ID K2HTC0_ENTNP Unreviewed; 1049 AA.
AC K2HTC0;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Unconventional myosin IB, putative {ECO:0000313|EMBL:EKE39390.1};
GN ORFNames=ENU1_130390 {ECO:0000313|EMBL:EKE39390.1};
OS Entamoeba nuttalli (strain P19) (Amoeba).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=1076696 {ECO:0000313|EMBL:EKE39390.1, ECO:0000313|Proteomes:UP000006769};
RN [1] {ECO:0000313|EMBL:EKE39390.1, ECO:0000313|Proteomes:UP000006769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P19 {ECO:0000313|EMBL:EKE39390.1,
RC ECO:0000313|Proteomes:UP000006769};
RA Hannick L., Karamycheva S., Lorenzi H., Caler E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Myosin I heavy chain is single-headed. Dimer of a heavy and a
CC light chain. Inability to self-assemble into filaments.
CC {ECO:0000256|ARBA:ARBA00011190}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; JH927639; EKE39390.1; -; Genomic_DNA.
DR RefSeq; XP_008858275.1; XM_008860053.1.
DR AlphaFoldDB; K2HTC0; -.
DR EnsemblProtists; EKE39390; EKE39390; ENU1_130390.
DR GeneID; 20074452; -.
DR VEuPathDB; AmoebaDB:ENU1_130390; -.
DR OMA; MAFHWQS; -.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000006769; Unassembled WGS sequence.
DR GO; GO:0062201; C:actin wave; IEA:EnsemblProtists.
DR GO; GO:0042641; C:actomyosin; IEA:EnsemblProtists.
DR GO; GO:0005911; C:cell-cell junction; IEA:EnsemblProtists.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblProtists.
DR GO; GO:0005769; C:early endosome; IEA:EnsemblProtists.
DR GO; GO:0030175; C:filopodium; IEA:EnsemblProtists.
DR GO; GO:0061851; C:leading edge of lamellipodium; IEA:EnsemblProtists.
DR GO; GO:0070687; C:macropinocytic cup cytoskeleton; IEA:EnsemblProtists.
DR GO; GO:0045160; C:myosin I complex; IEA:EnsemblProtists.
DR GO; GO:0097203; C:phagocytic cup lip; IEA:EnsemblProtists.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:EnsemblProtists.
DR GO; GO:0051015; F:actin filament binding; IEA:EnsemblProtists.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000146; F:microfilament motor activity; IEA:EnsemblProtists.
DR GO; GO:0032027; F:myosin light chain binding; IEA:EnsemblProtists.
DR GO; GO:0005543; F:phospholipid binding; IEA:EnsemblProtists.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:EnsemblProtists.
DR GO; GO:0033275; P:actin-myosin filament sliding; IEA:EnsemblProtists.
DR GO; GO:0048870; P:cell motility; IEA:EnsemblProtists.
DR GO; GO:0043327; P:chemotaxis to cAMP; IEA:EnsemblProtists.
DR GO; GO:0016197; P:endosomal transport; IEA:EnsemblProtists.
DR GO; GO:0006887; P:exocytosis; IEA:EnsemblProtists.
DR GO; GO:0046847; P:filopodium assembly; IEA:EnsemblProtists.
DR GO; GO:0120320; P:lateral pseudopodium retraction; IEA:EnsemblProtists.
DR GO; GO:0006909; P:phagocytosis; IEA:EnsemblProtists.
DR GO; GO:0044655; P:phagosome reneutralization; IEA:EnsemblProtists.
DR GO; GO:0006907; P:pinocytosis; IEA:EnsemblProtists.
DR GO; GO:0044656; P:regulation of post-lysosomal vacuole size; IEA:EnsemblProtists.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140:SF729; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
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|PROSITE-ProRule:PRU00782};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 29..713
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 753..941
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 993..1049
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 586..608
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 937..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1049 AA; 119363 MW; C42BEC0BCA288FE6 CRC64;
MSVGFKRNTE KERENEIAAF KSKKGFVQKG VDDLVMLPKI DENEIVDNLK KRYNYDAIYT
NIGPVLIVIN PFKDLGLTTD EYVHLYKGKF RQELPPHIFA LSEETYRNMK NEKCNQCCII
SGESGAGKTV AAKQIMQYIA AVSGGNEKVV YVKNVILDSN PLLEAFGNAK TLRNNNSSRF
GKYFEINFDD HADPVGGTIT NYLLEKSRVC TQQTGERNYH IFYQLLAGAP ENYYNDFYLT
TPDYFVYTNQ SNCMVVDGID DKKDYADCVK AMNTIGISAD EQYWIFQLVA AILHLGNVYF
TENSSGYAEI TDKSALETAA YLLEVDPGQL EHVMLVRKLT TGVGARAEVF DSPLTVEQAE
ATKNAIAKEI YDRIFTMLVQ KVNIALQKHG IEHQCVIGIL DIFGFEIFPV NGFEQFCINY
VNEKLQQYFI ELTLKTEQEE YIAEGIKWTP IKYFNNKVVC DLIEGKNPPG MFSLLDDICA
TMHAQTEGAD FKFLEKCCSV HSTNQHFIPS GETFTVQHYA GPVSYYCEGF CEKNKDTLFL
ECVECLQTSN NQLLYDLFPW TAEQEAAKTG QKKRPTTAGF KIKTSANELM AALSQCQPHY
IRCIKPNETK KPQDWDADRV KHQVKYLGLL ENVKVRRAGF AYRAPFARFL QTYKKLSPKT
WGTWGEWTGD AKEGCRLILE GLTNIEPGQW QFGTTKLFIR LPESIFAIEE MLEKMDFDKA
VEIQKAWKGY RNRKRALSQR AEAASILKGK KERRRESVDY TNNKWTADYI NYENEIPLQE
AMEGHMDELV NFDDWVMRLN KKGKIENRAL LLTDKAIYIA QRQIKKKILK YIVTFRGDLS
QISEVVLSTM QDNFMVIRVR GAYDSVLLCP HKTEFLMMLL ENYRALMNGQ SFPINFSDSI
SFRGKDEKKD KLLVFKKDDG PKTLPVEEQK SFSKHVLVRT GLPKETDTTP GSYNSSVSSY
SAPAASSSSN YSAPPMKSAP PAPQAAAPPP PKPKLPQVKA LYPYTAANDE ELSFKVGDII
TILEKDEGWW KGELNGQEGW IPNNYVKEI
//
