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Database: UniProt
Entry: A0A195CBE9_9HYME
LinkDB: A0A195CBE9_9HYME
Original site: A0A195CBE9_9HYME 
ID   A0A195CBE9_9HYME        Unreviewed;      1970 AA.
AC   A0A195CBE9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Myosin heavy chain, non-muscle {ECO:0000313|EMBL:KYM98127.1};
GN   ORFNames=ALC62_11117 {ECO:0000313|EMBL:KYM98127.1};
OS   Cyphomyrmex costatus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Cyphomyrmex.
OX   NCBI_TaxID=456900 {ECO:0000313|EMBL:KYM98127.1, ECO:0000313|Proteomes:UP000078542};
RN   [1] {ECO:0000313|EMBL:KYM98127.1, ECO:0000313|Proteomes:UP000078542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS0001 {ECO:0000313|EMBL:KYM98127.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYM98127.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Cyphomyrmex costatus WGS genome.";
RL   Submitted (MAR-2016) 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; KQ978009; KYM98127.1; -; Genomic_DNA.
DR   RefSeq; XP_018400291.1; XM_018544789.1.
DR   STRING; 456900.A0A195CBE9; -.
DR   GeneID; 108777817; -.
DR   OrthoDB; 2877572at2759; -.
DR   Proteomes; UP000078542; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProt.
DR   GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14911; MYSc_Myh2_insects_mollusks; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.250.2420; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR   Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF71; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51844; SH3_LIKE; 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000078542}.
FT   DOMAIN          35..85
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          89..783
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          661..683
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1889..1970
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1889..1927
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1939..1958
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         182..189
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1970 AA;  227069 MW;  BB0FB0F88AA3A147 CRC64;
     MADVDSRVDR SDPELRILSV DRNSFNDPAT QAEWTQKKLV WVPHETQGFV AAGIKGERGD
     EVEVEIAETG KRVLVAKDDI QKMNPPKFDK VEDMAELTCL NEASVLHNLK DRYYSGLIYT
     YSGLFCVVVN PYKRLPIYTE KIMERYKGIK RHEVPPHVFA ITDTAYRSML QDREDQSILC
     TGESGAGKTE NTKKVIQYLA YVAASKPKSN ATPSPALIIG ELEQQLLQAN PILEAFGNAK
     TVKNDNSSRF GKFIRINFDA SGYIAGANIE TYLLEKSRAI RQAKDERTFH IFYQLLAGAS
     VEQKKEFILE DPKHYPFLSN GALPVPGVDD SAEFFSTVKS MHIMGMTNED FSSIFRIVSA
     VMLFGSMQFR QERNSDQATL PDNTVAQKIS HLLGLSVTEM TKAFLKPRIK VGRDFVTKAQ
     TKEQVEFAVE AISKACYERM FRWLVNRINR SLDRTKRQGA SFIGILDMAG FEIFELNSFE
     QLCINYTNEK LQQLFNHTMF ILEQEEYQRE GIEWKFIDFG LDLQPTIDLI DKPMGIMALL
     DEECWFPKAT DKTFVEKLVG AHSVHPKFMK TDFRGVADFA IIHYAGKVDY SAAKWLMKNM
     DPLNENVVSL LQASQDPFVC HIWKDAEIVG MAQQALTDTQ FGARTRKGMF RTVSQLYKEQ
     LAKLMVTLRN TNPNFVRCII PNHEKRAGKI DAPLVLDQLR CNGVLEGIRI CRQGFPNRIP
     FQEFRQRYEL LTPNAIPKGF MDGKKACEKM IQALELDPNL YRVGQSKIFF RAGVLAHLEE
     ERDYKITDII VNFQAFCRGF LARRNYQKRL QQLNAIRIIQ RNCAAYLKLR NWQWWRLYTK
     VKPLLEVTKQ EEKLTQKEDE LKQVRDKLEL QLHSAQEYER KYQQAIEEKT MLAEQLQAEV
     ELCAEAEEMR ARLAARKQEL EEILHDLEAR IEEEEERSAA LTQEKKKLQL NISDLEEQLE
     EEEAARQKLQ LEKVQCDAKI KKLEEDLALS EDTNQKLLKE KKILEERAND LSQTLAEEEE
     KAKHLSKLKA KHEATIADLE ERLLKDHQQR QEVDRSKRKV ETEVSDLKEQ LAERKTQVEE
     MQLQLGKREE ELNQVMAKMD EEGAAKAQAQ KALRELESQL AELQEDLEAE KAARGKAEKQ
     KRDLNEELEA LKNELLDSLD TTAAQQELRS KREQELATLK KNLEEETSLH EATLADMRHK
     HTQELTALNE QMDALKKTKA VLEKAKGSLE AENADLATEL RSVSASRQES DRRRKQAEQQ
     LAEVNAKLAE VERNKQELVE KVTKLQQEAE SVMQQLETAE LKASAALKAS ATCESQFTEL
     QQQLEEETRQ KLALSSKLRA LESEKESLHD QLEEEEEAKR ALDKQLLSLN IQLAEAKKRA
     DDEAEAAVAL EEARKRCTKD IEGLQRQVEE LQAANDKLDK SKKKIQAELE DSIIELEAQR
     AKVLELEKKQ KNFDKVLAEE KAVSEQYAEQ RDAAEREARE KETRVLSLTR ELDELNEKVE
     ELERGRRGLQ SELDELVNNQ GTADKNVHEL EKAKRSLESQ LQEQKSQVEE LEDELQFTED
     AKLRLEVNMQ ALRAQFERDL QTKEEQAEEK RRGLVKQLRD LEAELEDERK QRAAAIAARK
     KMEADYKDIE QQLEMHNKVK EDALKQLKKL QTQIKDCTRE TEEARAARDE LAAASKETER
     KVKSLEADLL QLTEDFASSE RARRTAENER DELQEEVNNN ANKGTLMLDE KRRLEARIAT
     LEEELEEEQS NAEIVMDRAR KGQIVIEQLT TDLATERSTT QKLESHKMLL ERQNKELKAK
     LTELETAQRA KTKATIQQLE SKINNLDEQL ETEAKERFAQ QKINRKLEKK LKELSLQLED
     ERRNSDQYKE QAEKVNVRMK ALKRQLDEAE EEISRHKTMK RKAQREMDDI TESHEELMRE
     LTHLKNKLRR GGPPISLSST RLKRGSVQTG GSGDDSTTQD ESIDGEENAN
//
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