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Database: UniProt
Entry: A0A0G4MGX4_9PEZI
LinkDB: A0A0G4MGX4_9PEZI
Original site: A0A0G4MGX4_9PEZI 
ID   A0A0G4MGX4_9PEZI        Unreviewed;      3219 AA.
AC   A0A0G4MGX4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CRK33477.1};
GN   ORFNames=BN1708_001155 {ECO:0000313|EMBL:CRK33477.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK33477.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK33477.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK33477.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR   EMBL; CVQH01022527; CRK33477.1; -; Genomic_DNA.
DR   STRING; 100787.A0A0G4MGX4; -.
DR   OrthoDB; 1094820at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
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; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 2.
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; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 1.
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; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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:UP000044602}.
FT   DOMAIN          113..163
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          167..859
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..760
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1649..1692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1730..1753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2247..2287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2468..2511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2549..2572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          937..1262
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1309..1346
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1370..1432
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1462..1524
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1553..1580
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1833..1860
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1924..2050
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2372..2399
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2652..2679
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2743..2869
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          2989..3164
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2247..2262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2263..2284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260..267
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   3219 AA;  366913 MW;  D767D09F8BD5D585 CRC64;
     MSIRNNPFAR MASASASPSP GPGDSRPKST LFSSPSPLSN VSTPTGHART QSHTSFNPPL
     ASAGGSHRHS RSDSRNGTHL SNTFAPSFIK TEEMQRGTGA DAVKGIEGEN DFSGKRYVWL
     KDPQTAFVKG CVVEELGKNT LLVQCDDGTQ REVDADSVDK VNPAKFDKAN DMAELTHLNE
     ASVVHNLQMR YQADLIYTYS GLFLVTVNPY CPLPIYTNEY ISMYKGRSRE DTKPHIYAMA
     DQAFRNLVDE GENQSILVTG ESGAGKTENT KKVIQYLAAV AHSESPVKAR SQQSNLSQQI
     LRANPILEAF GNAQTVRNNN SSRFGKFIRI EFNRNGSIAG AFIDWYLLEK SRVVGINSHE
     RNYHIFYQLL KGSDRAMKQD FLLDGLDVED FAYTRNGHDT ITGVSDRAEW ESLIEAFDVM
     NFSDKDQSAI LRTIAAILHL GNISVVKESR AADQARLAPD AKEQAAKVCK LLGVPLEPFL
     KGLLHPRVKA GREWVEKVQT PEQVRLSLDA LAKGIYERGF GDLVTRINQQ LDRTGMGLDD
