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Database: UniProt
Entry: W9W492_9EURO
LinkDB: W9W492_9EURO
Original site: W9W492_9EURO 
ID   W9W492_9EURO            Unreviewed;      1334 AA.
AC   W9W492;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Myosin heavy chain {ECO:0000313|EMBL:EXJ62793.1};
GN   ORFNames=A1O7_03232 {ECO:0000313|EMBL:EXJ62793.1};
OS   Cladophialophora yegresii CBS 114405.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ62793.1, ECO:0000313|Proteomes:UP000019473};
RN   [1] {ECO:0000313|EMBL:EXJ62793.1, ECO:0000313|Proteomes:UP000019473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ62793.1,
RC   ECO:0000313|Proteomes:UP000019473};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., 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 Cladophialophora yegresii CBS 114405.";
RL   Submitted (MAR-2013) 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:EXJ62793.1}.
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DR   EMBL; AMGW01000002; EXJ62793.1; -; Genomic_DNA.
DR   RefSeq; XP_007755447.1; XM_007757257.1.
DR   STRING; 1182544.W9W492; -.
DR   GeneID; 19177832; -.
DR   VEuPathDB; FungiDB:A1O7_03232; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000019473; 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; 1.20.58.530; -; 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; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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};
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:UP000019473}.
FT   DOMAIN          120..170
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          174..871
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..772
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1117..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1139..1153
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         267..274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1334 AA;  153511 MW;  A6D3D1B270B388E5 CRC64;
     MLLHDRSPDT SPFSGHSQRP FTRSVHSDLS VQTPMSSSSY NKSLLFASPT PTPTAASRHE
     RQQSYSPTAS FSSVPSHMRN NSLQRQASSS STFAPKFIKS EEMRKSEDRI SAIEGENDFS
     GKRYVWVRDP EKAFIRGWIT EDLPGNKVAV QFDNGSTIEA DVDEVDKVNP AKFDKADDMA
     ELTHLNEGSV IHNLYTRYQA DLIYTYSGLF LVAINPYCPL PIYGNDYIRM YKGQAREDTR
     PHIFAVSDAA FRRLVEEGEN QSILVTGESG AGKTENTKKV IQYLAAVATS DLDTPITGRT
     PAKQLSNLSQ QILRANPILE SFGNAQTVRN NNSSRFGKFI RIQFTRSGQI AGAFIDWYLL
     EKSRVVKVSQ QERSYHVFYQ LLAGADQRMR DALLLSGMDV EDFAYTRAGN DTIGGISDRD
     EWNTLIEAFH IMNFSEKEQM AIFRTVAAIL HLGNVGVRQE SRATDQASLT TEARASVDKA
     CRLLGVQSEP FVKGLLHPRV KAGREWVEKV QTPEQVRLAL DALSKGIYER GFGDLVSKIN
     NQLDRGGVSS DDSHFIGVLD LAGFEIFETN SFEQLCINYT NEKLQQFFNH YMFVLEQEEY
     AREQIEWQFI DFGKDLQPTI DLIELPNPIG IFSCLDEDSV MPKATDKSFT EKLNSLWENK
     TTKYAPARTR QGFILTHYAA EVEYSTEGWL EKNKDPLNDN LTRLLAASKD EHIANLFSDC
     VDEVDEPYSP RSRVKKGLFR TVAQRHKEQL SILMRQLHST QPHFVRCILP NHKKKPKQFV
     APLVLDQLRC NGVLEGIRIA RTGFPNRLTF AEFRSRYEVL CKDMPKGYLG GQEAAKIMLN
     RLQMEQSNYR VGLTKVFFRA GVLADLEEQR DALIREIMSR FQSIARGFMQ RRMAFKQLYR
     AEATRVIQRN LNVYLDLQDN PWWRLFVRMK PLLGATRTAS EVKRRDEKIE QLQIRMKQEA
     AERQRVEDER RRAEIEAHRI QQTLDSERAL ALDKEEIFKR LQYRESELSE KLAEALTEQE
     ALEDQLDEAL DSKKKIDEEL TTRREQVLQA GQIITRLEAE KKDLQRQIEK LEDELVHVEK
     THTQNDDRLQ TISQELRSLK SNLSVKDRKI SELEANLQQA EKDKESRASS LEQELRSLKS
     QLAQRDRASE DLEKKLHRAE TLRTEESRRQ AEDFDVQIRA LKNELNQKER KLQDLESTLS
     KIDKDAEAKL ARTADELDQS KKLLRELQGQ NDELRKQVTA TALATSKHQE NLRRKEGELS
     ALMADVEQHE REKLELRREN EKLAGGFEDL TTKKREALAE MERLREQRTR MEREAVEVKR
     CLEKVMPFFT QHFA
//
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