ID A0A0H2RSS5_9AGAM Unreviewed; 1990 AA.
AC A0A0H2RSS5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Microfilament motor {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCHPADRAFT_996148 {ECO:0000313|EMBL:KLO15040.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO15040.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO15040.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO15040.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Type-I myosin implicated in the organization of the actin
CC cytoskeleton. Required for proper actin cytoskeleton polarization. At
CC the cell cortex, assembles in patch-like structures together with
CC proteins from the actin-polymerizing machinery and promotes actin
CC assembly. Functions as actin nucleation-promoting factor (NPF) for the
CC Arp2/3 complex. {ECO:0000256|ARBA:ARBA00025586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KQ085935; KLO15040.1; -; Genomic_DNA.
DR STRING; 27342.A0A0H2RSS5; -.
DR InParanoid; A0A0H2RSS5; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000053477; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
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:0051179; P:localization; IEA:UniProt.
DR CDD; cd01378; MYSc_Myo1; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
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 InterPro; IPR024660; UCS_central_dom.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF837; MYOSIN-3-RELATED; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF11701; UNC45-central; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000053477};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 741..1420
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1478..1667
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1761..1819
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1268..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1315
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1649..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1763
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1820..1844
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1896..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1913..1945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 834..841
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1990 AA; 216294 MW; 7CF5BAB77E805124 CRC64;
MGSDETVDAI LRKVTSKPAK ELSQEEIDTL ITLFTPSNPS SVHSKAYLAL SALRESSSSN
GSTDDSSSGS FLQSFLPALD RRLADVEESA LVEALSFTAA MFTVDRNAAS TLFTREGFED
SMMDALDLFE SSSVIAQLVA QVLSLACGHK SCLTALSPRC VPWLESAFKG KSDEKLKGMA
ALALLKISRA PQDASGLEDI PSASGMNVDN RRENDLYFAM RTTVIEGSVD LKGLSDAIEG
LAYFSTIPVF KDKLSKDSQI LKKLISFHSQ FRSKSSLVDL DIPGTVPYGL CSIIANLCAY
RPKLSDEEAQ IVKLKKMAQP KGQSDSASIS QETDEKLNDD DHVRERCRRL VNLGAVDLLV
SVTKVTDSPS ILMTVGQALL SVVENKDNRG RILQSGGAKA LMTIIRASHT KPSSENSRTE
AEYTDLTSIQ ALAKLAITSS PMQVFGPSEA ASFDAISPLS SLLLHPSSKL LQRFESIMAL
TNLASTSPEL ASRVAEAKGL LAKVEFMLLD DNVLVRRAAT ELICNLVSGS ELVFNHFSGE
GDGDTKNSVN QSKSRLHILV ALSDVEDEPT RLAASGALAV LSGSPIACQF LVILEFENHR
VFPVLRQLID PDGDSDQPAQ QAAGLVHRGV VCTRNIFVNS SDESLRRKIG EAAEKQQLVP
ALTKILKGAN SGTWTGAILQ PAAEALKWLM DAGVKIISPR HGVMAISKKA GKKVATTAKK
GGGGTKVAKA DWKEGFKKKQ VGVSDMTLLT KITNESVNEN LEKRWKGGDI YTYIGGVLIS
VNPFKDLGIY TDNVLQSYKG KNRLEVPPHV YSIAETAYYN MNAYHENQCV IISGESGAGK
TEAAKRIMQY IAAVSGGQDS SIQQIKDMVL ATNPLLESFG CAKTLRNNNS SRHGKYLEIM
FNDKGEPIGA QITNYLLEKG RVVGQIQNER DFHIFYQFTK AATDEQREAF GIQGPESYAY
TSASKCLDVS DIDDTKDYGE TIRAMQVIGL SDQEQSEIFR MLAIILWLGN VQFEEKDDGN
SQIADSSVTE FIAYLMETDH AMLEKVLTSK VVETQRGGRR GSVYDVPLNP AQASSGRDAL
SKAIYNNLFE WIVSRINVSM KPRGATAQLI GILDIFGFEI FEDNSFEQLC INYVNEKLQQ
IFIELTLKTE QEEYVREQIK WTPIQYFNNK VVCDLIEEKR PPGIFAALND ACATAHADPT
AADNSFVQRL SALSSNAHFD NRGSQFLVKH YAGDVMYNIS GMTDKNKDAL VKDLLDLIGS
SGNQFLQKLF PDRPDPNSKK RPPTAGDRIK QSAGALVENL MRAQPSYIRT IKPNQNRSST
EFDVKAVLHQ IKYLGLQENI RVRRAGFAYR NTFEKIVERF YLLSPATSYA GDYTWQGDSK
SGCERILLDT GIAKEEWQMG VTKAFIKSPE TLFALETMRD RYWHNMAGRI QRAWRNYIRY
RNECAKRIQR FWKNNKESLE YAKVRDYGHQ ILAGRKERRR FSLLSYRRFM GDYLDVDGDS
ALGQELRQVC GIGSEKVSFS SRIQILVSKL GRSSKPMPRF LVLTNKAAHI IVVNAKDGRN
VMMLERKINL VTIKSISMTN LRDDWVALNC GATEEGDPVF SCVFKTELAT HLLQLTSASI
SVLIGPTITY TKKKEKQAQI TAVKDETIPR NDVYKSHQIH VPSGEPPSSL SRPAAKRKPG
VVRPITSGKL LRKGGPSDSK PKAVSKLRPA VQALPGGKPA TAPAMVASTV SAPVASSSGV
PRAPPPPPSR NVAPPPPPPE PDVEMYRAKF AFEGQEGEMS LKKDDEVELV EKDDNGWWMV
KKGGVEGWAP SNYLELVPPK PKAAPAPPPP PPAGRRPPAP PIGASSTTPG AGKPTPSAAA
LKSITANASA KPVSVFPGIP AANGSAAPWK KNPAANGGSG DSSPAGSRPG SSLASKPPPP
AVGSKPKPPP VGAKPGAPKI PGKPAVPVAK PQSGAPNMPA RPGGGVKPSG GAVGQLDLAA
VLAKRAARSD
//
