ID A0A2K6GUN3_PROCO Unreviewed; 2049 AA.
AC A0A2K6GUN3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Myosin XVIIIA {ECO:0000313|Ensembl:ENSPCOP00000029899.1};
GN Name=MYO18A {ECO:0000313|Ensembl:ENSPCOP00000029899.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000029899.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000029899.1}
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; ENSPCOT00000040845.1; ENSPCOP00000029899.1; ENSPCOG00000027621.1.
DR GeneTree; ENSGT00940000155768; -.
DR Proteomes; UP000233160; 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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 1.
DR Pfam; PF00063; Myosin_head; 3.
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; 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; 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:UP000233160}.
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..1180
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..33
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 719..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..2049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1244..1348
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2026
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2027..2049
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 2049 AA; 232552 MW; 6F6662452D5AB917 CRC64;
MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELKSLEEMS LRRGFFNLNR SSKRESRTRL
EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLMQHP
GLGIPRPGPR SRVPELVSKK FPADLRLPPV VPLPAPALRE LELQRRPTGD FGFSLRRTTM
LDRGPEGQVY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GHNVESKSRD EIVEMIRQSG
DSVRLKVQPI PELSELSRSW LRSGEGPRRE PADAKTEEQI AAEEAWYETE KVWLVHKDGF
SLASQLKSEE LSLPEGKVRV KLDHDGAILD VDEDDVEKAN APSCDRLDDL ASLVYLNESS
VLHTLRQRYG ASLLHTYAGP SLLVLSPRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
AYRAMLMSRQ DQSIILLGSS GSGKTTSCQH LVQYLATIAG TSGNKVFSVE KWQALYTLLE
AFGNSPTIMN GNATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA NEATFNVFYY
LLACGDSSLR TELHLNHLAE NNVFGIVPLA KPEEKQKAAQ QFSKLQTAMK VLGISPDEQK
ACWLILAAIY HLGAAGATKA GRKQFARHEW AQKAAYLLGC GLEELSSAIF KHQHKGGTLQ
RSTSFRQGPE ESSLGDGMGT LSPSAGGCEW EASSRAGCHL WGWRGLLEAL KSSQHSLCSM
MIVDTPGFQN PEQGGSARGA SFEELCHNYV QDRLQRLFHE RTFVQELERY KEENIELAFD
DLEPTTGDSV AAVDEASHQA LVRSLSRANE ARGLLWLLEE EALVPGATED ALLERLLSYY
GPQEGDKKGQ SPLLRSSKPH HFLLGHSHGT NWVEYSVAGW LSYTKQNPAT QNAPRLLQDS
QKKIISNLFL GRAGSATVLS GSVAGLEGGS QLALRRATSM RKTFTTGMAA VKKKSLCIQI
KLQVDALIDT IKKSKLHFVH CFLPVAEGWA GEPRSASSRR VSSSSEMDLP SGDHCEAGLL
QLDVPLLRAQ LRGSRLLDAM RMYRQGYPDH MVFSEFRRRF DVLAPHLTKK HGRNYIVVDE
RRAVEELLES LDLEKSSCCM GLSRVFFRAG TLARLEEQRD EQTSRNLTLF QAACRGYLAR
QHFKKRKIQD LAIRCVQKNI KKNKGVKDWP WWKLFTTVRP LIEVQLSEEQ IRNKDEEIQQ
LRSKLEKVEK ERNELRLNSD RLETRISELT SELTDERNTG ESASQLLDAE TAERLRAEKE
MKELQTQYDA LKKQMEVMEM EVMEARLIRA AEINGEVDDD DAGGEWRLKY ERAMREVDFT
KKRLQQEFED KLEVEQQNKR QLERRLGDLQ ADGEESQRAL QQLKKKCQRL TAELQDTKLH
LEGQQVRNHE LEKKQRRFDS ELSQAHEEAQ REKLQREKLQ REKDMLLAEA FSLKQQLEEK
DMDIAGFTQK VVSLEAELQD ISSQESKDEA SLAKVKKQLR DLEAKVKDQE EELDEQAGTI
QMLEQAKLRL EMEMERMRQT HSKEMESRDE EVEEARQSCQ KKLKQMEVQL EEEYEDKQKV
LREKRELEGK LATLSDQVNQ RDFESEKRLR KDLKRTKALL ADAQLMLDHL KNNAPSKREI
AQLKNQLEES EFTCAAAVKA RKAMEVEIED LHLQIDDIAK AKTVLEEQLS RLQREKNEIQ
NRLEEDQEDM NELMKKHKAA VAQASRDLAQ MNDFQAQLEE ANKEKQELQE KLQGLQSQVE
FLEQSMVDKS LVSRQEAKIR ELETRLEFER TQVKRLESLA SRLKENMEKL TEERDHRIAA
ENREKEQNKR LQRQLRDTKE EMGELARKEA EASRKKHELE MDLESLEAAN QSLQADLKLA
FKRIGDLQAA IEDEMESDEN EDLINSLQDM VTKYQKRKNK LEGDSDVDSE LEDRVDGVKS
WLSKNKGPSK AASDDGSLKS SSPTSYWKSL APDRSDDEHD PLDTTSRTRY SHSYMSDSDT
EAKPTETNA
//
