ID A0A319AHT2_ASPLB Unreviewed; 1572 AA.
AC A0A319AHT2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Class V myosin {ECO:0008006|Google:ProtNLM};
GN ORFNames=BO96DRAFT_341388 {ECO:0000313|EMBL:PYH55003.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH55003.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH55003.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH55003.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; KZ821356; PYH55003.1; -; Genomic_DNA.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000247441; 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; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.190; -; 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; 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; 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 SUPFAM; SSF57997; Tropomyosin; 1.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 6..59
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..780
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1232..1501
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 915..1078
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 1572 AA; 179457 MW; FD426DE73EAB3716 CRC64;
MAHNYEVGTR AWQPDPTEGW VASEVKEKLV DGDKVQLVFL IENGETKTLE TTQAELQVDN
NPKLPPLMNP AMLEASEDLT NLSHLNEPAV LQAIKLRYAQ KEIYTYSGIV LIATNPFARV
DSLYVPQMVQ VYAGKHRASQ APHLFAIAEE AFADMLRDGK NQTIVVSGES GAGKTVSAKY
IMRYFATRES SDQPGKYTTS RADAISETEE QILATNPVME AFGNAKTTRN DNSSRFGKYI
EIMFDDRTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGATDPEK QELGLTSVED
FDYLNQGGTP TIDGVDDRAE FNATKKSLST IGVPEGTQAE IFRVLAALLH LGNVRITATR
TDSSLSSSEP SLVRACQLLG IDANEFAKWI VKKQLITRGE KITSNLTQQQ ATVVRDSVAK
FIYSSLFDWL VDRINQGLAT DSILNKFKSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
QEFNQHVFKL EQEEYVREQI DWTFIDFSDN QPCIDLIEAK LGILSLLDEE SRLPMGSDEQ
FVTKLHHNFA ADKQKFYKKP RFGKSAFTIC HYAVDVTYES DGFIEKNRDT VPDEHLEILR
GSSNDFVKEI LDTAAAVREK DSASISSKPV AAPGRKIGVA VNRKPTLGGI FKSSLIELMN
TINSTDVHYI RCIKPNEAKE SWKFEGPMVL SQLRACGVLE TVRISTAGYP TRWTYEEFAI
RYYMLCHSSQ WTSEIRDMCH AILQKALGDG TQQKQDKYQL GLTKIFFRAG MLAFLENLRT
SRLNGCAVMI QKNLRCKYYR RRYLEARASI LTTQALIRGF LARQRAAEIR QVKAATTIQR
VWRGQKERRN YSRIRANFVL FQSVAKGFLC RQNILDTIHG NAAKVIQRSF RSWRQLRAWR
QYRRKVIIVQ NLWRGKQARR EYKKLREDAR DLKQISYKLE NKVVELTQYL ESLKRENKSL
NSQLENYETQ VKSWRSRHNV LENRSKELQA EANQAGITAA RLTAMEEEMN KLQQHHNDAQ
ATIKRLQEEE KISRESIRTA NQELEKLQQL NTDAENEKAS LRQQIVDLEE QLELAKRVVP
ANGVNGDQQN GGPIQPPASG LINLVSSKKP KPKRRSAGAE RIDIDRFSGA YNPRPVSMAI
PSSAMGRQHF SGNAFSPGLD SVEVELENLL SEEDELNEEV TMGLIRNLKI PLPSSTPPPT
EKEVLFPAYL INLVTSEMWN NGFVKESERF LANVMQSIQQ EVMQHDGEDA INPGAFWLSN
VHEMLSFVFL AEDWYEAQKT DNFEYDRLLE IVKHDLESLE FNIYHTWMKV LKKKLYKMIV
PAIIESQSLP GFVTSETNRF LGKLLPSNNN PAYSMDNLLS LLNNVYKAMK AFYLEETIIT
QTVTELLRLV GVTAFNDLLM RRNFLSWKRG LQINYNITRI EEWCKSHDMP EGTLQLEHLM
QATKLLQLKK ATLNDIEIIQ DICWMLSPNQ IQKLLNQYLV ADYEQPINGE IMKAVASRVT
EKSDVLLLTP VDMEDSGPYE IAEPRVITAL ETYTPSWLQT PRLKRLAEIV SAQAMAQQER
LEMTESGATM ME
//
