ID A0A3B4ZN78_9TELE Unreviewed; 2029 AA.
AC A0A3B4ZN78;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSSPAP00000007699.1};
GN Name=MYO9B {ECO:0000313|Ensembl:ENSSPAP00000007699.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000007699.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000007699.1}
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; 144197.ENSSPAP00000007699; -.
DR Ensembl; ENSSPAT00000007846.1; ENSSPAP00000007699.1; ENSSPAG00000005822.1.
DR GeneTree; ENSGT00940000156845; -.
DR Proteomes; UP000261400; Unplaced.
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; 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; 2.
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 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}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 23..121
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 153..991
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1642..1691
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1710..1898
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..894
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1066..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1616..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2029 AA; 232204 MW; 26334E0156FE1E7E CRC64;
MATNAGGGGG GGGPASPNDH DGRSYLLQIY PRLPGQPSTC CNLKVQKDAT AASVISDVAS
ALGLDPGRLY VLAEVKECGG EEWVLEAGDL PVQRFLLWPR KAQEQHPQSL GFYFLLQERN
RDGSIHYVHL PTLSKEQEAL RLAERGFLPP PQDDFADLCN LPVLNEDSIL NNLRTRFYKK
KIYTYAGSIL IAINPFKFLP IYNPKYVKMY ENHQLGKLEP HIFAIADVAY YAMLRKRVNQ
CIVISGESGS GKTQSTNFLI HCLTALSQKG YASGVERTIL GAGPVLEAFG NAKTAHNNNS
SRFGKFIQVN YLESGVVRGA VVEKYLLEKS RLPFLFSLFS SFYALPFIRA LSSPVSRFHF
LIFYPLLLTA SPSSQQNFKI EDEEDLRHDF ERLQQAMEMV GFLSATKKQI FSVLSAILYL
GNVTYRRKST GRDEGLDVGP PEVLATLSDL LKVKEELLVE ALTKRKTVTV NDKLILPYSH
SEAITARDSM AKSLYSALFD WIVLRINHAL LNKKDMEESV PCLSIGVLDI FGFEDFETNS
FEQFCINYAN EQLQYYFNHH IFNLEQEEYQ AEGITWHNID YTDNVGCIHL ISKKPTGLLY
LLDEESNFPH ATDETLLAKF KQQHQGNKYF IPTPVMEPAF VIQHFAGRVK YQIKDFREKN
TDHMRPDIVA LLRSSDRAYV RQLIGMDPVA MFRWGILRAT IRGIAAFNEA GRAWAAKKSG
VVRPASRTPL GELKRSNAPI ERMYKRASML DFYFDHSEER PLEAFEDIFA SYESKKEMHA
EIISSIKNLQ LDGEDPRKLL QSWGRLRFPR HVLQKNKSTK QRQAIPKVNL LDSRSLKFIV
GLTLHDRTTK SLLHLHKKKK PPSISAQFQT SLTKLLETLN RAEPFFIRCI RSNAEKKEMN
LDEALVVQQL RYTGMLETVR IRRSGYGAKY TFQEFIEQFR VLLPKNASAS KEDISALLDR
KMGLDPTTYQ IGKTKVFLKE LERQQLQDML HKDVMRKIIF LQRWFRARLQ RKEFLDMRQA
AIVIQRSWRR YCQDEQQRRA ATLIQAVWRG HWQRLEYRRQ RRGATKIQAL VRGHSARRRC
QSMREEKRQK EEEKEAQKRA EEEERRRREE EEEEARRKAA EEEERIRMEE EARRKAEEEA
RRRAEEEEAA RKAQEAQKKK EEEEQRLARE PQTREDPDIE LVTEEMLDKN LPVQETEDEE
EEDKKVDEEN YGTSAEAGPQ LDDKEEMESV TLDLKPDPTS DGVTQAGTTS SAEHKKAQPS
AVARGGSSRS QEKREQRRRR GLEHNQRETE RAASSTTSSS AGSKDQTSAP KSKNLEKAKR
SDSKELDPYT FVNWKMKEDK GSKKDSRSSA PSAGPVRPST LSLQPADAAP ERNGLGEGVG
AVNLQRRHGA MKEKPDKWRG RRSDGDLSFR RRHQEGSGHQ DSGHSVPSTP DKYCTGFFSK
ILKKRPHKEA QTPDNGELPL AQMLTLASGH PSRPLSQPQG DRAGKGLGRN PTIKISRATR
VSEQWNASLD REITNANELR HLDEFLGNQV NDFRSRGKPL SATEAIFVTA TMQFRETIKA
MYSLTKPTIG YKGLMTGYQN KVIHLAGSKQ KEEVQLVVNL FQSVLDGFIR GEMKKEEAEP
AKPAKARKKR RKKDKSMESP LDHVFVNYQV NIMQSCDQCS SYIWGMEKAY MCSYCKMVCH
KKCICKIVTD CSTFCAKKSD EEFSGQHFGV RVCHLVNDKN PVPMVLEMML EHVEMHGLYT
EGIYRKSGSA NRMKELHQRL ETDPHLVHLE DYPIHTVTGL VKQWLRELPD PLMTFTHYSD
FLHAVELPEK LEQLQAVYKV LEELPTANFN TLERLVFHLV RVCKEEAHNR MSPNSLAIVF
APCILRCPDS ADPLLSMKDV AKTTTCVEMI INEQIRRYNE KMEEIEQLEY AETLALNQLK
LKRKNTHYWH VPLRFTPSFK GVVHEKVPSD LSVVPEEPLD SDTEAEKNLV ERLKSIKQEK
EDLACRLPEM EQPGSDQENL DSEASLSSES LLDEQQRSSA HSSEPEGQY
//
