ID A0A2S4KUW8_9HYPO Unreviewed; 1589 AA.
AC A0A2S4KUW8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Myosin MYO2 {ECO:0000313|EMBL:POR33985.1};
GN ORFNames=TPAR_05808 {ECO:0000313|EMBL:POR33985.1};
OS Tolypocladium paradoxum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=94208 {ECO:0000313|EMBL:POR33985.1, ECO:0000313|Proteomes:UP000237481};
RN [1] {ECO:0000313|EMBL:POR33985.1, ECO:0000313|Proteomes:UP000237481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRBC 100945 {ECO:0000313|EMBL:POR33985.1,
RC ECO:0000313|Proteomes:UP000237481};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POR33985.1}.
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DR EMBL; PKSG01000596; POR33985.1; -; Genomic_DNA.
DR STRING; 94208.A0A2S4KUW8; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000237481; 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; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 3.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000237481}.
FT DOMAIN 74..782
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1234..1503
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1036..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1589 AA; 180436 MW; ACE76EE411608BEF CRC64;
MASTYDVGTR AWQPDAAEGW VASQLVTKTI EGSKAKLVFQ LDNGETKTIE VPVEALHSGS
DAALPPLMNP TMLEASDDLT NLSHLNEPAV LQAIRLRYLQ KEIYTYSGIV LIATNPFARV
DSLYVPGMVQ VYAGRQRATQ APHLFAIAEE AFMDMIRDGK NQTIVVSGES GAGKTVSAKY
IMRYFATRES PENPGARSKR GPETMSETEE QILATNPIME AFGNAKTTRN DNSSRFGKYI
EIMFDEKTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGASDKQR QDLDILPVEE
FEYLNQGDCA TIDGVDDKAE FEATKKSLQT IGVCDAQQAD IFKLLAGLLH LGNVKITASR
NDSVLAPTEP SLERACDILG VNATEFAKWT VKKQLITRGE KITSNLSQAQ AIVVRDSVAK
FIYSSLFDWL VDIINHSLAT DEVLNRVSSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
QEFNQHVFKL EQEEYLREQI DWTFIDFSDN QPCIDLIEGK LGILSLLDEE SRLPMGSDEQ
FVTKLHQNYV SDKQHAFYKK PRFGKSTFTV CHYAIDVTYE SEGFIEKNRD TVPDEHMTVL
RATGNPFLKQ VLEAASAVRE KDVASASSNA VRPAGGRKIG VAVNRKPTLG GIFRSSLIEL
MNTINNTDVH YIRCIKPNEA KAAWQFEGPM VLSQLRACGV LETVRISCAG YPTRWTYEEF
ALRYYMLVHS GQWTSEIREM ANAILTKALG TSTGKGLDKY QLGLTKIFFR AGMLAFLENL
RTSRLNDCAI LIQKNLRAKF YRRRYLAVRE SVIRTQSAAR AYIARRQAQE LRTIKAATTI
QRVWRGQKQR KRFLLIRKDM VLFESAAKGY LRRKQIMETR VGNAALVIQR AWRSRTQLRS
WRQYRKKVAL VQSLWRGKRA RREYKKVREE ARDLKQISYK LENKVVELTQ SLGSMKEKNK
NLASQVENYE GQIKSWKTRH NALEARTKEL QTEANQAGIA VAKLQAMEDE MKKLQLAFDE
STANIKRMQE EERELRESLR LTNTELETAK QSSGEREKDN ISLRQELEAL RDALEVAKRS
APINGELTNG VAAPTTATGL INLVSSKKPK RRSAGAEPRD LDRFSGAYNP RPVSLAVTST
AHRQNLSGTT YLSGTTYIPG VDNIEMELET LLADEDGLNE EVTMGLIRNL KIPSPNTTPP
PSDKEVLFPS YLINLVTSEM WNNGFVKESE RFLANVMQSI QQEVMQHDGE EAINPGAFWL
SNVHEMLSFV FLAEDWYETQ KTDNYEYDRL LEIVKHDLES LEFNIYHTWM KVLKKKLHKM
IIPAIIESQS LPGFITNESN RFLGKLLQSN SAPAYNMDNL LSLLNSVYRA MKAFYVEDSI
LIQTVTELLR VIGVTAFNDL LMRRNFLSWK RGLQINYNIT RIEEWCKSHD MPEGTLQLEH
LMQATKLLQL KKATLNDIEI IQDICWMLSP NQIQKLLNQY LVADYEQPIN GEIMKAVASR
VTEKSDVLLL QAVDMDNSGN YEIAEPRSIT ALETYTPSWL QTPRLKRLAE IVSAQAIAQQ
EKLDYVDGEG FNGQETLTEE DEVKAEAGQ
//
