ID A0A0R0M696_9MICR Unreviewed; 1680 AA.
AC A0A0R0M696;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Myosin class II heavy chain {ECO:0000313|EMBL:KRH94657.1};
GN ORFNames=M153_18000010351 {ECO:0000313|EMBL:KRH94657.1};
OS Pseudoloma neurophilia.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pseudoloma.
OX NCBI_TaxID=146866 {ECO:0000313|EMBL:KRH94657.1, ECO:0000313|Proteomes:UP000051530};
RN [1] {ECO:0000313|EMBL:KRH94657.1, ECO:0000313|Proteomes:UP000051530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK1 {ECO:0000313|EMBL:KRH94657.1,
RC ECO:0000313|Proteomes:UP000051530};
RA Ndikumana S., Pelin A., Sanders J., Corradi N.;
RT "The genome of Pseudoloma neurophilia, a relevant intracellular parasite of
RT the zebrafish.";
RL Submitted (JUL-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRH94657.1}.
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DR EMBL; LGUB01000045; KRH94657.1; -; Genomic_DNA.
DR VEuPathDB; MicrosporidiaDB:M153_18000010351; -.
DR Proteomes; UP000051530; 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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
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:UP000051530}.
FT DOMAIN 4..53
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 57..728
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 601..623
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT COILED 789..1203
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1236..1567
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1615..1663
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 150..157
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1680 AA; 198391 MW; 22A4DCF6C0534DE6 CRC64;
MQQDEGKQIW IKDTENAFVL AKILSEEKET YTVLTKKDEQ KIVIKEDTLK TNPKKFDGIE
DLSALSNLNE ATVLHNLRKR YDLQKIYTYS GLFLVAMNPF KETGIYTQKY LDMYLDGKKQ
ELPPHIFAVA NEAYTSMLLN RKNQSILITG ESGAGKTENT KKVISFLAYI AQGHIPENDL
SIESKIIHTN PILEAFGNAQ TVRNFNSSRF GKFIKITFDS GRITGATIEK YLLERSRVTK
PNLYERNYHI FYQLLKSNNT ELLKKLNLVP DIKKYNILQH TPLNVPGIDD AVDFQKTLES
MKILGFDQSM IDSCLRIIAA ILHLGNIEFS EKDDKTEICN IEPVEIACKL LAIPLTTFIK
NILSPISILK KETLTRNRDC EQAKKVVDGF CRLLYENLFD EIIKMINDTL RCPIYESFIG
VLDIAGFEIF NKNDFEQFCI NFTNEKLQQF FNHHMFILEQ EIYQREKIEW NFIDFGHDLS
PTIELIESNN PIGILAFVDE ECLMPKANEE TLLLKLKQKV DSDRFVPSKF TQGFSLKHYA
GETNYEVDGW LEKNKEPFFE DIFDLISKSG NEFVSKLVPK RTQFEKKGFF RTVAQKHKEQ
LAVLMNELQN TFPHFIRCIL PNNMKRSDIF DNHFILHQLR CNGVLEGIRI SRLGYPNRME
FNNFIQRYQV IYKIFDEHEE YNGVEGSEKE FIREMCDHLL ISKKNYKIGL SKVFFKQGIL
AEMEEIREKK QIEIMNEFKA QIKGFLVRQT MQQSELKQDV ADNLINDFKK HLALRRSPWW
RIYQICKPLI DLRQNSELEE QQKQELLDLK EKMVESTNTI EKLQRILQSR EFEKSKLDEE
IKLINVSKNQ LQDLIDAVRN ENSLKTEELA AQKNQMEKLS QLISEKNEKF DQQDQILQKI
RLENTEMLKS LENLQKTSIQ EKNNHLQSYQ ALLKEKKDLA AQNIQLQSEI GTIQSENKGQ
FDNLIQEKDK QLIQIFDQLT NLKEEKADLE RKLKQFDEKI SHANDKQASI DKLYEDQKDL
NDKISAKLKE KEIDLQNNIL KINELSNNIT SLSNDLQNSK TIISKLKCEN EDLVLEIEKT
ENESIKLRNN LSDSFKDIND KNQTIDLLNE RINNFNTQIA ILKEENNQQY LVQGQNNGNE
EIYQMQVKRF EKQIKDLLLK NKMLQDNQSN AEIYKNEIVK KVSAEKQQEI EKLLKEISIY
NIEKKALLIK IKTITTENEN LKVMFQEKIE NSESSSDNSH IELEKKEELR NELEKKEEEC
MKLKNDLESL QERFDLELTE LNDQINNFKQ QEMYQKLNEK KLKDMKAIKE NLEKERNQIE
TFLKSFKEIY QNKINHYRKE MNDLENGSKN LSRENLQLKK DLNSLERENT DLKKRMDDFE
NNLTFYKKHS DEITNELIQK NRETQQKENE LHSLRNKINN LEISVNHMSQ IEKEEKDKSN
DKILFLENKN KSLNEMLQKY SEDYKKLYQM IKESDEEKQL REENLKINNQ LSHLRLKNET
LQNNCNSLKD QINQITESFN SLQNQTTSLK KQNELLNIQM TYKEKEIKNL KEEYETLQIK
RSEILNEEDK NNGEHSGQSQ VQEVKKENIQ EKIAFYDNKR ESLLQFENLE LKKTVEEMTK
KSENFKSDLI SLKNAHSTIL KEKELLELKK RQLERELADE KDQNRLFYMK ERKVERKAKR
//
