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Database: UniProt
Entry: A0A0V0U206_9BILA
LinkDB: A0A0V0U206_9BILA
Original site: A0A0V0U206_9BILA 
ID   A0A0V0U206_9BILA        Unreviewed;      1940 AA.
AC   A0A0V0U206;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Myosin-3 {ECO:0000313|EMBL:KRX45306.1};
GN   Name=unc-54 {ECO:0000313|EMBL:KRX45306.1};
GN   ORFNames=T05_11728 {ECO:0000313|EMBL:KRX45306.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX45306.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX45306.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX45306.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC       {ECO:0000256|ARBA:ARBA00004657}.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX45306.1}.
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DR   EMBL; JYDJ01000078; KRX45306.1; -; Genomic_DNA.
DR   Proteomes; UP000055048; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 3.
DR   Gene3D; 1.20.5.370; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 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; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000055048};
KW   Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT   DOMAIN          27..76
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          80..760
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          635..657
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1889..1940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          824..1406
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1902..1940
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         173..180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1940 AA;  224554 MW;  BB0B33FFA37CF3D9 CRC64;
     MTSVYEKDPA WKFLRQPVDL SKAKKYDSKK SCWIPDAQEG YIAAEIKSTK VDQLVVITEK
     GLEKTVRKEE TQEMNPPKFD RTEDMSNLTF LNDASVLHNL RQRYYSMLIY TYSGLFCVVI
     NPYKRLPIYG ESVVHMYQCK RRNEMPPHLF AVADEAYRNM MQDRGNQSML ITGESGAGKT
     ENTKKVISYF AVICSTHANK EKDGKKRASL EEQIVQTNPV LEAFGNAKTV RNNNSSRFGK
     FIRIHFNGHG KLAGADIEHY LLEKSRVIKQ AQGERCFHIF YQIMSGKIAG LKEKLFLSKD
     IRKYKFISQA EITIDGVDDK EEMQITDDAF DIMNFDPSEK ENLYKLCAAI LHMEAELAAK
     LLCVNCDEFL KALLKPKVKV GTEWVNKSQN LEQVTWGVGA LCKAIYARMF RWLILRCNRT
     LDVQELGRKF FIGVLDIAGF EIFDFNSFEQ LWINFVNEKL QQYFNHHMFV LEQEEYKSEG
     IAWEFIDFGL DLEACIQLIE KPLGIISMLD EECIVPKASD MTFVQKLNDQ HLGKHPNFQK
     ARPPKGKQSE AHFSIVHYAG TVRYNANGWL EKNKDPLNES VVNVLKASDG NKLLSEVWAD
     YFTQEDLAKK KTTPSKKKGK AASFLTVSMM YRESLGNLMS MLRATHPHFI RCIIPNESKK
     SGIIEAGLVL NQLTCNGVLE GIRICRKGYP NRLVYADFKQ RYAIFAADEA KKYDDPKKSS
     EAILNTLKQK DVLKAEEFQV GATKVFFKAG ILARLEELHD EELSKIMVGV QATARSYLAK
     LDSRRRKKAH EASLLIQKNV RKWLKLRSWS WFRLYGRVKP LLTQAKQHEE FEKIQAKIKE
     LEAASSAEKA RCADMEAQLA NALKEKSDLI LKLESEKSNS TEYEQKAKTL SSQMDDLNKQ
     HKNLHEKLEM AEEQHSNTQK AKKKLQEEVD KLTARIVELE LLVKKHESDK QSLDMQLRSL
     KDAALHQEDA HAKLSKEKKA SDDKVQKLTQ DLHAVEDKVV SAEKVNKKLE NSLEEAHDAL
     EREKRLRQEL EKAKRKTDGD LKVTQENMEE ILKLKQDLEM NVKKKEDEIS VLNHTLEDEQ
     STAVRLQKVV KDLQVRVAEV EEELNMERQN RNKIERRRKE LQDEMDELQQ QLEEAGGASQ
     AQMELNKKRE AEIAKLKREQ EEAALAHEAQ ISSLKKKHTD AVAELNEQLN ALQNSRIKLE
     KGKSVLQKEI EELHLAVDSE TKSKAVHEKQ VKSLEAQLVD LQTNHEETLR QLKELELQKS
     RLVNESTDLQ KQLEEQDVQL NNLLRAKQTL SAELERTKQS CEEEMKQSES FASQLRNVQE
     ELSSAKEQLE EEAEIKTELH RMLSKANAET QQWRAKYEQE GLRKTEELED AKKKLVIKLQ
     SMQEEIEAAN LKANSAEKLR QRVVAELEDA VADSERANGY AQSLERKQRG FDKILDEWKQ
     KCDDLSAELD SSQRENKAVV TELYKLRQAL EEATDREEAV RRENKMLAQE IQEINDQLGE
     GGKNYHEVQK TRRRLEMEKE ELQNALDEAE SALETEENKV MRHQIELVQV KQEVEKRLQE
     KEEEFENVRR NHAKALESVQ ATLEAESRGR MELMKAKKKL ESDINDLEIA LDQAAKGNVE
     AQRLIKRYQE QIRELQAQID EEQRLRNEMK EKCESVERKC HALCAEKEEL TAMLEGSDRA
     RRNASHEVHQ AKEQVNDLIV QLNAAIVNRR KLEAEYQLLQ SEMEEMMESS KVNEEKSRKA
     TLEAVRLSDE LKQEQDHCQV LEQRNKSLEQ QIKDMQSGLE EAELSVLKGN KKYSQKLENK
     IRDLEMELDI NQKKYQESEK NRRKSERQVK ELQYQVDETK KNEDRLHELI DKLQNKVKTY
     KRQIEETEQL ASLNLSKYRQ LQHQLQDAEE RADVAENSLA KMRAKNRSQP YRSSSTIASP
     RDLSKCRSLS ALNNSTDEES
//
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