ID Q9FPM4_PETCR Unreviewed; 1176 AA.
AC Q9FPM4;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Myosin subfamily VIII heavy chain {ECO:0000313|EMBL:AAG49341.1};
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043 {ECO:0000313|EMBL:AAG49341.1};
RN [1] {ECO:0000313|EMBL:AAG49341.1}
RP NUCLEOTIDE SEQUENCE.
RA Bramer B., Schmelzer E.;
RT "Cloning, expression and cellular targeting of the myosin heavy chains of
RT subfamily VIII and XI from parsley.";
RL Submitted (NOV-2000) 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; AF319457; AAG49341.1; -; mRNA.
DR AlphaFoldDB; Q9FPM4; -.
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; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
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}.
FT DOMAIN 131..180
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 184..842
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 20..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..745
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1038..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 969..1010
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 275..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1176 AA; 133726 MW; E63934AB5089338E CRC64;
MLSVSPSMLY RSSLEEMLDS LRRRDEEEKP RDLPPALPSR PTSKARRPST KRTLPTNFEN
NSEDLSCGKK QEVKHSRSGS FGGKKLKEGG LDESPYVVSP ALEDKQSVSS SASLPRFLNS
DLNDNFDYFI KKKLRVWRQL QNGQWESGHI QSISTEMASV LLKNGSVVTV SAEDLLPANP
DVLEGVDDLM ELSYLNEPSV LYNLEYRYSH DLIYSMSGPV LIATNPFKNV ELYGNDYVTA
YRQKLLDSPH VYSVANTAYN EMMRDGINQA IIISGESGSG KTETANVALQ YLESLGGGND
GIELQLMQTS HVLEAFGNAK TSLNDNSSRF GKSIAVYFND AGNICGAKIQ TFLLEKSRVV
HQARGERSYH IFYQLCAGAP SALKEKLNLK AASEYKYLNQ SCLGVNNVDD AQMFQILLKA
LSTLSISKED QEHVFEVVAA VLWLGNISFQ VIGNENHVEV VADEALSTAA SLIGCRCEDL
MLALSTSKSH TEKDNVAKNL ILQQAIDKRD ELAKFVYASL FNWLVYKING SMEKGELQDG
RSISILDIYG FESVQKNSLE QLFINYASER LHQHFIRHLL KLQQEEYDLD GIDWTNVEYR
DNKDCLDLFE KRQTGLISLL GEESRLSKTS NLTFAEKLNQ HCKTNPCFNR EQGGAFTIRH
YAGEVQYNSI DFLEKNRDSL HSDITGLLLS CSGQLPHLFA SNHVDDTSVF PQRSVGTKLK
AHLFKLMHQL ENSTPHFILC IKPNRKQIPG MFEKELVLKQ LRCCEILQVV RISRSGYPTR
LTHQEFAERY GILSKFDIIQ DPLSASVSVL QQFGIQPEMY QVGYTRLYFR TGQNDALEEA
RKQVLQGTLE VQKCFRCHQA RRYFHELKRG VTSLQSFVRA TNARRKYNHL INLKKQAVQK
TLDEQQRAVL QLQAVIRGWL VRRQSKRLLK LRKSNQENID SSHNLSWRIS DVKKQETHQE
SNQVLPLVIE ELRRRVLMAE TNLENKEQEN AALQDQVQQY EARWVEYEGK MKLMEDMWQK
QTASLQMSLA AVKKSLADST SVQSGKGEGS PSPHYYDSDD NNSMQTQTPD DTPIKITSSI
SEFGAGRLCN GNRNAVSHLM KEFEQRKQTF DNEAKAIIEV KSGGNPDEEL RSLKNKFETW
MKDYKARLRE AKTKLQKLPS AEKRRRNLWC GGISKW
//
