GenomeNet

Database: UniProt
Entry: A0A395RZ19_FUSSP
LinkDB: A0A395RZ19_FUSSP
Original site: A0A395RZ19_FUSSP 
ID   A0A395RZ19_FUSSP        Unreviewed;      1583 AA.
AC   A0A395RZ19;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Myosin myo2 {ECO:0000313|EMBL:RGP65049.1};
GN   ORFNames=FSPOR_7439 {ECO:0000313|EMBL:RGP65049.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP65049.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP65049.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP65049.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP65049.1}.
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; PXOF01000107; RGP65049.1; -; Genomic_DNA.
DR   STRING; 5514.A0A395RZ19; -.
DR   Proteomes; UP000266152; 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   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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; IPR004009; Myosin_N.
DR   InterPro; IPR036103; MYSc_Myo5.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF706; MYOSIN-11; 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; 2.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000266152}.
FT   DOMAIN          6..61
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          74..781
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1228..1497
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          188..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..678
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1107..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          951..1079
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1583 AA;  180266 MW;  81EFFB8F3ADC0B58 CRC64;
     MASAYEVGTR AWQPDTAEGW VASELINKTV DGSKVKLTFQ LENGDTKDIE VSAEALQSGS
     DPSLPPLMNP TMLEASDDLT NLSHLNEPAV LQAIRLRYLQ KEIYTYSGIV LIATNPFARV
     DSLYVPGMVQ VYAGRQRATQ APHLFAIAEE AFMDMIRDKK NQTVVVSGES GAGKTVSAKY
     IMRYFATRES PDNPGGRSKR GSESMSETEE QILATNPIME AFGNAKTTRN DNSSRFGKYI
     EIMFDEETNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LIAGASDQQR EELGLLPIEE
     FEYLNQGNCP TIDGVDDKAE FEATQKSLST IGVTNEQQAD IFKLLAGLLH LGNVKITASR
     NDSVLAPNEP SLEKACDILG VKAEEFSRWI VKKQLITRGE KITSNLSQAQ AIVVRDSVAK
     FIYSSMFDWL VDIINTSLAS EDVLSRVTSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
     QEFNQHVFKL EQEEYLREQI DWTFIDFSDN QPCIDLIEGK LGILSLLDEE SRLPMGSDEQ
     FVTKLHHNFT PDKSKFYKKP RFGKSAFTVC HYAIDVTYES EGFIEKNRDT VPDEHMAVLR
     ASSNEFLKTV LDAATAVREK DAASSSSNAV KPAAGRKIGV AVNRKPTLGG IFRSSLIELM
     STINNTDVHY IRCIKPNEAK EAWKFEGPMV LSQLRACGVL ETVRISCAGY PTRWTYEEFA
     LRYYMLVRSD GWTSEIREMA DAILKKALGT STGKGLDKYQ LGLTKIFFRA GMLAFLENLR
     TTRLNDCAIM IQKNLRAKYY RQRYLEAREA IILTQSAIRS WKARKQANEL RTVKAAITIQ
     RVWRGSKQRK SYLQFRKDMV LFESIAKGYL RRKTILEERL GNAALKIQRS WRSRRQLMAW
     RQYRKKVVLI QSLWRGRKAR KEYKTIREEA RDLKQISYKL ENKVVELTQS LGSMKERNKG
     LASQVENYEG QIKSWKKRHN DLEARTKELQ TEANQAGIAV ARLQAMEDEM KKLQVAFDES
     TANIKRMQEE ERELRESLRL TNTELETAKR SSTQHEKDNM SLRQELESLR DALELARRNA
     PINGELANGT TPGATVPSGL INLVASKKPK RRSAGAEPRE LDRFSGTYNP RPVSMAVTGT
     AHRQNLSGST FLPGVDNIEM ELETLLADED GLNEEVTMGL IRNLKIPSPS TTPPPSDKEV
     LFPSYLINLV TSEMWNNGFV KESERFLANV MQSIQQEVMQ HDGDEAINPG AFWLSNVHEM
     LSFVFLAEDW YEAQKSDNYE YDRLLEIVKH DLESLEFNIY HTWMKVLKKK LQKMIIPAII
     ESQSLPGFVT NESSRFLGKL LQSNSTPAYS MDNLLSLLNS VFRAMKAYYL EDSIITQTIT
     ELLKLVGVTA FNDLLMRRNF LSWKRGLQIN YNITRIEEWC KSHDMPEGTL QLEHLMQATK
     LLQLKKATLN DIEIIQDICW MLSPNQIQKL LNQYLVADYE QPINGEIMKA VASRVTEKSD
     VLLLQAVDMD DSGPYEIAEP RVITALETYT PSWLQTPRLK RLAEIVSAQA IAQQEKLDYT
     DGEEYENGHQ HELEGVDEVE VEQ
//
DBGET integrated database retrieval system