ID A0A0C9MLA3_9FUNG Unreviewed; 1619 AA.
AC A0A0C9MLA3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Myosin 5 {ECO:0000313|EMBL:GAN08274.1};
GN ORFNames=MAM1_0197c07782 {ECO:0000313|EMBL:GAN08274.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN08274.1};
RN [1] {ECO:0000313|EMBL:GAN08274.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN08274.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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; DF836486; GAN08274.1; -; Genomic_DNA.
DR STRING; 91626.A0A0C9MLA3; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000053815; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000053815}.
FT DOMAIN 86..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1247..1556
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 659..681
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1052..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 179..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1619 AA; 185659 MW; 9DA6048EC86C3FB8 CRC64;
MDSLSSGVAQ AVQVYTKGAK AWFEDEDEAW VSASVLSKEE SGTGVKIVFQ DDKDEGREHV
FECTYALLEK QKGANLPPLR NPPRLENTED LTNLSYLNEP SVLNTIRTRY FQRNIYTYSG
IVLIAANPFA SVPLYEPDII QQYSGRRRGE LEPHLFAIAE DAYRCMVREK SNQTVVVSGE
SGAGKTVSAT HIMRYFATAD DQESGKVKDV AQGMTEVEEQ IMATNPIMEA FGNAKTTRNN
NSSRFGKYIE IQFDNRCNIV GAKIRTYLLE RSRLIFQPES ERNYHIFYQL CTGAPINERK
NLELGDWNKF HYLNQSGVGS IPGVDDAAEF ELTQKSLSLV GISVEAQWHI FKLLAALLHI
GNIEIGGRQD ATLTEDQPAL ITATKLLGIK TSEFKKWLVK KQIITRNEKI VKNLSPTQAI
VVRDSVAKYI YASLFDWLVK VVNDSLSCQE EGLVRTFIGV LDIYGFEHFK KNSFEQFCIN
YANEKLQQQF NQHVFKLEQE EYVKEKIDWK FIDFSDNQKC IEVIESKLGI LSLLDEESRM
PSGTDQGFIN KLYSSFADPK YKDYFKKPRF SNSAFTVVHY AHEVEYDAEG FIDKNKDTVP
DELLTLLQNA ESAFLVDMLQ TATAAASAAS QEAKPTPVKK VGMAIAKKPT LGSIFKLSLI
SLMDTISKTN VHYIRCIKPN EAKVAWGFEP NMVLSQLRAC GVLETIRISC AGYPSRWTFE
DFAERFYALV NSQYWDPNLS PDINKLCHVI LDKYIKDADK YQIGLTKIFF RAGQLAYLEK
CRRERWDECT ILLQKNMRRF IVRIGYLRKL DLISRLQRVA RQKMGVRKLE LARQEIAAIK
IQTEWRRYIQ RKRYLKQRAF VIHLQAACRS HLTRKTFAHI REHFAAIKIQ SMVRGWRVRK
EFLAKRQIAI QIQTCIRRRL ARKALLAIKQ DARSANHFKE VSYKLESKVV ELTQSVTQYK
DEKDQLRLKA NALEMQVKDW SEKYEKLGER ARSLEQSADT SELERQLESL QVERNGIQND
YRTSLERIKK QDVEIARLNE ELQRHKDEIT KLKQAHNQQQ LRSPVSPSSA SPFASAGDED
VAELKSQIVA LKAQLSQSLK NHPKRQASIN AYRTLSPQRS GDRRGMSPDY NRGRSPSADP
RNRSPSSLAV RRSSIGDRRT EPNGSSNFNT GGTGAGATKM IYAEPEQMIP KQIGQRGSLD
ADKVGNPEEA INALLQDSEL LEEEIIEGLI QTLKIVPPEL QKLPAREEVV FPVHIIGKVV
TQMWRLGYLV ESERLLFRAM DTIQKDCLSF TGEDTIVPCS YWLSNTHELL SLVYSVEQEL
EREMHYNSIH GRRAVGWHDF EKLVSTMKFE LQCLEDNIYH HWLSELKKKL NKMAIPAVIE
NQSLPGFIAS DSNRFFGKIL SSNNQPAFSM DDLLNYLNRI YRTMKSYYVE PYVIEQVLTE
LLKLIGITTF NDLVMRRNFN SWKRAMQIQY NITRLEEWCK AHDVSEATNQ LEHLMQATKL
LQLKKATLED IKIIYDVCWF LAPTQVQKLI QNYCVADYED PISNEILRAV ASRVSSSDTG
DILLLDNVSI EDSDYDQPEP HNVVASSYIP SYLNLQHVQK LIALVTLNEK HRPQRMDSM
//
