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
//