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Database: UniProt
Entry: A0A0V1HE08_9BILA
LinkDB: A0A0V1HE08_9BILA
Original site: A0A0V1HE08_9BILA 
ID   A0A0V1HE08_9BILA        Unreviewed;      2729 AA.
AC   A0A0V1HE08;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Unconventional myosin-XV {ECO:0000313|EMBL:KRZ08447.1};
GN   Name=MYO15A {ECO:0000313|EMBL:KRZ08447.1};
GN   ORFNames=T11_13293 {ECO:0000313|EMBL:KRZ08447.1};
OS   Trichinella zimbabwensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ08447.1, ECO:0000313|Proteomes:UP000055024};
RN   [1] {ECO:0000313|EMBL:KRZ08447.1, ECO:0000313|Proteomes:UP000055024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ08447.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRZ08447.1}.
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DR   EMBL; JYDP01000086; KRZ08447.1; -; Genomic_DNA.
DR   STRING; 268475.A0A0V1HE08; -.
DR   Proteomes; UP000055024; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13201; FERM_C_MyoXV; 1.
DR   CDD; cd00124; MYSc; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 1.
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   Gene3D; 1.25.40.530; MyTH4 domain; 3.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR041795; MyoXV_FERM_C.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR   PANTHER; PTHR22692:SF26; MYTH4 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00015; IQ; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51016; MYTH4; 2.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50002; SH3; 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   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:UP000055024};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          111..794
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          957..1106
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          2085..2149
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          2241..2396
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          2401..2720
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          2409..2490
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   REGION          671..693
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1280..1360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2143..2191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1286..1360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2148..2164
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2165..2191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         204..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2729 AA;  312716 MW;  257C7ED8F6F6E143 CRC64;
     MPQAGAGKFA NLFVHAAIAN GIEEDLAEVF GRLPARLTIP KCAAFDTCTR NGPNLTGDLV
     WYKTKQGYAL PGKITEVDSA SSTAWVQSND KKEEIAEFQF TDLQKRASDA MSFEDLIQLD
     DLCNPAVLWA LKTRFEYGKT YTYIGEMLIS INPYRHFDVY GPEIMEQYRK KMTTSLPSHV
     YGFAEMVQRR LYAFDTSQWI IATGITGSGK TELCKLMVQY FAEGCGREMK EAAFNDKLYH
