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Database: UniProt
Entry: A0A026WFD8_OOCBI
LinkDB: A0A026WFD8_OOCBI
Original site: A0A026WFD8_OOCBI 
ID   A0A026WFD8_OOCBI        Unreviewed;      1144 AA.
AC   A0A026WFD8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Myosin-I heavy chain {ECO:0000313|EMBL:EZA54830.1};
GN   ORFNames=X777_05115 {ECO:0000313|EMBL:EZA54830.1};
OS   Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Dorylinae; Ooceraea.
OX   NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA54830.1, ECO:0000313|Proteomes:UP000053097};
RN   [1] {ECO:0000313|EMBL:EZA54830.1, ECO:0000313|Proteomes:UP000053097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA   Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA   Zhang G., Kronauer D.J.;
RT   "The genome of the clonal raider ant Cerapachys biroi.";
RL   Curr. Biol. 24:451-458(2014).
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; KK107238; EZA54830.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A026WFD8; -.
DR   STRING; 2015173.A0A026WFD8; -.
DR   OMA; MHLDRGV; -.
DR   Proteomes; UP000053097; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; cd14881; MYSc_Myo20; 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; 2.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 2.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036029; MYSc_Myo20.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140:SF498; DACHS, ISOFORM E; 1.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 2.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 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};
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:UP000053097}.
FT   DOMAIN          216..956
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          60..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..849
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          990..1042
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1058..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1026
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         304..311
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1144 AA;  124876 MW;  98B6BD7770540BD2 CRC64;
     MATLGLSKVF ILDKYFTELQ KFWETEKKLQ DASSSNEAVH LQQRLRSLST ELVTLRNRLH
     VSQPANASGP ASATSGPLSK SSEKGGAPAS PAPAVPPRTT LPPGGAVSHG IGHPAGHTLT
     ASAIVHPHVN HAGANALSHN STATNNLISE LDPSKQRHNG VSDDGIVSCV TALGCLRSPP
     ISSIIADVKN ARSNQSQHRC LPKVTAPSAG PATSTAFDDL IHLPGPLTED AVLKCLQARF
     CAKQYHTNVG PILVCVNPYT DVGNPLTLTS TRSVPLAPQL NKVVQEAVRQ QSETGYPQAI
     ILSGTSGSGK TYASMLLLRQ LFDVAGGGPE TDAFKHLAAA FTVLRSLGSA KTATNSESSR
     IGHFIEVQVT DGALYRTKIH CYFLDQTRVI RPLSDEKNYH IFYQMLAGLS HDERVKLSLE
     GYNLKNLRYL QHGDTRQDEA EDAVRFQAWK ACLGVLGIPF LDVVRVLAAV LILGNVGFTD
     GPGVEVGVLG ENELSSVATL LGVPPPALLR GLTSRTHNAR GQLVKSVCDA NMSNMTRDSL
     AKALYCRTVA TIVRRANSLK RLGSTLGTLS SDSNESVHNQ AEVTSQHAST IGSSAGGTGS
     RSMTALNNAV RHATDGFIGI LDMFGFEDPK PSQLEHLCIN LCAETMQHFY NTHIFKSSIE
     SCRDEGIRCD VEVDYVDNVP CIDLISSLRT GLLSMLDVEG SIHGTAESYV SKVKVQHKQN
     PRLFEPRTVD CRSFGIQHFA GRVTYDASDF LDTNKDVVPD DLVAVFYKHT CSFGFATHLF
     GSELKALYAS DTVPRGVSFR ISPTSHTDLL NGDEPISTLT QDFHTRLDNL LRTLVHARPH
     FVRCIRSNST ETPMHLDRGV TMRQIRSLQV LETVNLMAGG YPHRMRFKAF NARYRLIAPF
     KQLRRAEEQA VEDTKLILQN AQQLKSKFGA STSWALGKRH IFLSEGIRQQ LENLRAETRR
     RAATVIQARW RGWRVRKRWS LRRTTLGVTS GIGQKKSQQP PTRANTGTVQ RNVTAGTGTG
     TGTRPRPQPI AGTPPPDPSE KCADQKMIQQ TCTLFGLDLE RPPPVPPSRS YTVTGNTKLG
     YPQTRIMKMP FPEEGEGEVV LLKGETVLVV GASPRRGHLL VEHNNTTLHV PYQFMELKPC
     NINV
//
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