(data stored in ACNUC5448 zone)

HOGENOM: AEDAE_1668_PE28

ID   AEDAE_1668_PE28                      STANDARD;      PRT;   2163 AA.
AC   AEDAE_1668_PE28; Q17LW0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Myosin-VIIa;AltName: Full=Protein crinkled;
DE   (AEDAE_1668.PE28).
GN   Name=ck; ORFNames=AAEL001220;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_1668.PE28.
CC       Aedes aegypti supercontig supercont1.25 AaegL1  sequence 1..3904351
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MYO7A_AEDAE
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC       activity. Unconventional myosins serve in intracellular movements:
CC       can function in cells as a single-molecule cargo transporter. A
CC       very slow and high-duty-ratio motor, may be suitable for tension
CC       maintenance of actin filaments. Their highly divergent tails are
CC       presumed to bind to membranous compartments, which would be moved
CC       relative to actin filaments. Plays a key role in the formation of
CC       cellular projections and other actin-based functions required for
CC       embryonic and larval viability. Necessary for auditory
CC       transduction: plays a role in Johnston organ (JO) organization by
CC       functioning in scolopidial apical attachment and therefore to
CC       acoustic stimulus propagation from the antenna a2/a3 joint to
CC       transducing elements (By similarity).
CC   -!- SUBUNIT: Homodimerizes in a two headed molecule through the
CC       formation of a coiled-coil rod (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 2 FERM domains.
CC   -!- SIMILARITY: Contains 4 IQ domains.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- SIMILARITY: Contains 2 MyTH4 domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- GENE_FAMILY: HOG000007836 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL001220;AAEL001220-RA;AAEL001220-PA.
DR   EMBL; CH477210; - ;
DR   UniProtKB/Swiss-Prot; Q17LW0; -.
DR   EMBL; CH477210; EAT47711.1; -; Genomic_DNA.
DR   RefSeq; XP_001658316.1; XM_001658266.1.
DR   ProteinModelPortal; Q17LW0; -.
DR   EnsemblMetazoa; AAEL001220-RA; AAEL001220-PA; AAEL001220.
DR   GeneID; 5569086; -.
DR   KEGG; aag:AaeL_AAEL001220; -.
DR   VectorBase; AAEL001220; Aedes aegypti.
DR   eggNOG; inNOG09216; -.
DR   GeneTree; EMGT00050000000756; -.
DR   OMA; EMSAKKA; -.
DR   OrthoDB; EOG42FQZ9; -.
DR   PhylomeDB; Q17LW0; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030898; F:actin-dependent ATPase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   GO; GO:0032027; F:myosin light chain binding; ISS:UniProtKB.
DR   GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR   GO; GO:0048800; P:antennal morphogenesis; ISS:UniProtKB.
DR   GO; GO:0008407; P:bristle morphogenesis; ISS:UniProtKB.
DR   GO; GO:0035317; P:imaginal disc-derived wing hair organization; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 2.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 2.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS51016; MYTH4; 2.
