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Database: UniProt
Entry: A0A3Q3AT52_KRYMA
LinkDB: A0A3Q3AT52_KRYMA
Original site: A0A3Q3AT52_KRYMA 
ID   A0A3Q3AT52_KRYMA        Unreviewed;      2468 AA.
AC   A0A3Q3AT52;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Myosin XVIIIA {ECO:0000313|Ensembl:ENSKMAP00000019620.1};
GN   Name=MYO18A {ECO:0000313|Ensembl:ENSKMAP00000019620.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019620.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000019620.1}
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   RefSeq; XP_017287670.1; XM_017432181.1.
DR   STRING; 37003.ENSKMAP00000019620; -.
DR   Ensembl; ENSKMAT00000019886.1; ENSKMAP00000019620.1; ENSKMAG00000014471.1.
DR   GeneTree; ENSGT00940000155768; -.
DR   OrthoDB; 3687088at2759; -.
DR   Proteomes; UP000264800; 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; 1.20.5.340; -; 2.
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; 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:UP000264800};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443}.
FT   DOMAIN          222..313
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          407..1171
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1398..1420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1842..1863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2166..2199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2225..2261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2292..2452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1235..1332
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1398..1413
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2175..2199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2225..2255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2292..2313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2314..2343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2344..2359
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2367..2383
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2384..2423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         500..507
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2468 AA;  279218 MW;  5FA5F7F2CAB1773A CRC64;
     MFNLMKKDKE KDGAKKEKKK ERMSAAELRS LEEMSMRRGF FNLKRESKRS KVEISGPIPI
     KVANSTELSL TDLESDGLSN RSSVILDDQL STASSTDDLK GEGGGGQEGH RSSVRDRVAH
     FGSIAKQNSS QVGQMMKRFS FSQRSKEESP SESSTPSGQN SAAPSPQVEN KVFNILRKQS
     QKLQPGAADT KKVCIPQLVD KVFPAQLQLP AVVAPSTPET RELELQRRNT GDFGFSLRRT
     TMLDRSPDGG VYRRVVHFAE PGAGTKDLAL GLVPGDRLVE INGRNVENKS RDEIVEMIRQ
     SGDTVRLKVQ PILELSELSR CWLRNSEGLR RGVRHVKTEE QIAAEQAWYG SEKVWLVHKD
     GFSLATVVKT EAGSLPEGKV KIKLEHDGTL LDVDEDDIEK ANPPSYDRLE DLASLLYLNE
     SSVMHCLRQR YGGNLIHSFA GPNMVVINPL STPSMYSEKV MHMFKGCRRE DTAPHIYAVA
     QSAYRNLLTT RQDQSIVLLG KSGSGKTTNC QHLVQYLVSI AGSTGKIFSA EKWQAVYTIL
     EAFGSSSTAM NTNASRFSHV VSLDFDQAGQ VASASIQTML LEKLRVSRRP EAESTFNVFY
     YMMAGADSSL RTELHLNQLA ENSAFGIYPH SKPEDKQRAS QQFTKLQAAM KVLGISGEEQ
     KALWLILGAI YHLGAAGGTK DGDEVGRRQF ARHEWAQKAA YLLGCTLEEL SSLIFKHQAR
     GLQPTTSFRG GADDAGQGDS SGSKFTALEC LEAMASGLYS ELFTVVISLI NRALKSSQHS
     LCSLLIVDTP GFQNPRLAQQ QRGATFEELC HNYTQERLQT LFHERTFVRE LERYKEENIE
     LVLDDIESST SLSVAVIDQA SAQALVRALA RTEEARGLLW LMEEEAVQPG GSEETMLERL
     FSYYSSSQGE NKGASLLLRG EKPHLFLLGH SHGADWVEYN VQGWLSHAKN NPAAQNAAAL
     LQDSQKKNIS GLFLGRSSGA TVLSGSIAGL EGSSQLALRR ATSMRKTFTT GVAAVKKKSL
     CIQVKLQVDA LIDMVRRSKV HFVHCLLPKA EAVGGADLRV THGESPDAGL MNLDLHLLRA
     QLRGSKLLDA LRIYRQGYPD HMVFSEFRRR FDVLAPHLTK KHGRNYIVTD EKRAVEELLE
     SLELEKSNYH MGLSRVFFRA GTLSRLEEQR DVQTRRNISL FQSACRGYLA RQAFKKRKIQ
     DLAIRCIQKN IKKNRGVKDW PWWKLFTTVR PLIEVQLTEE QIRGKDEEIQ QLKQKLEKVE
     KERNELRLNS DRLESRITEL SSELTDERNT GESASQLLEA ETAERLRLEK DLKELQSKFD
     SMKKQTESME MEVMEARLIR ASELNGEMDD DDTGGEWRLK YERAIREIEF TKKRLQQEFD
     DKLEVEQQNK RQLERRISDL QADNEESQRN IQQLKKKTQR LTSELQDTKL HLEGQQSRNH
     DLEKKQRKFD GELSGAQDEV QRERSLREKL AREKDMLSAE VFSVRQQLED KDIELCAVNL
     KLEQLEAELQ DLNSQESKDE ASLAKMKKQL RDMEAKVKDQ EEELDEQAGT IQMLEQAKLR
     LEMEMERLRQ SHSKEIESKD DEVEEIRQSC SKKLKQMEVQ LEEDYDEKQK VLKEKRELES
     KLLSAQTQER SADIETEKRL RKDLKRTKAL LTDAQIMLDH IKNNAPSKRE IAQLKNQLEE
     SEFTCAAAVK ARKAMEVEID DLHVQMEDTS KTKQALEEQL SRLQREKNDL QSRMEEDQED
     LNELMKKHKA AVAQSAQNLA QISDLQSQLE EALKDKQEVQ EKIQVLQSQL DFQEQSMVEK
     SLVSRQEAKI RELETKLEFE KTQVKRLENL VARLKENLEK LTEERDQRFS SENREKEQNK
     RLQRQIRDVK EEMAELAKKE AEASRKKHEL EMDIESLEAA NQSLQADLKL AFKRIGDLQA
     AIEDEMESDD NEDLINSLQD MVTKYQKRKN RTQGLSDSDS EVEDRVDGVK SWLSKSKCSM
     KNLSDDGSLK SSRYAVNLDA KEGKEWKDWK EANKEDKEVE TNRPVSVMSS LSYRKRSNLD
     SVGSKDVLLS ALKENADSED VLTFQKAKSK TSDPHDDAYS VSCRKTSQLQ EVINGRESVI
     SQAYSEANSR ARRGIDSRWS QVDKESSFSR PSRNLSLISE NKPGTSFCLS SPPGFHRSIS
     HLEEGRGDRL RYGSSPSSPC FSRRSRSRSP GNVSQADSHM LLARSSRLSE FDIDMDDSRS
     VAFTERSAYS PHSSTGRSVS MPPPQARSTF DNYSVDDSDI KPVSHRSYLD PDLEKAINEV
     LSFKPITFKR RSLEDSEDEI SKNNKDEGKS LKNGDGTRPT SSVRHSESAV DCRSQSRSTS
     SCSKRSSKSK KKKRSHSSES HNSRGKTRHR SSSKRRSKRS KKKNQTSSSS SSSSSSDSES
     DSGSSSDAST ISYRSSSSVK KAPAKTVSDP DSEEGTTEGP PLNKMDEKKR KKKVDSLVMK
     YLYRPDSD
//
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