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Database: UniProt
Entry: M7BU29_CHEMY
LinkDB: M7BU29_CHEMY
Original site: M7BU29_CHEMY 
ID   M7BU29_CHEMY            Unreviewed;      1945 AA.
AC   M7BU29;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Myosin-7B {ECO:0000313|EMBL:EMP41316.1};
DE   Flags: Fragment;
GN   ORFNames=UY3_01417 {ECO:0000313|EMBL:EMP41316.1};
OS   Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX   NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP41316.1, ECO:0000313|Proteomes:UP000031443};
RN   [1] {ECO:0000313|Proteomes:UP000031443}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; KB494182; EMP41316.1; -; Genomic_DNA.
DR   STRING; 8469.M7BU29; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14927; MYSc_Myh7b; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.5.370; -; 5.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 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; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF29; MYOSIN-7B; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 1.
DR   PROSITE; PS50096; IQ; 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};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
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:UP000031443}.
FT   DOMAIN          30..79
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          83..784
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          661..683
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          848..1288
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1319..1937
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMP41316.1"
SQ   SEQUENCE   1945 AA;  224270 MW;  A9719641585E30FC CRC64;
     MMDLSEFGEA ADFLRKSYTE QLKLQTIAFD GKKRAWIPDD KEAYIEVEIK EISGGKVTVE
     TKNKDSRVVK EDDVQQMNPP KFDMIEDMAM LTHLNEASVL YNLKRRYSHW MIYTYSGLFC
     VTINPYKWLP VYTSPVVAAY KGKRRSEVPP HIYSIADNAY NDMLRNRENQ SMLITGESGA
     GKTVNTKRVI QYFAIVAALG DTPGKKGQAP ATKTGGTLED QIIEANPAME AFGNAKTLRN
     DNSSRFGKFI RIHFGPSGKL ASADIDIYLL EKSRVIFQQP GERSYHIYYQ IVSGKKPELQ
     DMLLLSLNPY DYHFCSQGVT TVDNLDDGEE LMATDHAMDI LGFSNEEKYG CYKIVGAIMH
     FGNMKFKQKQ REEQAEAENT ESADKAAYLM GISSADLIKG LLHPRVKVGN EYVTKGQNVE
     QVVYAVGALA KATYDRMFKW LVTRINKTLD TKLARQFFIG VLDIAGFEIF EFNSFEQLCI
     NFTNEKLQQF FNHHMFVLEQ EEYKKEGIEW IFIDFGLDLQ ACIDLIEKPL GILSILEEEC
     MFPKASDMSF KAKLYDNHIG KSPNFQKPRP DKKRKYEAHF ELVHYAGVVP YNIIGWLDKN
     KDPLNETVVG VFQKSQNKLL GSLYENYVSS SSDEPPKSGV KEKRKKAASF QTVSQLHKEN
     LNKLMTNLRA TQPHFVRCII PNETKTPGAM DAFLVLHQLR CNGVLEGIRI CRKGFPNRIL
     YADFKQRYRI LNPAAIPDDK FVDSRKATEK LLTSLELDHT QYKFGHTKVF FKAGLLGHLE
     EMRDERLAKI LTMLQARIRG RLMRIEYQKM ISRREALYTI QWNIRAFNAV KNWSWMKLFF
     KIKPLLRSAQ NEKEMATLKE EFQKLKEALE KSEAKRKELE EKQITMIQEK NDLSLHLQAE
     QDNLADAEER CDLLIKAKIQ LEAKVKELTD RLEDEEEMNA DLTSKKRKLE DECAELKKDI
     DDLEITLAKV EKEKHATENK VKNLIEEMAA LDEIIAKLTK EKKALQEAHQ QALDDLQAEE
     DKVNTLTKAK VKLEQQVDDL ESSLEQEKKI RMDLERAKRK LEGDLKLTQE SVMDLENDKQ
     QLEEKLKKKE FETNQLNSRI EDEQVLGAQL QKKIKELQAR IEELEEELEA ERAARAKVEK
     QRAEVSRELE ELSERLEEAG GVTAVQLEMN KKREAEFLKL RRDLEEATLQ HESTAAALRK
     KHDAPVAEAG QAHNLQRVKQ KLEKEKSEMK MEVDDLSSNI EYLTKNKANA EKLCRTYEDQ
     LSEAKSKVDE LQRQLADVST QRGRLQTENG SCLALSALGE LSRLLEEKES FINQLSRGKT
     SFTQTIEEIK RQLEEETKSK NALAHALQAS RHDCDLLREQ YEEEVEAKGE LQRTLSKANA
     EVAQWRTKYE TDAIQRTEEL EEAKKKLAIR LQEAEEAVEA AHAKCSSLEK TKHRLQTEIE
     DLSIDLERAN SAAAALDKKQ RNFDRILAEW KQKYEETQAE LESSQKESRS LSTELFKLKN
     AYEESLDNLE TLKRENKNLQ EEIADLTDQI SLSGKTIHEL EKVKKALESE KNDIQAALEE
     AEGALEHEES KTLRIQLELS QIKADVERKL AEKDEEFENL RRNHQRAMDS MQATLDAEAK
     ARNEAIRLRK KMEGDLNEME IQLSHANRQA AESQKLVRQL QAQIKDLQIE LDDTLRHNDD
     LKEQAAALER RNNLLVAEVE ELRAALEQAE RGRKLAEQEL LEATERVNLL HSQNTGLINH
     KKKIEADLAQ LSSEVEEAVQ ECRNAEEKAK KAITDAAMMA EELKKEQDTS AHLERMKKNM
     EQTIKDLQMR LDEAEQIALK GGKKQIQKLE ARVRELEGEL DIEQKRNAET QKGIRKYERR
     VKELTYQTEE DRKNLARMQD LIDKLQTKVK SYKRQFEEAE QQANSNLVKY RKVQHELDDA
     EERADIAETQ VNKLRSRTRD VITSK
//
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