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Database: UniProt
Entry: A0A0L0BU80_LUCCU
LinkDB: A0A0L0BU80_LUCCU
Original site: A0A0L0BU80_LUCCU 
ID   A0A0L0BU80_LUCCU        Unreviewed;      3518 AA.
AC   A0A0L0BU80;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Unconventional myosin-XV {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FF38_14441 {ECO:0000313|EMBL:KNC23543.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC23543.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC23543.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC23543.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC23543.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {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:KNC23543.1}.
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DR   EMBL; JRES01001343; KNC23543.1; -; Genomic_DNA.
DR   STRING; 7375.A0A0L0BU80; -.
DR   EnsemblMetazoa; KNC23543; KNC23543; FF38_14441.
DR   OMA; TFGVHQN; -.
DR   Proteomes; UP000037069; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
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:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR   GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13201; FERM_C_MyoXV; 1.
DR   CDD; cd01387; MYSc_Myo15; 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; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
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; IPR036057; MYSc_Myo15.
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   PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR   PANTHER; PTHR22692:SF26; MYTH4 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51016; MYTH4; 2.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000037069};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          64..749
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          921..1070
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          3033..3187
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          3192..3511
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          625..647
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1164..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1245..1264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1276..1324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1547..1569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1589..1643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1800..1822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1862..1954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1969..2067
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2083..2169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2385..2415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2435..2460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2500..2531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2821..2893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2928..2969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          822..854
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1175..1189
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1309..1324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1589..1603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1620..1636
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1800..1817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1870..1908
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1927..1954
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1969..2002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2009..2043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2083..2114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2385..2410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2510..2531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2821..2873
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2874..2893
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2931..2969
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         155..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   3518 AA;  396368 MW;  75F2133852E072FB CRC64;
