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Database: UniProt
Entry: A0A182SCD0_9DIPT
LinkDB: A0A182SCD0_9DIPT
Original site: A0A182SCD0_9DIPT 
ID   A0A182SCD0_9DIPT        Unreviewed;      1599 AA.
AC   A0A182SCD0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Anopheles maculatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles; Anopheles maculatus group.
OX   NCBI_TaxID=74869 {ECO:0000313|EnsemblMetazoa:AMAM003933-PA, ECO:0000313|Proteomes:UP000075901};
RN   [1] {ECO:0000313|Proteomes:UP000075901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=maculatus3 {ECO:0000313|Proteomes:UP000075901};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles maculatus species B.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMAM003933-PA}
RP   IDENTIFICATION.
RC   STRAIN=maculatus3 {ECO:0000313|EnsemblMetazoa:AMAM003933-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   EnsemblMetazoa; AMAM003933-RA; AMAM003933-PA; AMAM003933.
DR   VEuPathDB; VectorBase:AMAM003933; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000075901; Unassembled WGS sequence.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd17092; FERM1_F1_Myosin-VII; 1.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd01381; MYSc_Myo7; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 2.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 1.20.80.10; -; 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; IPR019749; Band_41_domain.
DR   InterPro; IPR031732; DUF4729.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
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; IPR036106; MYSc_Myo7.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR22692:SF33; MYOSIN; 1.
DR   PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR   Pfam; PF15866; DUF4729; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50096; IQ; 4.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          207..877
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1153..1389
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          1394..1599
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..778
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1086..1109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1029..1059
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         300..307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1599 AA;  184957 MW;  F340DB30638BC4C9 CRC64;
     MQRAKHLKTP TNTNQESTRN LPKSNSITPA QCPLPGCDQS VMASNLLQHY LRDHSNLSFI
     SIEDRETMLF HFEESAFPLN TPYCLGVLAY GGRQPEHHPV REGYAVENQF LPQRFKSLKN
     YLPVLVMGCR TTRFGDAESV LQGDHDEEKR GDYIWIEPVS GREFDVAIGA RVISAEGRRI
     QVRDDDGNEQ WLTPERRIKA MHASSVQGVE DMISLGDLHE AGILRNLLIR YNENLIYTYT
     GSILVAVNPY QILPIYTADQ IKLYKERKIG ELPPHIFAIG DNSYAHMRRY GQDQCIVISG
     ESGAGKTEST KLILQYLAAI SGKHSWIEQQ ILEANPILEA FGNAKTVRND NSSRFGKYID
     IHFNSAGVIE GAKIEQYLLE KSRIVSQNAD ERNYHIFYCL LAGLSPEEKR RLDLGQASDY
     RYLTGGGCIR CDGRNDAAEF ADIRSAMKVL CFSDHEIWEI LKLLAALLHT GNIKYNATVI
     DNLDATEIPE HINVERVANL LEVPLQPFID ALTRKTLFAH GETVVSTLSR DQSMDVRDAF
     VKGIYGRLFV LIVKKINQAI YKPKSSTRSA IGVLDIFGFE NFDHNSFEQF CINFANENLQ
     QFFVQHIFKL EQEEYNHESI NWQHIEFVDN QDALDLIAIK QLNIMALIDE ESKFPKGTDQ
     TMLAKLHKTH GTHRNYLKPK SDINTSFGLN HFAGVVFYDT RGFLEKNRDT FSADLLQLIS
     SSTNKFLQLV FAEDIGMGAE TRKRTPTLST QFKKSLDSLM KTLSQCQPFF IRCIKPNELK
     KPMMFDRALC CRQLRYSGMM ETIRIRRAGY PIRHNFRDFV ERYRFLINGI PPAHRTDCRM
     ATSKICATVL GRSDYQLGHT KVFLKDAHDL FLEQERDRVL TRKILILQRS IRGWVYRRRF
     LRMRQAAVTI QKYWKGYAQR QRYKKMRIGY MRLQALIRSR VLSHRFRHLR GHIVRLQARI
     RGYLVRREYG HKMWAVIKIQ SHVRRMIAMK RYHKLKLEYR RHHEALRLRR MEEEELKHQG
     NKRAKEIAEQ HYRDRLNEIE RKEMEIELEE RRRVEVKKNI INDAARKADE PVDDSKLVEA
     MFDFLPDSSS EAPTPHGGRE TSVFNDLPVN AGSHDDIIGP IHTISEEDEE DLSEFKFQKF
     AATYFQGNIT HYYSRKPLKH 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 NQLSDKITLK DQFGFSLYIA
     LFDKVSSLGS GGDHVMDAIS QCEQYAKEQG AQERNAPWRL FFRKEIFAPW HNPIEDQVAT
     NLIYQQVVRG VKFGEYRCDK EEDLAMIAAQ QYYIEYSTDM SMDRLYTLLP NFIPDYCLTG
     IEKAIDRWAA LVLTAYKKSY YLKEKAAALK VKEDVVSYA
//
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