ID A0A1A9VCQ6_GLOAU Unreviewed; 2304 AA.
AC A0A1A9VCQ6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Glossina austeni (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT033089-PA, ECO:0000313|Proteomes:UP000078200};
RN [1] {ECO:0000313|Proteomes:UP000078200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA Aksoy S., Warren W., Wilson R.K.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:GAUT033089-PA}
RP IDENTIFICATION.
RC STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT033089-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; 7395.A0A1A9VCQ6; -.
DR EnsemblMetazoa; GAUT033089-RA; GAUT033089-PA; GAUT033089.
DR VEuPathDB; VectorBase:GAUT033089; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000078200; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 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; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036057; MYSc_Myo15.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR PANTHER; PTHR22692:SF26; MYTH4 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 3.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 1.
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}.
FT DOMAIN 64..749
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 921..1072
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT REGION 625..647
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1167..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1567..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1822..2003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2064..2089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 815..851
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1176..1191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1195..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1615..1631
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1650..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1927..1961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1968..2002
FT /note="Basic and acidic 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 2304 AA; 258053 MW; 1D815E3347C9E6B1 CRC64;
MDWSEGDLVW FDPGMGHPIP GEVQEVHRAA QVIVVQALIK NKPQTFALQP GEGNLRPRQD
LDSSGVEDMT MLDDLHEASL LWNLRLRYDK GLIYTFAGSI LIAVNPYKMF PDSYGLEVAK
QYAGKPLGNM PPHLFAIGAA AHSALPSPQV VVISGESGSG KTESTKLVMQ YLAAVVPGGG
SASAVITEQI LEAAPLLEAF GNARTTRNDN SSRFGKYLEV YFKNGAIVGA KITQYLLEKS
RIVTQAPGER NYHVFYEMLG GLSEPERNKY GLLEADKYFY LNQGATDCAP GRVDWGSLQS
AMQVLGVSEG EREGIIRVLA SVLHLGNVYF HRRQLRHGQE GVEVGSDAEI KWAAHLLHIS
AEGLHRALTS RITEARSERL HTPLGIDQAL DSRDAFAKAL YAGLFNWLVS RINSIVQKGG
THDAHRISIL DIFGFEDLAE NSFEQLCINY ANENLQLYFN KHVFKLEQAE YSRERLEWTP
LTWDDNLPVI HLLAKKPVGI FHLLDDESNF PRASDMSFLE KCHYNHALNE LYSRPRIGAQ
EFGITHYAGQ VWYCVDGFLD KNRDALRSDV LELLGSSKLQ LVVDLTKQLR AQRDSGKTLP
KGNNGRFVTM KPRTPTVAAR FSDSLQQLLQ SMGRCNPWFV RCIKPNNEKL SLKMDMPCVL
QQLRYLGMLD TIRIRQRGYP VRLRFQHFVE RYRHMMRTPL PRGTPYRELC RILLESMPST
SIEGPDYQLG ATRIFLREAL HRILETGRSD CLKTAAVVIQ KNVRGMLVRR LISRKKVAAI
RIQAKWKGYR ERKNFLALLK AVLKAQALWR GKLGRKHVEK LRVEHKRRLE AQKAQKEREA
KKLARENLER SQLSYLDIPA ELAFIYSKID GWTPLHGDRH LVKVVGTVPG PPVAADLPKD
LDQFSFGKFS SVYCNGLRLS PRREPITAPF LTRAASRDQD FQNALAVFKL ILRWTNDKMM
DGNKEKVLSD YIVHKGLSSR GLRDEILVQL CNQVYNADED QAMRIWQLMA LSLSCFQPGP
AFSKYLIKFI VDNAPDSIRD IMLKKILRNT GSTNTQTCRN FPPSWVEWRA VTRLSDIAVA
LTLPDDVIQT VAIDSWTTCE EAASLAISTL GISNRGWTVV FDDGKLISDS CGLDYVLDLI
SEKELCPAFP ALRSDLMTTA AKFNRLIMPE SETNTPKRPQ VPPPEPPKIK VNPISESPIS
DSNNEQPIRK NSRNLLSRSS ALNERYFEQE KTRSKSLDDL LAGNDTDLEP STEPEPLTEL
GLSESRLNDR YHSAERLTPN MGKDGGPRYQ KSQYAGRRSH AGSHSSKYVD KSEYATRSSA
MSDTSEAPSL ASHVRRVRVP SQASDVDQFL DDLFSPVLDG SLDELSDARS LAASIRGGES
AEYRDGNDFF EAPFVDEDML WNVSCLSQKI KGGGEKSGGE ANSANLDEYI TGLFKPIFVN
DAVKVLTEQN DLIETIKGGG GTTHSPQKPT SSFVTSPIIG PISPLLGNSD SLLQIVNIPP
DADPAIYQHQ VQRAFLQSAM AQNLQIQQQL LAQNQALQTL LSQQDSAAGT TSPPLIPVLA
AVQQTPGANN SLTTKMNITA AEPQRNIRKQ SVKNRISQFS ENDRNRKASS ESNGSLIPPP
PPPPMPPPIE IKDPSETRHF LDPYGRAKTM RQNQRKTTPQ SQLNSSNGSL AGSVMEWEEY
EVDNSKSPSP AANIPILATQ IVRTQIKVET GSKNINNKPV FEQIQQQTSK TTKKSFEIGA
DRPPPGSVGK LKLSSEMRQR LEQVTAGHSI RSTVSTKSEQ RAPAKLEDTR KMMLQQQLSG
HFGNVEITVP DVQSVRSQIE RMEGKLSPQP NWPSHVPPAP SIPAPPPPIR PPNVAPPAPP
PVPKSPPVQA TKKEENDYRG QNKDVPAFIQ RQERDTFGVR HKWNTAEDSK NVYDSWGRSE
AAKLDMVYET SFKKEIKHER DRSRSRSRSR DRDDFSESVW DRTEVEGPGS SGSDREREKE
REKRERIYEM RQVEREKESN KVYQPAPPKV ITASTERSDA YGSTIERKYS YQGTVLEQKR
IVGATTMPNN STPATFRTHM AQKYEKERKR KTSASTIMSQ NTRRDEEVDV GDEWPLPAVP
APVLAPSSLK SPANACLTYN RVPWKLRVRK EVFHPNEAIG SPVALDLLFA QVISDVFGIT
PSLRISPQEK TAAINMLSGH GVTVDTIHSQ NVRALVKRHL IDLAREWPLY FARLFPIQGA
PQYSDVSIMG ISHNGIFLAR RDADYLIVVQ SMPYSEIQNI ITLPRPASLQ LNLRNGKTVA
LHATRAAAIQ AMVTSFVQEF RKMY
//
