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Database: UniProt
Entry: A0A0D2X1P1_CAPO3
LinkDB: A0A0D2X1P1_CAPO3
Original site: A0A0D2X1P1_CAPO3 
ID   A0A0D2X1P1_CAPO3        Unreviewed;      1677 AA.
AC   A0A0D2X1P1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Myosin-VIIa motor domain-containing protein {ECO:0000313|EMBL:KJE91149.1};
GN   ORFNames=CAOG_002327 {ECO:0000313|EMBL:KJE91149.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91149.1, 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|PROSITE-ProRule:PRU00782}.
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DR   EMBL; KE346362; KJE91149.1; -; Genomic_DNA.
DR   RefSeq; XP_004349077.1; XM_004349027.2.
DR   STRING; 595528.A0A0D2X1P1; -.
DR   EnsemblProtists; KJE91149; KJE91149; CAOG_002327.
DR   GeneID; 14900395; -.
DR   eggNOG; KOG3686; Eukaryota.
DR   eggNOG; KOG4229; Eukaryota.
DR   InParanoid; A0A0D2X1P1; -.
DR   OrthoDB; 1094820at2759; -.
DR   PhylomeDB; A0A0D2X1P1; -.
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   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
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; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 3.40.50.11210; Rap/Ran-GAP; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035974; Rap/Ran-GAP_sf.
DR   InterPro; IPR000331; Rap/Ran_GAP_dom.
DR   PANTHER; PTHR13140:SF856; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF111347; Rap/Ran-GAP; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50085; RAPGAP; 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   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
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}.
FT   DOMAIN          10..835
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          1243..1474
FT                   /note="Rap-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50085"
FT   REGION          295..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..701
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          758..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          947..978
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1030..1055
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1567..1677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1041..1055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1606..1620
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1642..1671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119..126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1677 AA;  186529 MW;  C3EAC8F450EB5FF5 CRC64;
     MVDTDKPEDA VFDDMVEIGD LHELSILANL QRRFERDIIY TYIGKIVLVA VNPYKQLSVA
     PPQNSINPFA KLSLHGAELA NTYRMKRAGE LPPHIFATAQ EAYHHMMRDR KSQCVVVSGE
     SGAGKTFSTQ LILNYLANAS AAAADKFGSV PGLPTSTSTS TSTSTSTTTA AASVQTAGAL
     TMKDSIGKRL LAAGPVLQAF GNATTVYNPN SSRFGNYIQI VFDSNGRIQG ANIQQYLLEK
     SRIIQQADRE RNYHVFYNLL TFEDLVAELQ MGPPSNYAYL IPHIPAAPNA AGAAPHLSAM
     PKSSSQSNFL NVNSGQPAPN RRSSMRRTSD AGPLIDDVGD GIKLRASLKT LEFTNEEVSD
     LFRVVFGVLL IGNVNLVAGE SSNMESTAIR NPVLLDMISK VLGLSQAHLK ALMTEQVSRF
     STGEVVTRTM SVQQALTTRD SIAKALYACI FHWVANRINR VIKGALGTDR PGGNSSSSTS
     AAELDVNALP AGCTAINVLD IFGFENFAHN SFEQLCINFA NEQLHQFFST YMFKVEQAVY
     VEEQINWEQM SFPDNQPCLD LIGHAKLSIL SLADEECIMP KATDLTLMEK ITKHNSTHPF
     FKAKANKLFG VRHYAGLVFY DPQGILVKNN DSLGEEALNL LRQSKKPLIG DMINLYYGPG
     KSSTAGKRKT IGTQFRDSLK QLMTSLSACN PFFVRCIKPN ISITPGLFEE AIVLEQLKYL
     GLLETVKIRK HGFPFRYKFD EFVARYRILL PRPPKPATSA TYGLGRTATK APSTPAPKPL
     DSRTLTQQLL DSLGKTVPSK SKGGAAAAPQ SLYKMGKTRV FLPLEYEMNL EQLLELAKVT
     CARRIQRTFR KWFHTRKLNV KARAIQRFYR TYRARRYFLK ARAIAKALQP VARGYIARVD
     ANKLRTAKRI EREERLRRER EEEERRKAEL AALERETKER QEAERRRIAE EEAERQRVEA
     ERLAEERRLR EQEEEKERLE RMRIAVEQAE RERIEREKID MLAAKERHQQ SNATASMAAR
     SFQDLSKEVD NDARANPNDE EAPLTSGNDG ASSGDLLSPS SLAAAAAAAA TSRMLASPVH
     ALPPVLESCA GYQIEGPSLV RARRGAAFIE VTRDNRWWKH FFYQKEHITV AAKHESLGTV
     LVSIVARSAE DIVSTAATDP ATYRAIVWTK LGFGLASFSP PDQDYSEAAG EIVKGKKKQY
     RAHELMDMAV DRFGHTLGDK WKLRENCFQV RNSDCDDKLL RLEEDNHKFY YPQHYKFGVL
     LMREGQTDET LLFSNCNDGR AGEPPRCPSF DAFLDLIGTK VRLQGFDKFR GGLDVKTDLT
     GTHSYAATRD AGPSTDEIMF HVSSMLPFAR DQPQQPERKR HIGNDVCLVV FNDGTTPYAP
     QTVKSHFIHV LIVVHLVSAA SEDGSVPAQY RVGVAYKDTV SEFSPPITHE LWAHGPELRE
     FLINKLINGQ RAALKCESFQ EPFRKYRSSV LDQLYHVAAE QRGEKAWRSR ASKQTVKTHL
     GSIRKFNSMD SDDLHALRLL RYEQDERKAA EKDFAEAAKK AKGGSLFLSG KRSSSATKLQ
     LENRFSSVTE ATTSSAPSSP VAVPRRGRAT TMVGAPSPLA LEGGPISPTS PTSPQSEKKR
     WRLLTSLRGT PKSPDGSSPV EPLSPVDTNF PDANTTLSSS PPIVNKQVAQ LRQQEDM
//
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