ID H2TZM6_TAKRU Unreviewed; 2090 AA.
AC H2TZM6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSTRUP00000030135.3};
GN Name=MYO9B {ECO:0000313|Ensembl:ENSTRUP00000030135.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000030135.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000030135.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000030135.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 STRING; 31033.ENSTRUP00000069697; -.
DR Ensembl; ENSTRUT00000030252.3; ENSTRUP00000030135.3; ENSTRUG00000011915.3.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000156845; -.
DR TreeFam; TF319651; -.
DR Proteomes; UP000005226; Chromosome 20.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd20884; C1_Myosin-IXb; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
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:SF2; UNCONVENTIONAL MYOSIN-IXB; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 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; 1.
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; 1.
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; 4.
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; 1.
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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Membrane {ECO:0000256|SAM:Phobius};
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:UP000005226};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..130
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 162..959
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1702..1751
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1770..1958
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..862
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1043..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1336..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2045..2090
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1158
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255..262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2090 AA; 238254 MW; D47FB62A330E3CBA CRC64;
MSVRDGAATV VTSVAGGGGG GRPASPNNHD GRSYLLQIYP RLAAQPTSCC SLRVHKDATA
ASVISDAAAV LGLDPGRMYV LAEVKESGGE EWVLEPGDLP AQRFLLWPRK AQEQHPQSLG
FYFLLQERNH DGTIHYVHLP SVAKEQEAQQ LTARGFLPPP QDDFADLCNL PVLNEDSILN
NLRTRFCKKK IYTYAGSILI AINPFMFLPI YNPKYVKMYE NHQLGKLEPH IFAIADVAYY
AMLRKKVNQC IVISGESGSG KTQSTNFLIH CLTALSQKGY ASGVERTILG AGPVLEAFGN
AKTAHNNNSS RFGKFIQVNY LESGVVRGAV VEKYLLEKSR LVSREKNERN YHVFYYLLFG
ASEEERKEFK LLPLEEYSYL KQQNFRIEDE EDLCHDFERL QQAMEMVGFL SATKKQIFSV
LSAILYLGNV TYKTKSNGRE EGLEVGPPEV LARLSELLKV KEELLVEALT KRKTVTVNDK
LILPYSHPEA ITARDSMAKS LYSALFDWIV LRINHALLNK KDMEESIPCL SIGVLDIFGF
EDFETNSFEQ FCINYANEQL QYYFNHHIFN LEQEEYQAEG ITWHNIDYTD NVGCIHLISK
KPTGLLYLLD EESNFPHATD ETLLAKIKQQ HQGNKYFVPT PVMEPAFVIQ HFAGRVKYQV
KDFREKNTDH MRSDIVALLR SSDSAYVRQL IGMDPVAMFR WGILRATIRG LAAFNEAGRA
RAAKTSGVVR PASRTPLGEL KQSNAPVDRM YKRVSMLDFY FDHSEERPLE AFEDIFASYE
NKKKQKNAKH RQAIPKSLLD SRSLKFIVGL TLHDRTTKSL LHLHKKKKPP SISAQFQTSL
TKLLETLNRA EPFFIRCIRS NAQKKEMYLD EVLVIQQLRY TGMLETVRIR RSGYGAKYTF
QEFVNQFRVL LPKDTKSFKE DISELLEKKM GLDPATYQIG KTKVFLKELE RQKLQDTLHK
DVMRKIIFLQ RWFRAHLQRK EFLDMRQAAI LIQSSWRRYL KEEQKRRAAT LIQAVWRGHW
QRSENHRKKQ VATKIQALYR GHSARKRCQS LRGEKRRKEE EEKEARKRAE EEEKRRREEE
EEARRQAEEE EERRRIEDEK ARIKAEEEEA KRQAEREEIA RMAEEAENKL VKEPQTREDP
DIELITEEML DDNLTAPETE EEVNTSSHRE DEGVKGEKLD DMEMDLELNG TLAEAGPQLE
ERDGEDDLEN HTPAESDSTS VLSSDGIFTL QPSTTGEEMD KKSLDDTSVC SDADQNRAKP
SAVNKGQLSR SQEKREQRRR RGLEHNQRET ERASSSAGSK DDTSSLKSKT QATRLKERAE
SKELDQYTFV AWKMKEDKAA KKETKTSPAA GPVRPSTLPL QPVSDRNGVS ESTGAVSLQR
RPGAIKEKPE KWRGGRRSDG ELSERTSPQQ PHSKEERRRK TPLSETASSS IDSLSPGSEG
AGALQLNSPS DSLSESSKGG SFRRKHQEGS AHQDSTQSIP STPDRSGGVF SKIFKKRPHK
EAQTPDNGEL TLAQILNERP AGGEAPTSGH PSRPPSQSQG DRAGKALGRN PTIKISRATR
VSEQWNASLD REITNANELR HLDEFLGNQV NDFRTRGKSL SATEAIFVTS TMQFRETIKA
MYSLPKPTIG YKGLMTGYQN KVIHLAGDKQ KGEVKLVVNL FQSVLDGFIR GEMKKEEAEP
AKPAKTRKKR RSKDKSMESP LDHSFTNYQV SIMQSCDQCN SYIWAMEKAY MCTYCKMVCH
KKCLCKITAD CSTFSAKKCD EESTGQHFGV RVCHLVNDKS PVPMVLEMML EHVEMQGLYT
EGIYRKSGSA NRMKELHQRL ETEPHAVCLE DYPIHTVTGL VKQWLRELPD PLMTFMHYND
FLHAVELPEK QEQLHAVYKV LEELPPANFN TLERLIFHLV RVCKVEDHNR MSPNSLAIVF
APCVLRCPDS ADPLLSMKDV AKTTICVEMI INEQIRRYNE KMEEIEQLEY AEALAVNQLK
LKRQNTHYWH LPLRFSPPYK GVVMHEKASS DLSVVPENEP LNPDTEKNLV ERIKSIKQEK
EDLACRLPEM EQPGSDQENL DSETSQSSES LLDELQRSSV HMSEPDGLDQ
//
