ID F6WYZ5_CALJA Unreviewed; 2032 AA.
AC F6WYZ5; U3DYZ8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Myosin XVIIIA {ECO:0000313|Ensembl:ENSCJAP00000046355.3};
GN Name=MYO18A {ECO:0000313|Ensembl:ENSCJAP00000046355.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000046355.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000046355.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000046355.3}
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR STRING; 9483.ENSCJAP00000046355; -.
DR Ensembl; ENSCJAT00000054975.3; ENSCJAP00000046355.3; ENSCJAG00000013358.6.
DR GeneTree; ENSGT00940000155768; -.
DR InParanoid; F6WYZ5; -.
DR Proteomes; UP000008225; Chromosome 5.
DR Bgee; ENSCJAG00000013358; Expressed in cerebellum and 6 other cell types or tissues.
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:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR CDD; cd01386; MYSc_Myo18; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR Pfam; PF00595; PDZ; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50163; RECA_3; 1.
DR PROSITE; PS51844; SH3_LIKE; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000008225}.
FT DOMAIN 220..311
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 361..413
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 417..1197
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 554..619
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1829..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1939..2032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1261..1365
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1939..1962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 510..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2032 AA; 230295 MW; ACD713458F0622A0 CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS LRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSV ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLVQHP
GPGIPRPGHR SRAPELVTKK FPADLRLPPV VPLPPPALRE LELQRRPTGD FGFSLRRTTM
LDRGPEGQVY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVESKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRSSEGPRRE PADLDPEAAS PAHSQAKTEE QIAAEEAWNE
TEKVWLVHRD GFSLASQLKS EELGLPEGKV RVKLDHDGAI LDVDEDDVEK ANAPSCDRLE
DLASLVYLNE SSVLHTLRQR YGASLLHTYA GPSLLVLGPR GAPAVYSEKV MHMFKGCRRE
DMAPHIYAVA QTAYRAMLMS RQDQSIVLLG SSGSGKTTSC QHLVQYLATI AGVSGNKVFS
VEKWQALYTL LEAFGNSPTI MNGNATRFSQ ILSLDFDQAG QVASASIQTM LLEKLRVARR
PANEATFNVF YYLLACGDGT LRTELHLNHL AENSVFGIVP LAKPEEKQKA AQQFSKLQAA
MKVLSISPDE QKACWLILAA IYHLGAAGAT KEATEAGRKQ FARHEWAQKA AYLLGCSLEE
LSSAIFKHQH KAGTLQRSTS FRQGPEESSP GNGTGPKLSA LECLEGMAAG LYSELFTLLV
SLVNRALKSS QHSLCSMMIV DTPGFQNPEQ GGSARGASFE ELCHNYAQDR LQRLFHEHTF
VQELERYKEE NIELAFDDLE PPTDDSVAAV DQASHQSLVR SLARTDEARG LLWLLEEEAL
VPGASEDALL ERLFSYYGPQ EGDKKGQSPL LRSSKPHHFL LGHSHGTNWV EYNVIGWLNY
TKQNPATQNA PRLLQDSQKK IISNLFLGRA GSATVLSGSI AGLEGGSQLA LRRATSMRKT
FTTGMAAVKK KSLCIQIKLQ VDALIDTIKK SKLHFVHCFL PVAEGWAGEP RSASSRRVSS
SSELDLPSGD HCEAGLLQLD VPLLRTQLRG SRLLDAMRMY RQGYPDHMVF SEFRRRFDVL
APHLTKKHGR NYIVVDERRA VEELLECLDL EKSSCCMGLS RVFFRAGTLA RLEEQRDEQT
SRNLTLFQAA CRGYLARQHF KKRKIQDLAI RCVQKNIKKN KGVKDWPWWK LFTTVRPLIE
VQLSEEQIRN KDEEIQQLRS KLEKVEKERN ELRLNSDRLE TRISELTSEL TDERNTGESA
SQLLDTETAE RLRAEKEMKE LQTQYDALKK QMEVMEMEVM EARLIRAAEI NGEVDDDDAD
GEWRLKYERA VREVDFTKKR LQQEFEDKLE VEQQNKRQLE RRFGDLQADS EESQRALQQL
KKKCQRLTAE LQDTKLHLEG QQVRNHELEK KQRRFDSELS QAHEEAQQEK LQREKLQREK
DMLLAEAFSL KQQLEEKDMD IAGFTQKVVS LEAELQDISS QESKDEASLA KVKKQLRDLE
AKVKDQEEEL DEQAGTIQML EQAKLRLEME MERMRQTHSK EMEGRDEEVE EARQSCQKKV
NRRDFESEKR LRKDLKRTKA LLADAQLMLD HLKNSAPSKR EITQLKNQLE ESEFTCAAAV
KARKAMEVEI EDLHLQIDDI AKAKTVLEEQ LSRLQREKNE IQNRLEEDQE DMNELMKKHK
AAVAQASRDL AQINDLQAQL EEANKEKQEL QEKLQALQSQ VEFLEQSMVD KSLVSRQEAK
IRELETRLEF ERTQVKRLES LASRLKENME KLTEERDQRI AAENREKEQN KRLQRQLRDT
KEEMGELARK EAEASRKKHE LEMDLESLEA ANQSLQADLK LAFKRIGDLQ AAIEDEMESD
ENEDLINSLQ DMVTKYQKRK NKLEGDSDVD SELEDRVDGV KSWLSKNKGP SKAASDDGSL
KSSSPTSYWK SLAPDRSDDE HDPLNNTSRP RYSYSNLSDS DDTEAKLTET SA
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