     SHFIGVLDIA GFEIFDDNSF EQLCINYTNE KLQQFFNHHM FVLEQEEYAR EQIEWQFIDF
     GRDLQPTIDL IEVSNPIGIF SCLDEDCVMP KATDKSFTEK LNSLWDKKSN KYRSSRLGQG
     FVLTHYAAEV EYSTQGWLEK NKDPLNDNIT RLLSESTDKH VANLFADCAD TDNDATGGRS
     RVKRGLFRTV AQRHKEQLHN LMTQLHSTHP HFVRCILPNH KKKPKQFNGP LVLDQLRCNG
     VLEGIRIART GFPNRLPFAE FRQRYEVLCR DMPHGYLEGQ AAAALMLDKL SLDKTLYRVG
     LTKVFFRAGV LAELEEQRDA LITDIMARFQ SVARGYIQRR IAFKRLFRTE ATRIVQRNFH
     VYLDLVDSPW WQLLVKMKPL LGATRSSTEV KKKDAMIRQL HDKIQQEASD RQRLEDERRN
     VHAEMLRVQK TLESERALAL DKEEIFKRLQ LREAELEEKL AGAIDDQERL EDQLDDLLAA
     KKLAEQDVEK YRSQLEQAAS LIARLEDEKA HLSRRTIELE ASIEETSHKQ SERSEQEAAL
     EDEIKMLQSQ LALKDRKARD LEGKLLQVDQ DLGVKLMSTE KDLQSAKSKE SQLLHENRNI
     QQQLSQLSKT STDYEDLVRK KESELTFIRS ENKKYELERR SFEEQKKAMA ADKEKISSRL
     HDVQAEITAM KTQKLQLERE AEDAKKLLEA RLSEDAQADE NRQVLESQIK DLKDQLYAVQ
     VELSRERQSR DDVLLLSDHK YNALKEEFDG LNESKIIIEK ELYVQQDTLR RTMEARATAE
     SERDEARQEI RRLRVAKTQA EEARIQAEVA GERAVSRVAR EREESLRGDL TAAQERLTWF
     EEECAKLNHQ VEDLNKLILS SGEFGLKNDQ AKERLERELT TVRSRLTASE NDNRALLNKL
     QQKGLEIARS TSRASDASRG QVLSLQREKA RIEEQNVKLN KQLGDAQLKI AGLEKKAEKL
     QLNVEDLNHE VARETKQSRN AEKATSTSAA QLAEVNRALD SEKQLRGQAQ STVRTLQSTL
     DSREKELEEL RTQMLQILKT VEPDAMPPMQ DDSTQDRNIA RNFDLVRKVE DLQQNLRVQA
     TARANAESQL ADLRAARSES PMRPKLEEIH PNEAPFTGSP TQRRSKAHAR KISNTSTPTR
     RHAPIDNEGF DSARSDRTAD LLSFNNRMDL KTEVEELQNQ LQLAHMQNRH LQSQVDRSTP
     VPETYSDESP SMRRMQKLEQ ANSRLHGMLD DSTAKVSALE KSIRSGELSL RDIQTRSHEE
     ILDVLNSQED SRRSLLHSHK NAVSELTEVK TYFEKMRHER ARLEVELRDS KSDLQEMTMA
     REQEAASRSQ LLEEFSDLQI RLDTETSKLA DLSSSLNLYK GRSDEYFSKL EQAEIAVLKA
     SRAEQFAKAQ AREAEETCAE AMAERKKMDG IIEDLQRQSQ RLEEKVEDVS TDLDAAMQAK
     KRLQHELEDY RNQRANEIED KESSLEQTRK KYQAEFATLT KELDLAREEK LFKQAEITRL
     REELDDLRSK WDDEVLNSST WSKEKARLES TLADVVSSRD EAVNAHGEAQ SKVVSLLSQV
     RTLRTSVDDV TSERDLLIRE KRSLEARFAE AKAGLEDLAK GDSPSLRDAA NADKEILDLK
     SSLAQKEDIT AAAIEKMRRA ESLAAEMQKE AMVERETSAQ LQKAKAALEK SLNEVQIKVV
     DLETKGYSSA SNDIKFLHKR IQELESQLED QETERSKSQR SKGLEIARST SRASDASRGQ
     VLSLQREKTR VEEQNVKLNK QLGDAQLKIA GLEKKAEKLQ LNVEDLNHEV ARETKQSRNA
     EKATSTSAAQ LAEVNRALDS EKQLRGQAQS TVRTLQSTLD SREKELEELR TQMLQILKTV
     EPDAMPPMQD DSTQDRNIAR NFDLVRKVED LQQNLRVQAT ARANAESQLA DLRATRSESP
     MRPKLEEIHP NEAPFTGSPT QRRSKVHTRK ISNTSTPTRR HAPIDNEGLD SARSDRTADL
     LSFNNRMDLK TEVEELQNQL QLAHMQNRHL QSQVDRSTPV PETYSDESPS MRRMQKLEQA
     NSRLHGMLDD STAKVSALER SIRSGELSLR DIQTRSHEEI LDVLNSQEDS RRSLLHSHKS
     AVSELTEVKT YFEKMRHERA RLEVELRDSK SDLQEMTMAR EQEAASRSQL LEEFSDLQIR
     LDTETSKLAD LSSSLNLYKG RSDEYFSKLE QAEIAVLKAS RAEQFAKAQA REAEETCAEA
     MAERKKMDGI IEDLQRQSQR LEEKVEDVST DLDAAMQAKR RLQHELEDYR NQRANEIEDK
     ESSLEQTRKK YQAEFATLTK ELDLAREEKL FKQAEITRLR EELDDLRSKW DDEVLNSSTW
     SKEKARLEST LADVVSSRDE AVNAHGEAQS KVVSLLSQVR TLRTSVDDVT SERDLLIREK
     RSLEARFAEA KAGLEDLAKG DSPSLRDAAN ADKEILDLKS SLAQKEDITA AAIEKMRRAE
     SLAAEMQKEA MVERETSAQL QKAKAALEKS LNEVQIKVVD LETKGYSSAS NDIKFLHKRI
     QELESQLEDQ ETERSKSQRS VRNVDRIVKD LQSQIDRKDK QNSQLSDDVS RMRDKVDKLL
     QTIEELQSAE SAIELAARRA ERELREEKER ALRLEREAEG LRSMRMEMGS VMGGSMRTRA
     PPNMWRTGFG IDDDRNSMID VPKRKSSISR APSLTKGFL
//
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