ID A0A0D2U996_CAPO3 Unreviewed; 1166 AA.
AC A0A0D2U996;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Amoeboid myosin I {ECO:0000313|EMBL:KJE91601.1};
GN ORFNames=CAOG_002719 {ECO:0000313|EMBL:KJE91601.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91601.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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; KE346362; KJE91601.1; -; Genomic_DNA.
DR RefSeq; XP_004349469.2; XM_004349419.2.
DR AlphaFoldDB; A0A0D2U996; -.
DR STRING; 595528.A0A0D2U996; -.
DR EnsemblProtists; KJE91601; KJE91601; CAOG_002719.
DR GeneID; 14900789; -.
DR eggNOG; KOG0162; Eukaryota.
DR InParanoid; A0A0D2U996; -.
DR OrthoDB; 1094820at2759; -.
DR PhylomeDB; A0A0D2U996; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
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 Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..686
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 724..916
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1109..1166
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 563..585
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 912..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1166 AA; 128455 MW; E57397FE4C010EDB CRC64;
MPQYHWQSKN VKSSGVEDMV LLSKISEDQI VDNLKKRYMD DLIFTYIGPV LISVNPFKSM
PYFTDREIEQ YQGASAHENP PHVYALSDNM YRNMLIEMEN QCVIISGESG AGKTVAAKYI
MQYIARVSGG GPAVQRVKDV ILESNPLLEA FGNAKTVRNN NSSRFGKYFE IQFSRGGEPD
GGKISNFLLE KSRVVGQNRE ERNFHIFYQL CFGANAQQKE AFGITEPQYY NYLNKSGCFT
VDGTDDVAEF HETTKAMGVM GLSNDIQNEV YKIVAGILHL GNLEYVENGN YAQVADPQFL
EFPAYLLGIE ADQLNQKLTS RIMESKWGGK TEVTNVTLNV EQTMYTRDAL SKALYSRLFD
FLVQTINAAM VKQKVELAIG VLDIYGFEIF TKNGFEQFCI NFVNEKLQQI FIELTLKAEQ
EEYVREGIQW TPIQFFNNKV VCDLIESKRP PGVMCVLDDV CATLHAQGDG ADGKFLEKLA
PAVSSNEHFS SMSGAFVIQH YAGRVTYDVD GFCERNRDVL FKDLIMLMQS SSSAFIRSLF
PEDTNNDDKK RPTTASTKIK TQANELVDTL MKCTPHYIRC IKPNETKQAH DWDAKRCTHQ
VQYLGLKENI RVRRAGFAYR QVFDKFLRRF AILTPETFPH WNGSPVEGVK FLLNKVDMDN
SQWQLGSTKI FVKNPESLFL LEELRERKFD AFCRKIQRAF RQYRARKHMH ELKQKATDIL
FGKKERRRGS LNRNFVGDYI GFQDNPALRA LLPKKERVEF ACDVMKYDRR FNGQKRDLLL
TSQALYLVAL EKVQKGPEKG KLVLEVKRRI EMAQISGVTL SPFQDDFVIL HVPSEYDNVF
ELIFKTEFLT TLSDKYLAAT QRKLTVNFSD KIQYTVKKGG FMDSAGTRMI AFSYGQGDLA
IVKPGGKGGI VTIGQGLPKD SRPNFQPVAR QSAPRGGGGG GRGRAPPAPS GGGGGAPPPR
GAAPPARGAP PTRGGMAPRA PAPQAPAPQQ QDDQEDDAPP PMRAAPPTRG AAPPMRGGMA
PRGGMAPRGA PAAAAGGPPS GGPTRGGLAP RGAPASAAGG PPGAGPARGG MAAAGPPRGG
AAPRGRGAGP AGPGRGGAAG PGPARPAPKA VPQCRAIYDY TANDTDELAL TTGDVVDILN
KDNPGWWQGR VGNRIGLFPS NYVEMV
//
