ID A0A137QN41_9AGAR Unreviewed; 1266 AA.
AC A0A137QN41;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Myosin type-2 heavy chain 1 {ECO:0000313|EMBL:KXN88688.1};
GN ORFNames=AN958_06232 {ECO:0000313|EMBL:KXN88688.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN88688.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN88688.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN88688.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) 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; KQ962129; KXN88688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137QN41; -.
DR STRING; 1714833.A0A137QN41; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000070249; 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; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 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}; 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:UP000070249}.
FT DOMAIN 14..63
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 67..768
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 646..668
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1245..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 835..954
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1251..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1266 AA; 145350 MW; B6ECE94AF4EA59A9 CRC64;
MAAVLPSAVA EAARQPAQVW VPDLKEGYLP GLVLNEDEDA AVVELEGGEV RRVPYDSLFK
MNPPKFDRVE DIADLTFLNE ASVVHNLRLR YYSGNPQTYS GLFLVAINPY QNLPLYTDVI
IQQYRNKRRD DNPPHIFAVA ERAWVNMGDE RENQSILITG ESGAGKTENT KKVIQYLAAI
ATDTQAPVQP THTRRLGLLE RQILQANPIL EAFGNAQTQR NNNSSRFGKF VRISFAPDGS
IAGANIDWYL LEKSRVVYRN EAERNFHVFY QLLAGGDQLL LDGDVENYEY LNKSRREIDG
IDDREEWDAL KAALDVVGFT PAEQFDLFRI VAAVLHIGNI VINATRADDA TMQDTSQAER
VCHLLGIPLA EFTRAVLRPR ALAGREWVTQ ARTRQQALDE LAALCKTLYE KSFGALVDQI
NRALDRPSSK STFIGVLDIA GFEIFEINGY EQLLINYTNE KLQQFFNHHM FILEQEEYAR
QNIKWDYVNF GLDLQPTIDL IESSGNVIGI LSCLDEECIM PKATDLTFTN KLHALWASGD
EEEEYRHPGK DKYEPTRFEQ GFIIQHYAAK VDYRTEGWLE KNKDPLNDNL TRVLAASSEK
YIASLFVEYS DVPMPGGPNN IFTQGKKRTL KKGAFRTVGQ RHKEQLSSLM TQLRSTQPHF
VRCIVPNNFK KPHRIEVPLV LDQLRCNGVL EGIRIARLGY PNRLPFVEFR QRYEILTPGI
IPRGYMDGRE ACRRMVSVLE LDESTYKIGT SKIFFKAGVL AELEDARRQL QKKLQDDELK
STTSAAAESE FKAAIGSYQQ KEQGYLERLE ATEIARATAA RGEAYDIFFI VRRQLETMEK
ALTDAKAEIK TVKEKFQAAE QKLRSMESKL EEEGREASDL AVIQKRLEEE LEDERESHQK
DLAERDFTID QTRKKYQAEL AQLSEELQSQ RDSLSRLREE NRKIRSDFDE LQLRYDDEVY
NSGGWKKEKE RMDTKIQDIT RAFEASTHAQ TEQQAQIVAL HQQVRELRGV LDDAEAERAM
LQKARRALQA ELETIKLDHV DTNKTMSDTE FQRLQLKKQD LERTLEEQGD RVAQALDRMK
KAEAYATECF NELERVRKEN AGLDRQNAQL EKQVKELNVR IVDLETRSYA NSPRPATISR
RVDSRIEELT SQLNQSNRDK STLGRSAEKL AKDAKFQQNE LERQRQKFEE ERKAYETRIQ
DLRNALDTVQ TKEHELQAAN RRVTREAGDY KQRALNLERE LERLHSRLER PASSSIGSPV
SSPRKQ
//
