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Database: UniProt
Entry: G0NE18_CAEBE
LinkDB: G0NE18_CAEBE
Original site: G0NE18_CAEBE 
ID   G0NE18_CAEBE            Unreviewed;      1975 AA.
AC   G0NE18;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=CBN-MYO-5 protein {ECO:0000313|EMBL:EGT58642.1};
GN   Name=Cbn-myo-5 {ECO:0000313|EMBL:EGT58642.1};
GN   ORFNames=CAEBREN_05456 {ECO:0000313|EMBL:EGT58642.1};
OS   Caenorhabditis brenneri (Nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN   [1] {ECO:0000313|Proteomes:UP000008068}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG   Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA   Wilson R.K.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC       {ECO:0000256|ARBA:ARBA00004657}.
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; GL379871; EGT58642.1; -; Genomic_DNA.
DR   STRING; 135651.G0NE18; -.
DR   EnsemblMetazoa; CBN05456.1; CBN05456.1; WBGene00144181.
DR   eggNOG; KOG0161; Eukaryota.
DR   HOGENOM; CLU_000192_8_0_1; -.
DR   InParanoid; G0NE18; -.
DR   OMA; CERMAKQ; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0032982; C:myosin filament; 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; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 4.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 6.20.240.20; -; 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; 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   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 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; SM00242; MYSc; 1.
DR   SUPFAM; SSF90257; Myosin rod fragments; 5.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Muscle protein {ECO:0000256|ARBA:ARBA00023179};
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:UP000008068};
KW   Thick filament {ECO:0000256|ARBA:ARBA00022433}.
FT   DOMAIN          28..77
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          81..788
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          663..685
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          973..993
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1063
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1934..1975
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1871..1933
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        973..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1975 AA;  226833 MW;  B1FC121C595DC7A0 CRC64;
     MTHEADPGWQ FLRQSPEQLL AATTKKFDSK KNVWVADPEE GFIAAEIKSS KGDTVVVVTS
     KGVEKTIKKD DAQQMNPPKY EKTEDMANLT FLNDASVLHN LRQRYYSMMI YTYSGLFCVV
     INPYKRLPIY SESVCQMYLG KRRNEMPPHL FAVSDEAYRN MTNDRENQSM LITGESGAGK
     TENTKKVISY FAMVGASQQS KKEKSKKDKA QVSLEDQIVQ TNPVLEAFGN AKTVRNNNSS
     RFGKFIRIHF NTAGKVAGAD IEHYLLEKSR VIKQAPGERS YHIFYQIYSD AVKGLREKLF
     LTRPIKEYTF VSQAEVTIDG VDDKEEMLIT DEAFDIMKFT ATEKSELFAI TAGIMHMGEL
     KFKQRPREEQ AELEDGKEGE LACKLYCVEA EKFIGSLLKP RVKVGTEWVN KGQNLDQVNW
     AVGALAKALF ARMFKWLITR CNKTLDAQDL SRDFFIGVLD IAGFEIFDLN SFEQLWINFV
     NEKLQQFFNH HMFVLEQEEY KREGIQWEFI DFGLDLQACI ELIEKPLGIV SMLDEECIVP
     KATDLTLASK LNDQHLGKHP NFQKPKPPKG KQAEAHLAIV HYAGTVRYNV KGWLEKNKDP
     LNDTAVTVLK ANAGNQLMAD LWADYQTQED VAAAAKEGKK AVGKKKGKSA SFMTVSMMYR
     ESLNKLMHML HQTHPHFIRC IIPNELKRSG MIDANLVLNQ LTCNGVLEGI RICRKGFPNR
     MPFLDFKQRY AVLAADAAKS GKDPKDAGEK IAAALIKDGS LKPEEFQTGL TKVFFKAGVL
     AHLEELRDEA LGKIMAKFQC ACRHYLAQCE YKRKLDQKVG LIVLQRNIRA WCTLRSWAWF
     KLFGRVKPLI KGNKKNEEFE ALEKKFKVLE EEKSQEERKR KDMEAENARL EAEKQALLIQ
     LEQERDSSAE GEERSAKLLS QKADLEKQMA NLNDQLCDEE EKNASLVKQK KKIEQDNEGL
     KKTVSDLETT IKKQESEKQA KDHQIRSLQD EIQSQDDVIS KLNKEKKHQE EVNRKLLEDI
     QAEEDKVNHL NKTKAKLESS LDELEDSLER EKRGRQDCEK QKRKVEGELK IAQELIEELN
     RHKHEQEQVL KKKDAELNSL QSRLEDEQSL VAKLQRQIKE LLARIQELEE ELDSERQSRS
     KAEKARNEMQ LELEELGDRL DEAGGATQAQ IELNKKREAE LAKLRQDLED AAINAETSMA
     ALRKKHNDAV AELSDQLDTV QKMRGKLERE KNDKQREVDE LQQSADVEAK QRQNCERMAK
     QLEAQLTDIT LKSDEQARLI QELTMSKNKT HSENQDLNRQ LEDAESQLSA LNRIKQQQHN
     QMEELKRTLD QETRERQSLH SQVSNYQLEC EQLRESLEEE QDAKTDVQRQ LSKANSEIQQ
     WRAKFEGEGV SRQEELEETR RKLTHKVQEM QEQIENANQK IGTLEKAKQR LAHDLEDAQV
     DADRANSIAN SLEKKQKGFD KVLEEWRRKC EALVAEVEQS QRETRAAATE TFRLRNQLEE
     SGEQTEAVKR ENKALAQELK DIADQLGEGG KSVHDLQKMR RRLEIEKEEL QQALDEAECA
     LEAEEAKVMR AQIEVSQIRS EIEKRLQEKE EEFENTRKNH SRTIESMQVS LETESRGRAE
     LLKTKKKLEG DVNELEIALD HSNKLNVDGQ KSIKKLQDTI RELQLQVEEE QRSLNEARDH
     VSHSERRSQV LQQEKEDLAV IYEQSERARR QAELELAEVK DSVNELANSN SLLLATKRKV
     EGDLQHLQSE VEEALSDAKT SDDKAKKAIM DASKLADELR SEQEHASNLD KSKRALESQV
     KDLQMRLDEA EAAGIKGGKR QLAKLDMRIH ELETELEGES RRHGETQKVL RNKDRKCREL
     QFQVDEDKKS TERMYDLIEK LQQKIKVYKR QIEDAEALAS GNLAKYRQLQ HVVEDAQERA
     DAAENALQKM RLKGRSTSGV FGPRGLAHSM STTGVNMRRG GSRGAFLDED SFAEE
//
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