ID N4THE9_FUSC1 Unreviewed; 2327 AA.
AC N4THE9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Myosin type-2 heavy chain 1 {ECO:0000313|EMBL:ENH61979.1};
GN ORFNames=FOC1_g10014932 {ECO:0000313|EMBL:ENH61979.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH61979.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KB731260; ENH61979.1; -; Genomic_DNA.
DR STRING; 1229664.N4THE9; -.
DR VEuPathDB; FungiDB:FOC1_g10014932; -.
DR HOGENOM; CLU_000192_5_2_1; -.
DR OMA; QRAMDIE; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
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:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR004009; Myosin_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000016928}.
FT DOMAIN 118..168
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 172..790
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..691
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1106..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2178..2200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2279..2302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1638..1665
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1764..1988
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2031..2065
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2327 AA; 267555 MW; F772438D94A30CBA CRC64;
MTFNANANGT AHRRSNPFAR TPSASPATNT NLRPKSAIFS SPSSTPGLST PLGHSRTQSN
GSLSAITHGF SGSAPRQQRS DSKSGTPTST TFAPSFIKTE EMKRHDTVKG IEGENDFSGK
RYVWLKDPQA AFVRGWIVEE MDGNRLLVQC DDGTQREADA ESVDKVNPAK FDKANDMAEL
THLNEASVVH NLHMRYQADL IYTYSGLFLV TVNPYASIPI YSNEYINMYR GRNREDTKPH
IFAMADEAFR NLVEEGKNQS ILVTGESGAG KTENTKKVIQ YLAAVAQADS TIKHKPHHSN
LSQQILRANP ILEAFGNAQT VRNNNSSRFG KFIRIEFTRN GAICGAYIDW YLLEKSRVVH
INPHERNYHV FYQLLKGASS SLKREFLIDG LTVENFNYTR DGHDTIVEPF LKGLLHPKVK
AGREWVEKVQ TPEQVRLGLD ALSKGIYERG FGDLVNRING QLDRTGMGLE DSHFIGVLDI
AGFEIFEQNS FEQLCINYTN EKLQQFFNHH MFVLEQEEYA REQIEWKFID FGRDLQPTID
LIELSNPIGV FSCLDEDCVM PKATDKSFTE KLNSLWDKKS SKYRPSRLGQ GFILTHYAAE
VEYSTEGWLE KNKDPLNDNI TRLLAASSNK HVASLFSDCA ESEEDHATGR SRVKRGLFRT
VAQKHKEHLH SLMAQLHSTH PHFVRCILPN HKKKPKQFNN LLVLDQLRCN GVLEGIRIAR
TGFPNRLPFA EFRQRYEVLC QDMPKGYLEG QAAASLMLEK LGLDRALYRV GLTKVFFRAG
VLAELEEQRD ALITQIMSRF QSVARGFIQR RAAYKRLFRT EATRIIQRNF NVYLDLAENP
WWQLIVKMKP LLGTTRTATE VKRRDAMIKD LNERMQLESQ NRMKLEEERR NCHAEMVRIQ
QTLESERALA LDKEEIFKRL QLREAELEEK LAGAIEDQER LEDELDDLLN AKNRAERDVE
TYRSQLEQAA TLIAKLEEEK RGLSTKISEV EQSMADITQR QAERSEQELA LQDEIKMLQS
QLSVKERKVQ DLETKLVKLD QDSELKLNAA QRELQSTKLR ETQLTHENED IQRQLNELSK
TSTDYEDLVR QKESELALLR TDNKNFESER QSLEDQKKSL TTEKEKNAEK YREAQAELVA
MKSRQSQLER EAEDAKSLLE ARLSEDAQAD QNRQVLESQI KDLKDELYKT QMDLSRERQS
RDDVQLLGEH RYQELKDEFD RLNESKIIIE KELYAQQDTL RRTMEARTTA EKERDEARQE
IRRLRVAKTQ AEEARMQAEV AGERQASKAA LDRENSLRKD LDAAQERLQW FEGECAKLNH
QIEDLNKLIL ESGEFGLKND QAKERLEREL TTVKSRLTAS ENDNRALLNK LQQKGLEIAR
SSSRASEASR GQIMSLQREK ARLEEQNTKL NKQLGDSQLA IASLEKRAEK LQLSLEDLSH
EVAREVKSSR NAEKATSTFT AQLAEANRTI ESERQLRTQA QTTIRTLQTS VDTRDKEVNE
LRAQMLDVLR TVDPEVPIPP QSDGADENVL IQNFDLVRKV EELQQNLRVQ TAARTNAENQ
LSEMRASRND PASRPKLEEI QLNEAPFQGS PTQKRAAKLH ARNYSNTSTP TRRFQELDHL
QDSTRSDRTI DTLNFNNRMD LKAEVEELQN QLQLKEMQNR HLQSQIDRST PIPENYDDQS
PSLRRIQKLE MVNTRLHEML DDSNKKVSAL ERTIRSGQLS LRDVQTRTHE EILEVLNSQE
DSRRALVHSH KDAVAELTDI KGHFERLRHD RAKAEVELRD VKSDLQEMTL AREQEAQNRN
QLLQEFADLQ IRLDAETSKF ADVSSSLEMY KSRADEYFSK LEQAEIAVLK ASRAEQFAKS
QAKEAEDTYA EVMAEREKMD ASIEDLQRQN QRLEEKVEDI STDLAAATQA KKRLQHELED
YRNQRAMEIE DKESSMEQTR KKYQAEFATL TNELDLAREE RLFKQAEIAR LREELDELRS
KWDDEVLNSS TWSKEKARLE STLADVASSR DEAVNAHNEA QGKVVTLLSQ VRTLRSSVDE
ITAERDHLLR EKRNVEARLE EAKSGLEDLV KGDSPSLRNA ANMDKEILEL RSHLAQQEDI
AAAAVEKMRR AEALVTEVQK DVMVERENSI QLQQQKASLE KVLNEAQLKL VDLETKGYSS
ASQDVKFLHK RIQELESQLE DQETERSKSQ RSVRNVDRIV KDMQGQIDRK DKQNTQLSED
VLRMRDKVEK LLKTIEELQS SESQNQLSAR RAERELREEK EKIARLEREL AGLKNLRNDK
GSGSVMGSVR SRMGPWRVSE GDDASMVDIP RRKSSLSRVP SFTKGFL
//
