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Database: UniProt
Entry: A0A423VKQ2_9PEZI
LinkDB: A0A423VKQ2_9PEZI
Original site: A0A423VKQ2_9PEZI 
ID   A0A423VKQ2_9PEZI        Unreviewed;      1595 AA.
AC   A0A423VKQ2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=VSDG_07195 {ECO:0000313|EMBL:ROV91458.1};
OS   Valsa sordida.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=252740 {ECO:0000313|EMBL:ROV91458.1, ECO:0000313|Proteomes:UP000284375};
RN   [1] {ECO:0000313|EMBL:ROV91458.1, ECO:0000313|Proteomes:UP000284375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YSFL {ECO:0000313|EMBL:ROV91458.1,
RC   ECO:0000313|Proteomes:UP000284375};
RA   Yin Z., Huang L.;
RT   "Host preference determinants of Valsa canker pathogens revealed by
RT   comparative genomics.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROV91458.1}.
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DR   EMBL; LJZO01000043; ROV91458.1; -; Genomic_DNA.
DR   STRING; 252740.A0A423VKQ2; -.
DR   Proteomes; UP000284375; 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:SF289; UNCONVENTIONAL MYOSIN-XIX; 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; 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};
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:UP000284375}.
FT   DOMAIN          6..61
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          74..784
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1226..1504
FT                   /note="Dilute"
FT                   /evidence="ECO:0000259|PROSITE:PS51126"
FT   REGION          189..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..681
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1040..1065
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1568..1595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1065
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         168..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1595 AA;  180323 MW;  FE6AA072CE6CE622 CRC64;
     MSTNFDVGTR AWQPDAAEGW VASEVVKKEI DGDKVVLTFK LENGEDKEIK VSLAALEKGT
     DESLPPLMNP TILEASDDLT NLSHLNEPAV LQAIKLRYLQ KEIYTYSGIV LIATNPFARV
     DSLYVPGMVQ VYAGKQRATQ APHLFAIAEE AFADMIRDAK NQTIVVSGES GAGKTVSAKY
     IMRYFATRES PEHPGAKSKK GAESMSETEE QILATNPIME AFGNAKTTRN DNSSRFGKYI
     EIMFDPSTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ MIAGVTDQQR QELGLLPVEQ
     FEYLNQGNTP TIDGVDDKAE FKATMSSLST VGVDESTQGD ILRLLAGLLH MGNVKIGASR
     NDSVLAPNEP ALEKACTTLG IDATEFAKWI VKKQLVTRGE KITSNLSQAQ AIVVRDSVAK
     YIYSSLFDWL VEVINRSLAT DEVLGQVSSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
     QEFNQHVFKL EQEEYLREQI DWTFIDFSDN QPCIDLIEGK MGILSLLDEE SRLPMGSDEQ
     FVQKLHNNFT VDKKSTFYKK PRFGKSAFTV CHYAVDVTYE SEGFIEKNRD TVPDEHMAVL
     RASSNNFLVS VLDAAASVRE KDVASATTSS VKPAAGPGRR IGVAVNRKPT LGGIFRSSLI
     ELMNTINNTD VHYIRCIKPN EGKEAWKFEG PMVLSQLRAC GVLETVRISC AGYPTRWTYE
     EFALRYYMLV PSTQWTSEIR EMANAILTKA LGSSSGGGQD KYQLGLTKIF FRAGMLAFLE
     NLRTDRLNNC AIMIQKNLKA KYYRRRYLEA RDAVVRVQAL ARAYMARRQA QELRTVKAAT
     TIQRVWRGQK DRKKFLRIRA DLILAQAAIK GYLRRREIME TRVGNAAVLI QKVWRSRQAL
     QTWRAYRKKV TLIQSLFRGR QARKGYKKVR EEARDLKQIS YKLENKVVEL TQSLGTMKVQ
     NKELKSQVES YQGQIKSWQA RHNALEARTK ELQAEANQAG IAGARLSAME DEMKELQARF
     EESAANVKRM QDEEKQLRET LRATGTELEV SKTEASRHES EKNSLRQQLA ELQDALELAR
     RTVPVNGDVN GNGAQPAANG LINLVSSKKP AKRRSVGDPR ELDRFSAAYN PRPVSMAVTG
     RQAVMSGTTL IAADSIEMEL EALLADEDGL NEEVTMGLIR NLKISSPNTN PPPSDKEVLF
     PSYLINLVTS EMWNNGFVKE SERFLANVMQ SIQQEVMQHD GDEAINPGAF WLSNVHEMLS
     FVFLAEDWYE AQKTDNYEYD RLLEIVKHDL ESLEFNIYHT WMKVLKKKLN KMIIPAIIES
     QSLPGFVTNE NNRFLGKLLQ TNSQPAYSMD NLLSLLNSVF RAMKAYYLED SIITQTITEL
     LRLVGVTAFN DLLMRRNFLS WKRGLQINYN ITRIEEWCKS HDMPEGTLQL EHLMQATKLL
     QLKKATLNDI EIIQDICWIQ DMTLIEHRLS PNQIQKLLNQ YLVADYEQPI NGEIMKAVAS
     RVTEKSDVLL LQAVDMDDSG PYEIAEPRVI TALETYTPSW LQTPRLKRLA EIVSAQAIAA
     QEKMEYGSQG GYENGYENGD IEEMDETPEA IEASA
//
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