GenomeNet

Database: UniProt
Entry: A0A498S4Q0_ACAVI
LinkDB: A0A498S4Q0_ACAVI
Original site: A0A498S4Q0_ACAVI 
ID   A0A498S4Q0_ACAVI        Unreviewed;       913 AA.
AC   A0A498S4Q0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN   ORFNames=NAV_LOCUS465 {ECO:0000313|EMBL:VBB25635.1};
OS   Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Acanthocheilonema.
OX   NCBI_TaxID=6277 {ECO:0000313|EMBL:VBB25635.1, ECO:0000313|Proteomes:UP000276991};
RN   [1] {ECO:0000313|EMBL:VBB25635.1, ECO:0000313|Proteomes:UP000276991}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) 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}.
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DR   EMBL; UPTC01000028; VBB25635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498S4Q0; -.
DR   STRING; 6277.A0A498S4Q0; -.
DR   Proteomes; UP000276991; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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; cd21759; CBD_MYO6-like; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.220.10; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR049016; MYO6_lever.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF745; UNCONVENTIONAL MYOSIN-VI; 1.
DR   Pfam; PF21521; MYO6_lever; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000276991}.
FT   DOMAIN          54..702
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          582..604
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          837..898
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         148..155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   913 AA;  105339 MW;  A0B45A95F9E27E44 CRC64;
     MNTHVWVSDD KDGFILCKII DIGYECLTLQ RLHETETFKA FYDNIFPAGE EVSRDVDDNC
     SLIHLNDGSL LNNCRLRYNR KQFYTYMANI LIAINPYEQI DGLYDVNMVR KYKGQSLGAL
     TPHIFAIADK AYRDMMRNHE SQSIIISGES GAGKTESQKH IIRFLCESWG HLVGTIEQRI
     LEISTILESF GNAKTACNNN SSRFGKFIEI HFNDKGIIVG GFISHYLLER SRLCGQNARE
     RNYHIFYQLI AGTDEQTRSK LKLDKLEIFN DGMRDELIDD YNDFQKLLNA FNRIDVSIDT
     RDTILEIVAA ILHLGNIEFF DETFSFKSGC DVKEESKTYL INAAELLGIE VTDLRTHLVS
     RLMQPTRGGT KGTLYSVPLR ASEASAARDA LAKAIYSRLF TAIINKITEC MPFNESTFSI
     GVLDTAGFEL FEQKLYGIFE LLDNESRLPQ SSTQHFTRTV HETHTSHPCL MVWTERLSRL
     TYKKAPLLVV PRSSRCHRTM RDDEGFIICH YAADICYDTA QFLDKNNDTL HASLQCLMEQ
     SRKSLVCELF IGSEFSNVER RDAPLGGKLV NASVGNKFRS QLDVLLAKLR KTGTHFVRCI
     KPNSEMKCNQ FDGAQILLQL KCAGMSSALR VMQRGFPSRI SYLSLYNIYQ KYLPSRLTTL
     DAQLFCKCLF RVVGLEEKDY KFGLTKAFFR HGKFAEFDKI LHLSKENFET LIEHMSSWLC
     CFRFRRIQFA VISLVKVERL LAYRAKCRIK IQNAVRTYLV RKSYRSRINA LLALSTLLKN
     INGMYSLVNE LDKTDSYKWG SSIVDALKED VETLKYQIKH NSYSTDTEMF HRCDALVNNT
     KEKLQHLRQK VDDTQMLLRK KHEKFEEEQK SELRKELNQQ INGQKEEAKQ IAQCLEESLE
     HTKIMERENH QLL
//
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