ID A0A0M9VNM8_9BASI Unreviewed; 1515 AA.
AC A0A0M9VNM8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Myosin 5 {ECO:0000313|EMBL:KOS13512.1};
GN ORFNames=Malapachy_0102 {ECO:0000313|EMBL:KOS13512.1};
OS Malassezia pachydermatis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=77020 {ECO:0000313|EMBL:KOS13512.1, ECO:0000313|Proteomes:UP000037751};
RN [1] {ECO:0000313|EMBL:KOS13512.1, ECO:0000313|Proteomes:UP000037751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 1879 {ECO:0000313|EMBL:KOS13512.1,
RC ECO:0000313|Proteomes:UP000037751};
RA Triana S., Ohm R., Gonzalez A., DeCock H., Restrepo S., Celis A.;
RT "Draft Genome Sequence of Malassezia furfur CBS1878 and Malassezia
RT pachydermatis CBS1879.";
RL Submitted (JUL-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:KOS13512.1}.
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DR EMBL; LGAV01000006; KOS13512.1; -; Genomic_DNA.
DR RefSeq; XP_017991144.1; XM_018134635.1.
DR STRING; 77020.A0A0M9VNM8; -.
DR GeneID; 28726510; -.
DR VEuPathDB; FungiDB:Malapachy_0102; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000037751; 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; 1.
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:UP000037751}.
FT DOMAIN 85..785
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1184..1464
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 662..684
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1071..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1515 AA; 171317 MW; 8632E4272E2B516F CRC64;
MAPHSQPLDA YEAGTKAWFP HDEQGWVSAT LSKVPDVKDD GHVTMVFVLD DTGTEHVVET
TLDKIQAPGG VDKELPPLRN PPLLEASDDL TALSHLNEGS ILHTILNRYQ QRIIYTYSGI
VLIAVNPFFD LNLYSPEIIQ AYAGRRRGEL EPHLFAVAED AYRCMIRDRK NQTIVVSGES
GAGKTMSAKY IMRYFATVED PDTVSLRRTN PSGMSETETA ILATNPIMEA FGNAKTTRND
NSSRFGKYLE IIFDDRHEIA GAKMRTYLLE RSRLVYQPEV ERNYHIFYQL CAGAPEELKA
KLFLEHASQF HYLSQGGPDH HEIAGVDDAA EFRATVNAFL TIGVSEERQE QIFTLLAALL
HLGNVAVTAT RNDAQISPDD TSLQRAAGFL GVDAGELRKW TLKRQIQLRG EKIVSNLNQV
QATAVRDAVA KYVYTCLFDW LVAEMNKTLE PSDAKAAATM IGVLDIYGFE CFKVNSYEQF
CINYANERLQ HEFNTHVFKL EQEEYVAEEI PWQFISFSDN QPCIDMIESK FGLLSLLDEE
SRLPSGHDSS FLQKVYGQLQ PKPEFKDFLA KPRFGAQSAF TVRHYALDVT YDVDGFMEKN
KDTLPEEHLS LLSTTTSPFL QAVLSARAVT DAAQPATSSR KVSGPSNLAK KPTLGTQFKA
SLGALMETIN STEVHYIRCI KPNDMKMAWE VQPQNVLSQL RACGVLETIR ISCAGYPSRW
TFADFVERYY LLVPSKLWDM TSLEKVRDLA HKILAATVEK DKYHFGKTKV FFRAGVLASF
EQMRRHVLNN RTCTIQTAWR RYAMQSRYRA LQKGVLAIQS MVRRRQAEAA YEVARQMRAI
LLLQTAARGA LQRQRLRQAS QAAVRIQAAV RGHQARAAFL HARTNGHATR LQTAVRGWLA
RRAALQRTRH VTLLQSLYRR KLARKALVER RTEAKSASHF QEVSYKLENK VVDLTQSLQD
RTRENKDLRA ALAELEAQLS SWQNRHEALD ARARGLQEEV QKPSVPAEEH EALLAEHEAL
SQELVQARGQ IRDLEVEIGT LKSQLRSVEA PDSVVQSLRN EIAMLREQLG RANAQNERNG
TTVPLGPRQR SASGDYVEEP LEEVVDEDLV RAAPSEEIIE LLEDEVQLDE DVLHGLIEYL
KIPAPSLQNP PGPKEVLFPA HLISLVTNEM WKYGLVRASE RFLANVMQTI QQHVMSFHGD
DAIVPGIFWL SNVHEILSFV CIAESDMLQG IGPGVDGSAR EFEWGDYERL VTIVKHDLDS
LEYNIYHTWM QEAKKRLNKM VVPALVESQS LPGFVTNDSS SRLLNRLLAG TNAPSYTMDD
ILALLNKIWK CLKSYYVEPS VTQQVITDLL KMIGVTSFND LLMRRNFCSW KRAMQIQYNI
TRLEEWCKSH DMPEGSLQLE HLLQATKLLQ LKKATMSDID IIYDVCWMLT PTQIQKLISH
YHVADYENPI SPDILKAVAS RVVPNDRNDY LLLPPEVDEA GPYELPVPRE VTGIETYCPA
YLNVPLLRNL ASKVA
//
