKPVRGG PSPRIGRSPV
RRRKDQVKDS QREGMRVYRN DDNSVRV
//
