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Database: UniProt
Entry: A0A2K5YXM8_MANLE
LinkDB: A0A2K5YXM8_MANLE
Original site: A0A2K5YXM8_MANLE 
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
//
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