ID A0A368GUI0_ANCCA Unreviewed; 1964 AA.
AC A0A368GUI0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Myosin head {ECO:0000313|EMBL:RCN46949.1};
GN ORFNames=ANCCAN_06989 {ECO:0000313|EMBL:RCN46949.1};
OS Ancylostoma caninum (Dog hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=29170 {ECO:0000313|EMBL:RCN46949.1, ECO:0000313|Proteomes:UP000252519};
RN [1] {ECO:0000313|EMBL:RCN46949.1, ECO:0000313|Proteomes:UP000252519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Baltimore {ECO:0000313|EMBL:RCN46949.1,
RC ECO:0000313|Proteomes:UP000252519};
RA Mitreva M.;
RT "Draft genome of the hookworm Ancylostoma caninum.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RCN46949.1}.
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DR EMBL; JOJR01000070; RCN46949.1; -; Genomic_DNA.
DR STRING; 29170.A0A368GUI0; -.
DR Proteomes; UP000252519; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0030017; C:sarcomere; IEA:UniProt.
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; -; 5.
DR Gene3D; 1.20.5.370; -; 4.
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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF58; MYOSIN-4; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000252519};
KW Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT DOMAIN 30..79
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 83..787
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 662..684
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 970..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1768..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1919..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1928..1956
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1964 AA; 225550 MW; F3A64A4CB652E0BA CRC64;
MALDYENDPG WQYLRRSREQ ALEDQSKPYD SKKNCWIPDA EDGYVAGEIT STKGDQITVV
TARGNEVTLK KELVQEMNPP KFEKTEDMSN LTFLNDASVL HNLRSRYAAM LIYTYSGLFC
VVINPYKRLP IYTESVAKMF MGKRRTEMPP HLFAVSDLAY RNMLQDHENQ SMLITGESGA
GKTENTKKVI AYFATVGASQ QEGGGASDGK KKVTLEDQIV QTNPVLEAFG NAKTVRNNNS
SRFGKFIRIH FSKAGRLASC DIEHYLLEKS RVIRQAPGER CYHIFYQIFS DFKPELKKSL
ELDKPLKDYW FVAQAELSID GVNDTEEFQM TDEAFDILNF SETEKMDCYR LMSALMHMGN
MKFKQRPREE QAEPDGTDEA EKASNMYGVN FEEFLKALTK PRVKVGTEWV SKGQNMEQVN
WATGAMAKGL YSRVFNWLVK KCNLTLDQQG IPRDFFIGVL DIAGFEIFDF NSFEQLWINF
VNEKLQQFFN HHMFVLEQEE YAREGIQWTF IDFGLDLQAC IELIEKPLGI ISMLDEECIV
PKATDLTLAQ KLNEQHLGKH PNFEKPKPPK GKQAEAHFAM RHYAGTVRYN VTNWLEKNKD
PLNDTVVTVM KASKGNDLLV EIWQDYTTQE EAAVKAKEGG GGKKKGKSGS FMTVSMLYRE
SLNNLMTMLN KTHPHFIRCI IPNEKKASGV IDAALVLNQL TCNGVLEGIR ICRKGFPNRT
LHPDFVQRYA ILAAKEAKSD DDKKKCAEAI MSRLVNDGAV TEEMFRIGLT KVFFKAGVLA
HLEDLRDEKL SIIMTGFQGQ IRWYLGLADR KRRMEQRAGL LIVQRNIRSW CTLRTWEWFK
LYGKVKPMLK AGKEAEELEK INDKVKQLEE SLAKEEKLRK ELEDSSTKLL EEKNSLFTNL
ESTKGQLSEA EERLAKLQAL KGDADKQLAE LNERLADQED RNADVQRAKK KVEAELESLK
KQIQDLEMSL RKAESEKQSK DHQIRSLQDE MQQQDEAISK LNKEKKHQEE INRKLMEDLQ
SEEDKSNHTN KVKAKLEQTL DDLEDSLERE KRSRADLDKQ KRKVEGELKI AQENIDEAAR
QRHDLENNLK KKESELHSIS SRLEDEQALV SKLQRQIKEG QSRISELEEE LESERQSRAK
ADRAKSDLQR ELEELGDRLD EQGGATAAQV ELNKKREAEL AKLRRDLEEA NMNHENQLGG
LRKKHTDAVA ELTDQLDQLQ KQKAKIEKEK IQAHHEAEEL AAQLDAETSA KLNNEKLAKQ
FELQLTELQS KCDEQSRQLQ DFNSLKGRLH NENSDISRQL EDAESQLNQF SRLKSQLTSQ
LEEARRTADE EARERQTLAA QAKNFQHEAE QLQESLEEEI ESKNEVMRQL SKANAEIQQW
KARFEGEGLI KADELEDAKR RQAQKINELQ EALDAANSKI ASLEKTRSRL VGDLDDAQVD
VERANAFASA LEKKQKGFDK IIDEWRKKTD DLAAELDAAQ RDARNTSTEL FKAKNAQEEL
VEVVEGLRRE NKSLSQEIKD LTDQLGEGGR SVHEMQKIIR RLEIEKEELQ HALDEAEAAL
EAEESKVLRA QVEVSQIRSE IEKRIQEKEE EFENTRKNHQ RAMDSMQASL ETEAKGKAEL
LRVKKKLEAD INELEIALDH ANKANADAQK NLKRYQEQIR ELQLQVEEEQ RQRDDVREQF
FNAEKRSTLL QSEKEELLVA NEAAERARKQ AEYEAADSRD QVNELSGQAA SLAAAKRKLE
GEIQAIHADL DETLNEYKAA EERSKKAMAD ATRLAEELRQ EQEHSQHIDR MRKGLEQQLK
EMQVRLDEAE AAALKGGKKV IAKLEQRVRE VESELDAEQR RYQDANKNLG KADRRVRELQ
FQVDEDKKNF ERLQDLIDKL QNKLKTQKRQ IEEAEELANL NLQKYRQIQH QLEDAEERAD
VAENSLSKMR AKSRSSASVA PGGLQTSQSA TVMRSASRAR ASDF
//
