ID I3JH43_ORENI Unreviewed; 1999 AA.
AC I3JH43;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Myosin-10 {ECO:0000313|Ensembl:ENSONIP00000008186.2};
GN Name=LOC100690391 {ECO:0000313|Ensembl:ENSONIP00000008186.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000008186.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000008186.2}
RP IDENTIFICATION.
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 STRING; 8128.ENSONIP00000008187; -.
DR Ensembl; ENSONIT00000008191.2; ENSONIP00000008186.2; ENSONIG00000006492.2.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000158808; -.
DR HOGENOM; CLU_000192_4_1_1; -.
DR TreeFam; TF333601; -.
DR Proteomes; UP000005207; Linkage group LG11.
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; cd14920; MYSc_Myh10; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
DR Gene3D; 1.20.5.370; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF76; MYOSIN-10 ISOFORM X1; 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; 3.
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:UP000005207}.
FT DOMAIN 41..91
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 95..791
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..691
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1050..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1613..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1708..1739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1952..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1074
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1999 AA; 230465 MW; 33F4AA6C15A20633 CRC64;
MSRPTGGGAN DVTRFLSSGT APGSPNSNNS MFSAASQADW AAKRLVWVPS EKQGFESASI
REERGDEVEV ELTDSQRRVT LSREEVQRMN PPRFSKVEDM ADLTCLNEAS VLHNLRERYY
SGLIYTYSGL FCVVVNPYKN LPIYTESIVE MYRGKKRHEM PPHIYAISEA AYRSMLQGES
GAGKTENTKK VIQYLAHVAS SHKGGTLGRK KEAVQGELER QLLQANPILE AFGNAKTVKN
DNSSRFGKFI RINFDVAGYI VGANIETYLL EKSRATRQAK DERTFHIFYQ LLCGASEETR
ADLLLGTADQ YRFLSGGSIP VPGQSDSENF TQTMDSMAIM GFTPEELMSM LKVISAVLQF
GNISFMKEKN HDQASMPDNT AAQKLCHLLG VNVLEFTRAI LTPRIKVGRE YVQKAQTKEQ
ADFAVEALAK ATYERLFRWL VHRINRALDR RQRQGASFIG ILDIAGFEIF QLNSFEQLCI
NYTNEKLQQL FNHTMFILEQ EEYQREGIEW NFIDFGLDLQ PCIDLIERPA NPPGVLALLD
EECWFPRATD RSFVEKLSGE QGSHPKFFKS KQPRGEADFS IIHYAGKVDY KANDWLVKNM
DPLNDNVASL LHQSSDHFVS ELWKEVDRIV GLDQVSSGES SAPVTFGAAG LKTKKGMFRT
VGQLYKESLT KLMATLRNTN PNFLRCIIPN HEKRAGKLSP HLVLDQLRCN GVLEGIRICR
QGFPNRIPFQ EFRQRYEILT PNAIPRTFMD GKQASELMIS ALELDKNLFR VGQSKVFFRA
GVLAHLEEER DLKITDTIIR FQSAARGFLS RKAFLKKQQQ LSALRVMQRN CAAYLKLRNW
QWWRLFTKVK PLLQVTRQDE EIQTREAALQ KAKEQLTRAE QDYTELDKKH AQLLEEKAVL
ADQLQAEAEL FAEAEEMRAR LASRKQELEE VLGELETRLE EEEERGVQLA NEKKKMQQNI
QDLEEQLEEE ESARQRLLLE KVTLETKVKS LETDLATAVE QRERLGKEKK QLEERLNEVT
DQLTEEEEKT KSLNKLKNKQ EAVIADLEER LKREEQGRLE QEKFKRRMES EAMEAQEQLS
DLGMLSSDLR GSLAQKEKEI TSLQGRLEEE GARRTEAQRS LREALSQVSE LKEEVENERG
MRERAEKQRR DLSEELEALR TELEDTLDST AAQQELRSRR EAELSELQRC VEEETRRHET
QLSELRVKHS AALDSLQEQL DNSKRARQSL EKAKATLEEE RQNLTSELKS LQASRSESER
GRKRADNQLQ ELSARLAQAD REREDREERM HKLQCEIESL SGNLSSSDSK SLRLAKEISS
LESQLHDARE LLQDESRQKM ALASRVRALE EEKNGLMERL EEEEERGKEL SRQIQTHSQQ
LTELRKQSEE VNSAVEAGDE IRRKLQRELD SAIQRERQKE EEKERVERQR ERLREEIEDM
TIALQRERQN CTALEKRQKK FDQCLAEEKA VSARLAEERD RAEADSREKE TRCLALSRAL
QEAQDQKEEL ERANKQLRLE MEQLVNQQDD VGKNVHELER TRRTLETEAQ NLRIQTQELE
EELSEAENSR LRLEVTLQAL KAQFEREIST NEEKGEEKRR ALSKQVRELE IQLEEERSQR
SQSVSSKKQL EAELQEAEAQ VETANRGKEE AMKQLRRLQG QMKEVLRELD EAKVTRDDVI
SQSKDSEKKI QTLEAEVLHL TEELAVSERQ KRQAQQERDE IADEMVSSSS GKNVLSEEKR
RLDARVNQLE EDLEEEQTNN ELLTERLRKT ALQVETLTVQ LQGERTLAQK AEAAREQLEK
QNKELKARLG EMEGAVRGKH RMSVAALEAK IETMEEQLEQ ERQERAIANK LMRKTEKKLK
EVMMQAEDER RHADQYREQL DKSMVRLKQL KRQLEEVEEE NSRSSAQKRK LQRELEELTD
SSQTMNREIS SLRNQLRRAA LPLSMRGRRA LVDDLSLENS DSEEPPASPT PSSGVPGTLT
PSSEHSLDPP PPYSVNNAE
//
