ID A0A0M8P6Y9_9EURO Unreviewed; 2400 AA.
AC A0A0M8P6Y9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ACN38_g7460 {ECO:0000313|EMBL:KOS41670.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS41670.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS41670.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS41670.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-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}.
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:KOS41670.1}.
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DR EMBL; LHQQ01000125; KOS41670.1; -; Genomic_DNA.
DR STRING; 229535.A0A0M8P6Y9; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000037696; 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; -; 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; 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; 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:UP000037696}.
FT DOMAIN 110..160
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 164..859
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..760
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1172..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1448..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2258..2281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2369..2400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 937..971
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1609..1643
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1718..1786
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1949..2040
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2400 AA; 275568 MW; 7E97539EA3A42874 CRC64;
MLPSQLNGSP NRASLFARPS SSQGTHLPQA RPKSAIITPS HGLESARGHL RNTSVSQLSP
TLSLSGNRER SNSAKNSPSS GTFAPSFIKS EELRRGADQI RGLEGENDFS GNKYVWLRDP
QKAFVRGLVL EESEGGRLLV QTDDGDQREL DADQVDKVNP AKFDKADDMA ELTHLNEASV
VHNLHTRYQS DLIYTYSGLF LVTINPYCPL PIYTNEYIKM YKGRGREETR PHIFAMADEA
FRNLVEEGQN QSILVTGESG AGKTENTKKV IQYLAAVATS DTPYGRSGAK QLTGLSQQIL
RANPILEAFG NAQTVRNHNS SRFGKFIRIE FSRSGQISGA WIDWYLLEKS RVVKPNANER
NYHVFYQLLQ GADRKTREKL LLADLQIEDF AYMRDGNDSI VGVSDQDEWN SLIEAFHVMD
FGEEDQLCIL RTLAAVLHLG NVSVAKASVR ADQATLAPEG YSSMEKACYL LGIEPEAFVK
GLLHPRVKAG REWVEKVQTP DQVRMALDAL SKGIYERGFG NLVARINGQL GRSMASDDNY
FIGVLDLAGF EIFDNNSFEQ LCINYTNEKL QQFFNHHMFV LEQEEYAREQ IEWQFIDFGK
DLQPTIDLIE LTNPIGIFSC LDEDCVMPKA TDKSFTEKLH GLWDRKTPKY RASRLNQGFI
LTHYAAEVEY NTSDWLEKNK DPLNDNITRL LAASKAPHVA HLFSDCADSE EDGAGNHPRS
RVKKGLFRTA AQRHKEQLSS LMAQLHSTHP HFVRCILPNH KKRPKMLHAP LVLDQLRCNG
VLEGIRIART GFPNRLPFTE FRQRYEVLCQ NMPKGYLEGQ SVTRTMLEKL GMDRGWYRVG
RTKVFFRAGV LADLEGKRDQ LIRTIMSKFQ SVARGFVQRR ISNKRLYRAE ATRIIQQNFH
AYLDLKGSPW WRMFSRMKPL LGDTRNAKEV KMRDDKIQQL EAKMKQDVTD RNKLDEERRR
TEIEIQKIQH TLESERALAL DKEEIFKRLQ DREVELAEKL AGAIADQEGL EEQLDELVDA
KRKIDDQLQL RITQLEQAGL IIQQLESEKN SLQSQVEELD SKLSETEIQF SGKNDQIQEL
GQEIKMLQSH LSLKDRKLQD LEAKLLKTDQ DLDIKLANTS KELDTSKKQI RDLSEENKSI
RDQISELSST STGYEDLIRR KESEIAVLRN DVQKHDEEKR SVESEKTSLA ARHGTMQSRL
REVQAERDAM RSEQTQLQRE AADLKNLLEN KRSEDAEAGE SRKLLEQQVN DLKSQLFQAQ
ADLSRERQSR DDVQMLSEHN LAQLTQKYET LNDSKITIEK EMYIQQDSLR RATEARVAAE
TTRKELQGEL IKLRERFTDA ETARMNAEAE IERKIMTQAE ERMTSSRKDL EEKARQLEEV
ETERSHLSSR IQELMHSISE SDNFRLRHDQ HKERLERELV TLRGRLTASE NDNKSLLTKI
QQKNLDIARS NSKASDSNRL RLTNLQKEKA RLDEETKKLS RQVEDSQVMI TSLEKQKEKL
SLSLEDLNHE VNREHKTSRN AEKAASTANL QLAEANRKLE TERQLRNQAQ ANTRQTQGTL
DRANKEIEDL HHQLILLHKV FEPEATEPAQ SWEAVQPHLS KQVDLAQVLE TVQNKLGVTE
EKYARAETQL AEMRRRHADE MKELDTKYSS SKRALLEEID QNEVANNRTP AHLRKNSENA
AKKYSNPTTP NRRYNAFEAP NDSARSDRTV DTQGYQRRMD TAAELEELQN KLQMTEMQNK
HLQSQLGRST PTADIWQDDS PSIRRMQLLE RENGRLHDQL DDSSKKVSSL ERSIRSGELS
LRDVQAKSHE ELYDLINSQE QSRRSLLKVH NETMSEFGDA KAHFEKLKRA RATLEVELRD
ARSETQELQV GREQDGVSRN QLLQEFSDLQ IRLDAETSRS ADLESSLMLY KSRSDEYFNK
LEQAEIAVMK ASRAEQFAKS QGQEAEETCA QIMSERKEMD ALVEDLQRQA QSLEARMEDQ
AAELQGALQA KQRLQNELED YRNQRAIDLE DKETSMEQTR QKYQREFSTL NNELEMERER
VINGRGETSR LREELEDLRS KWDNEVLNSS TWAKEKARMD VVLQDVTNSR DEAVNAHNEA
QSKVVSLLSQ VRTLRTSVED VHAERDLLLK DKKMLEGRLA EAGERLEDLA KGESPSMRNA
ASMDRELLEL KSRIAQQEDV SAAAVGKMRR ADALATEMQK EVTAEREANA QLFKDKAAVE
KQLKEAQLRC VDLETKSYSS GSQDVRFLHK RIKELETHLE DQESKHSSEQ RSLRNVDRTV
KDLQSQIDRR DKMNTQLNDD VNRARDKIER LLRNIEELQH NDSDAQLLAR RAERDLREER
EKALRLEREL EGWKALRVER GSTIGRGPVA FSDAGSRRGS AVYGSNDIPQ RHPSNTKGFL
//
