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
//