ID C4JLJ4_UNCRE Unreviewed; 2413 AA.
AC C4JLJ4;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Myosin-11 (Myosin heavy chain) {ECO:0000313|EMBL:EEP78856.1};
GN ORFNames=UREG_03702 {ECO:0000313|EMBL:EEP78856.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP78856.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476616; EEP78856.1; -; Genomic_DNA.
DR RefSeq; XP_002544185.1; XM_002544139.1.
DR STRING; 336963.C4JLJ4; -.
DR GeneID; 8439565; -.
DR KEGG; ure:UREG_03702; -.
DR VEuPathDB; FungiDB:UREG_03702; -.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_5_0_1; -.
DR InParanoid; C4JLJ4; -.
DR OMA; QRAMDIE; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
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; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 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; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
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; IPR008989; Myosin_S1_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; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW 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:UP000002058}.
FT DOMAIN 117..167
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 171..863
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..764
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1668..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2259..2280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 934..979
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1008..1567
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1610..1644
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1718..1786
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1949..2011
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 264..271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2413 AA; 276717 MW; B1FC24736EA66B21 CRC64;
MSSPSINVAQ RRQNPFSRNS LSPSPAPRET LAIRSGRPKS VAFAAPAQVH PPSHTRTSSF
VPSTSDTFLG QLSRRRSNSV RNNTPSSSTF APEFIKYEEL RKGADQIRGQ EGDNDFSGKR
YVWLRDPEKA FIRGLVLEET ENGMLVVQCD DGSRREINIE NVDKVNPARF DKADDMAELT
HLNEASVVHN LHSRYQSDLI YTYSGLFLVT VNPYCPLPIY SNEYIKLYKG RNREDTKPHI
FATADQAFRS LVEEGENQSI LVTGESGAGK TENTKKVIQY LAAVATGESK SVSKHMSNLS
QQILRANPIL EAFGNAQTVR NNNSSRFGKF IRIEFTPSGQ ISGAFIDWYL FEKSRVVKLN
SQERSYHVFY QLLRGADAET KELLHMANLD IEDFAYLRNG NDSIAGVSDA DEWNTLMEAF
NVMNLSQVDQ LAILRTIAAV MHLGNVSVGK ESSRADQAKL LPDSYPSVQY ACDLLGVPVE
PFVKGLLHPR VKAGREWVEK VQTPEQVRFT LDALAKGIYE RGFGDLVTRI NNQLDRSRIG
GDDSCFIGVL DIAGFEIFEN NSFEQLCINY TNEKLQQFFN HHMFVLEQEE YSREQIEWQF
IDFGKDLQPT IDLIELSNPI GIFSCLDEDS VMPKATDRSF TDKLHSLWDR KSPKYRASRL
SQGFVLTHYA AEVEYKTENW LEKNKDPLND NVTRLLSTSN DGHIANLFSD CADSDAGSTT
VTRSCVKKGL FRTVAQRHKE QLSDLMAQLH STHPHFVRCI LPNHKKKPKL FNGPLVLDQL
RCNGVLEGIR IVRTGFPNRL PFAEFRHRYE VLCRGMPKGI LDGQAAVHMM VEKLALDTSL
YRIGLTKIFF RAGVLAELEE QRDTLIREIM TTFQSVARGY VQRHLVNKRL YRAEAARIIQ
RNFHVYLDLK ASPWWTLFMN MKPLLGETRS AAEVKKRDER IQQLEAKAQQ DQAALEEERR
RADAEMQRIK KTLESERALA LDKEEIFKRL QLREIELTEK LAGAIADQES LEDQVDELIA
SKKRTEDDLD LRRSQLEQAA QLMSRLETEK KELQMRISKL DHQLQTVEET YQQKDSDIEK
LNQEIKVLNS HLSLKERKLH DLEAKVLKSG QDLDIKLADT TKELQSTRQQ VKELKDENRD
IQQQLSTLSS TSTDFEHLLR QKESELSMIR SDIRKHEADK KRLEAERDSF STRHGDMQRR
IYELQAQIDA MKSENANLER EAADAKKLLE ARISEDAQSG QTRKMLDQQV KDLKAQLYQV
QTELSRERQS RDDVQMLGEH RYAQLKEEFD KLNESKITIE KEMYIQQDAL RRAKEARTAA
EESRIELQAE IIKLRERITK AESARLDAET AAETKLKAQA NERVTSLRKE LDAKIRQLEE
TDAERTRLAA QVQNLSKIMA EKEDFKIRND QHKERLEREL VTVKGRLVAS ENDNRALLNK
IQQKNLDIAR SNSRASDTQR ARLAQLQNEK VRLEETNKKL TRQVGDSQLT ITSLEKQKEK
LALSLEDLNH EVAREHKASR NAEKAASASN IQLAEANRTL ETERQAKAQA QANTRRLQDS
LDQAHKEIQD CHQQLILLHK VFSPEITEIP ASWEEVKPNI SKQVDMAATL ESVQESLRVS
EEKRARAESQ LAEMRRRHVD EVAELDARFS SSKRALLEEI DLNQVANTRS PGHFRKNSEP
FKRYSNPSTP NRRFNLIETA GDSGRSDRTV DTVAFQKRMD LAAEVEMLQN QLQMSEMQNR
HLQSQLDRAT PVRDTWQDES PSVRRMKLLE RENGRLHEKL DDSAKKVSAL ERTIQSGELT
LRDVQAKSHE ELYDLLNSQE NSRKSLLQVH KSTLADLTEA KSQFDKLKHA RSSMEVELRD
VTSELRDLQL AREQDAASRS QLLQEFSDLQ IRLDAEASKV VDLTSSLSLY KSRADEYFSK
LEQAELAVLK ASRAEQFAKS QAKELEDSCA TIMAERKQMD NLIEDLQRQT QSYEEKIEDL
SADFDAALQA KRRLQNELED YRSQRAMDIE DKEASMEQTR KKYQMEFSGL TSELEIEREN
VLHIRGENTR LREELEDLRS KWDDEVLNSS TWAKEKSRME MTLQDISNSR EEAIRAHNDA
QSKVVSLLSQ VRNLRTSFDE VTAERDQATK EKRSLEGRLA ETAERLESLA NGENPSMRNA
AEMDRDLLEL KSKLAQQEDV ATAAVGKMRR AEALATEIQK EMVAEREATA QLFKDKAALE
KQLKEAQLRC IDLETKGYSS ASQDVRFLHK RIQELETQLE DQESKRSAEQ RSVRNVDRTV
KDLQSQIERR DKMNAQLTDD IAKSRDKIER LLQNIDELQT SESENQLQAR RAERELREEK
EKSLRLEREL DGWKSLRVER GSAIARSTTF TGLSDIGIGE RFGSRRGSGV FVGGTNAVIE
VPQRKTSNTK GFL
//