     AMHILQSFLN AKTAANDNST RGGKIYSLQY QNKKLTGAKL AYCLLEKTRL VSHVRGERNF
     HIFYEMIAGL KQQTRQSFGL NKPENFFYLN QGKCVNLGSR EENNFELLEN ALEIIKITLD
     QRHYIFRLLS AILHLGNIYF EEQTEDSNRK LVIANQNEVQ WVAYLLQMDP DEITHRLTTK
     VIESRDQKVV HALTLDRALD IRDAIAKELY MGLIRWIIMK INNQLCNNDN DCNEINILDL
     YGFECFKVNS FEQLCINYIN ERIQRLFVRV QFCSEQMEYI REDIVWDRNV GANLLNNSIF
     NILVKQPNGI LSLLDDECSF PKGSDESFLI KCQNNYDDSP LFTAKTKRQL GFVVQHFFGH
     ARYNVVGFVD KNREVHSAQT VEFLLESQNI LIAQMFEKQK LALSKRSAEN ENFDTYRIRA
     PTFAMQLHEE FNQLTKRIEK YMVHFVRCIN PNKTKEADVL DMQFVLEQIK CLGLTEVLHM
     QKFGFTIKMK FRDFLVRYGC LKPETATVEG KDEKNMCLYI LTSLAHQYFQ DFRIGKTKVF
     MKDIVAEHLD SILSERLSSS VIIIQKYCRG LLARRKFHHL YDWITHLQAI VRGSQARKKF
     SLIKAKVAEE AQQYAKQSRN LEVFRELSIK PNSQDGNANL QQRNSCAIVS VNHLEMPQNL
     SEMLLTKTNL DADKNIVRAD RRIASHHEQE FILPHDLHEY SFNKYAQQYF KNHTWQMRRD
     PINTPFLHKD SEADMQLSLT LFRLILRYMN DTSLSSSQEI ILSNYIIQKG IDNKNLRDEI
     YAQVINQIHG NPNQANAERG WRLLGLCVSA FPPTDAMFKY ALNYVMNADC DGFKNLLKTK
     LLQSIHDNNT TVRRYPPCIL EHKAIRSKAK MALLSYLSDG NKVGSQIDSW TKAEEFAELA
     LKNGGISECT GWTVSLECQD AVIRLNGNQY LLDVLSYIEL PQLFPAQKSD YLITMKQHKK
     PHLEPSTIQE RLEALERRPN LRTLVSDDFH SSKLKKGGSI TSLVHRARLQ HGEKLDSASV
     KQEWLNWNEK CAAQSKIRPD HLNLDHDGSV TNNARCQSRM SSNSYQTDHS ILTADTSNQT
     RPPSSVNTLR SSKFCETSHP SVDENQRKTF SWSKTSTRQE APALANNLSS QAEQSENKQN
     CQNYDKENVD KKNSIPAEQA AIQDIAYMSI NRRPISNYSS LSSHFRAISI PGRNSEVDEF
     LDQLFNPVLG NMNDPKSLAA TIKGGGDESD NKNQPVAVEQ AQTMYSSVYS FMPQYASPVF
     MMMPYDAARM FMPNQRDSQV QGMQQFSNVK AQGNFNADQA NVLMPVPLMP VSFGSYMQAN
     SIGQEVFKGP SNMLPLSMIQ NSSPKAWTRL HEYQHPSPPN GVGSDVMYTS FNPHTVNPNS
     TDEHCMHENN FNNDLSNKVK EEMTSLSEAG SFFPNSSQLW KGRDEMKSKN EDDSDQKLFY
     QWEQISKSDA AAKCKPLSTP TKTLIKEETG SLLSRDSFAS RDIINRNNTK SVASLDASKE
     HENIDNSNYS TLTTSESKIH QKESDNMKNY KTLSREHLYG NLTYDSENRW INPCENLYQT
     EDAHCRSNTP TAYRLEQPQL TNAESFDTLT VSHRDASEFG YDSRVSMRDG LMKIPPSICS
     TLTRESRIDS RPSFKTQDYF SSTLVGLKEK RRGPALTYGN VAWKLVIRKE LFFPNDSLQD
     PAALDAVFYQ IVRDTFNEKD SFRLEKAERN QMIRLLTSNG IELETLTSAN ISPSFKKHVV
     QIARSWPLYF CRLYPVTVSN KFGEDRPHYV GISESGIWLI DRQGEGNDET LRIVECYEFE
     DIDHTEATEN EFLLSTVNGV IIRVSTKSAE EITNLANKYM FGPNQGKEYV RATADYITEE
     PNLLSFRKGD IIQLVKTMPD AHPGSGWLYG KINTKYGFFP KEHLDPISDS EEEEDDDDDE
     NVEQTSEVPN GLEASNQMTP TSPPPVSAHS TQDKLTMMEF AMLHFREAQK YESTQNSTLT
     TLKRKSKKEW TWKDVADLVK FTKSPIQNPL LKLDKGDVCK LAVDCFLNLM MYMGDYPLKK
     DTNYLDCVYK ITAACREHPI LRDEVYCQVI KQITNNKSSK PDSALMGWRM LSILTAYFDS
     SDVFRPYLQK YLSDSASDNR RAYHGTAMEC FQNFRQTLQF GGRRFILSPQ ELESISQGKN
     LKRQVYHLPG GTKKVINTKS VTVVEEIIKE LCIDLNVRSS LEQQEFSLCV VIESDNVMRI
     LSNDEYILDI TSELEEMKRE YFLLLKRIVW MHPLRKDSEL YTDIMFFQVL PDYIEGLLVV
     MRGPDSVSAA TMDDIATLGA LLACADDDWD GQMVTARDIV HLLPKTVHNI RHVTLELWTD
     RINQKLRQLS PKTLPIVARA KFLDLLQTWP LFGSTFFYIP SVSDPRAKGE CLMALNRHGV
     QFLDIHTHEV LFEFRLNEIL STQKSYPDGT TSMNQQSTVE HMDIKIGNML QQHVLTLRTD
     QGAEISRLFG QYIYVDSQSR GLLGIEGKH
//
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