ID A0A182RJ78_ANOFN Unreviewed; 2397 AA.
AC A0A182RJ78;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 3.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Myosin class i heavy chain {ECO:0008006|Google:ProtNLM};
OS Anopheles funestus (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN006294-PA, ECO:0000313|Proteomes:UP000075900};
RN [1] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT Middle East: occurrence data, distribution maps and bionomic precis.";
RL Parasit. Vectors 3:117-117(2010).
RN [2] {ECO:0000313|Proteomes:UP000075900}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA Besansky N.J.;
RT "A chromosome-scale assembly of the major African malaria vector Anopheles
RT funestus.";
RL Gigascience 8:0-0(2019).
RN [3] {ECO:0000313|EnsemblMetazoa:AFUN006294-PA}
RP IDENTIFICATION.
RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN006294-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 62324.A0A182RJ78; -.
DR EnsemblMetazoa; AFUN006294-RA; AFUN006294-PA; AFUN006294.
DR VEuPathDB; VectorBase:AFUN006294; -.
DR VEuPathDB; VectorBase:AFUN2_011296; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000075900; 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 GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 2.
DR CDD; cd17208; FERM_F1_DdMyo7_like; 2.
DR CDD; cd14883; MYSc_Myo22; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.20.80.10; -; 2.
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); 2.
DR InterPro; IPR019749; Band_41_domain.
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; 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; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46049; AGAP003327-PA; 1.
DR PANTHER; PTHR46049:SF5; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY H MEMBER 3; 1.
DR Pfam; PF00373; FERM_M; 2.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00784; MyTH4; 2.
DR Pfam; PF00788; RA; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00295; B41; 2.
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; 2.
DR SUPFAM; SSF47031; Second domain of FERM; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 2.
DR PROSITE; PS50057; FERM_3; 2.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51016; MYTH4; 2.
DR PROSITE; PS50200; RA; 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};
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 17..711
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1280..1430
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 1435..1754
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 1843..2003
FT /note="MyTH4"
FT /evidence="ECO:0000259|PROSITE:PS51016"
FT DOMAIN 2006..2113
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 2008..2316
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 592..614
