ID V2YM03_MONRO Unreviewed; 1287 AA.
AC V2YM03;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Microfilament motor {ECO:0000313|EMBL:ESK92714.1};
GN ORFNames=Moror_15967 {ECO:0000313|EMBL:ESK92714.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK92714.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK92714.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK92714.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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}.
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:ESK92714.1}.
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DR EMBL; AWSO01000259; ESK92714.1; -; Genomic_DNA.
DR RefSeq; XP_007847971.1; XM_007849780.1.
DR STRING; 1381753.V2YM03; -.
DR KEGG; mrr:Moror_15967; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000017559; 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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
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 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; PF14604; SH3_9; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
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 Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 39..718
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 776..965
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1057..1116
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..613
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 956..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1115..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1147
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1287 AA; 140942 MW; F5CA243EFFD3F0DB CRC64;
MAPSKKAGKK VTPAKKGGST TKGGVAKADW KEGFKKKTVG VSDMTLLTTI SNESINENLQ
KRWTTGEIYT YIGAVLISVN PFRDLGIYTD EVLQRYRGKN RLEVPPHVFS IAESAYYNMN
AYHENQCVII SGESGAGKTE AAKRIMQYIA AVSGGQDSSI QEIKDMVLAT NPLLESFGCA
KTLRNNNSSR HGKYLEIMFN SHGEPVGAKI TNYLLEKGRV VGQVENERNF HVFYQFTKGA
SDEQREMFGL QGPEAYAYTS LSNCLEVQDI DDVHDYGETI KAMQVIGLSE HEQSEIFRML
AIILWLGNVQ FVEDDDGNSA IADAGVPDFV AYLLEVDSAS VQKVLTTRVM ETQRGGRRGS
VIDVLLNPAQ AGAGRDALAK AVYNNLFEWI VSRINIAMKP RTAHAQVIGI LDIFGFEIFE
DNSFEQLCIN YVNEKLQQIF IELTLKTEQE EYVREQITWT PIKYFNNKIV CDLIEERRPP
GIFAALNDAC ATAHADPAAA DNSFVQRTAA LASNPHFEAR GAQFLVKHYA GDVMYNVSGM
TDKNKDSLTK DLLDLVASSG NQFLQTLFPD RPDPNSKKRP PTAGDRIKSS ANTLVDNLMK
AQPSYIRTIK PNQNRSSTEY DTKAILHQIK YLGLQENIRV RRAGFAYRNT FEKMVERFYL
LSPNTSYAGE YTWHGDAKSG CEQILKDTGI AKEEWQMGVT KAFIKNPETL LALETMRDRY
WHNMAARIQR AFRNYMRYKH ECARRIQRFW KNNKEGIAYA QVRDYGHQVL AGRKERRRFS
LLSYRRFMGD YLDVNGKSVF GEELGSACGI GGDEVTFSSK IQLLISKIGR SSKPSPRWLV
VTKKAVHIAV TNHKDGQLVT TLERKIPLVT IKGMSMSNLR DDWVVLHGNV SEEGDPVFSC
YFKTELVANL MTLTQGSINL QIGPTIDYAK KKEKRAQIKF IKDETIRKDD VYKSHTVHVP
SGEPPGSLSR PPAKRKAGVV RPITQGKLLR AGGPSKPTST AKPKPAVRPL PGQSAAAPAA
TASAPVSKPA AIPKPSAGGS TRGPPPPPPP PARPAEPEVE MYKAKYAFQG QEGEMPLQKD
DLVEVIEKEG DGGWWLVKKD GVEGWAPSNY LELVPPKAAP AAPPPPPRKV PPKPTPAATP
VATPAAPKPP VASLTANPSA KPVSVFPGMA PSNGSATPWK RTPTASMPDE SPASSRPSSV
IGNKPAPPVA SKPKPPAPPV GAKPTPPGAK PTPPKAPGKP PVPTAPRPTP AAGGPPKVGG
AKPPPAPAGQ MDLASMLAKR AQRLNDS
//
