ID A0A3Q2DY49_CYPVA Unreviewed; 1966 AA.
AC A0A3Q2DY49;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Unconventional myosin-XVIIIa-like {ECO:0000313|Ensembl:ENSCVAP00000024702.1};
GN Name=MYO18A {ECO:0000313|Ensembl:ENSCVAP00000024702.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000024702.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000024702.1}
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; 28743.ENSCVAP00000024702; -.
DR Ensembl; ENSCVAT00000003525.1; ENSCVAP00000024702.1; ENSCVAG00000009120.1.
DR GeneTree; ENSGT00940000155768; -.
DR OMA; LSQIFFR; -.
DR Proteomes; UP000265020; 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 GO; GO:0048731; P:system development; IEA:UniProt.
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 InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
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; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
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.
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:UP000265020};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT DOMAIN 225..316
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 410..1168
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1232..1329
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 80..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1904..1927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1966 AA; 223903 MW; 85FD277D9592A6CD CRC64;
MFNLMKKDKE REGSRKEKKG KNDRMSAAEL RSLEEMSVRR GFFNLKREAK RESKTKVEIS
NPIPIKVAST TELSLTDIES DNVSNRSSVV LDDQISVASS TDEQRGEGEK DGHRSSVRDR
VAHFGSLAKQ NSSQMGQMMK RFSFSQRSKE ESPSEGSTPS GQNSAAPSPQ VENKVFNMLR
KHSQRGQPEA ADPRKVFIPE LVDKVFPAAL QLPAVVAPSV PETRELELQR RNTGDFGFSL
RRTTMLDRSP DGGVYRRVVH FAEPGAGTKD LALGLVPGDR LVEINGRNVE NKSRDEIVEM
IRQSGDTVRL KVQPILELSE LSRCWLRNIE GLRREARHVK TEEQITAEQA WYGSEKVWLV
HKDGFSLATV LKTESGSHPE GKVKIQLEHD GTILDVDEDD IEKANPPTYD RSEDLASLVY
LNESSVIHCL RQRYGGNLIH SFAGPNMVVI NPLSTPSMYS EKVMHMFKGC RREDTAPHIY
AVAQSAYRNL LTTQQDQSVV LLGKSGSGKT TNCQHLVQYL VSMAGSTGKI FSAEKWQAVY
TILEAFGNCS TTMNSNASRF SHVVSLDFDQ AGQVASASIQ TMLLDKLRVS RRPEEESTFN
VFYYLMAGAD SALRTELHLN QLNESSAFGI QPLSKTEDKQ RALQQFTKLQ AAMKVLGISV
EEQKALWLIL GAIYHLGAAG ATKAGRRQFA RHEWAQKASY LLGCNLDELS SLIFKNQARG
MQPLFRGGTD DAGQGDGLGS KFTALECLES MASGLYSEVF TVLISLINRA LKSSQHSLCS
ILIVDTPGFQ NPRLAQQQRG ATFEELCHNY TQERLQTLFH ERTFVQELDR YKEENIELVL
DDVESSPSLS IAAIDQAPSQ ALVRTLARME EARGLLWLME EEGVKPGGSE ELMLERLFSY
YSAGLGENKG ANLLLRGEKS HLFLLGHSHG TDWVEYNIQG WLGHAKNNPA AQSAATLLQD
SQKKNISGLF LGRSSGATVL SGSIAGLEGS SQLALRRATS MRKTFTTGVA AVKKKSHCIQ
VKLQVDALID MVRRSKVHFV HCLLPKAEAV GGSEPRVPHG ESSDSGLMTL DVGLLRAQLR
GSKLLEALRI YRQGYPEHMV FSEFRRRFDV LAPQPTKKHG RNHIVPDEKR AVEELLESLE
LEKSSFHMGL SKVFFRAGTL SRLEEQRDVQ TRNNISLFQA ACRGYLARQA FKKRKIQNLA
IRCIQKNIKK NRGVKDWPWW KLFTTVRPLI EVQLTEEQIR GKDEEIQQLK QRLEKVEKER
NELRLNSDRL ESRVTELSTE LTDERNTGES ASQLLEAETS ERLRLEKDMK DLQTKFDSMK
KQMESMEMEV MEARLIRASE LNGELDDDDT GGEWRLKYER AIREIEFTKK RLQQEFDDKL
EVEQQNKRQL ERRISDLQAD IEESQRNIQQ LKKKNQRLIA ELQDTKLHLE GQQSRNHDLE
KKQRKFDSEL SAAQDEAQRE RSLREKLARE KDMQSGDCFS LRQQLEDKDL ELRTVQLKLD
QFEAELQDLN SQESKDEASL AKMKKQLRDM EAKIKDQEEE LDEQAGTIQM LEQAKLRLEM
EMERLRHTHF KEIESKDDEV EEIRQSYSKK LKQMEVQLEE EYDEKQKVLK EKRELEAKLL
SAQSKLVKFK ELKALISLLL QAVVLAFPVS CRTLISVLLS VCQLEEQLSR LQREKNDLQS
RMEEDQEDLN ELMKKHKSAV AQVRNLAQIN DLQTQLEEAL REKQEVQEKM QVLQSQLEFQ
EQSTVEKSLA NRQEAKIREL ETKMEFEKTQ VKRLENLVAR LKENVEKLTE ERDQRITSEN
REKEQNKRLQ RQIRDIKEEM GELAKKEAEA SHKKHELEMD IESLEAANQS LQADLKLAFK
RIGDLQAAIE DDMESDENED IMNSQGQSDT DSELEDRVDG VKSWLSKNDS SAKNLSDDGS
LKGRSSPSRW RSRTDRSDDE EDAPGTPGSK HRYSSHLKDD GEEEES
//
