ID A0A0D2BEP9_9EURO Unreviewed; 1302 AA.
AC A0A0D2BEP9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV08_04256 {ECO:0000313|EMBL:KIW17065.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW17065.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW17065.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW17065.1,
RC ECO:0000313|Proteomes:UP000053328};
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 Exophiala spinifera CBS89968.";
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; KN847494; KIW17065.1; -; Genomic_DNA.
DR RefSeq; XP_016237281.1; XM_016378604.1.
DR STRING; 91928.A0A0D2BEP9; -.
DR GeneID; 27331339; -.
DR VEuPathDB; FungiDB:PV08_04256; -.
DR HOGENOM; CLU_000192_8_0_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000053328; 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: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};
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:UP000053328}.
FT DOMAIN 88..138
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 142..839
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..740
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1085..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 235..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1302 AA; 149510 MW; A83152E7A75C4D73 CRC64;
MSLATPMSPA SMSRSMHFAS PTPASRHERQ HSYSPTASFT SIPHHVRTQS LQRQSSTSST
FAPKFIKSDE MRKSEDRISA IEGENDFSGK RYVWVKDPEK AFVRGWITEE LSGNKVLVQF
ENGSQIETDI DEVDKVNPAK FDKADDMAEL THLNEASVIH NLYTRYQADL IYTYSGLFLV
TVNPYCPLPI YGNDYVRMYK GQTREDTRPH IFAVSDAAFR RLVEEGENQS ILVTGESGAG
KTENTKKVIQ YLAAVATSDL DTPLTGRTPG KQLSNLSQQI LRANPILESF GNAQTVRNNN
SSRFGKFIRI QFTRSGQIAG AFIDWYLLEK SRVVKVSQQE RSYHIFYQLL AGADQRTRDI
LLLSGMDVAD FAYLRAGNEI ISGVSDRDEW NTLIEAFHIM NFSEKEQMEV FKTIAAILHL
GNVAVRQESR AADQATLTPE AKASVDKACR LLGVQTEPFI KGLLHPKVKA GREWVEKVQT
PEQVRLALDA LAKGIFERGF GDLVNKINAQ LDRGGVSSDD SHFIGVLDIA GFEIFENNSF
EQLCINYTNE KLQQFFNHYM FVLEQEEYAR EQIEWQFIDF GKDLQPTIDL IELPNPIGIF
SCLDEDSVMP KATDKSFTDK LHSLWEKKTP KYAAAKTRQG FILTHYAAEV EYSTEGWLEK
NKDPLNDNLT RLLACSKDSH IANLFGDCVD EIDEPYSPRS RVKKGLFRTV AQRHKEQLSS
LMRQLHSTQP HFVRCILPNH KKKPKQFNAP LVLDQLRCNG VLEGIRIART GFPNRLTFAE
FRSRYEVLCE NMPKGYLGGQ EAAKIMLDRL KMDGQNYRVG LTKVFFRAGV LADLEEQRDS
LIRDIMSRFQ SVARGFMQRR VAFKQLYRAE ATRVIQRNLN VYLDLQANPW WRLFVRMKPL
LGATRTASEV KRRDEKIEML QSKMQKEAAE RHRIEDERRR AEIDAQRVRQ TLEAERALAL
DKEEIFKRLQ FRESELTEKL SEAITEQETL EDQLDAALDS KKKTEEELNT RREQVLQAGQ
IITRLEAEKK EMQRQIERLE EELENVEKHH SSTDNRLENI SQELRTLKSQ LGVKDRKIAE
LEASLHQAER ERDNKSTSLE QEMRSLRSQI SQRERTTEEL EKKLQRSESL RAEETKRKAD
DYESQIRALK SELSGKDRKV HDLEGALSKI DKDAESKLAH ANDELGNTKK LLRELQGQND
ELRKQITSMT SASSKHEETL RRKEGELSAL MADIEAHEAE KAALRREIDG LSGRHGDMQA
KHRELQDDIE VMRTQRVKME KEAIEVRKAL EKVMPFFSQN FS
//
