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Database: UniProt
Entry: C6JVY8_PHATR
LinkDB: C6JVY8_PHATR
Original site: C6JVY8_PHATR 
ID   C6JVY8_PHATR            Unreviewed;      1488 AA.
AC   C6JVY8;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Myosin F {ECO:0000313|EMBL:ACS35542.1};
OS   Phaeodactylum tricornutum (Diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=2850 {ECO:0000313|EMBL:ACS35542.1};
RN   [1] {ECO:0000313|EMBL:ACS35542.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UTEX 646 {ECO:0000313|EMBL:ACS35542.1};
RX   PubMed=20217677;
RA   Heintzelman M.B., Enriquez M.E.;
RT   "Myosin diversity in the diatom Phaeodactylum tricornutum.";
RL   Cytoskeleton 67:142-151(2010).
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; GQ141546; ACS35542.1; -; mRNA.
DR   HOGENOM; CLU_249324_0_0_1; -.
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   CDD; cd00124; MYSc; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
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; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 7.
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.
PE   2: Evidence at transcript level;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   Coiled coil {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|PROSITE-ProRule:PRU00782}.
FT   DOMAIN          94..847
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          163..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          713..735
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          1206..1283
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        165..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         227..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1488 AA;  169840 MW;  F0C6603ACE4CB7BF CRC64;
     MSWMPLDPPR VGDPVYVRDD SYAWLPARVL QIRNPDHHQV LVRVDLPANW DRTTVAFPKD
     INTDTESHLD GREVWIDLTS YTNHQLPRRN ADKVVARDMA ELQFLHEAAV LYQIKARHAS
     QRPYTRVGDI VVAVNPYTWI EGLYDPAQQA LYANRLVWDD HGNQDTSTIP REEKKDDGMH
     TGSSASSSAF VSAYDRLGFE PHVYEISALA YRGMIQEGKN QTIIVSGESG AGKTETVKIV
     VQHLAMLEHT APSVSVDTNP ASLDIVRHVV ESSPLFEAFG NAMTTKNSNG SRFGKVTRLH
     FAPDWTADTQ DTFCYSLKGS SYQTYLLETN RIVYQTAGER SFHIFYQLLS ASSDLKRTML
     GEEWIDATEK DFCYLGEPRE CQVDGHSDAQ SFIKTLHALE LFGWEGDALQ SLFGALGAVL
     RIGNLTFQEQ EEGEAIVSSD TALRLLADAV GLSTTDLESA FTHLIIKANN DTIEVPLSAE
     ISKNTTDALA KQMYSFIFDS VVMKVNQWTA SSKSSEAEAA ISLVDICGFE SFETNRFDQL
     CINYANEKLQ HKYVQDNLLK KRVEHEREEI ELFDTTLMDN SDILDLIEGR EGLINVMNEE
     CMRPNGNNKT FVFKLTNVHR KNARFLRKKL DRSTQFGISH FAGDVMYDAS EFIERNTDKV
     PESLLTLFTK SSNVLIREQF VAFLQKSEEK RSTRATRKKS TVTTVLDKFR VSLKDLMLTM
     SDTHTRYIRC IKPNDTMSIA IADHLLTVKQ LQCAGLVTAI DLTRESFPNK YSFSTAVQRF
     HSLMNSEQKH DLKDMKLHDK AQYMMSSLFT PLIEQYRNSD FTMPFVCGKT KIFFRSGALE
     VLETQRRELH FMKASILQQQ IRGIQSRSNY RRMKFAVISS QAAYRGKTKR SEFRRAQQSI
     ILLQAWARRS RTQRKYLRLK RAVVVLQMRA RRIYHAHLRL NATKLQKQIR VFQSRKKCQC
     LKVAMVTCQD DDRVATTISR FGSAIPAVVL IQGWMRRLQT QARYCRLKRA VTNVQMWIRL
     QLARKMLARQ QRAAIKIESI VRSYNESVRC STTQKVASKI STWWRAVSLR LAFRLKRLLV
     LIIQSHTRGA LVRKKRCQQH LKSAGTNLVN EEWLGGHRFC ASAPIDSASV LQAWVGRTRL
     QSQKLNSMIG FEASDQIPIQ KVVGGKIDAN DGEVLYTVSL HSSASRNQDS LLHTQESKGW
     EDNALLEKLK NENMMYANEI AILKEDIRQV TAEAETHKAE INNEYEDRLI DYEKEVIELQ
     EALKLAEAEK RELQRQADAS KKSYFKKIRR YKEKATNNHR AHQEYLEDVQ QIFEAKTARF
     LADLETLRCD KDKRIADLEH QAALLQKSKS CTGEPAVESS RISLVVHSDW PPSLLVEAEQ
     LARDLYSLTS AASILRVVEA SQLNSGSPAL YIEQKVTSQV QMIVPRLLEM IELIDTDHDE
     KNEGYHEVYN CEEADDESKL SDIYDLDLSK GAPSTTLSDE RFTLCGRT
//
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