ID A0A3P9PTL3_POERE Unreviewed; 2278 AA.
AC A0A3P9PTL3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSPREP00000025222.1};
GN Name=MYO9B {ECO:0000313|Ensembl:ENSPREP00000025222.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000025222.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000025222.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000025222.1};
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_008406170.1; XM_008407948.2.
DR STRING; 8081.ENSPREP00000025222; -.
DR Ensembl; ENSPRET00000025473.1; ENSPREP00000025222.1; ENSPREG00000017023.1.
DR GeneID; 103464107; -.
DR KEGG; pret:103464107; -.
DR GeneTree; ENSGT00940000156845; -.
DR OMA; SWFRMAL; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000017023; Expressed in caudal fin and 1 other cell type or tissue.
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; 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; PF00130; C1_1; 1.
DR Pfam; PF00612; IQ; 3.
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; PS51257; PROKAR_LIPOPROTEIN; 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 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:UP000242638};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 30..128
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 160..995
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1710..1759
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1778..1966
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..898
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1075..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1528..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2057..2198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2231..2278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1480..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2065..2096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2234..2256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2257..2272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 253..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2278 AA; 258666 MW; 178A6AD6B86FD9AD CRC64;
MSVRDGAATM ATNAGGGGGG GVGCNDPDDR MYLLQIYPRL ASQVSTCCNL RVQKNATTAS
VISDAAATLG LDPGGLYVLA EVKESGGEEW ILEAGDLPVQ RVLLWPRKAQ EQHPQSAGFY
FLLQERNRDG SIHYVHLPPS SKEQEVQQLA ARGFLPPPQD DFADLCNLPV LSEDSILNNL
RTRFYKKKIY TYAGSILIAI NPFKFLPIYN PKYVKMYENH QLGKLEPHIF AIADVAYYAM
LRKRVNQCIV ISGESGSGKT QSTNFLIHCL TALSQKGYAS GVERTILGAG PVLEAFGNAK
TAHNNNSSRF GKFIQVNYLE SGVVRGAVVE KYLLEKSRLV SREKNERNYH VFYYLLLGAS
EEERTEFKLL PPEEYFYLKQ ENFKIEDEED LRHDFERLQQ AMQMVGFLPA TKKQIFSVLS
AILYLGNVTY RRKSSGRDEG LDVGPPEVLA TLSDLLKVKE ELLVEALTKR KTVTVNDKLI
LPYSHSEAIT ARDSMAKSLY GALFDWIVLR INHALLNKKD MEESVPCLSI GVLDIFGFED
FETNSFEQFC INYANEQLQY YFNNHIFNLE QEEYQSEGIT WHNIDYTDNV GCIHLISKKP
TGLLYLLDEE SNFPHATDKT LLAKFKQQHH GNKYFIPTPV MEPAFVIQHF AGKVKYHIKD
FREKNTDHMR PDIVALLRSS DRAFVRQLIG MDPVAMFRWG ILRATIRGLA AFNEAGRSWA
SKTAGVIRPA SRTPLGELQR SNTPIERMYK RASMLDFYFD HSEERPLEAF EDIFASYENK
KEMHSEIISS IKNLQLDGED PRKLLQSWGR LRFPRHVLQK NKSVRQKQAI PKSLLDSQSL
KFIVSLTLHD RTTKSLLHLH KKKKPPSISA QFQNSLTKLL ETLTKAEPFF IRCIRSNAEK
KEMHLDEALV LQQLHYTGML ETVRIRRSGY PAKYTFQEFS EQFRVLLLKN FSASKEDIAE
LLEKKMGFKP TTYQIGKTKV FLKELERQQL QDMRHREVMR KIIFLQRWFR AHLQRNEFLE
MKRAAILIQA SWRRYCRKEQ RRRAATVIQA VWRGHRQRSE YHRQKHGATK IQALVRGHSA
RRRCQSIREE KRKKKEEEEE ARKREEEERR RREEEEEEAR RKAEEEERLR IEEVKRRAEE
EAAREAQKKL EEKEAREPQT REDPDIELVT EETLDENVPE EEQGKDEDME GEEEDLELYG
TEAEAGPQLD GEQEPGLAPN APTGISSQQE DKKSSASATT SLHAELKRPQ PGLSNKVPSS
RSLEKREQRR RRGLEHSQRE SERAASSSSS SSATSRDQVS PSKSRNQETS KLKERSDSKE
LDQYTFVAWK VKEEKGGKKE GKTSAPSAGP VRPSTLPLHP ADFTQDKNGL GEGGGAVNLQ
RRSGAIKEKP EKWKGRRSNG EGYEGTGSPP PHSKEEATKK PSLRDMSHSS VDSLSPSSDG
AWAVSVRDPW TVAAREGNHD SQGDSSRSSS FRKRHQDGSG QPDSLPSIAT TPDKSGGFFS
KILKKRAKEA HTPDNGELTF AQSLNEKSML GEAPPSGPVV RPVSQPFSDR TGKSIGRNPT
IKISRATRVS VHWDASLDRV IANGNELRNL DEFLGNQVND FRSRGKSLSP IESIFVTATM
QFREQIKSMY SLSNPTIGYK ALMTGFKNKV IHLATDKQQE DVQLVVNLFQ SVLDGFIRGE
VKKEEAEPVK PTKARKKRRK KDKIMESLLD HGFINYQVSI VQSCDQCSSY IWGMEKAYMC
SNCKMVCHKK CLNKIAINCS SFCAKKNDEE VTGCNFGVRV CHLVSDKNPV PTVLEMMLEH
VEMHGLYTEG IYRKSGAANR MRELHQRLEM DAYVDILEDY PIHTVTGLVK QWLRELPDPL
MTFAHYNDFL HAVELPEKQE QLQAIYKVLE ELPTANFNTL ERLIFHLVKV SKEEEHNRMS
PNSLAIVFAP CILRCPNTAD PLLSMKDVAK TTTCVEMLII EQIRRYNEKM EEIEQLEYAE
ALAVKQLNLK RKNTTSCPLS LRLTAHYKGG VIREKVSSDL TVVPENEPLD SDIETENNLV
ERIKSIKQEK EELAFRLPEM EQPGSDQENL DSEASLSSES LLDEQQQRSS AHGSEPEGHS
GVQLRRHRPV KHVKPPEIIQ RTKPSVGRPF LGNLTPSSST SSLSSCASTA SETSTASTRR
PPQRRNPVIP DTVKLPPGVL PQQMATGSSQ TFPPPGNREI LYPVRIREHP GRRKDSTQSL
YLDNPESGLL LHFSSCPPSA SSSSSSIATA TLQQKDTRAP KSHRRFSDPD IPYMDDEV
//
