ID A0A2K6AI13_MANLE Unreviewed; 2042 AA.
AC A0A2K6AI13;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Myosin XVIIIA {ECO:0000313|Ensembl:ENSMLEP00000039717.1};
GN Name=MYO18A {ECO:0000313|Ensembl:ENSMLEP00000039717.1};
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:ENSMLEP00000039717.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000039717.1}
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR Ensembl; ENSMLET00000063336.1; ENSMLEP00000039717.1; ENSMLEG00000043771.1.
DR GeneTree; ENSGT00940000155768; -.
DR OMA; LSQIFFR; -.
DR Proteomes; UP000233140; 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: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; 1.20.5.340; -; 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 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; 2.
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:UP000233140}.
FT DOMAIN 220..311
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 349..401
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 405..1188
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 542..607
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT REGION 1..32
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..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1942..2042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1252..1356
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1964
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1987..2002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2004..2019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2042 AA; 231695 MW; 7E43991C6CF2E29F CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS LRRGFFNLNR SSKRESKTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLVQHS
GPGIPRPGHR SRAPELVTKK FPVDLRLPPV VPLPPPALRE LELQRRPTGD FGFSLRRTTM
LDRGPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVENKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRSGEGPRRE PSDAKTEEQI AAEEAWNETE KVWLVHRDGF
SLASQLKSEE LSLPEGKVRV KLDHDGAILD VDEDDVEKAN APSCDRLEDL ASLVYLNESS
VLHTLRQRYG ASLLHTYAGP SLLVLGPRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
AYRAMLMSRQ DQSIILLGSS GSGKTTSCQH LVQYLATIAG ISGNKVFSVE KWQALYTLLE
AFGNSPTIMN GNATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNIFYY
LLACGDGTLR TELHLNHLAE NNVFGIVPLA KPEEKQKAAQ QFSKLQAAMK VLGISPDEQK
ACWLILAAIY HLGAAGATKE APEEQAAGRK QFARHEWAQK AAYLLGCSLE ELSSAIFKHQ
HKGGTLQRST SFRQGPEESG LGDGTGPKLS ALECLEGMAA GLYSELFTLL VSLVNRALKS
SQHSLCSMMI VDTPGFQNPE QGGSARGASF EELCHNYTQD RLQRLFHERT FVQELERYKE
ENIELAFDDL ESPTDDSVAA VDQASHQSLV RSLARTDEAR GLLWLLEEEA LVPGASEDTL
LERLFSYYGP QEGDKKGQSP LLRSSKPHHF LLGHSHGTNW VEYNVTGWLN YTKQNPATQN
APRLLQDSQK KIISNLFLGR AGSATVLSGS IAGLEGGSQL ALRRATSMRK TFTTGMAAVK
KKSLCIQMKL QVDALIDTIK KSKLHFVHCF LPVAEGWAGE PRSASSCRVS SSSELDLPSG
DHCEAGLLQL DVPLLRTQLR GSRLLDAMRM YRQGYPDHMV FSEFRRRFDV LAPHLTKKHG
RNYIVVDERR AVEELLECLD LEKSSCCMGL SRVFFRAGTL ARLEEQRDEQ TSRNLTLFQA
ACRGYLARQH FKKRKIQDLA IRCVQKNIKK NKGVKDWPWW KLFTTVRPLI EVQLSEEQIR
NKDEEIQQLR SKLEKVEKER NELRLNSDRL ESRISELTSE LTDERNTGES ASQLLDAETA
ERLRAEKEMK ELQTQYDALK KQMEVMEMEV MEARLIRAAE INGEVDDDDA GGEWRLKYER
AVREVDFTKK RLQQEFEDKL EVEQQNKRQL ERRLGDLQAD SEESQRALQQ LKKKCQRLTA
ELQDTKLHLE GQQVRNHELE KKQRRFDSEL SQAHEEAQRE KLQREKLQRE KDMLLAEAFS
LKQQLEEKDM DIAGFTQKVV SLEAELQDIS SQESKDEASL AKVKKQLRDL EAKVKDQEEE
LDEQAGTIQM LEQAKLRLEM EMERMRQTHS KEMESRDEEV EEARQSCQKK LKQMEVQLEE
EYEDKQKVLR EKRELEGKLA TLSDQVNRRD FESEKRLRKD LKRTKALLAD AQLMLDHLKN
SAPSKREIAQ LKNQLEESEF TCAAAVKARK AMEVEIEDLH LQIDDIAKAK TVLEEQLSRL
QREKNEIQNR LEEDQEDMNE LMKKHKAAVA QASRDLAQIN DLQAQLEEAN KEKQELQEKL
QALQSQVEFL EQSMVDKSLV SRQEAKIREL ETRLEFERTQ VKRLESLASR LKENMEKLTE
ERDQRIAAEN REKEQNKRLQ RQLRDTKEEM GELARKEAEA SRKKHELEMD LESLEAANQS
LQADLKLAFK RIGDLQAAIE DEMESDENED LINSEGDSDV DSELEDRVDG VKSWLSKNKG
PSKAASDDGS LKSSSPTSYW KSLAPDRSDD EHDPLDNTSR PRYSHSYLSD SDTEAKLTET
NK
//
