ID A0A194WAX6_9PEZI Unreviewed; 2437 AA.
AC A0A194WAX6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Myosin type-2 heavy chain 1 {ECO:0000313|EMBL:KUI73492.1};
GN ORFNames=VM1G_08810 {ECO:0000313|EMBL:KUI73492.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI73492.1};
RN [1] {ECO:0000313|EMBL:KUI73492.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI73492.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) 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; CM003107; KUI73492.1; -; Genomic_DNA.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000078559; Chromosome 10.
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; 1.20.5.340; -; 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 Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
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; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}.
FT DOMAIN 114..164
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 168..860
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..761
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1634..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1728..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2252..2290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 938..1433
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1463..1518
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1840..1888
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1924..2050
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2107..2225
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1671..1697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1728..1748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2252..2273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2274..2290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261..268
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2437 AA; 277880 MW; F1608F7B795E2581 CRC64;
MGTVRNSPFM RQSSPSPSPG PPPNNGRPKS ALFGSPLSPT PSSPTPTGPS HVRGKSLVAN
LTPVNSDAKY NHARNASKGD APQSSTFAPS FIKSEEMRRG SEVVDGIEGE NDFSGKRYVW
LKDPQTAFVK GWVVEELEGN RILVQCDDGS QREVDAESVD KVNPAKFDKA NDMAELTHLN
EASVVHNLHM RYQSDLIYTY SGLFLVTVNP YCPLSIYTNE YVNMYRGRNR EDNKPHIFAM
ADEAFRNLVE EGQNQSILVT GESGAGKTEN TKKVIQYLAA VANSESSTRN RGQHSNLSAQ
ILRANPILEA FGNAQTVRNN NSSRFGKFIR IEFGRNGSIS GAFIDWYLLE KSRVVRINAN
ERNYHVFYQL LKGGDEELKQ EFILDGMDVD DFAYTRDGQD AIAGVSDRDE WDTLMEAFSV
MGFSDKEQGS ILRTVAAVLH LGNITVVNES RTTDQARLAP DAKQVAERVC RLMGIPLEPF
LQGLLHPKVK AGREWVEKVQ TPEQVRLGID ALAKGIYERG FGDLVTRINR QLDRTVMGMD
ESHFIGVLDI AGFEIFEENS FEQLCINYTN EKLQQFFNHH MFVLEQEEYA REQIEWQFID
FGCDLQPTID LIELPNPIGI FSCLDEDCVM PKATDKSFTE KLHSLWDKKS NKYRSARLRH
GFILTHYAAE VEYSTEGWLQ KNKDPLNDNV TRLLAASTDK HIANLFADCA DNDDEAVAVR
SRVKKGLFRT VAQRHKEQLS SLMSQLHSTH PHFVRCILPN HKKRPKLFNN LLVLDQLRCN
GVLEGIRIAR TGFPNRLPFA EFRVRYEVLC QDLPKGYIEG QAAVTMMLQR FKMDKSLYRV
GLTKVFFRAG VLAELEEQRD KLISEIMGRF QSVARGFTAR RIAYKRLYRT EATRVIQQNF
RVYLDLCKNP WWQLLVKMKP LLGATRTATE VKKRDEMIRQ LNDKMRQETA DRQKLEEDRR
NVHVEMMRVQ QTLESERALA LDKEEIFKRL QQREAELEDK LAGAIEDAEK LEDELDDLLE
AKKRAEEDVE KFRSQLEQAA SLIGRLEEEK TELAGRVSTL ETALKDLSKS QNERSEQEAA
LEEEISMLQS QLALKDRKAQ DLESKLLKVD QDAEVKLHAA QKELQSYKSK QQQLMAENRD
VQQQLSELSK TSTDYEDLVR KKESELVLLR GDNKKYEMER RAFEDQRKTL AAEKDKATSR
MRDVQAQLDA LKSQQSQIQR EAEDAKRVLE TRLSEDAQAD ENRQVLEGQI KKLKGELYDA
QMELSREKQS RDDVLLLGEH NLEQLQEEYD SLNEAKIVIE KELYAAQDTL RRAVDARTTA
EKERDEARQE IRKLRSAYSQ AEEARREAEL AGERAASKLA REHEASLRSD LDAAQERLKW
FEEECAKLNH EVEDLNKLIL SSGEFGLKND QAKERMEREL HTVKSRLAAS ENDNRALLNK
LQHKGLEIAR SSSRASQASR GQLTVLQREK ARLEDLNVKL NKQLGDSQVK VASLEKKLEK
INLNLEDLNH EFQREAKTSR NAEKITSGLN VQLAEANRNL ESERQLRTQT QGTVRALQAT
LDSRDKELHE LRSQVLQALK MVDPESVPPV QIDGSTERVF SEKYDLVRKI EELQQNLRVQ
TAARTNAESQ LVDLRAARGS PERPRLAEID FNEAPFDASP SYRRSRAKGR RPSSSSSPSR
RYNTDGDPSD NSVRSEKTAD ILSFNNRMDL KAEVEELQNQ LQITQMQNRH LQSQLERSTP
ASTDFSEEDP SLQRVKKLEK VNSRLHNMLD DSSKKVSALE KALRTGELSL HDIQTRSHEE
ILDLLNSTEE SRRSLLHSHK DAVAELTDVK EHFDKLRHDR AKLEVDLRDT RGDLQEMTQA
REQEAASRNQ LLQELSDLQI RLDAETSKLA DVAATLNLYK GRADEYFSKL EQAEIAVLKA
SRAEQFAKSQ AKEAEETYAE VMAERKKMDR TVEDLQRQNQ RLEEKVEDIS TDLEAATQAK
KRLQHELEDY RNQRANDIED TESSMEQTRK KYQAEFATLT KELDLAREEK LFKQAEITRL
RDELDDLRSK WDDEVLNSST WSKEKSRLEA TLADVSASRD EAANAHNEAQ GKIVNLLSQV
RTLRSSVDEV TAERDALFRE KRSVEARLEE AKAGLEDLAK SEIPSLRNAA SIDKEILELK
SNLAQQEDIA AAAVEKMRRA EALASEVQKD IVVERETSVQ MQKEKAALEK TLNEVQVKLV
DLETKGYSSA SQDIKFLHKR IQEACTSFIS SRPISSTAGD KTSNTQQLEN QLETQENDRA
KSQRSVRNVD RTVKDLQSQI DRKDKQNTQM QEDLGRMRDK VDKLLKTIDE LQASESSNQL
QARRAERELR EEREKAAQLE REIESWKNLR SEKGSVAGSV AGSVIGWRGG MARTGTMANL
RGSGLANVVD DDAESHVTIP KRKSSISRVP SLTKGFL
//
