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Database: UniProt
Entry: A0A0K9P1L5_ZOSMR
LinkDB: A0A0K9P1L5_ZOSMR
Original site: A0A0K9P1L5_ZOSMR 
ID   A0A0K9P1L5_ZOSMR        Unreviewed;      1509 AA.
AC   A0A0K9P1L5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Myosin XI B {ECO:0000313|EMBL:KMZ62878.1};
GN   ORFNames=ZOSMA_43G00600 {ECO:0000313|EMBL:KMZ62878.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ62878.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. Plant myosin class XI subfamily.
CC       {ECO:0000256|ARBA:ARBA00008049}.
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:KMZ62878.1}.
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DR   EMBL; LFYR01001305; KMZ62878.1; -; Genomic_DNA.
DR   SMR; A0A0K9P1L5; -.
DR   STRING; 29655.A0A0K9P1L5; -.
DR   OMA; NQDNNDH; -.
DR   OrthoDB; 5489458at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR   CDD; cd15475; MyosinXI_CBD; 1.
DR   CDD; cd01384; MYSc_Myo11; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 3.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 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; IPR002710; Dilute_dom.
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; IPR037975; MyosinXI_CBD.
DR   InterPro; IPR036018; MYSc_Myo11.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF836; MYOSIN-6; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM01132; DIL; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 5.
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:UP000036987}.
FT   DOMAIN          8..57
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          62..732
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1156..1455
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          613..635
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          877..936
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          971..1047
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         156..163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1509 AA;  171839 MW;  065DEED83A85B9CE CRC64;
     MESTLSVTIG SLVWAEDAKV SWIDGEVVEI HGEKITISCT NGKTVVTNAS KVYHKDAEAS
     PCGVDDMTKL AYLHEPGVLQ NLKSRYDMNE IYTYTGNILI AVNPFRRLPH LYDTHMMKQY
     KGAAFGELSP HPFAVADAAY RLMINEGVSQ SILVSGESGA GKTESTKQLM RYLAYMGGRA
     VSEGRTVEQQ VLESNPVLEA FGNAKTVRNN NSSRFGKFVE IQFDQRGRIS GAAIRTYLLE
     RSRVCQVSDP ERNYHCFYML CAAPPEDIAR YKLGDPKSFH YLNQSKCIKL DGIDDAKDYL
     DTRRALDVVG INADEQDAIF RVVAAILHLG NVEFSKGKET DSSKPKDDKS WFHLKIAAEL
     FMCDEKALED SLCKRVIVTR DETITKNLDP ESAVHSRDSL AKIVYTRLFD WLVNKINSTI
     GQDPESKCLI GVLDIYGFES FKTNSFEQFC INLTNEKLQQ HFNQHVFKME QEEYTKEEID
     WSYIDFIDNK DVLDLIEKKP GGIIALLDEA CMFPRSTHDT FAQKLYQTFK NHKRFTKPKL
     SRSDFTICHY AGDVTYQTDL FLDKNKDYIV AEHQALLNAS RCSFVSTLFP PLSVDSSKSS
     KFSSIGARFK QQLQSLLETL NATEPHYIRC VKPNNLLKPA IFENNNVLQQ LRCGGVMEAI
     RISCAGFPTR RSFLEFVDRF GILVPEVLDG SFDEITAATQ LLEKVKIEGC QIGKTKVFLR
     AGQMAELDTR RNEVLGRSAN IIKRKMRSYL ACKYYISLKR SAIKMQSICR GELSRRIYEN
     MRRQAACLKI QTYLRMYLVR ISFKELLSSS ITIQAGLRGM TSRNELRFRR QTSAAIIIQS
     RCRQYLARTH FMRILKATMT TQCAWRGKVA RLELRKLKMA ARETGALQAA KNKLEKQVEE
     LTWRLQLEKR MRSDIEEAKT NENAKLQSAL HEMQLQFTET KSLLIKEREA AKIASAVPVI
     REVPVVDTET MQKLSAENMK LKDLVSSLEI KIDETEKIFK ETSKVSEDRL KKTVEAEAKI
     VHLSQAMQRL EEKLSNMESE DQILRQLALE KSPVKRMTEH LAIPITPTKN VSDNDQVDVT
     ELKEAQSAPT AIKDENFDPK LMRSYIERKL ENVDTLINCM GQKIGFSQGK PVAAFTIYKC
     LLHWKSFESE KTSVFDRLVQ LIGHKIEDQE SNDHLAYWLS NTSSLLFLLQ HSLKATGSTG
     VIPPRKPPTS LFGRMTQGFR SSPNIAVEGL DVVRQVEAKY PALLFKQQLT AYVEKIYGII
     RENVMKEISV MLSMCIQEPR INRVNILRTG RSFGTQSNIP SSHWQTIIAT LNSLLKTFQE
     NFVPHILVQK TFLQIFSQIN VQLFNSLLLR RECCTFSNGE YVKAGLAELE LWVAKARPEY
     AGSSWDELKH VRQAVGFLVI FQKYRISFDE IANDLCPVLS VQQLYRICTQ YRDDKYNTQS
     VSSPVLSSMR VLMSEDSNDA ASNAFLLDED SSISFSADEI CSSSQEKEFS EVKPSEELLK
     NPDFLFLDE
//
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