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Database: UniProt
Entry: G3U2K0_LOXAF
LinkDB: G3U2K0_LOXAF
Original site: G3U2K0_LOXAF 
ID   G3U2K0_LOXAF            Unreviewed;      1987 AA.
AC   G3U2K0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Myosin heavy chain 10 {ECO:0000313|Ensembl:ENSLAFP00000022058.1};
GN   Name=MYH10 {ECO:0000313|Ensembl:ENSLAFP00000022058.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022058.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000022058.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022058.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000022058.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022058.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   Ensembl; ENSLAFT00000037088.1; ENSLAFP00000022058.1; ENSLAFG00000005826.4.
DR   GeneTree; ENSGT00940000155159; -.
DR   HOGENOM; CLU_000192_4_4_1; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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   CDD; cd14920; MYSc_Myh10; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 1.20.5.340; -; 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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF24; MYOSIN-10; 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; 6.
DR   SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
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:UP000007646}.
FT   DOMAIN          42..92
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          96..794
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          672..694
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1138..1160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1708..1729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1885..1987
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1708..1728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1885..1926
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1961..1976
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         189..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1987 AA;  230474 MW;  8B07CF34A5D30047 CRC64;
     RGDCSWILLL TMAQRTGLED PERYLFVDRA VIYNPATQAD WTAKKLVWIP SERHGFEAAS
     IKEERGDEVM VELAENGKKA MVNKDDIQKM NPPKFSKVED MAELTCLNEA SVLHNLKDRY
     YSGLIYTYSG LFCVVINPYK NLPIYSENII EMYRGKKRHE MPPHIYAISE SAYRCMLQDR
     EDQSILCTGE SGAGKTENTK KVIQYLAHVA SSHKGRKDHN IPGELERQLL QANPILESFG
     NAKTVKNDNS SRFGKFIRIN FDVTGYIVGA NIETYLLEKS RAVRQAKDER TFHIFYQLLS
     GAGEHLKSDL LLEGFSNYRF LSNGYIPIPG QQDKDNFQET MEAMHIMGFS HEEILSMLKV
     VSSVLQFGNI SFKKERNTDQ ASMPENTVAQ KLCHLLGMNV MEFTRAILTP RIKVGRDYVQ
     KAQTKEQADF AVEALAKATY ERLFRWLVHR INKALDRTKR QGASFIGRVF GKRLHIFQLN
     SFEQLCINYT NEKLQQLFNH TMFILEQEEY QREGIEWNFI DFGLDLQPCI DLIERPANPP
     GVLALLDEEC WFPKATDKTF VEKLVQEQGS HSKFQKPRQL KDKADFCIIH YAGKVDYKAD
     EWLMKNMDPL NDNVATLLHQ SSDRFVAELW KDVDRIVGLD QVTGMTETAF GSAYKTKKGM
     FRTVGQLYKE SLTKLMATLR NTNPNFVRCI IPNHEKRAGK LDPHLVLDQL RCNGVLEGIR
     ICRQGFPNRI VFQEFRQRYE ILTPNAIPKG FMDGKQACER MIRALELDPN LYRIGQSKIF
     FRAGVLAHLE EERDLKITDI IIFFQAVCRG YLARKAFAKK QQQLSALKVL QRNCAAYLKL
     RHWQWWRVFT KVKPLLQVTR QEEELQAKDE ELLKVKEKQT KVEGELEEME RKHQQLLEEK
     NILAEQLQAE TELFAEAEEM RARLAAKKQE LEEILHDLES RVEEEEERNQ ILQNEKKKMQ
     AHIQDLEEQL DEEEGARQKL QLEKVTAEAK IKKMEEEILL LEDQNSKFIK EKKLMEDRIA
     ECSSQLAEEE EKAKNLAKIR NKQEVMISDL EERLKKEEKT RQELEKAKRK LDGETTDLQD
     QIAELQAQID ELKIQLAKKE EELQGALARG DDETLHKNNA LKVVRELQAQ IAELQEDFES
     EKASRNKAEK QKRDLSEELE ALKTELEDTL DTTAAQQELR TKREQEVAEL KKALEEETKN
     HEAQIQDMRQ RHATALEELS EQLEQAKRFK ANLEKNKQGL ETDNKELACE VKVLQQVKAE
     SEHKRKKLDA QVQELHAKVS EGDRLRVELA EKANKLQNEL DNVSTLLEEA EKKGVKFAKD
     AAGLESQLQD TQELLQEETR QKLNLSSRIR QLEEEKNSLQ EQQEEEEEAR KNLEKQVLAL
     QSQLTDTKKK VDDDLGTIES LEEAKKKLLK DVEALSQRLE EKALAYDKLE KTKNRLQQEL
     DDLTVDLDHQ RQIVSNLEKK QKKFDQLLAE EKNISARYAE ERDRAEAEAR EKETKALSLA
     RALEEALEAK EEFERQNKQL RADMEDLMSS KDDVGKNVHE LEKSKRALEQ QVEEMRTQLE
     ELEDELQATE DAKLRLEVNM QAMKAQFERD LQTRDEQNEE KKRLLIKQVR ELEAELEDER
     KQRALAVASK KKMEIDLKDL EAQIEAANKA RDEVIKQLRK LQAQMKDYQR ELEEARASRD
     EIFAQSKESE KKLKSLEAEI LQLQEELASS ERARRHAEQE RDELADEIAN SASGKSALLD
     EKRRLEARIA QLEEELEEEQ SNMELLNDRF RKTTLQVDTL NTELAAERSA AQKSDNARQQ
     LERQNKELKA KLQELEGTVK SKFKATISAL EAKIGQLEEQ LEQEAKERAA ANKLVRRTEK
     KLKEIFMQVE DERRHADQYK EQMEKANARM KQLKRQLEEA EEEATRANAS RRKLQRELDD
     ATEANEGLSR EVSTLKNRLR RGGPISFSSS RSGRRQLHIE GASLELSDDD TESKTSDVNE
     TQPPPSE
//
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