ID A0A1J7IRQ1_9PEZI Unreviewed; 1588 AA.
AC A0A1J7IRQ1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative myosin MYO2 {ECO:0000313|EMBL:OIW29867.1};
GN ORFNames=CONLIGDRAFT_348686 {ECO:0000313|EMBL:OIW29867.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW29867.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW29867.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW29867.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-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; KV875097; OIW29867.1; -; Genomic_DNA.
DR STRING; 1408157.A0A1J7IRQ1; -.
DR InParanoid; A0A1J7IRQ1; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000182658; 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; 1.20.5.190; -; 3.
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; 4.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 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; 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};
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:UP000182658}.
FT DOMAIN 6..61
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..781
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 656..678
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1015..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1039
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1062
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1588 AA; 179797 MW; 1FAD1D402087C16D CRC64;
MSESYDVGTR AWQPDPTEGW VASEVINKSI NGDKVSLVFQ LENGETKTVE VSAEGLQSGN
DPNLPPLMNP TMLEASDDLT NLSHLNEPAV LQAIRLRYAQ KEIYTYSGIV LIATNPFARV
DSLYVPGMVQ VYAGKQRATQ APHLFAIAEE AFMDMLRDNK NQTIVVSGES GAGKTVSAKY
IMRYFATRES PDNAAARSRR GPEAMSATEE AILATNPIME AFGNAKTTRN DNSSRFGKYI
EIMFDKSTNI IGAKIRTYLL ERSRLVFQPL KERNYHIFYQ LVAGISDKER QELNILPVEQ
FEYLNQGNTP TIDGVDDKAE FNATRQSLKT IGVTDAQQTE VFRLLAGLLH LGNVKIGASR
NDSVLAPTDS SLELACRILG IDAAEFAKWT VKKQLVTRGE KIVSNLTQAQ AIVVRDSVAK
FIYSSLFDWL VEIINESLAT EEVLSKVSSF IGVLDIYGFE HFAKNSFEQF CINYANEKLQ
QEFNQHVFKL EQEEYLREQI DWTFIDFSDN QPCIDLIEGK MGILSLLDEE SRLPMGSDEQ
FVTKLHHNYA ADKNKFYKKP RFGKSAFTVC HYAIDVTYES EGFIEKNRDT VPDEHMAVLR
ASTNKFLGSV LEAASAVREK DAASASSNSV RPAGGRRIGV AVNRKPTLGG IFKSSLIELM
STINNTDVHY IRCIKPNEAK EAWKFEGPMV LSQLRACGVL ETVRISCAGY PTRWTYEEFA
LRYYMLVPST QWASEIRQMA TAILTKALGS GTGNGLDKYQ MGLTKIFFRA GMLAFLENLR
TNRLNDCAIM IQKNLRAKYY RRKYLAARQA IVSFQAAARA WLARKAAQEL RTVRAAVTIQ
RVWRGQKERK QFLRIRKDVI LAQAAIKGFL RRKEIMETRV GNAVLIIQRT WRSRQAMRAF
RQYRKKVVII QSLWRGRSAR KDYKVKKAEA RDLKQISYKL ENKVVELTQS LGTMKAQNRE
LKGQVENYEG QISAWRNRHN ALEARAKELQ TEANQAGVAA ARLEQMEAEM KKLQTSFEES
SANVKRMQEE ERQLRDSLRA TSTELEVARQ ESERHEAEKN SLRQQLAEMQ DALELARRSV
PVNGEVVQNG NGVMPPLANG LINLVASKKP KRRSAGAEPH DVNRYSMAYN PRPVSMAVTG
MNRQNTLSGA TFIPGVDNIE LELESLLADE EGLNEEVTMG LIRNLKIPSP NTTPPPSDKE
VLFPSYLINL VTSEMWNNGF VKESERFLAN VMQSIQQEVM QHDGDEAINP GAFWLSNVHE
MLSFVFLAED WYEAQKTDNY EYDRLLEIVK HDLESLEFNI YHTWMKVLKK KLQKMIIPAI
IESQSLPGFV TNENNRFLGK LLQSNSTPAY SMDNLLSLLN SVFRAMKAYY LEESIITQTI
TELLKLVGVT AFNDLLMRRN FLSWKRGLQI NYNITRIEEW CKSHDMPEGT LQLEHLMQAT
KLLQLKKATL NDIEIIQDIC WMLSPNQIQK LLNQYLVADY EQPINGEIMK AVASRVTEKS
DVLLLQAVDM DDSGPYEIAE PRSITALETY TPSWLQTPRL KRLAEIVSAQ AIAQQEKLEY
GSQDGDYDDQ GNDLAVVQES SEAIEAGA
//
