ID L5KTY0_PTEAL Unreviewed; 1844 AA.
AC L5KTY0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Myosin-XVI {ECO:0000313|EMBL:ELK14899.1};
GN ORFNames=PAL_GLEAN10013728 {ECO:0000313|EMBL:ELK14899.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK14899.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030555; ELK14899.1; -; Genomic_DNA.
DR STRING; 9402.L5KTY0; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0515; Eukaryota.
DR InParanoid; L5KTY0; -.
DR Proteomes; UP000010552; 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:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd14878; MYSc_Myo16; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036042; MYSc_Myo16.
DR InterPro; IPR029353; NYAP_C.
DR InterPro; IPR039482; NYAP_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47335; UNCONVENTIONAL MYOSIN-XVI; 1.
DR PANTHER; PTHR47335:SF1; UNCONVENTIONAL MYOSIN-XVI; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF15452; NYAP_C; 1.
DR Pfam; PF15439; NYAP_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT REPEAT 92..124
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 125..157
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 158..192
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 221..253
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 254..286
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 401..1122
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1001..1023
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1246..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1516..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1634..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 475..482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1844 AA; 205483 MW; C894005D4A9F05A0 CRC64;
MEIDQCLLET LPLGQRQRLV KRMRCEQIKA YYEREKAFQK QEGFLKKLKH GKNQKVHFNL
ADMIQDAIIH HDDKEALLLL KEGADPHTPV SSGGSLLHLC ARYDNAFIAE ILIDRGVNVN
HQDEDFWTPM HIACACDNPD VVLLLVLAGA NVLLQDVNGN TPLDYAVEGT ESSSILLTYL
DENGVDLTSL HQMKLQRPMS MLTDVKHFLS CGGNVNEKND EGVTLLHMAC ASGYKEVVSL
LLEHGGDLNI VDNQYWTPLH LAAKYGQTNL VKLLLMHQAN PNLLNCNEEK ASDVAASEFI
EEMLLKAEIA WEEKMKEPLS VPTLAQEEPY EEIIQDLPVV SSKLSPLVLP IAKQDSLLEK
DIMFKDSTKG LCKRQSLDST PENATVNGPT KTEQVKLMPP APNDDLATLS ELNDGSLLYE
IQKRFGNNQI YVSQLYLSSM GQPCSSLPPH IFSCAERAFH QLFQEQRPQC FILSGERGSG
KSEASKQIMR HLTCRSSTSR PIFDSKFKHA MCILEAFGHA KTTLNDLSSC FIKYFELQFC
ERKKHLTGAR IYTYMLEKSR LVSQPLGHSN FHIFYLLMDG LSPEEKYRLH LNNLGAHRYL
NQTLQNDVST AEHSLNRERF TVLKQALKVV GFSTLEVENL FVILAAIVHI GDIRFTALTE
ADSAFVSDLQ LLEQVAGMLQ VSIDELVSAL TTDIQYFKGD MITRRHTIVM AEFYRDLLAK
SLYSRLFSFL VNTVNCCLHS QDEPHSTQTL DIGILDIFGF EEFQKNEFEQ LCVNMTNEKM
HHYINEVLFL HEQTECVQEG VTMETAYSPG NQTGVLDFFF QTPSGFLSLL DEESQMIWSV
EPSLPKKLQS LLESSNTNAV YSPMRDGNGN VALKGQGTAF TVMHYAGRVM YEIVGAIEKN
KDSLSQNLLF VMKTSENVVI NHLFQSKLSQ TGSLLSLHPF KFRGHKSALL SKKITASSFI
GENRNYLELS KLLKKKGSST FLQRLERGGP LTIASQLRKS LTDIIGKLQK CSPHFIHCIK
PNNSKLPDTF DNFYVSAQLQ YIGVLEMVKI IRYGYPVRLS FSDFLSRYKP LVDTLPGEKK
KLSAEERCRF VLQQCKLQGW QMGVRKVFLK YWHANQLNDL CLQLQRRIIT CQKVIRGFLA
RQHLLQKRSI RQQEVTSINS FLQITEDMGL KTYDALVIQN ASDIARENDR LRNETNATYH
KEKLEARSKQ EEGTKRAEDK SGLRYFHCSS IPVPVAVDSL VQSLAGPSAR SPSLHSVFSL
DDSSGLPSPR KQPPPKPKRD PTTRLSASYE AVSACLWAAA KESSTEVLTR PRPHSDDYST
MKKIPPRKPK RSPNTKLSGS SEEISGSGPG VRRAPGTRRR AAGPQYAPGA VPGVPTPLAH
SEPEPEPEPE PVYIEMVGRA ESPDQAEAVY EEMKYFVPHE NGGGRGVGAW VTASPPLLCE
SRSPITLEDG DASCQTPGPC KDACDIPAPF PNLLPHRPPL LVFPPTPVTC SPASDESPLT
PLEVKKLPVL ETNLKYPVQS EASSPLSPQY SKNPKGDGDR PPSPGLPVFN GSHKVSPPPT
PPPAPAPPAA THRQNPHFTF PPETAMVNTG KAATNSDLSK VQQKPNSAPA ASPGSSFSKI
PYSPGKATAR VDHRKVNSNS SSPVLYSPPN SRPLSSPLDE LTSLFNSGRS VLRKSAAGRK
IREPEGFETN MNLTSRDDPA TSEIASETQD RNANNHGIQL SNSLSSAITT ENGNSVSNGL
PEEDGYSRLS VSGTATSTFQ RHRESHTTQV IHQLRLSENE SVALQELLDW RRKLCEERED
WQQILQHSEP RAPPPPPCKK PTLLKKPEGA SCSRLPSEFW DTTI
//
