ID A0A0D2CCR6_9EURO Unreviewed; 1332 AA.
AC A0A0D2CCR6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_00378 {ECO:0000313|EMBL:KIW47712.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW47712.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW47712.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW47712.1,
RC ECO:0000313|Proteomes:UP000053342};
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 oligosperma CBS72588.";
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; KN847332; KIW47712.1; -; Genomic_DNA.
DR RefSeq; XP_016267928.1; XM_016400875.1.
DR STRING; 215243.A0A0D2CCR6; -.
DR GeneID; 27352452; -.
DR VEuPathDB; FungiDB:PV06_00378; -.
DR HOGENOM; CLU_000192_7_2_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000053342; 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; 1.20.58.530; -; 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:UP000053342}.
FT DOMAIN 118..168
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 172..869
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..770
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1114..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1332 AA; 153002 MW; 2E5878F8D38AB7E3 CRC64;
MLLHDRSPDT SPFNGHSQRH HSFSRSYNSD MSLATPMSPA SMSRSMHFAS PTPASRHERQ
QSYSPSASFT SIPHHVRTQS LQRQSSTSST FAPKFIKSDE MRKSEDRISA IEGENDFSGK
RYVWVKDPEK AFVRGWITEE LPGKKVLVQF ENGSQIETEI DEVDKVNPAK FDKADDMAEL
THLNEASVIH NLYTRYQADL IYTYSGLFLV TINPYCPLPI YGNDYVRMYK GQTREDTRPH
IFAVSDAAFR RLVEEGENQS ILVTGESGAG KTENTKKVIQ YLAAVATSDL DTPLTGRTPG
KQLSNLSQQI LRANPILESF GNAQTVRNNN SSRFGKFIRI QFTRSGQIAG AFIDWYLLEK
SRVVKVSQLE RSYHIFYQLL AGADQRIRDA LLLSGMDVEN FAYIRAGNET ISGVSDRDEW
NTLIEAFHIM NFSEKEQMAI FKTIAAILHL GNVAVRQESR AADQATLTPE AKASVDKACR
LLGVQTEPFI KGLLHPKVKA GREWVEKVQT PEQVRLALDA LAKGIYERGF GDLVNKINGQ
LDRGGVSSDD SHFIGVLDIA GFEIFENNSF EQLCINYTNE KLQQFFNHYM FVLEQEEYAR
EQIEWQFIDF GKDLQPTIDL IELPNPIGIF SCLDEDSVMP KATDKSFTDK LHSLWEKKTP
KYAAAKTRQG FILTHYAAEV EYSTEGWLEK NKDPLNDNLT RLLACSKDSH IANLFGDCVD
EVDEPYSPRS RVKKGLFRTV AQRHKEQLSS LMRQLHSTQP HFVRCILPNH KKKPKQFNAP
LVLDQLRCNG VLEGIRIART GFPNRLTFAE FRSRYEVLCE NMPKGYLGGQ EAAKIMLDRL
KMDGQNYRVG LTKVFFRAGV LADLEEQRDS LIRDIMSRFQ SVARGFMQRR VAFKQLYRAE
ATRVIQRNLN VYLDLQANPW WRLFVRMKPL LGATRTASEV KRRDEKIEML QTKMQQEAAE
RHRVEDERRR AEIDVQRVRQ TLEAERALAL DKEEIFKRLQ YRESELTEKL SEAITEQETL
EDQLDAALDS KKKTEEELNT RREQVLQAGQ IITRLEAEKK DMQRQIERLE EEIENVEKHH
SSTDNRLENI SQELRTLKSQ LGVKDRKIAE LESSLHQAER EKDNKSTSLE QEVRSLRSQI
SQRERTTEEL EKKLQRSESL RAEETKHKTE DYESQIRALK SELSGKERKV HDLEGTLSKI
DKDAETKLAH ANDELGNAKK LLRELQGQNE ELRNQITSMT SASSKHEEAL RRKEGELSAL
MADIEAHEEE KAILRREIDG LSGQHGDMQA KHRGLQDDIE AMRTQRIKME KEAIEVRKAL
ERVMPFFSQN FS
//
