ID S0ED00_GIBF5 Unreviewed; 2402 AA.
AC S0ED00;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Related to myosin II {ECO:0000313|EMBL:CCT70278.1};
GN ORFNames=FFUJ_06233 {ECO:0000313|EMBL:CCT70278.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT70278.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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; HF679028; CCT70278.1; -; Genomic_DNA.
DR SMR; S0ED00; -.
DR STRING; 1279085.S0ED00; -.
DR EnsemblFungi; CCT70278; CCT70278; FFUJ_06233.
DR VEuPathDB; FungiDB:FFUJ_06233; -.
DR HOGENOM; CLU_000192_5_3_1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000016800; Chromosome 6.
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; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
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; 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 PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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}; 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:UP000016800}.
FT DOMAIN 118..168
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 172..864
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..765
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1181..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2252..2294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2352..2384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1712..1739
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1838..2062
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2105..2139
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2402 AA; 275625 MW; 39DD4DF797C3E786 CRC64;
MSFNANANGT AHRRSNPFAR TPSASPATNT NLRPKSAIFS SPSSTSGLST PPGHSRTQSN
GSLSAITHGF SGPAPRQQRS DSKGATPTST TFAPSFIKTE EMKRHDTVKG IEGENDFSGK
RYVWLKDPQA AFVRGWIVEE MDGNRLLVQC DDGTQRDVDA ESVDKVNPAK FDKANDMAEL
THLNEASVVH NLHMRYQADL IYTYSGLFLV TVNPYASIPI YSNEYINMYR GRSREDTKPH
IFAMADEAFR NLVEEGKNQS ILVTGESGAG KTENTKKVIQ YLAAVAQADS TIKHKPHHSN
LSQQILRANP ILEAFGNAQT VRNNNSSRFG KFIRIEFTRN GAICGAYIDW YLLEKSRVVH
INSHERNYHV FYQLLKGASS ALKREFLIDG LTVENFNYTK DGHDTIVGVS DHDEWESLME
AFNVMGFSDE EQRSILRTVA AVLHLGNITV VKESRTADQA RLAPDAKEQA AKVCKLLGVP
LEPFLKGLLH PKVKAGREWV EKVQTPEQVR LGLDALSKGI YERGFGDLVN RINGQLDRTG
MGLEDSHFIG VLDIAGFEIF EQNSFEQLCI NYTNEKLQQF FNHHMFVLEQ EEYAREQIEW
KFIDFGRDLQ PTIDLIELSN PIGVFSCLDE DCVMPKATDK SFTEKLNSLW DKKSTKYRPS
RLGQGFILTH YAAEVEYSTE GWLEKNKDPL NDNITRLLAA SSNKHVASLF SDCAESEEDH
ATGRGRVKRG LFRTVAQKHK EHLHSLMAQL HSTHPHFVRC ILPNHKKKPK QFNNLLVLDQ
LRCNGVLEGI RIARTGFPNR LPFAEFRQRY EVLCQDMPKG YLEGQAAASL MLEKLGLDRA
LYRVGLTKVF FRAGVLAELE EQRDALITQI MSRFQSVARG FIQRRAAYKR LFRTEATRII
QRNFNVYLDL AENPWWQLIV KMKPLLGTTR TATEVKRRDA MIKDLNERMQ LESQNRMKLE
EERRNCHAEM IRIQQTLESE RALALDKEEI FKRLQLREAE LEEKLAGAIE DQERLEDELD
DLLNAKNRAE RDVETYRSQL EQAATLIAKL EEEKKGLSTK ISEVEQSMAD ITQRQAERSE
QELALQDEIK MLQSQLSVKE RKVQDLETKL VKLDQDSELK LNAAQRELQS TKFRETQLTH
ENEDIQRQLN ELSKTSTDYE DLVRQKESEL ALLRTDNKNF ESERQSLEDQ KRSLTTEKEK
NAEKYREAQA ELVAMKSRQS QLEREAEDAK NLLEARLSED AQADQNRQVL ESQIKDLKDE
LYKTQMDLSR ERQSRDDVQL LGEHRYQELK DEFDRLNESK IIIEKELYAQ QDTLRRTMEA
RTTAEKERDE ARQEIRRLRV AKTQAEEARM QAEVAGERQA SKAALDRENS LRKDLDAAQE
RLQWFEGECA KLNRQIEDLN KLILESGEFG LKNDQAKERL ERELTTVKSR LTASENDNRA
LLNKLQQKGL EIARSSSRAS EASRGQIISL QREKARLEEQ NTKLNKQLGD SQLAIASLEK
RAEKLQLSLE DLSHEVAREV KSSRNAEKAT STFTAQLAEA NRTIESERQL RTQAQTTIRT
LQTSVDTRDK EVNELRAQML DVLRTVDPEV PIPPQSDGAD ENVLIQNFDL VRKVEELQQN
LRVQTAARTN AENQLSEMRA SRNDPASRPK LEEIQLNEAP FQGSPTQKRA AKLHARNYSN
TSTPTRRFQD LDHLQDSTRS DRTIDTLNFN NRMDLKAEVE ELQNQLQLKE MQNRHLQSQI
DRSTPIPENY DDQSPSLRRI QKLEMVNTRL HEMLDDSNKK VSALERTIRS GQLSLRDVQT
RTHEEILEVL NSQEDSRRAL VHSHKDAVAE LTDIKGHFER LRHDRAKAEV ELRDVKSDLQ
EMTLAREQEA QNRNQLLQEF ADLQIRLDAE TSKFADVSSS LEMYKSRADE YFSKLEQAEI
AVLKASRAEQ FAKSQAKEAE DTYAEVMAER EKMDASIEDL QRQNQRLEEK VEDISTDLAA
ATQAKKRLQH ELEDYRNQRA MEIEDKESSM EQTRKKYQAE FATLTNELDL AREERLFKQA
EIARLREELD ELRSKWDDEV LNSSTWSKEK ARLESTLADV ASSRDEAVNA HNEAQGKVVT
LLSQVRTLRS SVDEITAERD HLLREKRNVE ARLEEAKSGL EDLVKGDSPS LRNAANMDKE
ILELRSHLAQ QEDIAAAAVE KMRRAEALVT EVQKDVMVER ENSIQLQQQK ASLEKVLNEA
QLKLVDLETK GYSSASQDVK FLHKRIQELE SQLEDQETER SKSQRSVRNV DRIVKDMQGQ
IDRKDKQNTQ LSEDVSRMRD KVEKLLKTIE ELQSSESQNQ LSARRAEREL REEREKIARL
ERELAGLKSL RNDKGSGSVM GSVRSRMGPW RVSEGDDASS MVDIPRRKSS LSRVPSFTKG
FL
//