ID A0A2N1JBB1_9BASI Unreviewed; 1519 AA.
AC A0A2N1JBB1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Myo2p {ECO:0000313|EMBL:PKI83833.1};
GN Name=MYO2 {ECO:0000313|EMBL:PKI83833.1};
GN ORFNames=MVES_002226 {ECO:0000313|EMBL:PKI83833.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI83833.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI83833.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI83833.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) 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; KZ454990; PKI83833.1; -; Genomic_DNA.
DR STRING; 2020962.A0A2N1JBB1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000232875; 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; 1.20.5.4820; -; 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:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 1.
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 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|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000232875}.
FT DOMAIN 77..776
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1188..1468
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 653..675
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 949..1072
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1519 AA; 171347 MW; 1C0CFFA1EC85A4E2 CRC64;
MAGTISRQLD AYVEGTKAWF PDPNAGWISA TQTSAPSIGE DGSVTITFIV DDTGEERIVT
TSVPNLLKSN GTAEELPPLR NPPLLEAADD LTGLSHLNEG SGMSCRMIYT YSGIVLIAVN
PFFSLNLYSP EIIQAYAGKR KGELEPHLFA VAEDAYRCMM RDQKNQTIVV SGESGAGKTM
SAKYIMRYFA TVEDPDKPRV RRSESGTDGM SATEEAILAT NPIMEAFGNA KTTRNDNSSR
FGKYLEIIFD KNYEIAGAKM RTYLLERSRL VYQPEIERNY HIFYQLCAGA PQELKDYLAL
APASEYHYLR QGGAVNLAIA GVDDAEEFRS TERALATLGL GPAVQMHIFS LLAALLHLGN
IVVSATRSDA AISSEDPSLL RAADTLGVDP ALLRQWMLKR QMQLRGEKIM SNLSQTQATA
VRDSVAKYVY TSLFDWLVVQ MNKSLAPKEA LEHASMIGVL DIYGFECFKQ NSYEQFCINY
ANERLQHEFN RHVFKLEQEE YIAEQIPWEF IDFSDNQPCI DMIESKFGIL SLLDEESRLP
NGSDTAFLEK VYAQIPAKEE LQPFLSKPRF GAQSSFSVRH YALDVTYEVD GFMEKNKDTV
PDELLALLAG TSNEFLGGVL AAQGSAPEAA PVPGRKGPPA KKPTLGSQFK GSLGSLMDTI
NSTEVHYIRC IKPNDVKVAW EVEPQNILGQ LRACGVLETI RISCAGYPSR WDFTDFVERY
YLLAPSKHWN MSSMEGVMQL SKHILSATLD EGMYHVGLNK IFFRAGVLAS FEQMRKNVLY
ARTRQIQTSW RKFHAQSRFQ SLQRASLAIQ VATRRHQAML RFQTERVRRI ALRLQTQVRA
FLTRRRTNAL RSTIVLLQTA WRAKKARQVA IATREAQDAT GLQRLIRGAL ERRRVAQHCK
KVVLVQSLYR RRCAKRAFAQ RKTEAKSATH FQEVSYRLEN KVVDLTQSLQ TRTKENRELR
AQLVDLQSQL ATWQNRHEEL GARARGLQEE VERPSVPTPK FEQIRTEGAQ LTAQLDQAQE
RIIQLEHDIG TLQSQLNARM QEEQELAPDS VVQSLRSEIA VLREQLGRAN ALNAKNGGTV
PLASAAARDG RRLSRRSADM SEGFEEEAEP DIYEPHVNPE EIIELLENEV QLDEDVLQGL
VRYLKIPAPS LQNPPSMKEV LFPAHLISLV TNEMWKYGLV RESERFLANV MQTIQQHVMD
FYAEEAVVPG IFWLSNVHEI LSFVCIAESD MLQGVGPGID GSARDFEWGD YERLVTIVKH
DLDSLEYNIY HTFMQQAKKQ LNKMVVPALV ESQSLPGFIT NDSGGRLLNR LLAGNHAPTY
AMDDILGLLN KTWKCLKSYY VEPSVTQQAI TELLKMIGVT SFNDLLMRRN FCSWKRAMQI
QYNITRLEEW CKSHDMPEGS LQLEHLLQAT KLLQLKKATM GDIDIIYDVC WMLTPTQIQK
LISHYHVADY ENPISPEILK AVASRVVPND RNDHLLLPPE VDEAGPYELP VPREVTGIET
YCPAYLNVPL LRNLASKVA
//
