ID T5AL61_OPHSC Unreviewed; 2395 AA.
AC T5AL61;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Myosin type II heavy chain {ECO:0000313|EMBL:EQL03339.1};
GN ORFNames=OCS_00955 {ECO:0000313|EMBL:EQL03339.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL03339.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL03339.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL03339.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
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; KE652217; EQL03339.1; -; Genomic_DNA.
DR eggNOG; KOG0161; Eukaryota.
DR HOGENOM; CLU_000192_5_2_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
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; -; 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; 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 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; 2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000019374}.
FT DOMAIN 116..166
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 170..862
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..763
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1120..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1636..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2249..2293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2361..2395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 940..1065
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1284..1435
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1465..1576
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1835..1883
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1933..2059
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2109..2143
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 263..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2395 AA; 273183 MW; D8A8B73C04324252 CRC64;
MSYNANSSAQ RRNNPFSRTA SPASPPTSAS RPRSILASSP VPLPGAPSPA PHSRSQSNSS
FGAAAIVLGG ASRHFRSDSR NGAPTSSTFA PSFIKVEEMA RSADAVDGIE GENDFSGKRY
VWLKDPQTAF VKGWVVDELE DNRIRVQTDD GTQLEVDAES VDKVNPAKFD KANDMAELTH
LNEASVVHNL HMRYQADLIY TYSGLFLVTV NPYCPLPIYS NEYINMYKGR SREDTKPHIF
AVADEAFRNL VEEGQNQSIL VTGESGAGKT ENTKKVIQYL AAVAQSETAA RSKSQHSNLS
QQILRANPIL EAFGNAQTVR NNNSSRFGKF IRIEFNRNGA ITGAFIDWYL LEKSRVVLIN
PHERNYHVFY QLLKGANDLV KGKLLLKGLG VEDFTYTRSG HDSITGISDK DEWDSLMEAF
GVMGFAEDEQ LSILRTVAAV LHLGNIEVVR ESRATDQARL APNAKQEAAK VCQLLGVPLE
PFLRSLLHPK VKAGREWVEK VQTPDQARLS LDALSKGIYE RGFGDLVTRI NRQLDSAGMG
MDDSHFIGVL DIAGFEIFEQ NSFEQLCINY TNEKLQQFFN HHMFVLEQEE YAREKIEWQF
IDFGRDLQPT IDLIELSNPI GIFSCLDEDC VMPKATDTSF TDKLNSLWDK KSAKYRPSRL
GQGFILTHYA AEVEYSTEGW LEKNKDPMND NITRLLASSS DKHVAALFAD CAETDEEMNG
GRSRVKKGLF RTVAQRHKEQ LHSLMTQLHL THPHFVRCIL PNHKKRPKQF NNPLVLDQLR
CNGVLEGIRI ARTGFPNRLP FAEFRQRYEV LCSNMPKGYL EGQAAASLML EKLGLDKALF
RVGLSKVFFR AGVLAELEEK RDALITEIMA RFQSVARGFI QRRLAYKKLF RTEATRIIQR
NFLVYHDLVQ NPWWQLIAKM KPLLGATRTA TEVKRRDAMI KQLNDQMRNE AENRHKLEEE
RRNCHSEMVR IQQTLESERA LALDKEEIFK RLQNREAELE EKLAGAIEDQ ERLEDQLDDL
MEAKNRAERE VEKYRSQLEQ AATLIAKLEE EKSRLSSKAV DLECAVQDIS QKQSQRSEQE
AALEDEIKVL QSQLALRDRK TQDLEGKLLQ IDQDSEVKLH STQKELESTK MRESQLRREH
ETIQKQLSQL SKTSTDYEDL VRSKESELAL LRSDKRKFEN ERRSLEGQKK ALTDEKEKVT
SKFRDVQAEL TAMKSKQTQL EREANEAKTL LEARLSDDAQ ADENRALLDA QIKDLKDELF
ETSRDLSRER QSRDDVLLLS DHKYQSLQEE FETLNESKII IEKELYAQQD TLRRTMEART
TVEKERDEAR DEIRRLRAAK TQAEEARLQA EVIGERQASQ AAREREESLR RDLDAAHERL
QWFEEECGKL NRQIEHLNKL ILSSGEFGLK NDQAKERMER ELGTVKSRLA ASENDNRALL
NKLQQKGLEI ARSTSRATEA SRGQVHSLHK EKARLEEQNA KLNRQLGDAQ VTITSLEKRT
EKLQLGLEDL NHEVAREVQS SRNAEKASSN YTAQLAEANR TIDSERQLRS QAQSTVRTLQ
ASLDSRDKEL EELRGQILSA LKTADPEVDI PLPPEAGSQK SLLDKFDLVR KVEALQQNLR
AQAAARTNAE KQLTELRASR HETPNRPKLE EIHHNEAPFS GSPTQRRTAK VNSRRFSNTS
TPTRRGHDSE LQDSTRSDKT FDAVGANNRM DLKAEVEELQ NQLQLAQMQN RHMQSQLERS
SPAPDSYDEQ SPSIRRMQKL EKVNSRLHDM LDDSAKKVST LEKNIRTGEL SLRDIQARSH
EEILDVLNSQ EESRRSLLHS HKDAVAELTD VKSHFDKMRH ERAKLEVELR DTKSDLQEMS
LAREQESQNR SQLLQEYTDL QIRLDAETSK LADVASSLDM YKSRADEYFG KLEQAEIAVL
KASRAEQFAK SQAREAEDTY AEVMAERQKM DSAIEDLQRQ NQRHEERVED LSTALESVTQ
AKRRLQHELE DYRNQRAMDI EDKESSMEQT RKKYQAEFAT LTKELDLARE EKLYKQAEIA
RLREELDELR SKWDDEVLNS STWSKEKARL ESTLADVASS REEAVNAHNE AQGKVVSLLS
QVRTLRLSVD EITSERDLLL REKRSMETRL EEAKAGLEEL AKGESPSLRD AATVDKEVLE
LKSNLAHQED VAAAAVDRMR RAEALATEIQ KDIAAERETG TELQRQKASL EKSLNEAQLK
LVDLETKGYS SASQDIKFLH KRIQELESQL ESQETERNKS QRSHRNVDRT VKDLQSQVER
KEKQNAQLSE DVSRMRDKVD KLLKTIDDLQ ASESTKQLSA RRAERDLREE KEKTLRLERE
LHGWKGLKGS ASAVGSLRSR LGPWKGSEAD AGSASEAAPR KSSVSRAPSL TKGFL
//
