ID V5FZY0_BYSSN Unreviewed; 2399 AA.
AC V5FZY0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Myosin type II heavy chain {ECO:0000313|EMBL:GAD97648.1};
GN ORFNames=PVAR5_6328 {ECO:0000313|EMBL:GAD97648.1};
OS Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD97648.1, ECO:0000313|Proteomes:UP000018001};
RN [1] {ECO:0000313|Proteomes:UP000018001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA Oka T., Ekino K., Fukuda K., Nomura Y.;
RT "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL Genome Announc. 2:E0116213-E0116213(2014).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC 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:GAD97648.1}.
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DR EMBL; BAUL01000208; GAD97648.1; -; Genomic_DNA.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_5_3_1; -.
DR InParanoid; V5FZY0; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000018001; 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; -; 2.
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:UP000018001}.
FT DOMAIN 114..163
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 167..860
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 739..761
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1449..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1684..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2370..2399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 931..979
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1008..1070
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1610..1655
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1719..1787
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1831..1900
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1950..2062
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2119..2357
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..21
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 COMPBIAS 1449..1466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260..267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2399 AA; 275258 MW; B505939D50839B93 CRC64;
MLPSQLNSPS RRANPFGRSS VSPSPGPQPL PSRPRSAVFT SPVNPAMEAK GHLRNSSTSN
LSPTSLAAPG GRQRSSSVRQ NAHTGTFAPQ FIKSEELRRG ADQVRGMEGD NDFSGKRYVW
LKDPEKAFVR GLVVEEKEGG RLLVQCDDGT REVDSDQVDK VNPAKFDKAD DMAELTHLNE
ASVVHNLHSR YQSDLIYTYS GLFLVTVNPY CPIPIYTNEY VKMYKGQSRE DTRPHIFAMA
DQAFRNLVEE GENQSILVTG ESGAGKTENT KKVIQYLAAV ATADTPASRS GAKQFSNLSQ
QILRANPILE AFGNAQTVRN NNSSRFGKFI RIEFTRSGQI VGAWIDWYLL EKSRVVKPNP
QERNYHVFYQ LLRGADKELR DTLHLGDFDF DDFCYMKDGN DSIAGVSDED EWNSLMEAFH
VMNFSSTDQL CILRTIAAVL HLGNIAIGKE SLRGDQAALA PGAYENVQRA CDLLGIDPEA
FVKGLLHPKV KAGRELVEKV QTPEQVRAAL DALAKGIYER GFGDLVSRIN SQLDRNGIAG
DDSCFIGVLD IAGFEIFENN SFEQLCINYT NEKLQQFFNH HMFILEQEEY AREQIEWQFI
DFGKDLQPTI DLIELTNPIG IFSCLDEDCV MPKATDKSFT EKLHSLWDRK SPKYRASRLN
QGFVLTHYAA EVEYSTTDWL EKNKDPLNDN ITRLLAASND KHVANLFSDC GDGDEELASK
SRVKKGLFRT AAQKHKEQLA KLMNSLHSTH PHFVRCIIPN HKKRPKLFNA PLVLDQLRCN
GVLEGIRIAR TGFPNRLPFT EFRQRYEVLC RDMPKGYLDN QSATQMMLDK LGMDKAWYRV
GLTKVFFRAG VLAELEEKRD KLIRDIMSRF QSVSRGFIQR RIANKRLYRA EATRIIQRNF
HGYLDLKANP WWRLFMRMKP LLGETRTATE VKRRDEQIQK LESKVQKELA DRQKLEEERR
RADQEIQRVK QTLESERALA LDKEEIFKRL QLREVELTEK LAGAIADQET LEDQLDDLIA
AKKKAEEQLE VRRTQLEQAG QIIERLEGEK HELQERLLEL DDKLKGVETT HQERDTQVHN
LSQEIKMLQS HLSLKDRKLH DLEAKLLKSD QDLDVKLANT TKELDISKKK VKELVEENRS
IRQQIADLSS TSTGYEEMLR RKEGELSVLR NDLQKHETDK RNLESEKLSL STRHDNMQKR
LREVQAEMDA MKTERANLER EAADTRKLLE EKMSEDAQAG QSRAMLDEQV RDLKAQLFQV
QAELSRERQS RDDVQMLAEH ELEQLKEKYE SLNESKIIIE KEMYIQQDSL RRATEARAAA
EKARKDLQNE LIRLRERYTE AENARLNAES EAERNIIKQA NERQNSLRRD LEAKAKQLDE
VEAERGRLAG RVQELMQAIA DSENFRIRHD QHKERLEREL VTVKGRLTAS ENDNRALLNK
IQQKNLDIAR SNSRAGENQR VRMSQLQNEK GKLEEENKKL ARQLGDAQLS ITSLEKQKEK
LSLSLEDMNH EVAREHKASR NAEKAASAAN IQLAEANRSL ETERQLRTQA QANTRKLQAA
LDQANKEIED SHQQLMVLHK VFDPEIDESP KSWESVQPDL SKKVNMAALL EAAHSNLRVT
EEKYARAESQ LAEMRRRHED EMKELDARYS SSKRALLEEI DQNQVAAARS PTHLRKNSEA
AMKRYSNPTT PNRRFNINDA AQDSGRSDRT VDTVTFQKRM DMAAELEELQ NKLQMTEMQN
RHLQAQIERS TPVRDMWQDD SPSVRRVQLL ERENGRLHEK LDDSAKKVSA LERSIQSGEL
SLHDVQAKSH EELYDLINSQ EHSRRSLLQV HKNAMAELAD AKSQSEKLKR AKATLEVELR
DARSDAQELQ LARDQDEASR NQLLQEFADL QIRLDAETSK ATDLASSLSL YKSRADEYFS
KLEQAEIAVL KASRAEQFAK SQAKEAEDTC ASIMAERKQM DALVEDLQRQ TQSYEEKIED
LSADLDGALQ AKRRLQNELE DYRNQRAMEI EDKEASLEQT RKKYQMEFSS LTNELEIERE
NVLHSREENT RLREELEDLR SKWDNEVLNS STWAKEKARL EMTLQDVSTS RDEAVAAHND
AQAKVVSLLS QVRNLRTSVD DVSAERDMLL KEKKMLEARL TEAGERLEDL VKGESPSMRN
AASMDRELLE LKSKLAQQED VSAAAVGKMR RAEALATEMQ KEVTAERETN AQLFKEKSAL
EKQLKEAQLR CIDLETKGYS SASQDVRFLH TRIKDLETQL EEQESKRNAE QRSVRSVDRT
VKDLQSQIER RDKINAQLTD DITKSRDKVE RLLKTIEELQ QSDSETQLQA RRAERELREE
REKALRLERE LEGWKALRVE RGSVVGRPGM GAFSDMGSRK GSGVFDMPQR KPSNTKGFL
//
