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Database: UniProt
Entry: A0A2A2LKK6_9BILA
LinkDB: A0A2A2LKK6_9BILA
Original site: A0A2A2LKK6_9BILA 
ID   A0A2A2LKK6_9BILA        Unreviewed;      1809 AA.
AC   A0A2A2LKK6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=WR25_17126 {ECO:0000313|EMBL:PAV86761.1};
OS   Diploscapter pachys.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX   NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV86761.1, ECO:0000313|Proteomes:UP000218231};
RN   [1] {ECO:0000313|EMBL:PAV86761.1, ECO:0000313|Proteomes:UP000218231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF1309 {ECO:0000313|EMBL:PAV86761.1};
RA   Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA   Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT   "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL   Curr. Biol. 0:0-0(2017).
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:PAV86761.1}.
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DR   EMBL; LIAE01006637; PAV86761.1; -; Genomic_DNA.
DR   Proteomes; UP000218231; 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; -; 5.
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; 2.
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   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}; 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:UP000218231};
KW   Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT   DOMAIN          26..75
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          79..786
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          661..683
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          868..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1039..1062
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1603..1625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1771..1792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1809 AA;  208963 MW;  7711838908065BF1 CRC64;
     METDAGWQFL RQSQEQMLAS MTKKFDSKKN IWIADPEDGF VAAEIKSSKG DTHVVVTAKG
     VEKTIKKDDA QQMNPPKFEK TEDMANLTFL NDASVLNNLR QRYYSMMIYT YSGLFCVVIN
     PYKRLPIYTE SVAKMYLGKR RNEMPPHLFA VSDEAYRNMV NDHENQSMLI TGESGAGKTE
     NTKKVISYFA MVGATQTKKV DEKSDKKKNA TLEDQIVQTN PVLEAFGNAK TVRNNNSSRF
     GKFIRIHFNH AGKLAGGDIE HYLLEKSRVI KQAPGERCYH IFYQIYSDAI KGLKDRLFLT
     RPIKDYHFVA QAEVTIEGVD DKEEMMLTDE AFDIMKFDQR EKDELFAITA GIMHMGELKF
     KQRPREEQAE LENGKEGELA CKLYQVEPEK FIGALLKPRV KVGAEWVNKG QNLEQVNWAV
     GALAKALYAR MFAWLIQRCN KTLDAQDLPR DFFIGVLDIA GFEIFDLNSF EQLWINFVNE
     RLQQFFNHHM FVLEQEEYQR EGIKWEFIDF GLDLQACIEL IEKPLGIISM LDEECIVPKA
     TDLTLAQKLS DQHLGKHPNF QKPKPPKGKQ AEAHLAIVHY AGTVRYNVLS WLEKNKDPLN
     DTAVTILKAN AGNALMDALW SNYDTQEDIA NQAKEGKTVP GKKKGKSASF MTVSMMYRES
     LNKLMNMLHQ THPHFIRCII PNEQKKAGVI EATLVLNQLT CNGVLEGIRI CRKGFPNRMP
     YLDFKQRYAI LAADAVKTGK DVKDAGEKIV GQLEKKGQLK VEEFQCGLTK VFFKAGVLAR
     LEELRDEALS IIMTKFQCAA RGYLALCEYK RRKEQRVGLL IVQRNVRAWC TLRNWTWFKL
     FGCVKPMIKG NKKDEEFEAL EKKYKELEEE KNKEEKRRKE LESETDRMNA EKQALLAQLE
     QERDANAETE ERSAKLLAQK ADLEKQNADL NDQLADQEDK NSTLSKAKKK VEQDCENLKK
     NVADLETTIK KQESEKQSKD HQIRSLQDEI AAQDEVINKI NKEKKHQEEV NRKLLEDIQA
     EEDKVNHLNK LKTKLESSLD ELEDQIEREK RGRQDLEKQK RKVEGELKLA QETIEELNRQ
     RHEQEQALKK KDAEIHNLQS RLEDEQSLVA KLQKHIKELL AKIQELEEEL EAERQSRAKA
     EKARNEMQLE LEELGDRLDE AGAKLEKEKA ALQREVDELQ QTLDVDAKQR QNCERLAKQL
     ESQLTDMTLK SDEQARLIQE LTMGKSKMHN ENSDLNRQLE DAESQLAALN RIKQQQHSQL
     EELKRQLEQE SRERSTLHSQ AANYQLECEQ LREQLEEEQD AKTELQRQVS KANAEAQQWR
     AKFEGEGVNR SEELEEARRR LTHKVQEMQE HLEQANQKIA TLDKTRQRLQ HELEDAQVDA
     DRANQIATSL EKKQKGFDKV IDEWKRKCEA LVAEVEQSQR ETRAAATETF RLRNQLEESH
     EQTEAVKREN RALAQELKDI ADQLGEGGKS VHDLQKLRRK LEIEKEELQQ ALDDAEAALE
     GEEAKVLRAQ VEVSQIRSEI EKRLQEKEEE FESTRKNHAR AIESMQATLE NETRGKAELL
     RMKKKLESDI NELEIALDHA NKANVESQRN LKRYQETVRE LQTQAEDEAR HRDEAREHAA
     TAERRAQALQ QEKEDMAVGF EQAERSRRQA ELLAAEHKEA LNDFVAQNMG LTSIKRKLES
     ELQQLHSEIS DALNEAKNSE DRAKKCAMDA AKVSDELRAE QEHSANLERA KKANESHIKD
     LQTRLDEAEA NQAKGGKKAI AKLDARVHDL ESELDSEQRR HTETAKNLRN KDRRCRELQF
     QVAKIHQKR
//
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