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Database: UniProt
Entry: H0ZED0_TAEGU
LinkDB: H0ZED0_TAEGU
Original site: H0ZED0_TAEGU 
ID   H0ZED0_TAEGU            Unreviewed;      1827 AA.
AC   H0ZED0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 85.
DE   SubName: Full=Myosin XVI {ECO:0000313|Ensembl:ENSTGUP00000008942.2};
GN   Name=MYO16 {ECO:0000313|Ensembl:ENSTGUP00000008942.2};
OS   Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC   Estrildinae; Taeniopygia.
OX   NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008942.2, ECO:0000313|Proteomes:UP000007754};
RN   [1] {ECO:0000313|Ensembl:ENSTGUP00000008942.2, ECO:0000313|Proteomes:UP000007754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20360741; DOI=10.1038/nature08819;
RA   Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA   Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA   Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA   Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA   Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA   Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA   Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA   McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA   Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA   Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA   Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA   Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA   Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA   Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT   "The genome of a songbird.";
RL   Nature 464:757-762(2010).
RN   [2] {ECO:0000313|Ensembl:ENSTGUP00000008942.2}
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   STRING; 59729.ENSTGUP00000028597; -.
DR   Ensembl; ENSTGUT00000009039.2; ENSTGUP00000008942.2; ENSTGUG00000008643.2.
DR   GeneTree; ENSGT00940000158920; -.
DR   HOGENOM; CLU_002267_0_0_1; -.
DR   TreeFam; TF332267; -.
DR   Proteomes; UP000007754; Chromosome 1.
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; 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:UP000007754}.
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..1145
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1024..1046
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1211..1251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1282..1319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1336..1389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1566..1633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1651..1827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1282..1302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1342..1359
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1566..1586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1606..1627
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1651..1679
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1692..1727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1733..1749
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1762..1819
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   1827 AA;  203052 MW;  76E6347637761E83 CRC64;
     MEIEQCLLES LPLGQRQRLV KRMRCDQIKA YYEREKAFQK REGYGKKLKH GKNQRVCFNL
     ADMIQDAIIR HDDKEVLRLL KDGADPHMLL SSGGSLLHLC ARYDNAFAAE ILIDRGVNVN
     HQDEDFWTSM HIACACDNPD IVLLLLLAGA NVLLQDVNGN IALDYAVEGT ESSSILLMYL
     EENGVELNSL RQMKIQRAMT MLTDVRQLIS SGGSVNQKNE EGVTLLHVAC ANGYKNVASL
     ILDHGADLNV VDNQYWTPLH LAAKYGQTNL VKLLLMHQAN PNLLNCNNEK PSDVAASDFI
     EEMLLKAEIV WEEKMKDPLA VSTLSQEEPY EEIMHDLPTI SNKLNPLALP IAKQDSLLEK
     DTMFKDAAKG LCKQQSQDSA SENITVNTTT KLEQIKLMPP APNDDLASLS ELTDSSLLYE
     IQKRFNNNQI YTYIGDILLL VNPFKELPIY STMVTQLYLS NSGKLCSSLP PHIFSCAERA
     YHMLFQEQRP QCFILSGESG SGKTEACKQI VKHLTCRANC SRNTFDTKIK HVNCILEAFG
     HAKTPLNFFS SCFIKYFELQ FCERKKTLIA ARIYTYMLEK SRVVIQPLNQ SNFHVFYLMM
     DGLSAEEKYT LYLSNLSAHR YLSQTVSEET MLAANPQNRE KLTILKQALG ALGFNSLEVE
     NLFVILSAIL HLGDIRFTSL TDAETAFVSD LQLLEQVAGM LQVSPDELAS ALTTDVQYFK
     GDTIVRRHTI EMADFYRDLL AKSLYGRLFS FLVNTINCYL QNQDESGSDQ VFEIGVLDIF
     GFEEFQKNTF EQLCVNMTNE KIHQYINEVL FLQEEAECVQ EGVAMETMYS PGNHTAVLDF
     FFQKPSGFLS MLDEESQSVW SVEQGLSKRI QSYLDTSDTN TVYSSTKDGN GNLAPKDLGS
     TFTVMHYAGR VTYEIAGAIE KNKDSLSQNL IFVMKTSENV VINQLFQSKL TQTGSLVPPY
     HSLKIKGCKA ALLSKKSSVT CASGEAKKYI ELSKLLKKKG TSSFLQRLER GGPTTVAIQL
     RKSLADIIGK LQNCTPHLVH CIKPNNSKLP DTFDNFYVSA QLQYIRVLDM VKIIRHGYPV
     RLSFTDFLSR YKDLADTAAG EKKKLSAKER CHLVLQQCKL QGWQIGVRKV FLKYWQADHL
     NDLCLQLQKK IITCQKVVRG FLARRHLLQK RSIKQQEVTS IKSFLQNAED MGLKTYDDLV
     IQNASDIARE NDRLRNEMNG AYHRDKGEAR SRPEEGQKRA EDKGGKVSED SFAGCRTSKH
     FHSSSVPVPM AVDGLVHSAA GSSIRSPSLH SVFSMDDSNS LPSPRKQPPP KPKRDPNTRL
     SASYEAVSAC LSAASKETAN EVLTRPRPHS DDYSTMKKIP PRKPKRSPNT KLSGSYEEIP
     GQKPGNVKKA STVVKPGVYD TVTVQRTAST DGPQHGVLNL FMSQGEEENE PVYIEMVGNA
     VKNSSVEAES PEQGESVYEE MKYFLPEEGS NGNRIIPVVT GSPPLLFESK KNVNIEDGTL
     DGNSQAALIY RDSCDIPAPF PNLLPHRPPL LVFPPTPVTC SPASDESPLT PLEVKKLPVL
     ETNLKYPVQS EGSSPLSPQY SKGQKGENER PVSPGLIVFS VSTKVTPPST PPPTLPPPPP
     PVPPPASYRA STHFASPPET CATFLINAGK TGTNSDLSKV PQRTNPAQLG CSSSPFSKLP
     YSPKLARADH RKLNSNSSSS FAYNPTNSRS LTSPLDELTS LFNSGRSVLR KSAAGRKIRE
     PEGAETNLNL RSREDPNTPD PGSETQDKNA NNHGTQSSNP LSSSVTAENG NSVSNGLPEE
     NDFSRLSAST TAGSSIQRHR ESHTSQE
//
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