ID V5INB2_NEUCR Unreviewed; 1594 AA.
AC V5INB2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Myosin-2 {ECO:0000313|EMBL:ESA42634.1};
GN ORFNames=NCU01440 {ECO:0000313|EMBL:ESA42634.1};
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110 {ECO:0000313|EMBL:ESA42634.1, ECO:0000313|Proteomes:UP000001805};
RN [1] {ECO:0000313|EMBL:ESA42634.1, ECO:0000313|Proteomes:UP000001805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC {ECO:0000313|Proteomes:UP000001805};
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA Lander E.S., Nusbaum C., Birren B.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; CM002240; ESA42634.1; -; Genomic_DNA.
DR RefSeq; XP_011394531.1; XM_011396229.1.
DR SMR; V5INB2; -.
DR STRING; 367110.V5INB2; -.
DR PaxDb; 5141-EFNCRP00000007543; -.
DR EnsemblFungi; ESA42634; ESA42634; NCU01440.
DR GeneID; 23568361; -.
DR KEGG; ncr:NCU01440; -.
DR VEuPathDB; FungiDB:NCU01440; -.
DR InParanoid; V5INB2; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
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:UP000001805}.
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; 181017 MW; 7A221CC43E327CDD CRC64;
MSESYDVGTR AWQPDPTEGW VASEVVKKTV DGNKVTLIFE 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 SLGTMKNQNR
ELKTQVENYE 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 DYDTQSMNDL AEVDEGQEIV EASA
//
