ID A0A087Y002_POEFO Unreviewed; 1850 AA.
AC A0A087Y002;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Myosin XVI {ECO:0000313|Ensembl:ENSPFOP00000011355.2};
GN Name=MYO16 {ECO:0000313|Ensembl:ENSPFOP00000011355.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000011355.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000011355.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AYCK01006144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 48698.ENSPFOP00000011355; -.
DR Ensembl; ENSPFOT00000011371.2; ENSPFOP00000011355.2; ENSPFOG00000010948.2.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000158920; -.
DR OMA; RVMYDIV; -.
DR Proteomes; UP000028760; 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 GO; GO:0048731; P:system development; IEA:UniProt.
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; 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; PF15439; NYAP_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 4.
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; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
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:UP000028760}.
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 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..1154
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 369..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1055
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1231..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1625
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1733..1795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1850 AA; 204500 MW; 4DDD5E3D7E547A9C CRC64;
MEIDQCLLES LPIGQRQRLV RRMRCDQIRA YYEREKNLQR QQGGVKVRVP SRKYRIRFRQ
SDVIQDAIIR HDDKEVLRLL KDGVDPNTAT SSGGSLLHLC ARHDNVFAAE LLIERGLNVN
QQDEDLWTAL HVACVCDHAD MVLLLLLAGV NILLQDINGN IPLDYTFEGT ETSYILRKYL
EDNGVNVASM HTMKTQRPTT MLSDVKHLVT TGGTLNQAND EGVTLLHIAS ASGYREVVSV
LLESGADPHP ADNNFWTPLH LAAKYGQTSI VRKLLRHGAN PTLLNCNQDK PSVDLAVSEP
MAEMLLSAEE SWLQRLKDPG APLPPTDQRY DGGSHDLNTP LKTLNPLGLS ISKRDSLLEK
CAMFREAGGA LSRQPSQDNG LDSPFSSGPS KLEQVKLMPP APNDDLASLS ELTDSSLLYE
MQKRFGNDQI YTYIGHILLL INPNKELPIY STLVSQLYLS STGRLCSSLP PHIFSSAERA
YHMMQQERRP QCFVLSGESG SGKTEACKHI VRHLTARSGP KGFGLEPRMK RVNCILEAFG
HAKTPRNSSS SRFIKLLTIQ FCEKEKTILR AHIYTYMLEK TRLVHLPPQQ QNFRIFYLMA
EGLSPEDKTA LYLNNVLAHR YLTGATPGDS PPVALASAQS REHLAAVKQA LRALGFNKQE
VDSVFTLLSA VLHIGDLCFT ALTDANSAFP SDLQLLERVA GLLQVSANDL STALTSDVQY
IKGDVITRRH TVEMAEQYRD QLAKSIYGRL FYYLVNSIND YLQGQDDSIG DPAMEIGILD
MFGFEEFQRN EFEQLCVNMI NQRLRLYVSE VLFQQEQAEC LQEGITMEIP VSGNSHVAVL
DFFLQRPQGL LCVLDEESQS LRPAEQTLYK RLSAQLDSIS ICGLSLTTKD GNGNPPPKDQ
GPAFTVSHYA GEVSYDLTGS LSKNKDSFPQ NLLLTMKTSE SVLLQQLFQS KLTQTGSLVP
AVQGRIGLRG TKVALMVQRV PSASSVNATC IPQQPRRYHD LTKILKKKGS SSFLQRLERC
GPVTAAVQLR NSLSEIMSKL QTCTPHFVEC VRPNSSGQPA SFDSFHVSTQ LQYIGVLDMV
RMIRYGYPVR LSFSTFLSRY KDLIVPTLGD KKKLSAEEKC RFVLQQSKLQ GWQMGSSKVF
LRYWQADQLN DRCYQLHKRI ITCQKVVRGW LARQRVSHRL SLQHKEESSV QRFLQGAEDI
GLQTYDQLVI QNASDIARES DRLRCHGNGM VEKSGKVHEG HVNGGSRISR HFRSSSVPIP
LAVDSMVHFS ASPPVKPALQ QAAQNSEDGA GNGSLSSPRK QPPPKPKRDP NTRLSASYEA
VSSGLTMAPK VASDIRTKPR PHSDDYTTMR KVPPPKPKRS PNTKLTGSYE EINAVAPQLH
QLRPADVKMA LLSRGGGFGG FGGVMQRAAS LDAPKGVALS LYKGQDEEDV YIEMLGSQPR
TRSLQEPPDS PDLLDSEAVY EEMKYLPPED GGNGGENKQM PASATATMEV SHTQSLPNSA
AAKAQLGKDG SCDIPAPFPN LLPHRPPLLV FPPSPVTCSP ASDESPLTPL EVKKLPVFET
NLNYATGPDS PLSPQFSRQR ADSSPSLTVL MPEKKSTPPL TPPPPPPPPS APPPPYRPPS
HFPFPPEANF LALTRAASVT GSSDSPKISS QRAGGEPMGK PPPYSPVKMS RPEPRRAHSC
SSSPLLFNPA NGRPLTSPLE ELNTLFSSGR SLLRKSTPGR KMRDGGRFNS NINLPGREES
GSAPTSPSLQ LQDKNANNHS LHPPSPVPVE NGNQISNGSL EDESHSKSNS STTSLHRHLD
SHHTQLLQRL HLTNRDESAT LRELLRWRQV QCEGRNSHKQ RPPQSPPLPP
//
