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Database: UniProt
Entry: E6ZIC7_DICLA
LinkDB: E6ZIC7_DICLA
Original site: E6ZIC7_DICLA 
ID   E6ZIC7_DICLA            Unreviewed;      1975 AA.
AC   E6ZIC7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   22-FEB-2023, entry version 49.
DE   SubName: Full=Slow myosin heavy chain 2 {ECO:0000313|EMBL:CBN81811.1};
GN   Name=SMYHC2 {ECO:0000313|EMBL:CBN81811.1};
GN   ORFNames=DLA_XVIII00690 {ECO:0000313|EMBL:CBN81811.1};
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489 {ECO:0000313|EMBL:CBN81811.1};
RN   [1] {ECO:0000313|EMBL:CBN81811.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kuhl H., Tine M., Hecht J., Knaust F., Reinhardt R.;
RT   "Analysis of single nucleotide polymorphisms in three chromosomes of
RT   European sea bass Dicentrarchus labrax.";
RL   Comp. Biochem. Physiol. Part D Genomics Proteomics 6:70-75(2011).
RN   [2] {ECO:0000313|EMBL:CBN81811.1}
RP   NUCLEOTIDE SEQUENCE.
RX   DOI=10.1016/j.ygeno.2011.06.004;
RA   Kuhl H., Tine M., Beck A., Timmermann B., Kodira C., Reinhardt R.;
RT   "Directed sequencing and annotation of three Dicentrarchus labrax L.
RT   chromosomes by applying Sanger- and pyrosequencing technologies on pooled
RT   DNA of comparatively mapped BAC clones.";
RL   Genomics 0:0-0(2011).
RN   [3] {ECO:0000313|EMBL:CBN81811.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tine M., Kuhl H., Beck A., Bargelloni L., Reinhardt R.;
RT   "Comparative analysis of intronless genes in teleost fish genomes: Insights
RT   into their evolution and molecular function.";
RL   Mar. Genomics 4:109-119(2011).
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; FQ310508; CBN81811.1; -; Genomic_DNA.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd01377; MYSc_class_II; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
DR   Gene3D; 1.20.5.370; -; 4.
DR   Gene3D; 1.20.5.4820; -; 1.
DR   Gene3D; 1.20.58.530; -; 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   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   InterPro; IPR014751; XRCC4-like_C.
DR   PANTHER; PTHR45615:SF15; MYOSIN HEAVY CHAIN 7-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; 4.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57997; Tropomyosin; 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};
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}.
FT   DOMAIN          33..82
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          86..775
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          659..681
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          839..1266
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1295..1920
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         179..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1975 AA;  226994 MW;  5AF3F2A10BCD03A6 CRC64;
     MSGDALMAEF GAAATFLRKT DKERLEAQTR PFDIKRQCFV PDPDVEYVKA TVTSRDGDKV
     TVDTEFGKTV THKEADIHPQ NPPKFDKIED MAMFTFLHEP AVLFNLKERY AAWMIYTYSG
     LFCVTVNPYK WLPVYDQSVV NAYRGKKRSE APPHIFSISD NAYQYMLADR ENQSVLITGE
     SGAGKTVNTK RVIQYFASIA AVSGKKDAAQ EKKGTLEDQI IQANPALEAF GNAKTIRNDN
     SSRFGKFIRI HFGVSGKLSS ADIETYLLEK SRVTYQLKAE RDYHIFYQIL SQKKPELLEM
     LLITNNPYDY AFISQGETTV ASIDDADELM ATDDAFDVLG FTQEEKNGIY KLTGAIMHHG
     NMKFKQKQRE EQAEPDGTED VDKVAYLMGL NSADLIKGLC HPRVKVGNEW VTKGQNVQQV
     YYSIGALSKS VYEKMFLWMV VRINQSLDTK QPRQHFIGVL DIAGFEIFDF NTFEQLCINY
     TNEKLQQFFN HHMFVLEQEE YKKEGIVWEF IDFGMDLAAC IELIEKPMGI MSILEEECMF
     PKASDATFKA KLYDNHLGKS PNFQKPRVVK GRPEAHFSLG HYAGIVDYNI GNWLVKNKDP
     LNETVVGLYQ KSNLKLLGVL FAGYAGAESA QDAGGKGGKG AKKKGSSFQT VSALHRENLN
     KLMTNLRSTH PHFVRCIIPN ETKTPGAMEN PLVMHQLRCN GVLEGIRICR KGFPNRIQYR
     ILNPNAIPEG QFIDNKKAAE KLLGSLDIDH EQYKLGHTKV FFKAGLLGVL EEMRDDRLAL
     IITGIQARAR GLLARIEFQK IVERRDALLV IQWNVRAFMG VKNWPWMKMY FKIKPLLKSA
     ENEKEMANMK EEFTKLKEAY AKSEARRKEL EEKMVTLLQE KNDLQLQVQS EQDNLTDAEE
     RCEGLIKSKI QLEAKSKELT ERLEDEEEMN AELTAKKRKL EDECSELKKD IDDLELTLAK
     VEKEKHATEN KVKNLTEEMA ALDEIIAKLT KEKKALQEAH QQTLDDLQSE EDKVNTLTKA
     KAKLEQQVDD LEGSLEQEKK VRMDLERAKR KLEGDLKLTQ ESVMDLENDK QQLEEKLKKK
     DFEISQQLSK IEDEQAMSAQ LQKKLKELQA RIEELEEELE AERAARAKVE KQRADLAREL
     EEISERLEEA GGATAAQIEM NKKREAEFQK MRRDLEEATL QHEATAATLR KKNADSVADL
     GEQIDNLQRV KQKLEKEKSE LRLELDDVVS NMEQIIKVKA NMEKMCRTLE DQMSEYKTKA
     EEGQRTINDF TMQKAKLQTE NGEFARQLEE KDSLVSQLTR GKQSYTQQIE DLRRQLEEEV
     KAKNALAHAV QSSRHDCDLL REQYEEEQEA KAELQRSMSK ANSEVAQWRT KYETDAIQRT
     EELEEAKKKL AQRLQDAEEA VEAANAKCSS LEKTKHRLQG EIEDLMVDVE RSNAAAAALD
     KKQRNFDKVL AEWKQKYEES QTELESAQKE ARSLSTELFK LKNSYEESLD HLETMKRENK
     NLQEEISDLT EQLGEGGKSI HELEKIRKQL EQEKVEIQTA LEEAEGSLEH EEGKILRSQL
     ELNQVKADIE RKLAEKEEEM EQAKRNNQRV VDTLQTSLES ETRSRNEALR VKKKMEGDLN
     EMEIQLSQAN RQAAEAQKQL KGVHTHLKDS QLQLDDTLRA NDDLKENIAI VERRNNLLQA
     ELDELRSVVE QTERGRKLAE QELLDVSERV QLLHSQNTSL LNQKKKLEGD TAQLQNEVEE
     AVQECRNAEE KAKKAVTDAA MMAEELKKEQ DTCAHLERMK KNMEQTIKDL QHRLDEAEQI
     AMKGGKKQIQ KLEARVRELE TEVDMEQKRS SDSVKGIRKY ERRIKELTYQ TDEDKKNLSR
     LQDLMDKLQL KVKSYKRATE EAEEQSNANL GKLRKLQHEL EEAEERADIA ESQVNKLRAR
     SRDSGAKVSN HSEYCMQYTM SNFCDSGIKN LSNISSLYRK HMTRSESFFN NVVKL
//
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