DR   PROSITE; PS50002; SH3; 1.
DR   HOGENOMDNA; AEDAE_1668.PE28; -.
KW   AAEL0012203; AAEL001220-PA ; Q17LW0; CH477210;
KW   Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Motor protein;
KW   Myosin; Nucleotide-binding; Repeat; SH3 domain.
SQ   SEQUENCE   2163 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGDYIWIEPV SGREFDVAIG ARVISAEGRR IQVRDDDGNE LWLTPERRIK AMHASSVQGV
     EDMISLGDLH EAGILRNLLI RYNDNLIYTY TGSILVAVNP YQILPIYTAD QIKLYKERKI
     GELPPHIFAI GDNSYANMRR YGQDQCIVIS GESGAGKTES TKLILQYLAA ISGKHSWIEQ
     QILEANPILE AFGNAKTVRN DNSSRFGKYI DIHFNNSGVI EGAEIEQYLL EKSRIVSQNA
     EERNYHIFYC LLAGLSSDEK RKLNLGYASD YRYLTGGGCI KCDGRNDAAE FADIRSAMKV
     LCFSDHEIWE ILKLLAALLH TGNITYRATV IDNLDATEIP EHINVERVAN LLEVPFQPFI
     DALTRKTLFA HGETVVSTLS RDQSMDVRDA FVKGIYGRLF VLIVKKINSA IYKPKSSTRS
     AIGVLDIFGF ENFKHNSFEQ FCINFANENL QQFFVRHIFK LEQEEYNHES INWQHIEFVD
     NQDALDLIAI KQLNIMALID EESKFPKGTD QTMLAKLHKT HGTHRNYLKP KSDINTSFGL
     NHFAGVVFYD TRGFLEKNRD TFSADLLQLI SSSTNRFLQM VFAEDIGMGA ETRKRTPTLS
     TQFKKSLDSL MKTLSSCQPF FIRCIKPNEL KKPMMFDRAL CCRQLRYSGM METIRIRRAG
     YPIRHKFKDF VERYRFLISG IPPAHRTDCR LATSKICASV LGRSDYQLGH TKVFLKDAHD
     LFLEQERDRV LTRKILILQR SIRGWVYRRR FLRMRQAAVT IQKFWKGYAQ RQRYKKMKIG
     YMRLQALIRS RVLSHRFRHL RGHIVRLQAR IRGYLVRREY GLKMWAVIKI QSHVRRMIAM
     NRYQKLKLEY RRHHEALRLR RMEEEELKHQ GNKRAKEIAE QHYRDRLNEI ERKEIEQELE
     ERRRVEVKKN IINDAARKAD EPVDDSKLVE AMFDFLPDSS SEAPTPHGGR ETSVFNDLPV
     NQDNHEDIIG PIHTISEDEE DLSEFKFQKF AATYFQGNIT HFYSRKPLKH PLLPLHTQGD
     QLAAQALWIT ILRFTGDLPE PRYHTMDRDN TSVMSKVTAT LGRNFIRSKE FQEAQMMGLD
     PEAFLKQKPR SIRHKLVSLT LKRKNKLGED VRRRLQDEEY TADSYQSWLE SRPTSNLEKL
     HFIIGHGILR AELRDEIYCQ ICKQLTNNPS KSSHARGWIL LSLCVGCFAP SEKFVNYLRS
     FIREGPPGYA PYCEERLKRT FNNGTRNQPP SWLELQATKS KKPIMLPITF MDGNTKTLLA
     DSATTARELC NQLSDKIALK DQFGFSLYIA LFDKVSSLGS GGDHVMDAIS QCEQYAKEQG
     AQERNAPWRL FFRKEIFAPW HNPIEDQVAT NLIYQQVVRG VKFGEYRCDK EEDLAMIAAQ
     QYYIEYNTDM SMDRLYTLLP NFIPDYCLTG IEKAIDRWAA LVLQAYKKSY YLKDKAAALK
     VKEDVVSYAK YKWPLLFSRF YEAYRNSGPN LPKNDVIIAV NWTGVYVVDD QEQVLLELSF
     PEITAVSSQK TNKVFTQTFS LSTVRNEEFT FQSPNAEDIR DLVVYFLEGL KKRSKFVIAL
     QDYKAPGEGT SFLSFLKGDL IILEDESTGE SVLNSGWCIG CCERTQERGD FPAEIVYVLP
     SLTKPPPDIL ALFSVEDAHH GKRLNSIHSN GGTETREHPH TLADYSLDHF RPPPKRTMSK
     ALSTLSSKRG GDELWRYSRE PLKQPLLKKL LAKEELAEEA CLAFIAIMKY MGDLPSKRPR
     IGNEITDHIF DGPLKHEILR DEIYCQLMKQ LTDNRNRMSE ERGWELMWLS TGLFACSQQL
     LKELTVFLRT RRHPISQDSL HRLQKTIRNG QRKYPPHQVE VEAIQHKTTQ IFHKVYFPDD
     TDEAFEVDSS TRAKDFCQNI SQRLNLRSSE GFSLFVKIAD KVISVPEGDF FFDFVRHLTD
     WIKKARPTRD GTNPQFTYQV FFMKKLWTNT VPGKDKNADL IFHYHQELPK LLRGYHKCSK
     EEAVKLAALV YRVRFGESKQ ELQAIPQMLR ELVPSDLIKL QTTNDWKRSI VAAYNQDAGM
     SPEDAKVTFL KIVYRWPTFG SAFFEVKQTT EPNYPEMLLI AINKHGVSLI HPSSKDILVT
     HPFTRISNWS SGNTYFHMTI GNLVRGSKLL CETSLGYKMD DLLTSYISLM LTNMNKQRTI
     RIK
//

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