ID A0A0V0X7T2_9BILA Unreviewed; 1852 AA.
AC A0A0V0X7T2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Myosin-4 {ECO:0000313|EMBL:KRX83863.1};
DE Flags: Fragment;
GN Name=unc-54 {ECO:0000313|EMBL:KRX83863.1};
GN ORFNames=T06_1997 {ECO:0000313|EMBL:KRX83863.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX83863.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX83863.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX83863.1};
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:KRX83863.1}.
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DR EMBL; JYDK01000010; KRX83863.1; -; Genomic_DNA.
DR Proteomes; UP000054673; 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; -; 4.
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 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:UP000054673};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 78..127
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 131..834
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 709..731
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 949..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224..231
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:KRX83863.1"
SQ SEQUENCE 1852 AA; 214996 MW; 2284BC4AF0851308 CRC64;
RFFLCSVQLE QKQTSITLNC TLRTTHPVAA GCCGVSLFPI SRCVCSAMSY VNPEDDPGWQ
YLRQKAEQAL QDQMKAYDSK KNCWIPDATE GFIAAEIKST KGDMITVMSA KGNEVTLKKE
MVQEMNPPKF EKTEDMANLT FLNEASVLHN LRQRYYSMMI YTYSGLFCVV INPYKRLPIY
TESVIKLFMG RRRNEMPPHL FATSDEAYRN MVQDRANQSM LITGESGAGK TENTKKVIAY
FAIVGATQAA MASGDKKPQQ ATLEEQIVQT NPVLEAFGNA KTVRNNNSSR FGKFIRVHFN
KLGKLTGGDI EHYLLEKSRV IRQAPGERCF HIFYQMMSGQ LKGLRESLRL TKDLRYYHFV
SQAELTIDGV DDKEEMKVTD YSFDVMGFEQ EEKDNLYKLC AAIMHMGEMK FKQRPREEQA
EVDTLEDAEN ACHCFGVNHE EFAKALIKPR VRVGTEWVNK GQNLDQVHWA VGALAKAIYS
RMFHWLIVRC NKTLSMKDME KAFFIGVLDI AGFEIFDLNS FEQLWINFVN ERLQQFFNHH
MFVLEQEEYQ REGIKWEFID FGLDLQACID LLEKPLGIVS MLDEECIVPK ATDMTYVQKL
NDQHLGKHPN YQKAKPPKAK QAEAHFALVH YAGTVRYNVN GWLEKNKDPL NDTAVNVLKH
ANGNQLLLDI WKDYQTQEEA LEASKTGSSK KKGKSSSFMT VSMMYRESLN NLMSMLNSTH
PHFIRCIIPN EQKKSGLIEA SLVLNQLTCN GVLEGIRICR KGFPNRVQYP DFKHRYAILA
SDEAHSSEDA KVASEKMVDR MVVDKVFSEE EHRIGLTKIF FKAGVLARLE EIRDQKLSDI
LTGFQAQARW YLGKIDAKRR EEQRTGLLII QRNIRTWLKL RNWHWFKLYG KVKPMLRSSK
MEEEMQKLED KIKELEGNLN NEEKTRKDLE GQLAKLIQEK NDLFTQLQSE KGNLSSSEEK
IQKLTSQKSD LERQVNDLSD RLNNQEERGA ELQKAKKKVE SECENLNRKI LDLELSLRKA
ESEKQSRDNQ IRSLQDEMTS QDELAGKLNK EKKHQEEVNR KLMEDLQSEE DKVNHLNKLK
SKLEQQLDDL EDSLEREKRA RQDVEKGKRK VEGDIRVAHE NIDEINKQKH DLESNLKKKE
QEMQALSSKL EDEQGLVAKM QRQIKELQTR IQELEEELEQ ERQARSKSEK VRNDLQRQLE
ELSERLDEAG GATQAQLEMN KKREAELAKL RRDLEEANMN HEGQLASLRK KHNDAVAEMS
DQLDQVQKAK AKSDKEKVAY QRELEDLHAA MDQENKAKQD ADRFSKQLEL QMAELQAKND
EQTRQLHDYT NMKNRINSEN ADLMRQLEDA ESQLNSLNRL KSQYQTQLEE AKRTADEETR
ERHNLAAQLK NMEHENQSLR EQLEEEAESK TEMQRHISKL NAEIQQWKAK FESEGLARVD
EIEEAKRKLT QKVQEMQEAF EAANGKIASL EKIRHKLLGE IDDAQVDVER ANNYAAQLEK
KQKGFDKIVD EWKKKCDDLS SELDASQREN RHLSTECFKL KNSQDELIEQ IEAVRRENKN
LVQEIKDITD QLGEGGRSVH ELQKVVRRLE LEKEELQQAL DEAESALEAE ESKVMRAQVE
VSQIRQEIEK RIREKEEEFE NTRKNHQRAL DSMQATLESE AKGRAEALRL KKKLESDINE
LEIALDHANK ANADAQKNIK MYQDQVKELQ MHIEDEQRQR EEIREQFHAS EKRCAMLQSE
KEEYMTASEQ AERARRQAEA ELYELREQVN ELSSTNASLS AIKRKLEGEL QALHAELDDT
LNELKKVDEQ CKKAMTDAAR LAEELRQEQE HSMHVERMRK GLEQQVKVRK SK
//
