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Database: UniProt
Entry: A0A1D2NMM5_ORCCI
LinkDB: A0A1D2NMM5_ORCCI
Original site: A0A1D2NMM5_ORCCI 
ID   A0A1D2NMM5_ORCCI        Unreviewed;      1952 AA.
AC   A0A1D2NMM5;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Myosin heavy chain, non-muscle {ECO:0000313|EMBL:ODN06196.1};
GN   ORFNames=Ocin01_00497 {ECO:0000313|EMBL:ODN06196.1};
OS   Orchesella cincta (Springtail) (Podura cincta).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX   NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN06196.1, ECO:0000313|Proteomes:UP000094527};
RN   [1] {ECO:0000313|EMBL:ODN06196.1, ECO:0000313|Proteomes:UP000094527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Mixed pool {ECO:0000313|EMBL:ODN06196.1};
RX   PubMed=27289101; DOI=10.1093/gbe/evw134;
RA   Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA   Smit S., van Straalen N.M., Roelofs D.;
RT   "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT   in the Genome of the Collembolan Orchesella cincta.";
RL   Genome Biol. Evol. 8:2106-2117(2016).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC       ECO:0000256|PROSITE-ProRule:PRU00782}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ODN06196.1}.
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DR   EMBL; LJIJ01000009; ODN06196.1; -; Genomic_DNA.
DR   STRING; 48709.A0A1D2NMM5; -.
DR   OMA; QRAMDIE; -.
DR   OrthoDB; 2877572at2759; -.
DR   Proteomes; UP000094527; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProt.
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   Gene3D; 1.20.5.340; -; 3.
DR   Gene3D; 1.20.5.4820; -; 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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
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; PF00063; Myosin_head; 2.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 3.
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|PROSITE-ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000094527}.
FT   DOMAIN          1..552
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          430..452
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1462..1495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1630..1718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1887..1916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1723..1771
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1796..1830
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1462..1483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1657..1681
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1682..1713
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         74..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1952 AA;  223598 MW;  3426939E5CD52D5A CRC64;
     MFICVVMYCS LTYSGLFCVV VNPYKRLPIY TEKIMELYKG KKRHEVPPHV FAITDTAYRS
     MLQDREDQSI LCTGESGAGK TENTKKVIQY LAYVAASKPR GSGTHHSTGE LEQQLLQANP
     ILEAFGNAKT VKNDNSSRFG KFIRINFDTS GYIAGANIET YLLEKSRAIR QAKDERSFHI
     FYQLLAGATE PQRKEYVVEN AANYTFLTNG GLPVPGVDDI AEFQSTVNAM CIMGMQPEDL
     SSIFRVVSSV LHFGNMQFKQ ERNSDQATLP DNTVAQKIAH LLGLSVTDMT RAFLKPRIKV
     GRDHVTKAQT KEQVEFAVEA IAKATYERMF RWLVNRINRN GLPWPSRFAV VHYAGKVDYS
     ANQWLMKNMD PLNENVVQLL QAGSDPFVTL IWKDAEIVGM AQQAMSDTQF GARTRKGMFR
     TVSQLYKEQL SKLMVTLRNT NPNFVRCIIP NHEKKSGKID PPLVLDQLRC NGVLEGIRIC
     RQGFPNRIPF QEFRQRYELL TPNVIPKGFM DGKKACEKMI NALELDKNLF RIGQSKIFFR
     AGVLAHLEEE RDFKITDLIV NFQAFCRGSL ARKMYTRRVQ QLNAIRIIQR NCAAYLKLRN
     WQWWRLYTKV KPLLEVTKND EKLTQKESEL KQIQEKLVQH QEVEQEMQQK LHKAIEEKSV
     LAEQLQAETE LCAEAEEMRA RLALKKQELE EILHDMEARV EEEEERVVAL NNEKKKLQLN
     IQDLEEQLEE EEAARQKLQL EKVQCDGKIK KLEEEMVVAE DTNGKLIKEK KSLEEKNNDL
     SQALAEEEEK SKHLAKLKAK HEASIGDLEE RLKKEQQIRQ DNERTRRKIE SELQDLKEQI
     NEKRGQVEEL QLSLAKKDEE ISNLLTKIDE ESASKATAQK NLRELESQLA ELHEDLEAEK
     AARAKAERMK RDLNEELEAL KNELLDSLDT TAAQQELRTK REQELAALKK SLEDETMSHE
     QMVQDLRHKH GSEVQELMEQ FENLKKARAS LEKNKSTLEA ENADLANELK SLQGAKTENE
     RKRKTQDGLI QELQMKLAES ERSKNEMTER LSKVLAELET LSTQLEEADS KASSATKNSA
     VMENQLAETQ TSLEEETRQK LALTARLKQL ESEKEQLVEQ LEEEEESKKN MEKTLAALNQ
     TVAELKKKSE EDTADIIVLE TNQKKLLKDI ELLRAQNDEL SANCEKLEKS RKKLQQELED
     AGIDLEAQRS KVVELEKKQR NFDKILAEEK MISERFSQEK DVAEREETKL LSLNRELEEK
     DVAMEELERT KRQLQNELDE LVNSQGTADK NVHELEKHKR SLESQLTEQK TQIEELEDEL
     QLTEDAKLRL EVNMQALKTQ FERDLQAKEE AAEEKRKGLI KQLRDTEAEL EDERKNRTAA
     VNARKKLESE YNELMNQMEA NAKMKEDALK QLKKIQGQIK DYQRDAEEAR LSRDEAVAVA
     KEAEKKLKHM EAELLQLQEE LASSERARRA AESERDEYAE EVSNGGNHRT LLTDDKRRLE
     ARIQALEEEL EEEQSNSEMQ SERARKATLL NEQFSSELQV ERSNNQKIEN SRALLERQNK
     ELKQKLTELE TTQKLKAKTT IASLENKLQQ LEEQLELESK ERLAQQKAVR RQDKKIKELN
     KLRRGTATGL NLTGRLSKRG SLPTGGADDS VVSQEDSFDG EDEKSSHTSS GRVKKCQDKM
     SSHNRGSTGT RGRSNVNASR FQSGASGSGS DRVDYSTPEG KKITTLENEI AYYQAKIQQL
     FTEKDEVVQN ALKFQNLYKR AQAEAALLKQ RGDTSLKDVM ESHSAVQDVP RRVCASAASS
     QQLMEYEAKI EELQDKLKFT EERVMAVNKH AQTARADLDL EKEVSAKYKA ELMKLKVGIE
     SVLSEVNRMR VDHEGNHHVV VAVPQSPCDS SASAANRNGR AHDLDSPMSR SDSDEELEEV
     LACETPSESM LMMMNNFSED KLAALGIDLD DD
//
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