ID A0A2P5B739_PARAD Unreviewed; 1221 AA.
AC A0A2P5B739;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Myosin head, motor domain containing protein {ECO:0000313|EMBL:PON44571.1};
GN ORFNames=PanWU01x14_265560 {ECO:0000313|EMBL:PON44571.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON44571.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) 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:PON44571.1}.
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DR EMBL; JXTB01000347; PON44571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5B739; -.
DR STRING; 3476.A0A2P5B739; -.
DR OrthoDB; 5489458at2759; -.
DR Proteomes; UP000237105; 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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030048; P:actin filament-based movement; IEA:UniProt.
DR CDD; cd01383; MYSc_Myo8; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
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; 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; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036022; MYSc_Myo8.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 2.
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}; Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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}; Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT DOMAIN 149..198
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 202..872
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..774
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 1003..1051
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 17..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1221 AA; 138027 MW; 90BE104C232C8016 CRC64;
MMLSASPSMI VRSSLEEMLD SLRRRDEEEK PKDLPPALPA RPTSRGRLPP ARRSLPNNFK
VVGDDGSPEC LPSENEETKR KDSDWGAQRN GFACKKMKKD QNVESPYVVA PEEVKIELTG
SSDRAGLASA SPPRVRGTDW DDNIGYFMKK KLRVWCRLPS GQWELGIIQS TSGEDATVSL
SNGNVVKVTA SELLPANPDI LEGVDDLVQL GYLNEPSILH NLQHRYSKDM IYSKAGPVLI
AVNPFKDIQI YGDDFISAYR QKRLDGPHVY AAVDTAYNEM MRDEVNQSII ISGESGAGKT
ETAKIALKYL AALSGGHSDI EHRILQANYV LEAFGSAKTC RNHNSSRFGK LIEIHFSTLG
KICGANFQTC KHSRVVQLAN GERSYHIFYQ LCAGAPSNLK ERLNLRMASE YKYLNQSDCL
KIDGVNEAEK FHVLKEALNL VRICKEDQEC VFSMLAAVLW LGNISFRAVD NGNQVEVLAD
EATTNAAKLM GCSAEELILS LSVHKTEVGK GSIADILTLQ QAIDRRDALA KFIYSSLFEW
LVEQINKSVQ VGKRQIGRSI SILDIYGFES LQKNSFEQMF INYANERLQQ HFIRHLLKLE
QEDYELDGID WTKVDFEDNQ ECLDLFEKKP SGLISLLDEE SNLPKASDLT FANKLKQHLN
LNSCFKGERG RAFSVRHSAG EVLYDTNGFL EKNKDLWHAD VCQLLSSCHS ELLQLFASKM
LSQSRKPATT LCQISSSDVL RQSVGTKFKV QMFKLMLQLE STRPHFICCI KPNNKQLPSI
DQVDLVLQQL RSCRVLEVLR ISRSGYPTRM QHHEFAGRYG FLLSKTSVAR DPLSISIAVL
QQLGILPEMY QIGYTKVFLR TGQIEKLENR RKQVLLGVVG VQKCFRGHQA RRHFYELKKG
LKTYFYNADA PSESIRGKNN IVFKWRTANA PKTLDELQAV ICLQSVIRGS LVRKHFIGTH
ELKKLQPESV KSRKNPGRKI SEVKVFAERS VPGEQVHTMP LALKEFQQRV IKAEETLEQK
EEENAALREQ VQQFEARWSE YEAKMKSMEE MWQKQMASLQ MSLAAARKSL AVDNGVGQPG
RLDGAFSPRY YDSEDATSMG SRTPGASTPL KFSNSVHDVG SGRDTNGTLS AVSNLVKEFE
QQRQTFDDEA KVLVGVKTGQ PALNINSDEE LRKLKLRFEM WKKEYKLRLR ETKVKLHKLN
HSEAERSRRR WWGGRISTRA S
//