ID   A0A0N5CDU2_STREA        Unreviewed;      1484 AA.
AC   A0A0N5CDU2;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Myosin motor domain-containing protein {ECO:0000313|WBParaSite:SPAL_0001603600.1};
OS   Strongyloides papillosus (Intestinal threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001603600.1};
RN   [1] {ECO:0000313|WBParaSite:SPAL_0001603600.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   STRING; 174720.A0A0N5CDU2; -.
DR   WBParaSite; SPAL_0001603600.1; SPAL_0001603600.1; SPAL_0001603600.
DR   Proteomes; UP000046392; 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   Gene3D; 1.10.10.820; -; 1.
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; 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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 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|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}.
FT   DOMAIN          82..778
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          648..670
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1169..1209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          842..1150
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1258..1359
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1385..1481
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1169..1205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1484 AA;  173895 MW;  E935CC8BBA3D5FB1 CRC64;
     MSNTDRNIIK SLLTVPEKLI KEELNSNNYC DKVWILDLPY KLCTLISQID SNEVVVGFKD
     NNGIFKKKNV KKQLTQSVSS NHYVDDMCNL SELNEASVIA CLKARYINAN LIHTYSGLFC
     VFINPWTSSV SKIYTKDVKD FYKNEFKVEK ILPPHIYYVA MSAYDGILSG NKNQSILITG
     ESGAGKTENT KKIIEYIIEA SDSSSSKCNK MQNDLINSGI VLEAFANAQT IHNCNSSRVG
     KFIKLDFDKN GKLNNAKINC YLLEKSRVVF QNLGDRNFHI FYQLLSDGVD KKRKMSLGLK
     KPPNEYAFLS HGKIKNDANL NDKEDAQSTI NALLMLNFTE EDISQIFEVL SIILLMGEIK
     FGERKGLDIS FVESMEYVKE VCRLSQIDSS KFVDALTQPT IKIGDKLIRK NQNLKKTLSS
     VLGLSKLIYD KLFNWVVDRC NEILLNNDSN NYSSSFIGVL DMAGFEIMNI NSFEQFCINY
     TNERLQQFFN HFMFIKEQSE YLNEQIEWNE INFGVDLQPS IEMIEAPMGL LTLLQEECVV
     PNGNDISMLE KLTKTLDGEI FQKARQSVKN NNNSHFTIKH YAGIVGYNIE GWVEKNRDTV
     DNNVLEIMGT SNHSLLKIFF KNINNANNNT NKNSRTSTTV TSLYRESLHN LIEVLHSTNA
     NFIRCIVPNY EKRAFLMNET LVLNQLRCNG VLEGIRICQR GYPNRMSFND FINRYKCLLN
     YNSKEIQNSL RRQVGSKNRD AAVILCNYIP IDKEGYQIGK TKIFLKIGVV SQLENLRKKY
     LFDCTSNFQG ICRWYIEQKI LKYKYNKWDA ILTIQDNVKQ YIYTNQWDWW KIFLKVKQII
     PIKQNEKKIV DLINQNKQLL KELEEMKILL SEVEKEMELL KRELSILQKD LETKDDTYNE
     LKIEFTNSEK LLCFMEKRFD EQQSTLSKMQ SVLKQNERSL EKLKQEKELL EKEICQLKES
     YHTEQTLRQN FESEYEEYYN KYETLEKKHS QLLENSKNYI ECLHSMEAKL DEQKDLSQKQ
     NNKIVDLQNT IVELNDNINK LDSILNSERH LKRKIEDLKD DMEEKLEDLR DKLERSKGRE
     ETLKNQCIEK DRKIEKLENK IDQKSEYMDE CINELKKMHK ETQQEMKNQL DEYRRKCSKL
     EQDNRTLKIR VADVDDINEK SIIEDTDSYS SYKSNSRLGS RQPSLQSISY QSSTSNMTSS
     RYSTRSSLLR RRETEPDIFM AASMVSNENL STYGSLNRSP SFNSSRYTSN DMGKEKKICN
     LEKQIQNLNQ ENQLAKRELE VYKTNLVDME RRNSSLKNQI NAMTIENNNL NNKIERQEDE
     ILMYEERLKK YQKEANIWKQ KYEEMVDESR KELLMHRKKS EEKLKEICFE YSKKLHSYST
     SDRNKIKIQE ELDETKALLD STKAQLYEVK KHSKSQSILG DNWENKYRSC MTEIESLRDE
     NASLKNKVRR QYKEIELLTQ QNEIKEECAM FEKKVDSFQE RVPS
//