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Database: UniProt
Entry: G0M6R5_CAEBE
LinkDB: G0M6R5_CAEBE
Original site: G0M6R5_CAEBE 
ID   G0M6R5_CAEBE            Unreviewed;      2570 AA.
AC   G0M6R5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=CBN-HUM-4 protein {ECO:0000313|EMBL:EGT30557.1};
GN   Name=Cbn-hum-4 {ECO:0000313|EMBL:EGT30557.1};
GN   ORFNames=CAEBREN_05244 {ECO:0000313|EMBL:EGT30557.1};
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   -!- 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; GL379786; EGT30557.1; -; Genomic_DNA.
DR   STRING; 135651.G0M6R5; -.
DR   EnsemblMetazoa; CBN05244.1; CBN05244.1; WBGene00143969.
DR   eggNOG; KOG4229; Eukaryota.
DR   HOGENOM; CLU_000192_14_0_1; -.
DR   InParanoid; G0M6R5; -.
DR   OMA; YITREST; -.
DR   Proteomes; UP000008068; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0005516; F:calmodulin binding; IEA:EnsemblMetazoa.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd14874; MYSc_Myo12; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.190; -; 1.
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; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR   Gene3D; 1.25.40.530; MyTH4 domain; 3.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR22692; MYOSIN VII, XV; 1.
DR   PANTHER; PTHR22692:SF26; MYTH4 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00784; MyTH4; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00015; IQ; 2.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00139; MyTH4; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS51016; MYTH4; 2.
DR   PROSITE; PS50002; SH3; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          1..652
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   DOMAIN          800..949
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          1963..2028
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          2093..2248
FT                   /note="MyTH4"
FT                   /evidence="ECO:0000259|PROSITE:PS51016"
FT   DOMAIN          2254..2563
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          530..552
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1046..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1339..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1536..1555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1565..1595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1686..1724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1377..1405
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1406..1422
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1690..1721
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         83..90
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   2570 AA;  295786 MW;  55AEF9CE5B35F300 CRC64;
     MENLIEIPDQ SEAGIAQNLH ERFKKGELYT KASNVLVFVN DYNKTSNQDQ QGFKKCHVTG
     MAKNALDKII SMSSNAETIV FSGESGSGKS HNAFNVFKFL TSEPKSKVTT KHSNAIESVF
