ID U5HG67_USTV1 Unreviewed; 1647 AA.
AC U5HG67;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Myosin-2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MVLG_06085 {ECO:0000313|EMBL:KDE03419.1};
OS Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther
OS smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=683840 {ECO:0000313|EMBL:KDE03419.1};
RN [1] {ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1A1 Lamole {ECO:0000313|Proteomes:UP000017200};
RA Cuomo C., Perlin M., Young S.K., Zeng Q., Gargeya S., Alvarado L.,
RA Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Mehta T.,
RA Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Microbotryum violaceum strain p1A1 Lamole.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KDE03419.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE03419.1};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Butler R., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KDE03419.1, ECO:0000313|Proteomes:UP000017200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1A1 Lamole {ECO:0000313|EMBL:KDE03419.1}, and p1A1 Lamole
RC {ECO:0000313|Proteomes:UP000017200};
RX PubMed=26076695; DOI=10.1186/s12864-015-1660-8;
RA Perlin M.H., Amselem J., Fontanillas E., Toh S.S., Chen Z., Goldberg J.,
RA Duplessis S., Henrissat B., Young S., Zeng Q., Aguileta G., Petit E.,
RA Badouin H., Andrews J., Razeeq D., Gabaldon T., Quesneville H., Giraud T.,
RA Hood M.E., Schultz D.J., Cuomo C.A.;
RT "Sex and parasites: genomic and transcriptomic analysis of Microbotryum
RT lychnidis-dioicae, the biotrophic and plant-castrating anther smut
RT fungus.";
RL BMC Genomics 16:461-461(2015).
RN [4] {ECO:0000313|EnsemblFungi:MVLG_06085T0}
RP IDENTIFICATION.
RG EnsemblFungi;
RL Submitted (JUN-2015) to UniProtKB.
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; AEIJ01000680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GL541740; KDE03419.1; -; Genomic_DNA.
DR STRING; 683840.U5HG67; -.
DR EnsemblFungi; MVLG_06085T0; MVLG_06085T0; MVLG_06085.
DR HOGENOM; CLU_000192_9_0_1; -.
DR InParanoid; U5HG67; -.
DR OMA; EIMFDDR; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000017200; 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; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
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 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:UP000017200}.
FT DOMAIN 101..829
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1312..1594
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..731
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1178..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1002..1029
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1054..1113
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1187..1211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1647 AA; 184084 MW; F6F79A490943273A CRC64;
MATPGMAKSA SSTSLSQHRP SSSVIETYVV GTRTWHEDKT SGWIAGQVTA SSLDDSHEHV
QLEFETEAGQ IIKVSTSLSA LSRASASNST LPPLRNPPLL EATEDLTNLS HLNEPGVLHT
ILHRYSLRQI YTYSGIVLVA VNPFSSLSVY APSIVQAYAG RRKGELEPHL FAIAEDAYRC
MAGNNGEAGG NQTIIVSGES GAGKTVSAKY IMRYFATVED PLKPGKRKTS TTSGMSETEE
QILATNPIME AFGNAKTTRN DNSSRFGKYI EILFDGEQTI VGARIRTYLL ERSRLVYQPE
TERNYHIFYQ LLAGAPSSER KNLGLEAASN FAYLNQGGAP SYAIPGVDDA EEFRATQKAL
STVGITIERQ WQIFKLLAAL LHLGNINITS SRTDALLDDE DKSLAFATRL LGIDKAEFKK
WLIKKQIVTR TDKIVSNLNA AQANVVKDSV AKHIYASMFE WLVAVVNESL TNEAVEANVK
SFIGVLDIYG FEHFKKNSFE QFCINYANEK LQQEFNAHVF KLEQEEYIRE QINWTFIDFS
DNQPTIDLIE GKLGILSLLD EESRLPSGSD ANFVQKLYTT VGAKPETASS VFKKPRFGST
AFTIAHYALD VTYEVEGFLE KNRDTVPDEH LVLLSTTTNS FLKEVLDRAD AAKIAAQAQD
KPVERPGSAL GDVANKRASV AGAPGGGAMK RVGATARKPT LGSIFKLSLI SLMDTIDSTN
AHYIRCIKPN EAKRAWEFEP QMVLGQLRAC GVLETIRISC AGYPTRWTFA EFAERYYMLV
NSSVWGTESR EMCKRILEAS IKEEDKYQVG LTKIFFRAGL LARFEQLRSQ RLNALAILMQ
KNVRRHQALK SYLNLRRAVI GTQARWRATL ARRAAEKERR DRAAVIIQSK MRGHLQRLRF
VRARQAIVAV QAIARATLVR RAFKQERIEA AAVRLQSLVR GMFVRRRTRQ DRRRIVLLQS
CVRRRAAQKE LQGLKTEARS VVHFKEVSYK LENKVVELTQ TLQRRTGENR ELTNKLKALD
AQLAGWVAKH EEADTKAKLL QVELDKPTVA LPEYEALEQQ RKALDEQLQA AQKKIVEHEQ
EMQKAIAQHA AQVKELEATH VTLKESLAKA SDDSATVAGL RSEIASLREQ LTRQVALANA
NKAVRPEGTN FNMATGASRG LENGAGGVAM ATVGGLSPAG LPGTAKRRQR RHSDVTADHS
PIPEETDRWE APRPVSVAYP QENGFAKRTG TKGYLPEVYD DPAEEIMRLL EEEEPLDEDV
LSGIIRHLKI PGANLQTPPS PKEVLFPAHL ISLVTNEMWK YGMMRESERF LANVMQTVQQ
HVMSFQGDDV IVPGIFWLSN VHEILSFVCI AESDILQGIG PGGDGIGREY EWDDYERLVT
IVKHDLDSLE YNIYHTWMQE TKKRLHRMVI PALIESQSLP GFVTSEGSGR LFGRLVGGGA
ASTPAFSMDD ILNLLNKVWK SLKSYYVEHS VVQQAVTELL KLIGVSSFND LLMRRNFSSW
KRAMQIQYNI TRLEEWCKSH DMPEGTLQLE HLMQATKLLQ LKKATLADID IIYDVCWMLT
PTQIQKLIAN YYVADYENPI SAEILRAVNS RVVAGDKNDH LLLPPEVEEA GPYEVPLPRE
VTGIETYVPA WLNAPHLRGL VQLVSAS
//
