ID A0A421J4M4_9ASCO Unreviewed; 2831 AA.
AC A0A421J4M4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Myosin-1 {ECO:0000313|EMBL:RLV83288.1};
GN ORFNames=JA9_002834 {ECO:0000313|EMBL:RLV83288.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV83288.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV83288.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV83288.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC {ECO:0000256|ARBA:ARBA00010289}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC 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:RLV83288.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NSDU01000024; RLV83288.1; -; Genomic_DNA.
DR STRING; 2028340.A0A421J4M4; -.
DR Proteomes; UP000286412; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
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 GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0051641; P:cellular localization; IEA:UniProt.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11858; SH3_Myosin-I_fungi; 1.
DR Gene3D; 1.10.10.820; -; 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 Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035535; Fungal_myosin-I_SH3.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR019035; Mediator_Med12.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF09497; Med12; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01281; Med12; 1.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000286412};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 35..727
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 785..974
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1142..1202
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 600..622
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 967..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2694..2713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1012..1061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1222
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2831 AA; 319379 MW; F4D8DF005F2670CF CRC64;
MAIVKRGART KARQEAPAKS GIKKAEFDLH KKKEVGVSDL TLLSKISDDS INDNLHKRFM
NNTIYTYIGH VLISVNPFQD LGIYTKEYLN MYKGKNRLEV PPHVFAIAES MYYNLKSYGE
SQCVIISGES GAGKTEAAKQ IMQYIANVSV DDKASTTSEI TQIKDMVLAT NPLLESFGCA
KTLRNNNSSR HGKYLEIFFN PSNYQPVAAH ITNYLLEKQR VVSQITNERN FHIFYQLTKS
CPPEYKQSFG LQGPETYVYT SAAKCIDVDG INDGKDFADT LQAMHTIGLS KAEQDNIFRS
LASILWIGNI SFVENEEGNA AIRDDTVTTF VAYLLEVDAN ILKKSILERV IETSHGMRRG
STYHVPLNIV QATASRDALA KGIYNNLFDW IVERVNISLR GRAEAMEKKT IGILDIYGFE
IFDHNSFEQI CINYVNEKLQ QIFIQLTLKA EQDEYVQEQI KWTPIDYFNN KVVCDLIEAT
