ID Q1A5W7_HAECO Unreviewed; 957 AA.
AC Q1A5W7;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Myosin heavy chain {ECO:0000313|EMBL:ABC40754.1};
DE Flags: Fragment;
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6289 {ECO:0000313|EMBL:ABC40754.1};
RN [1] {ECO:0000313|EMBL:ABC40754.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16490342; DOI=10.1016/j.biotechadv.2005.12.004;
RA Nikolaou S., Hu M., Chilton N.B., Hartman D., Nisbet A.J., Presidente P.J.,
RA Gasser R.B.;
RT "Class II myosins in nematodes-- genetic relationships, fundamental and
RT applied implications.";
RL Biotechnol. Adv. 24:338-350(2006).
RN [2] {ECO:0000313|EMBL:ABC40754.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16547732; DOI=10.1007/s00436-006-0129-8;
RA Hu M., Chilton N.B., Hartman D., Nisbet A.J., Presidente P.J., Gasser R.B.;
RT "Isolation and characterization of class II myosin genes from Haemonchus
RT contortus.";
RL Parasitol. Res. 99:200-203(2006).
RN [3] {ECO:0000313|EMBL:ABC40754.1}
RP NUCLEOTIDE SEQUENCE.
RA Nikolaou S., Hu M., Chilton N.B., Hartman D., Nisbet A.J.,
RA Presidente P.J.A., Gasser R.B.;
RT "Isolation and characterization of class ii myosin genes from Haemonchus
RT contortus.";
RL Parasitol. Res. 99:204-204(2006).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000256|ARBA:ARBA00004657}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ310761; ABC40754.1; -; mRNA.
DR AlphaFoldDB; Q1A5W7; -.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
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; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
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}; Methylation {ECO:0000256|ARBA:ARBA00022481};
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 31..80
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 84..788
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 664..686
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 936..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT NON_TER 957
FT /evidence="ECO:0000313|EMBL:ABC40754.1"
SQ SEQUENCE 957 AA; 109258 MW; DE4842F8BDE44E50 CRC64;
MANGDFEKDP GFQYLGLSRE ARAESANRPF DSKKNVWVPD AEDGFVAAEI QSVQGDQVTV
VTAKGNSVTV KKDEAQEMNP PKFDKTEDMA NLTFLNEASV LANLKDRYKD MMIYTYSGLF
CVVINPYKRL PIYTESVIKF YMGKRRNEMP PHLFATSDEA YRNMVQDREN QSMLITGESG
AGKTENTKKV ISYFAIVGAT QQAAEKKEGT KGGTLEEQIV QTNPVLEAFG NAKTVRNNNS
SRFGKFIRTH FSAQGKLAGG DIEHYLLEKS RVVRQAPGER SYHIFYQIMS GHNPKLRESL
KLTHDLKYYH FCSQAELTID GVDDKEEMGL TQEAFDIMGF EDDEVMDLYK SCAAIMHMGE
MKFKQRPREE QAEPDGDEDA QNVAHCLGVN HEELLKSLTK PRVRVGTEWV NKGQNLEQVH
WAVAGLGKAI YARMFKWLIG RCNKTLDAKQ IERRYFIGVL DIAGFEIFDF NSFEQLWINF
VNERLQQFFN HHMFVLEQEE YKREGIQWTF IDFGLDLQAC IELIEKPLGL ISMLDEECIV
PKATDMTYVQ KLNDQHLGKH PNFQKPRPPK GKQSEAHFAV VHYAGTVRYN ATNFLEKNKD
PLNDTAVALL KTHSTSCKLM LDIWADYQTQ EEAAEAAKSG TGGGKKKGKS ASFMTVSMIY
RESLNNLMNM LYQTHPHFIR CIIPNEKKTS GLIDSALVLN QLTCNGVLEG IRICRKGFPN
RMLYDDFKHR YAILAADAAK AEDVKAASVA ITDKLVTEGK LKDEEFKIGN TKVFFKAGIL
ARLEDHRDEI LKVIMTNFQS RCRWYLGLTD LKRRQQQQAG LLIVQRNVRS WCTLRTWEWF
KLYGKVKPML KAGKEAEEME KLSGKIKELE ETIQKGDESR KQLESQVAGL IEEKNALFLS
LEKEKANLQD AEERNQKLAA LKADLDKQLA EVQDRLAEME DRNSDLGRLK KKKKKKK
//