ID A0A0V0RPV9_9BILA Unreviewed; 1390 AA.
AC A0A0V0RPV9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Unconventional myosin-Va {ECO:0000313|EMBL:KRX16529.1};
GN Name=MYO5A {ECO:0000313|EMBL:KRX16529.1};
GN ORFNames=T07_4420 {ECO:0000313|EMBL:KRX16529.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX16529.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX16529.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX16529.1};
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {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:KRX16529.1}.
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DR EMBL; JYDL01000105; KRX16529.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0RPV9; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
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; 1.20.5.190; -; 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; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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:SF289; UNCONVENTIONAL MYOSIN-XIX; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000054630}.
FT DOMAIN 94..765
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1070..1340
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 643..665
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1390 AA; 160377 MW; 95D3573C29D33845 CRC64;
MFVSLECENV EEMTKIKKQN DFDDSRFFQT NYSKGTSVWI ADDKEIWISG NIIENSTADD
GHFLTLQLEN DKKVKLRFSK KSELPLLRNP EFLMDSNDLT SLSYIQEPDI LYALKNRFER
ECIYTYFGIA LVAVNPYKDV DLYDKSIYKL YRNGNVRQLD PHIFGIAEEA FSSLDQQKQN
QSIIISGESG AGKTVSANHV FRYLTQACAH RHAIDSLIIA SNSLIEAFGN AKTVQNDNSS
RFGKFTRIFF DDRLNASGAQ MEAYLLEKSR ISFQGKCERN YHIFYQMSTA RESTPLLKGF
NMKHHSSYKY LCSNEDACML TANDSKKFEE TVNCFKILGF KDDEIREIFA VLIGILHFGN
LSFSGEANNK KAIRKNSAND LNRCCELLGL NEEDLAEKFT YQRLAIRREV VHRQLNSADA
DALKDGICKY IYESLFRWII KKINDRLSEK SPLSEMNFIG VLDIYGFEIF PTNSFEQLCI
NFANELLQQQ FYKHVFKLEQ EEYVKENICW SFIDFRDNEA CLLLFEARLG IFSLLDQECQ
LPRPSDNNFY NELKNSKQCQ ESCSFKLPAI AGDEFLVVHY AGTVKYCVRD FVKKNLDTVN
ESFNEVLRNS RNCFLVQLLQ AGSCPQLQKS SKRTVGSQFR KSLSTLMDTL NSTNPHYVRC
IKPNDEKLPF TFNNARTIQQ ITACSLLETL KISAAGHPTR WKYESFFDRY FLLLTMKERN
EQSTTLSDKC RQICERFLNN ENFEFGSTKI FFRTGQIALL EAERHMKLNQ SVLLIQKCVR
KFIAARRGIR KIETATRTVQ NACFAWLAWR RIKFLQIHRA AIAIQSFFKM IIQRKRYLLI
QNVVLNLQSY GRAILVRSTF QKKKKAAIII QRYVRTWLKK KQTNLISSSQ LQSRQINDAL
SKISSVVVEI NNNDNTFGTS LLMAKEPKLE SANLSAKSVN ECRCSENDDG LEKCQLIFKI
FNECTSSTAF REEFVKRLKK DTIVKNLLHV LLMEANKSEI LPAKNMDDCM SSSTTAKKNG
QLSPSLQVFD HVGFVNALVN ECYQNQTCLP VILLLAFRYY DVLGIPEKST QLYFEVENAI
TDSTSCFLFL FWLQNMRRLN HLLSQYSGSS QFSTPAIEHL IEKYKFRRTD AQIILSHCQW
QVSNIYRNLF HECIAPRICP LLVPALLEFK SDDVNKFITK RGAKKGKKFE DKHMEMLIHH
LDTVHNAAMI VPFDAKAMLC LFSDIAKLIL TVSFNELMFR RDLCNLRSGV RIKHNVCILV
QWFKKHQFVQ IEIILQPLLQ VANLLQARKT DADIQGFNEI CSSLKVSQII NVLRHYSPIG
DYEPKVSASF ICNVKQKLLA LRKETETGNE PTIIPENYLN ANDLLNFEPC DVDLKTVEIP
TSVEAYATKI
//
