ID A0A0M3IQR9_ASCLU Unreviewed; 126 AA.
AC A0A0M3IQR9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Myosin N-terminal SH3-like domain-containing protein {ECO:0000313|WBParaSite:ALUE_0002109701-mRNA-1};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0002109701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0002109701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR AlphaFoldDB; A0A0M3IQR9; -.
DR WBParaSite; ALUE_0002109701-mRNA-1; ALUE_0002109701-mRNA-1; ALUE_0002109701.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 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; IPR027417; P-loop_NTPase.
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 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}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Muscle protein {ECO:0000256|ARBA:ARBA00023179};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 39..88
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 92..126
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
SQ SEQUENCE 126 AA; 14194 MW; F748024AB2D5B545 CRC64;
MLKVRSTMDE LGKFEDDPGY VYLEVSREER ATSAAKPFDS KKNCWIPDAE DGFVAAEIKS
ATGDKVTVVT AKGNEVTVKK EEVQEMNPPK FSKTEDMANL TFLNEASVLN NLKERYFSMM
IYTYSG
//