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 794..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2315..2397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2315..2334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2335..2354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2381..2397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2397 AA; 272218 MW; 2A2F9405A9BE788C CRC64;
MAVPVFLEGR IGSTPDKGVP DMTCISDIDE NGINRNLKVR YERDQIYTYT GSILIAVNPY
KEIDCYTQEY VAKYHGQKLG LLEPHVFAMA EAAYRNIRDN NTNQSCVISG ESGAGKTETT
KFILQYLCSV TCDVSTWVQQ QILEANTILE AFGNAKTIRN DNSSRFGKFM QVCFDSKWCI
KGCIIQDYLL EQSRITFQSP GERNYHVLYQ LVAEGTTNKE LAAALHLRDA SFYRYLNSSG
GTGDAGTDQS ALEIVTESKR FEALRLAFNV LQISQPLIDG IFRVLSAIMW LGNLNFADVD
GERCELAPED DEIVKIVAQL LGLQEADLVQ VLLKRQINVR GNITEIPLKL QEAGENRHAM
AKALYSRTFA WLISHINTCI NPGQDASRFL GVLDIFGFEN FNTNSFEQLC INYTNEKLHK
FFNHYVFALE QEIYRQEEIR FSHIQFTDNT QCLELIEKPP RCILKLLTEQ CHMPKGSDTA
YLTNLHSEFE SNGSYVKGQD RRHWESEFGI RHYAGCVSYT VKGFVDKNRD VQQDVLFDHM
SRSMNTFVQE IASFQDLLSI QHVQSASSAT STVSRGTSKG KLTVSDTFRQ QLQALVDVLQ
STNPWYVRCI KPNCDKLPND YDDQLVLDQL RYLGMLDIIR IRREGFPVHL TFDDFVQKYQ
CLTKRFRNMS SQDQALAVIR ELNVPTTEWQ MGRTKVFLRS VVHEPLEDAR KQVINSKALI
IQRNWKRFSQ QRQYRRLRTA ALKIQHAYKG WKLRIEFLKK RRAAIVIQSH LRGVFAREVA
TALREMRRVD EEMRKRERLE AERREREAAQ AEADRKALEE SERVAKEEIL ALSQMAEQIN
SKLHSQQHAA NNNSRLAQGS LQQNGPAGGD CKGAGSLQPG GAKGAGSASL QSNDSVDLDN
LFAFLSEVQP NANSNAIIDE IGEKMDNLVE DLDVELESVI QQEIEGLTSE RNNNVAAAST
LKGGPLINGN NNAISSSNNN NNNINNNKPT TPKPMGGIPS LPEPTMPPPP PPIENNNHTL
PAAQPHHPAT LHHIRRHEEP IYEAVIHLKE LPPPPLDAHE KVPPIPQHQP AQVPIVPSQH
HSTVAPPPPV HAHQQPVPPP HAHQAPMHHP VSQPGATHPP QPEAPPQPPP HAHAAPSHAY
VHLENGTAGH KLRPKSPAVI RSASPIQRTG PNGPMSPSSP KHSRPSSRAS STGGGHPFAE
REQRRKYRVE KKLQEMQQMD ITEREKELLR DDVYYDILEF AESFYNTHER SPEGTIMATL
TRKGRKSVDM VPKYEMITYY RGTTIPSSHI HMYDPENVTI ACNIFRDLCK YIRGELNSER
ELQVIQFIIG QGIEREELRD EIFVQCMRQA TNNPSVDWTD RVWLLLCLTI VAFQPSKLLF
RYFVSFLKKN LESLEGKLRQ YVQWCLDNCK NTKVRCRQYP PSSVEVAAMR RLGTIVCRFF
FLDGRTKAID VHPTDTASDA VAKLAEKLGL CNIEGWAIYQ SRPDGEEHVK SHDYLYDIIA
AWEAKQTKIH ASSSTLRKNA TTLGSGENRF VFKKRLFKST RELSQDPVEV NMLYAQAVYS
VVKCDDFPVS EKVALQLAGL QAQVALGDPS NQPKPEYYSD VPSYLPERIS KTREEQFWVP
ILAQAHRQYG SGRTELTAKV LYLSCVMQYP LYGTTMFAVS YRGYWSYGNS LILGVNCEGI
ILIKPDDKFV LYEFRYAEVE SIMLDPSDSF ITISLNRHTS TSTDQQRCFV FETAQKNEIG
SLIVSYYPAL SNWITENEVP PKKSKGITNE DRVRLHHNLV VCRRHLVDAE ILRKPQDPSG
GFLRNTLRRL SKHRLEKLRA EHGSPVHDHG ETYKGFPHAY WAFSRQALPQ SLSKLPDQEE
QAMLQVFNSI LTYAGLGQNG ETVQRAEDEH ITLIQSIMDR CMRKESLLNE LYLQLIKQTT
DHPDPNSRVN LRHWALLSLA CSVILPPQKV VRKYLLGHLK RCASDFITEE GKYARFAEKC
FFKTQGTRRR QWPPSREEII CTINRRPIYA RFHFMDGQYH SVEFHPSSTS REVMEIVKKK
IGLQENALGY AIYEVLGASE RSLLPDEKVA DVMSKWEKYR TAAAQAVQQN QSSNLPPACR
RQHHLFLFKK HLFCDQYMNL DDPVEKELLY HQVLHGLRTE RFPITEMEAI MLTALQGQLE
LGDSSDIVQD YRPIAAHCLP PRFVPNIPRD SVAMHHQSLR GTTPAEAKKS FLNLIQSWPL
HKATIFDVMQ SFTSNWPRML WLAVDQKGLH LLEHRSRNTL CTYDYQSILS FSPNMNCLMI
ITGSDKKQSK VILTTAQAFQ IANLIREYME VLQRQQQSHV DDTQKENQSS GANQPPPAPL
VPPHNQPLPP PHQHLPVQQQ GVGGTVGTAT DLRKAGQRPP SMLLRQSSAA LVAPQPS
//
