ID G4UHR2_NEUT9 Unreviewed; 1594 AA.
AC G4UHR2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Putative myosin MYO2 {ECO:0000313|EMBL:EGZ75548.1};
GN ORFNames=NEUTE2DRAFT_105463 {ECO:0000313|EMBL:EGZ75548.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ75548.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ75548.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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; GL891107; EGZ75548.1; -; Genomic_DNA.
DR STRING; 510952.G4UHR2; -.
DR eggNOG; KOG0160; Eukaryota.
DR HOGENOM; CLU_000192_3_1_1; -.
DR OMA; EIMFDDR; -.
DR Proteomes; UP000008513; 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; 2.
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; 4.
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:UP000008513}.
FT DOMAIN 6..61
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..782
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1229..1498
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 657..679
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 924..1080
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 1594 AA; 181032 MW; 118A094B0A60D9F1 CRC64;
MSESYDVGTR AWQPDPTEGW VASEVVKKTV DGNKVTLTFE CENGETKTVE VSLEALQSGG
HESLPPLMNP TMLEASDDLT NLSHLNEPAV LQAIRLRYAQ KEIYTYSGIV LIATNPFARV
DSLYVPGMVQ VYAGKQRATQ APHLFAIAEE AFMDMLRDGK NQTIVVSGES GAGKTVSAKY
IMRYFATRES PDSPGSRVKK GGHESMSQTE EAILATNPIM EAFGNAKTTR NDNSSRFGKY
IEIMFDKATN IIGAKIRTYL LERSRLVFQP LKERNYHIFY QLVAGVTDKE RQELGLLPVE
QFEYLNQGNT PTIDGVDDKA EFNATKASLK TIGVDEGKQT EIFKLLAGLL HLGNVKIGAM
RNDSSLDPSE PSLVKACEIL GIDAPEFAKW IVKKQLVTRG EKIVSNLTQA QAIVVRDSVA
KYIYSSLFDW LVEIINHSLA SEEVLTRVTS FIGVLDIYGF EHFAKNSFEQ FCINYANEKL
QQEFNQHVFK LEQEEYLREQ IDWTFIDFAD NQPCIDLIEG KLGILSLLDE ESRLPMGSDE
QFVTKLHHNY AADKHKFYKK PRFGKSSFTV CHYAIDVTYE SDGFIEKNRD TVPDEHMAVL
RASTNQFLVS VLDAASAVRE KDLASASSNA VKPAAGRRIG VAVNRKPTLG GIFKSSLIEL
MNTINGTDVH YIRCIKPNEA KEPWKFEGPM VLSQLRACGV LETVRISCAG YPTRWTYEEF
ALRYYMLVPS TQWTSEIREM ANAILTKAFG ASTGKGLDKY QLGLTKIFFR AGMLAFLENL
RTTRLNDCAI LIQKNLKAKY YRKRYLAARN AIVSFQALIR ANKARNSAQE RRTTKAAITI
QRVWRGYKDR KQFLEVRNDV IRAQAAIKGY MKRKKIMEER VGNAVLIIQR NWRSRQQLRS
WRDYRRKVTI VQSLWRGKTA RKDYKALRAE ARDLKQISYK LENKVVELTQ SLGTMKTQNR
ELRTQVENYE GQVAIWRNRH NQLEARAKEL QAEANQAGIA AARLEQMEAE MKKLQASFEE
SVANVKRMQE EERELRESLR ATSVELDSAR IESQRQEAEK NSLRQQLADL QEALEQARRQ
VPINGDILNG NGIAPQVPTG LINLVSSKKP KRRSAGAEPR EMDRYSMAYN PRPVSMAVPG
LNRQTTLSGS TFVPGVDSIE LELEGLLADE DALNEEVTMG LIRNLKIPSP STNPPPSDKE
VLFPAYLINL VTSEMWNNGF VKESERFLAN VMQSIQQEVM QHDGEEAINP GAFWLSNVHE
MLSFVFLAED WYEAQKTDNY EYDRLLEIVK HDLESLEFNI YHTWMKVLKK KLFKMIIPAI
IESQSLPGFV TNENNRFLGK LLQSNTAPAY SMDNLLSLLN NVYRAMKAYY LEDSIITQTI
TELLRLVGVT AFNDLLMRRN FLSWKRGLQI NYNITRIEEW CKSHDMPEGT LQLEHLMQAT
KLLQLKKATL NDIEIIQDIC WMLSPNQIQK LLNQYLVADY EQPINGEIMK AVASRVSEKS
DVLLLQAVDM DDSGPYEIAE PRVITALETY TPSWLQTPRL KRLAEIVSQQ AIAQQEKMEF
GSQAGDYQHG DYDIQSMNDL AEVDEGQEIV EASA
//