     KSFGSAKTLK NDEATRFGCS MDLLYKRNIL TGLNLKYTVP LEVPRVISQK PGERNFNVFY
     EIYHGLNDEM KAKFGIKGLQ KFFYINQGNS TENIQSDVNH FKSLEDALHS LGFSDDHCIS
     IYKVISTILH IGNIYFRTKR NPNVEHDVVE IGNMSEVKWV AFLLEVDIDQ LVNFLLPKSE
     DGTTIDLNSA LDNRDSFAML VYEELFKWIL SRIGLHLKCP LHTGVISIID QYGFEKYNNN
     GVEEFLINSV NERLENLFVK HNFHDPLVDY AKDGITVDYK VPNSIENGKT VELLFKKPYG
     LLPLLTDECK FPKGSHESYL EHCNLNHTDR SSYGKARSKE RMEFGVRHCI GTTWYTVTDF
     FSRNKRLVSL AAVKLLRSSK NPIIGLLVES YSANTNDMIV SQAQFILRGA QEIAEKINGS
     HAHFVRCIKS NNERQPKKFD IPLVNRQIKN LLLAELLSFR LQGYPVRMSK TTFARKYRCL
     LPGDIAMCQN EKEIIQDILQ GQGVKYENDF KIGTEYVFLR ERLADRYENQ QNKICSEAAI
     VIQKNLKSFV AQKIYKRKRA AIIKLQAGLR GWKARKDYIA KREEMFKAIG RTMKRNKRLD
     AYHQALGGDG SNQLQHTLVG YIDINEDAKK ALERPTSDSE ATETLTQYLT VPVKNFLPNM
     KSISLEEYAE ENFKGHLLEP RREPIMTPFL HKESEFDFRL SVEIFKMILK YMNDRKLSRK
     QREDLGRYIV QQGISNPCQR DEILVQIINQ IHKNPDKTAT DHGWKLVHMA ISVFPPTENI
     IPMLIGFFNQ EAAPLREQLF STLQRRLKIY DSEIARELPP SNLELQATPN IPNTIAEINC
     YDGLSYDLHL SPWSTTSELA ERILKQRGVG IALGWTVEVE TPNRVFVPTG NHFIHDVFSQ
     IEGSKIDTET PHKIFFNFPP EKLVKKAPAE QKPVVEPIEE TATPKLPRHY PTPEEWSKQP
     PRVESRNTPQ DHQKQDDESD ESLLREYNEE AGYAYTLPRK NKAKQQDSEG NETSESEDDV
     GDDADNRVEY ESVRPQENMK STETIQDHSH ILKSPILPRK TYSRNEHHEE YTPMNFAPPP
     TFTYPQQMPM MQYVPVMMTP SMIPGQQIAM IPQQMMMQPQ FSYVPQYPQI PQYRPPEPIL
     SPQSVRSDVP PMMAPVMYDG HESTRSRDFR KMKRGEVPSQ YSTIRNMPVP EHGKDVDQFL
     DAVFDQCLSK DERRAAEFNS QQLASTIKGG RVRPEGYYEP PQQTYSPVPP RYPTLRRVDD
     SPVRSRAKSL PRILSPRHDH YIRNTHSRNS YSNESTSSDD QMNYRTRSRE RSLPRFHSNN
     GYNYDPNQPV YMMPVQMNGH GEMILLSPVG SEQRAQIKNG THDRSRRHHA TSGVERYMAK
     RSPSVDMLKP HKSRRTPDIM LEQTHVRPHL AQSPVGRHTG RIEEFSLPRG DSRTREKMEN
     PLLARQYQRT NPYQNGYVVP PPPSSYRSPS PAPTAGDRKV NFLEFFVSQN FIQGLSRLPQ
     EAYVEPAVKN TKNNSEYLSP HRFNLDEQKA VIRHEKETAK NALNMLSNQL RKLPPPVDNV
     RLIRPVTPSQ RPITPAPVPS EPQIVQTPSP PPQPTPPQPA PIRQEWVVRD SVERKPETQE
     RIRGSFIKEP LVPQPPRAPV VAEKPAVKFV KAPWKLTIRK EMFYPGEVLN DIQIIDQVFA
     QIVEDCKKSY PYRIRLEDRK QVEDILRHYE VPPSDLNNQS NIHPDVKVAI IEKARLWPLY
     FNQIYEVIEK RPDESVSIIF AISEHGIRLL VHTPHDLEHP LKIQDYFPFE TIADVSLEAN
     DILSVHVRHE NEENAYSAVR IKTNQAPQIK KTLEKCLSGG VVPKRKFVRA LEDYVTSEVN
     HLSFKQGDVI ELLPVPEAET PPVGNWLYGR IENRFGFLLA QYVDSANGDM VPPIRYENSA
     GRDERVKFFD DEVPFSSERY TMLDFATKYF RKPKDKKKQE EWAWEDISQA VRYSDRGISQ
     SLLADLGSEE SKYAVETFHS IMKFMGDEPL KKSESMTDVV FKVLIICHRH PTLRDEVYCQ
     LIKQTTSNTS TKPNSALRAW RLLTIITAYF PSSLTLKPYI LQYLGDNADD WQRPYHGTAR
     ICQTNMIQTF KYGGRKVLLN ALEVQQITDG CQLRRQAFYI SREHSVSQTL RPITVAEEMI
     QELCSLLNVR SLHEQQEFSL CYTIGKDKRV NYCKNDNYLM DIITESEHKK LPFQFHLKRT
     VWVHPLRYDN AAYIDSMFDQ VIDDYLRGSL ISTNSLGQLT AATTEEIIKL AAYLFLLLPD
     NPKGLTAKIL PQIVPKSVIE PKHRHQEEMV TRINRQLKMF GGRMRPAEAK SHFLELLSTW
     PSFGVLHYRL KSVVENGNQL PEVILTINKS GIQLLQPKSK EVFKQRNYDQ IESVESIRKT
     AYKIVRLVIN TPEGEETLDI KTDEADEISH LIGQYMFVTC GIEDRGSTEL
//
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