RPQPGLFAAL NDSIKTAHAD SDAADQVFAQ RLSMVGANNR HFEDRKGKFI IKHYAGDVVY
DVAGMTDKNK DAMLRDLLEM LSTSQNTFVN SVLFPPELLA VLTDKKKRPE TASDKIKKSA
NLLVDTLSQC QPSYIRTIKP NQTKRPKEYD NAQVLHQVKY LGLKENVRIR RAGFAYRTTF
DKFVQRFYLL SPKTGYAGDY IWNGDDISAV REILKSCHIP DTEFQMGTSK VFIKTPETLF
AMEDMRDKYW HNMAARIQRA WRRYIKRKDD AARLIQNAWK VKKHGNQFEQ LRDYGNGLLQ
GRKERRRMSM LGSRAFMGDY LGCNYNSGFG RFVLNQVGLN EHVVFSAKGE ILLSKFGRSS
KRLPRIFVLG RSSLYIIAEN LVERRLQLSK EFVIPINSIN YVGLSTFQDN WLAVSLHSPT
PTTPDVLINL DFKTELVTHL KKLNPGLTIK IGPTIDYQKK PGKYHTVKFV RSDVSTIPIH
GDVYKSGTVS VRPGLPPDSQ NPKRPRATSS KVDYSKYYNR GGRLAPARTV APAQPSYQQR
TNVAPPAQPS YQQRTPAAPP SHATQQQASY QPSTPAVPAH QQPNNVRKAP PPAPSLNNNH
QEAVTAATAA MNHVHVQQPA TVVQNHNSNP TAPSRPAKKA APAPPAKKSA PPPPPSLSAA
KPKWPTFKAN YDYDGSVSGS MALSANDVVY ITQNNGQWSL AKSLDESKEG WVPTAYISEC
PPPSNLGASK SPPPPPPPSA NTRAVPEQGG NAGAPASTQQ EGGLSNGLAG ALLAKKNEET
NLAGSIADAL KKRSATRDSD DEEEDDDDDC DKDELIAMKF SMDKPNLDIY PLSVGVEDKK
DSNTKHSYPD FKPWKESTPS DPGSFNDAEA SKENNASYLN KGYYEPPAVP NEYSSARSLV
QASLFSSSDS TNEALEDLSR IMAGAFRSRD ESINKIKHES HQFKIPPRVT LTASKKEAWL
RDLADPEVPL SKISGKLPHG IRNKILVESI CNKYVPLPRA IWFTKCILFS EIQALKKKYS
TKFSGVKSTS TIVNYELHWL HEWTQQIADY VQKFAREMNG ISSTERKSAY MSKLLHLLRY
LQSLYLECLV DRRLFLSCII NILKEGLPLE AKQVSELISM SWEDSDKPLD LLIGIEKQYG
QRLVALMLIK SFWRVILPLD YLCKELSEAL LLNYYFIRRA STFNPKQPPQ KQNSNALPSK
LKSKILDLVA ESIKYLFKHN SNTFILPNYW VLTSEELSSI LLNDKNTKME AAQVQLIKDQ
LKIIKYRNES LILNSKHIQA VSSEQQHDFA TKPRYSSQAT KDESVSTEAD YWFINRSQGD
LLKVVDSLDR YRLDDGLAIL LRPQQENGCW RIYLKLLIHW CITDYRDVAI SSQGILIACN
FIKGKVLQKP IDSQRKAEFE SEILEIIYQV VSDPTVKIKS YNLYVLINEL YQLKIITISS
YIRRLIASGV FYVSPEEGSQ KLILNNEIST HLSILKNLPV TNNKQCDSIL RKWVSDDFNF
KTKFDTGKII LQENIIENLL ESKERAFFQS SGIEYFQNLE VGLKFLLINW LTTQLKNTIM
SSTKLIHVYP STISILYDLF CACDNLTVFF KGIIKLILRN DGGIIIFYLD SLYLIAKLVV
RHFKLIKYIN TSPSEVPTVL ELMKLILLHY KDLQARDFDY TKFRSIWIFF GSMISSSELQ
FSSVGDHKSI QKSKNKGKVA LSSAEILTEW SNPWQNLSPS TEDLKSVIDD IIAEPVPLLS
EEENAESCKT LKLTLASNTV LGNFSELLSK FEETLGNLQY DEEVSLVRLI VHHDRLLKAS
KESTDVSTLI KSHINEMSDS TRIILLLKKL LCYELIDYSL VVQLLTCENH GFSVESNDDT
ITQILFGRNV RTGLFPNQQV MLQILRETYL AKNSVSVLPI ILKSFKLTNS HVPIEQNQKE
NMLSVLRTCC LYHIRDVIDV LGKHLTNSEI IRVCNELAGI SPDSSISLIN DIPALGKVAN
EFSLPICQIL LRTITSNELE YLGTQEASRQ VEIITESLLY SFHSDFPKDN SFFGEITNYC
GPEYKYMFLR VLETKFLTCT KFDGGRLSLC TEQGENLLPI LKDFFKKFSV SYTKDAYVTG
DLFTELNKFL QELLPIAKSS IIDENTTVDL QNAISVYLRI IIIHKVPLIT TILTKDGERF
TFVRNLIELL KSNFLSSNND GLSILLYDLL LLMKSSLTSA LTLQANGMIE NSPAAIQDDF
NGHPETDAPP TEQHSKQMFV NDAISSISRI FNLPEPSSSN PFEAYKKEEV QACSIMLDEE
ELESGSDYAV FNDSGLVAVP VDKKRSSSEK PKPFKIKSFE IIEGTTGGED LNDSCINLSM
FGAYVLRENP L
//
