ID A0A0D2IVR7_9EURO Unreviewed; 1335 AA.
AC A0A0D2IVR7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Myosin heavy chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z518_01215 {ECO:0000313|EMBL:KIX10134.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX10134.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX10134.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX10134.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN847475; KIX10134.1; -; Genomic_DNA.
DR RefSeq; XP_013277270.1; XM_013421816.1.
DR STRING; 1442369.A0A0D2IVR7; -.
DR GeneID; 25289286; -.
DR VEuPathDB; FungiDB:Z518_01215; -.
DR HOGENOM; CLU_000192_7_16_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000053617; 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; 1.20.58.530; -; 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 SUPFAM; SSF57997; Tropomyosin; 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:UP000053617}.
FT DOMAIN 121..171
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 175..872
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 52..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..773
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1121..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 943..1089
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1335 AA; 153602 MW; 1D75AF535F07B8FA CRC64;
MLLHDRSPDA SPFNGASQQR HYAFNKSYNS DMSMASSMPN SSISKSLLFA SPAPAQPSRH
ERQQSYSPSA SLSSIPSHVR TQSLQRQSSA SNTFAPKFIK SEEMRKSEER ISAIEGENDF
SGKRYVWVKD PEKAFVRGWI TEDLPGNRVL VQFDNGSQIE TDVDEVDKVN PAKFDKADDM
AELTHLNEAS VIHNLLTRYQ ADLIYTYSGL FLVTVNPYCP LPIYGNDYVR MYKGQAREDT
RPHIFAVSDA AFRRLVEEGE NQSILVTGES GAGKTENTKK VIQYLAAVAT SDLDTPLTGR
APGKQLSNLS QQILRANPIL ESFGNAQTVR NNNSSRFGKF IRIQFTRSGQ IAGAFIDWYL
LEKSRVVKVS QQERSYHVFY QLLAGASQRM RDALLISGMD VEDFAYTRAG NDTIGGVSDR
DEWNTLIEAF HIMNFSDKEQ MAIFRTMAAI LHLGNVAVRQ ESRAADQASL TPEAKASVDK
ACQLLGVQTE PFVNGLLHPK VKAGREWVEK VQTPEQVRLA LDALSKGIYE RGFGDLVSKI
NTQLDRGGVS SDDSHFIGVL DIAGFEIFET NSFEQLCINY TNEKLQQFFN HYMFVLEQEE
YAREQIEWQF IDFGKDLQPT IDLIELPNPI GIFSCLDEDS VMPKATDKSF TDKLHSLWEK
KTPKYAPART RQGFILTHYA AEVEYSTEGW LEKNKDPLND NLTRLLAASK DEHISSLFGD
YVDEMDEPYS PRSRVKKGLF RTVAQRHKEQ LTSLMRQLHS TQPHFVRCIL PNHKKKPKQF
NAPLVLDQLR CNGVLEGIRI ARTGFPNRLS FAEFRSRYEV LCENMPRGYL GGQEAAKIML
DRLKMDRSNY RVGLTKVFFR AGVLADLEEQ RDSLIRDIMS RFQSRARGFT QRRQAFKQLY
RAEATRVIQR NLNVYLDLQA NPWWRLLVRM KPLLGATRTA SEVKKRDEKI EQLQAKMRQD
AAERHRVEDE RRRAEIDVQR IQQTLEAERA LALDKEEIFK RLQYRESELT EKLSEAIAEQ
ETLEDQLDEA MVSRKKAEEE LSTRREQVLQ AGQIITRLEA EKKDLQRQVD KLEDELENVE
KTHSQNDDRL ETISRELRTL KTQLGVKDQK IFDLDTSLKR AEKDKEDRTT SLEQELRSLR
SQLTQRDRAT EDLEKKLRRA ESLRAEDNKR HTEDHESQIR VLRSELNNKD RKMQELEDDL
SKMDKEAETK LTNTSHELTI TKKLLRELQG QNDELRKQVT SMSMTSSKHE EALRRKEGEL
SALMADVQQH EREKSGLREE NDALAGRHES MQAKHRELQG DLDNLRAQRA RMEREAAEVR
RCLERVMPFF TQNFS
//
