ID A0A0V1CMQ7_TRIBR Unreviewed; 2005 AA.
AC A0A0V1CMQ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Myosin-4 {ECO:0000313|EMBL:KRY50587.1};
DE Flags: Fragment;
GN Name=unc-54 {ECO:0000313|EMBL:KRY50587.1};
GN ORFNames=T03_16155 {ECO:0000313|EMBL:KRY50587.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50587.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY50587.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY50587.1};
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:KRY50587.1}.
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DR EMBL; JYDI01000146; KRY50587.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CMQ7; -.
DR Proteomes; UP000054653; 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; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF7; MYOSIN-3; 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; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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:UP000054653};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 70..119
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 123..826
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 701..723
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 941..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216..223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY50587.1"
SQ SEQUENCE 2005 AA; 232795 MW; 3480481CE324D6B5 CRC64;
LEQKQTSITL NCTLRTTHPV AAGCCGVSLF PISRCVCSAM SYVNPEDDPG WQYLRQKAEQ
ALQDQMKAYD SKKNCWIPDA TEGFIAAEIK STKGDMITVM SAKGNEVTLK KEMVQEMNPP
KFEKTEDMAN LTFLNEASVL HNLRQRYYSM MIYTYSGLFC VVINPYKRLP IYTESVIKLF
MGRRRNEMPP HLFATSDEAY RNMVQDRANQ SMLITGESGA GKTENTKKVI AYFAIVGATQ
AAMASGDKKP QQATLEEQIV QTNPVLEAFG NAKTVRNNNS SRFGKFIRVH FNKLGKLTGG
DIEHYLLEKS RVIRQAPGER CFHIFYQMMS GQLKGLRESL RLTKDLRYYH FVSQAELTID
GVDDKEEMKV TDYSFDVMGF EQEEKDNLYK LCAAIMHMGE MKFKQRPREE QAEVDTLEDA
ENACHCFGVN HEEFAKALIK PRVRVGTEWV NKGQNLDQVH WAVGALAKAI YSRMFHWLIV
RCNKTLSMKD MEKAFFIGVL DIAGFEIFDL NSFEQLWINF VNERLQQFFN HHMFVLEQEE
YQREGIKWEF IDFGLDLQAC IDLLEKPLGI VSMLDEECIV PKATDMTYVQ KLNDQHLGKH
PNYQKAKPPK AKQAEAHFAL VHYAGTVRYN VNGWLEKNKD PLNDTAVNVL KHANGNQLLL
DIWKDYQTQE EALEASKTGS SKKKGKSSSF MTVSMMYRES LNNLMSMLNS THPHFIRCII
PNEQKKSGLI EASLVLNQLT CNGVLEGIRI CRKGFPNRVQ YPDFKHRYAI LASDEAHSSE
DAKVASEKMV DRMVVDKVFS EEEHRIGLTK IFFKAGVLAR LEEIRDQKLS DILTGFQAQA
RWYLGKIDAK RREEQRTGLL IIQRNIRTWL KLRNWHWFKL YGKVKPMLRS SKMEEEMQKL
EDKIKELEGN LNNEEKTRKD LEGQLAKLIQ EKNDLFTQLQ SEKGNLSSSE EKIQKLTSQK
SDLERQVNDL SDRLNNQEER GAELQKAKKK VESECENLNR KIQDLELSLR KAESEKQSRD
NQIRSLQDEM TSQDELAGKL NKEKKHQEEV NRKLMEDLQS EEDKVNHLNK LKSKLEQQLD
DLEDSLEREK RARQDVEKGK RKVEGDIRVA HENIDEINKQ KHDLESNLKK KEQEMQALSS
KLEDEQGLVA KMQRQIKELQ TRIQELEEEL EQERQARSKS EKVRNDLQRQ LEELSERLDE
AGGATQAQLE MNKKREAELA KLRRDLEEAN MNHEGQLASL RKKHNDAVAE MSDQLDQVQK
AKAKSDKEKV AYQRELEDLH AAMDQENKAK QDADRFSKQL ELQMAELQAK NDEQTRQLHD
YTNMKNRINS ENADLMRQLE DAESQLNSLN RLKSQYQTQL EEAKRTADEE TRERHNLAAQ
LKNMEHENQS LREQLEEEAE SKTEMQRHIS KLNAEIQQWK AKFESEGLAR VDEIEEAKRK
LTQKVQEMQE AFEAANGKIA SLEKIRHKLL GEIDDAQVDV ERANNYAAQL EKKQKGFDKI
VDEWKKKCDD LSSELDASQR ENRHLSTECF KLKNSQDELI EQIEAVRREN KNLVQEIKDI
TDQLGEGGRS VHELQKVVRR LELEKEELQQ ALDEAESALE AEESKVMRAQ VEVSQIRQEI
EKRIREKEEE FENTRKNHQR ALDSMQATLE SEAKGRAEAL RLKKKLESDI NELEIALDHA
NKANADAQKN IKMYQDQVKE LQMHIEDEQR QREEIREQFH ASEKRCAMLQ SEKEEYMTAS
EQAERARRQA EAELYELREQ VNELSSTNAS LSAIKRKLEG ELQALHAELD DTLNELKKVD
EQCKKAMTDA ARLAEELRQE QEHSMHVERM RKGLEQQVKE MQVRLDEAEQ AALKGGKKII
QKLEQRIREL EQELDLEQRR HQETDKNMRK QDRRIKETEF QLEEDKKNAE RMQDLIDKLQ
QKLKTYKRQI EEAEELAATN LSKYRQLQQQ LEDAEERADI AENSLAKLRA KNRSSTSVGG
NMAISHSASG ILRSASRARM TNNMD
//