     MDWSEGDLVW FDPGVGHPIP GEIQEVHRAA QVIVVQAVIK GKPQTFALQP GEGNLRPRQD
     LGSSGVDDMT MLDDLHEASL LWNLRLRYDK GLIYTFAGSI LIAVNPYKMF PDSYGLEVAK
     QYAGKPLGTM PPHLFAIGAA AHAALPSPQV VVISGESGSG KTESTKLVMQ YLAAVVPGGG
     SASAVITEQI LEAAPLLEAF GNARTARNDN SSRFGKYLEV YFKNGAIVGA KITQYLLEKS
     RIVTQAPGER NYHVFYEMLG GLSEAERTKY GLLEADKYFY LNQGATDCAP GRVDWDSLQS
     AMQVLGVSEG EREGIIRVLA SVLHLGNVYF HRRQLRHGQE GVEVGSDAEI KWAAHLLHIS
     AEGLHRALTS RITEARSERL HTPLSIDQAL DSRDAFAKAL YSGLFNWLVS RINSIVQKGG
     THDAHRISIL DIFGFEDLAE NSFEQLCINY ANENLQLYFN KHVFKLEQAE YSRERLEWTP
     LTWDDNLPVI HLLAKKPVGI FHLLDDESNF PRASDMSFLE KCHYNHALNE LYSRPRIGAQ
     EFGITHYAGQ VWYCVDGFLD KNRDALRSDV LELLGSSKLQ LVSDLTKQLR AQRDSGKTLP
     KGNNGRFVTM KPRTPTVAAR FSDSLQQLLQ SMGRCNPWFV RCIKPNNEKQ SLKMDMPCVL
     QQLRYLGMLD TIQIRQKGYP VRLRFQHFVE RYRHLMRSPL PRGTPYRELC RILLESMPNT
     GIEGPDYQLG ATRVFLREAL HRMLESGRSD RLKTSAVVIQ KHVRGMLVRR QLARKKKAAT
     RIQTKWRGYR EQKKFRDLRR GAIKAQALWR GKMGRKRVVK LRADYQRRLE AQRAQKEREA
     KKQAKENLER SQISYLDIPA ELAFIFSKSE GWTPIHGDRH LVKVVGTVPG PPVAADLPKD
     LDQFSFGKFS SVYCNGLRLS SRREPITTPF LTRAASRDQD FQDSLAVFKL ILRWTNDKTM
     DGNKEKVLSD YIVHKGLSSR GLRDEILVQL CNQVYNADDL QAQRIWQLMA QCLSCFQPGP
     AFSKYLMKFI VDNAPDSMRD MLLKKILRNA NSANNCRNFT PSWVEWRAIS RMSDIAVALT
     LPDDANQTVA IDSWTTCEEA ASLAVSTLGI SNRGWTVVLD DGKLVTDSCG LDYVLDLISE
     KELCPAFPAL RSDLMTTGAK FNRTILSDHD GNTPRRPQVP PPEPPKIKVN PTSESPISDS
     NDEKPIRKNS RNLLSRSSAL NERYFEQEKS RSKSLDDLLA GDITDLDPAT ETEPLTNLGL
     SESRLNERYH SAERLTPMGK ETGPRYQKSQ YAGRRSHAGS HSSKYMDKSE YATRSSAMSD
     TSEAPSLASH VRRVRVPSQA SDVDQFLDDL FSPVLDGSLD ELSDARSLAA SIRGGKAMPD
     LSFELDDTEF LEAPDSEMND LIWDSHTLAC KIKGGGENSA NSEEAPSANL DEYITGLFKP
     IFVNDAVKVL TEQAELIETI KGGGTAQAQT SGNSTFVTSP IVGPISPILA SNSENLLQIV
     NLPPDADPAV YQHQVQRAFL QSAMAQNLQI QQQLLAQNQA LQTLLSQQDT APTGTTSPPP
     LMPVLASVQQ SSASSNSITS KITIASSEHT NVRKQSVKNR ISQFSENDRN RKVSSDSGGS
     LIPPPPPPPM PPPIEVKDPS ETRHFLDPYG RAKTVRIGKW RWPPPQDGPQ FETEEDFFAF
     KMRQNQRKTT PQSQFHSSNG SLTGSAMEWE EFEVNDSSKS PSPAVVMPVH TTQMVRTQIK
     IETGPKNTNK QPTMEQLQPQ QTVITTKVAK KSFEIGADRP PPGSVGKLKL SSEMRQRLEQ
     VTAGHSVRST VSTKSEQRAP AKLEDTRKLM LQQQLSGHFA QIESNNNAVA DLHSVRSQVE
     RMEEKLSPPP IWPSHVPPAP NIPAPPPPIR PPNVAPPAPP PVPKSPPVRP DQEEIEYRSQ
     SKDVPAFIQR QERDTFGARH NWNGSDDSKD AYDSWGRTEA AKLDMVYEKS FKKESKNNHE
     RDRSRSRSRS RDRDDFSESV WDRSEVEGPA SSGSDREREK EREKRDRIYE MRQVEREKES
     NKVYQPAPPK VVTATIERQD RTDSFGPMVS TERKYSYQAM ASNNNNNINN KRPITSAPSP
     TTSMTSNTPA TFRTHMAQKY EKERKRKSSA TSTTVSQSTR RDEETDGGDE WPLPAIPAPV
     PAPPSLKSPA NACLTYNRVP WKLRVRKEVF HPNEPIGPPI ALDLLFAQVS SDIFGLTPSL
     RISPQEKAAA INMLNGHGVT VETVRSQNVR ALVKRHLIDM AREWPLYFAR LFPVQGAPQY
     PDVSIMGISH NGLYLARRDA DYLIVVQSVP FNEIQNAITL PRPASLQLNL RNGKNVQLHA
     ARAAAIQAMI TSFVQEFRKI YKTTPSFFVS RYYLLLVFGS KMSESLRGSK SSNSRHNSSS
     SGSGNGSHGR NLDSIPHKFS SIVNKVESLI NKMNYDKHNH NNRHDGEKCS SSHKENKRKT
     KIKQEYKQNN RYDHSIALNC NNRTTSMDSL NNLTDIEIDS FDDRDTNDTR TTNTNTTNTT
     TTSNNTNDIY SDSDDAEIAH ITGTTSVQVH RRIELDQLTD ETIREFNEQC SSLSHDMEFY
     NSWQNEEELE HSSTHTSKHS NEDDIYDDSI QHQFNSCQQN TEIDQHTTTT TTTKDANNNE
     CSASEIDTQD WLDKLEMNEE EEPVEKHQEY KTETNKPLTH IQQIVNNITQ QSSNLKEQHS
     KQNYNEIEID STINEDGSSN SFTNQTSTAI NGNMAKTRRS SVASSGSVGR METILEEPTE
     CKISVKEILQ RFETMNKNET QSKASTLSSG VRAAAQTLNV PIERLESRQS NHREQINSNQ
     HSVITQQHNM RNTSSPLMSG SYEEQHLHHQ QQQQQLQQQQ THHNLQQQQQ QSHHHQREQL
     REPHSRNMHH GISDSIDHHT QITQASHHYN GHGDEDERLD DREHFNEHHQ YAKQQSFLHS
     SRKNSNQHHS STNPHTREHH SAVQQTQQSQ NLDANYMAEE HNGGTTSPSV TRYSLLQFAM
     QHFRNDQIVD SRSHGRDASE RSSNRSYAEL VKWQGTPMRI PLLRLPNDLA PLALECFDCI
     LRYCGDIPME PDLTEVKCVY TVLMHCHKYL ALRDEVYCQL MKQTTANRSP CPDSTQRGWR
     LLSILAAYFG CSDALRPYLI EHLTSAASDR RRSCHGTAAV CLTNLRKTAR CGGRKNVPSV
     EEVTAVSAGR SARRQIYRLP GGAERVVNTR CSTVVADVIS ELCALLGIES ETEQQEFSLY
     CIVQGDAFTM PLAADEYILD VTTELLKSGQ PFYLIFCRSV WHFALKRDPA PTPLYVEVLF
     NQVAPDYLEG LLLELPSTGV PPPEVVRDMA RIAALLHRAA DLSHVPAMKE IKFLLPKPAL
     GIREIRPAQW VGLVQSAWPQ VANLSPGQVK AQFLNVLSAW PLFGSSFFAV KRIWADEGPH
     VDDSPMWRDL ILALNRRGVL FLDPNTHETM QHWPFMEVIS TRKVRSEDGA LFLDMKVGNL
     MQQRVIRVQT EQAHEISRLV RQYITMAQIS QRDKRDVN
//
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