ID A0A2K5YXM8_MANLE Unreviewed; 1906 AA.
AC A0A2K5YXM8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSMLEP00000020319.1};
GN Name=MYO9B {ECO:0000313|Ensembl:ENSMLEP00000020319.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000020319.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000020319.1}
RP IDENTIFICATION.
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 STRING; 9568.ENSMLEP00000020319; -.
DR Ensembl; ENSMLET00000043815.1; ENSMLEP00000020319.1; ENSMLEG00000034335.1.
DR GeneTree; ENSGT00940000156845; -.
DR OMA; SWFRMAL; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0048495; F:Roundabout binding; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IEA:Ensembl.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR GO; GO:0035385; P:Roundabout signaling pathway; IEA:Ensembl.
DR CDD; cd20884; C1_Myosin-IXb; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd17217; RA_Myosin-IXb; 1.
DR CDD; cd04407; RhoGAP_myosin_IXB; 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; IPR046989; RA_Myosin-IXb.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR028557; RhoGAP_myosin_IXB.
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; 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; 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}; 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:UP000233140};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..114
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 146..926
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1484..1533
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1555..1740
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 1028..1263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1832..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1906 AA; 216494 MW; 39D65AA57C7C9AC5 CRC64;
MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD AIASLRLDGT
KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY
VHMQLVAQAT ATRRLVERGL LPRQQADFDD LCNLPELTEG NLLKNLKHRF LQQKIYTYAG
SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE
SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVSYLESGIV RGVAIAWPPK TTVFLPILTC RNYHVFYYLL LGVSEEERRE FQLKQPEDYF
YLNQHNLKIE DGEDLKHDFE RLKQAMEMVG FLPATKKQIF AVLSAILYLG NVTYKKRATG
REEGLEVGPP EVLDTLSQLL KVKREILVEV LTKRKTVTVN DKLILPYSLS EAITARDSMA
KSLYSALFDW IVLRINHALL NKKDVEEAVS CLSIGVLDIF GFEDFERNSF EQFCINYEEY
QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP HATSQTLLAK FKQQHEDNKY
FLGTPVMEPA FIIQHFAGKV KYQIKDFREK NMDYMRPDIV ALLRGSDSSY VRELIGMDPV
AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGMLLTPS SFCHCALPTP PLSDLHNQMI
KSIKGLPWQG EDPRRLLQSL SRLQKPRAFI LKSKGIKQKQ IIPKNLLDSK SLKLIISMTL
HDRTTKSLLH LHKKKKPPSI SAQFQTSLNK LLEALGKAEP FFIRCIRSNA EKKELCFDDE
LVLQQLRYTG MLETVRIRRS GYSAKYTFQD FTEQFQVLLP KDAQPCREVI STLLEKMKVD
KRNYQIGKTK VFLKETERQA LQETLHREVV RKILLLQSWF RMVLERRHFL QMKRAAVTIQ
ACWRSYRVRR ALERTQAAVY LQAAWRGYWQ RKLYRRRKQS IIRLQSLCRG HLQRKSFSRM
ILEKQKAEEK EREALEAERA GAEEGGLGQA AGGQQVAEQG PEPAEDGRHL ASEPEVWPSD
RSPPEHSSPE KEAPSPEKTL PPQKTVAAES HEKVPSSREK RESRRQRGLE HVKFQNKHIQ
SCKEESALRE PSRRVTQEQG VSLLEDKKES REDETLLIVE TEAENTSQKQ PTEQPEAMAV
GKRRISFSTS DVSKLLPSPA KAQPATETAD GERSMKKPAV QKKKPGDASS IPDAGLSPGS
QVDSKSTFKR LFLHKTKDKK YSLEGVEELE NAVSGQVVLE TATMKKGLEA PSGHQHRHAA
SEKRTKEPGG KGKKNRNVKI GKITVSEKWR ESVFRQITNA NELKYLDEFL LNKINDLRSQ
KTPIESLFIE ATEKFRSNIK TMYSVPNGKI HVGYKDLMEN YQIVVSNLAT ERGEKDTNLV
LNLFQSLLDE FTRGYTKNDF EPVKQSKAQK KKRKQERAVQ EHNGHVFASY QVSIPQSCEQ
CLSYIWLMDK ALLCSVCKMT CHKKCVHKIQ SHCSYTYGRK GEPGAEPGHF GVCVDSLTSD
KASVPIVLEK LLEHVEMHGL YTEGLYRKSG AANRTRELRQ ALQTDPTAVK LENFPIHAIT
GVLKQWLREL PEPLMTFAQY GDFLRAVELP EKQEQLAAIY AVLEHLPEAN HNSLERLIFH
LVKVALLEDV NRMSPGALAI IFAPCLLRCP DNSDPLTSMK DVLKITTCVE MLIKEQMRKY
KVKMEEISQL EAAESIAFRR LSLLRQNALW PLKLGFSSPY EGVLNKSPKA RDSQGEELEV
LLEEEAAGGD EDREKEILIE RIQSIKEEKA SWSAGSIPGG PLVRRREPPA RRPDQVHSVY
VTPGVHLPTQ GALEPLEEDG QPPGAKRRYS DPPKYCLPPA SGQANG
//