ID H3BXF1_TETNG Unreviewed; 1845 AA.
AC H3BXF1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Myosin XVI {ECO:0000313|Ensembl:ENSTNIP00000000664.1};
GN Name=MYO16 {ECO:0000313|Ensembl:ENSTNIP00000000664.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000664.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000000664.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 Ensembl; ENSTNIT00000002903.1; ENSTNIP00000000664.1; ENSTNIG00000013925.1.
DR GeneTree; ENSGT00940000158920; -.
DR Proteomes; UP000007303; 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; 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; 4.
DR SMART; SM00015; IQ; 1.
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:UP000007303}.
FT REPEAT 100..132
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 133..165
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 229..261
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 262..294
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 407..1157
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1058
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1295..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1845 AA; 204482 MW; B7D4862316475A8D CRC64;
GCFQLCNVFR QNMEIDQCLL ESLPIGQRQR LVRMRCDQIK AYYEREKSLQ RHTGAADHRR
KPRVQFGLAD VIQDAIVRHD DKEVLRLLKE GADPNTLIPS GGSLLHLCAR HDNVFAAEVL
IERGVNVNLQ DEDLWTALHV ACVCDHADVV LLLLLAGVNM LLQDVNGNIP VDYASEGTES
SWILRKHLEE NGVDVSSIHT MKMQRRSTMM SDVRQLVATG EGLSQSNEDG VTLLHIACAG
GYREVVSMLL EKGADPDAAD DNFWTPLHLG SKYGQTSVIS QLLRHGANPT LLNCNHHKPS
DIGASEHITE MLLNAEESWL QRQADPSAPL PSADQCYDGG SHDVNTPVKN MNLGLPLSKR
DSLLEKCTLF REAGVALIRH PSQDNGLDGP FSSGTSKVEQ VKLMPPAPND DLASLSELTD
SSLLYEMQKR FSNDQIYTYI GHILLLVNPN KELPIYSTLV SQLYLSSTGR LCSSLPPHIF
SSAERAYHMM LQERRPQCFV LSGESGSGKT EAFKHIVRHL TGRSSPKGFA LEPKMKHVNC
ILEAFGHAKT PRNNNSSRFI KLMTIQYCEK RKMPLGARLC TYMLEKSRLV HFHPHQHNFN
IFYLMAEGLS PEENSTFYLS NVLAHRYASG EPPQVAKASA QSKEQLTEVK QALRALGFNK
QEVESVFMLL AAVLHLGDVH FTPLTDADTA FPSDPQLLER VSGMLQVCPN DLSSALTSDV
QIFKGDAITR RHTVEMSEQN RDQLAKAIYG RLFSYLVNTA NGYLQGQDDL LGDPAFEIGI
LDIFGFEEFL KNGFEQLCVN IVNERLRRYV SEMLFQQEQA ECVLEGVPME PPCSPCNQPA
VLDFFLQQRP QGLLSLLDEE SQSPRPVEQM LYKRLSAQLE SSSGHGLSLT TKDGNGNPPP
KDQGPAFTVH HYAKQISYDL TGSLSRNKDA LPQNLVFTMK SSESVLLRQL FRSKLTQTGS
LVPTAQGRAG SRGPKAALLL YKMPSASLVT AGAIPSKPQR SLDLTRILKK KCPSSFLQQL
ERCGPITVTI QLKNSLSEVI SKLQACTPHF VECVRPNTSG QPDSFDSFHV SAQLQYIRVL
EMVRTIRYGY PVRLSFPCFL SRYKDLTIPM LGDKKKVSPE ERCRLVLQQT KLQGWQMGSS
KVFLRYWQAD QLNDRCYQLH KKIITCQKVV RGWLARRRLH HRQSSRQKMV HSVQRFLQGA
EDMGLRTYDQ LVIQNAADIA RESDRLRCHA PLAKAHPLVR GLSQSERKRI NPPGVLRVRL
VYVFTWSTFR GVEKTGKVFE GPVNISHSNE EVLAVGSLSS PRKQPPPKPK RDPNTRLSAS
YETVSAGLTM AAKESPTPAL SKPRPYSDDY TTMREVPPPK TKQRPNTKLS GSYEEINAVA
PHIHQLRPAD VKLALLSRSA GFGGFGGLMQ KAASIDAPQG VGLSLYKGQD EEDVYIEMMG
SQQRARSLQE PPDSPIQADS EAVYEEMKYF PTEDGVTSAA AVTKATNTPS QSTLNSFKTL
HGKDGSCDIP APFPNLLPHR PPLLVCPPSP VTCSPASDES PLTPLEVKKL PVFETNLNYA
TAPDSPLSPQ CSRQRADSSP SLTVFIPEKK STPPLTPPPP PPPAQPPPYR APSHFPFPPE
ASFLTLTRAA SVAGSSDTPK ALSSQRASGE PLGKPPPYSP VKMTRPEPRR AHSCSSSPLL
FNPANGRALT SPLEELNTLF SSGRSLLRKS TSGRKMRDGE RFNSNINLPG KDECGSAPTS
PSLQLQDKNA NNRSTQSSSP VPIENGNQIT NGLMEDESHS KPNTSTSTSL HRHMDSHHIQ
VINRFRLLSG DEAAASGDLQ RWRREQCEGR GDWKGCPPPH TPLPP
//
