ID A0A3B3RT71_9TELE Unreviewed; 1984 AA.
AC A0A3B3RT71;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Myosin-10 {ECO:0000313|Ensembl:ENSPKIP00000021704.1};
GN Name=MYH10 {ECO:0000313|Ensembl:ENSPKIP00000021704.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021704.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000021704.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; ENSPKIT00000002345.1; ENSPKIP00000021704.1; ENSPKIG00000005708.1.
DR GeneTree; ENSGT00940000155159; -.
DR Proteomes; UP000261540; Unplaced.
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 Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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 Gene3D; 4.10.270.10; Myosin, subunit A; 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: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; 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}.
FT DOMAIN 30..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..786
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 664..686
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1016..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1984 AA; 229815 MW; B465D171DA939385 CRC64;
MAQRGQEDAE RYLFVDRAVV YNPATQADWT AKKLVWVPSE RHGFEAASVR EERGDEAVVV
ELAENGKRAV VSKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKERYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQGKM VRTSSSTLLN
GESGAGKTEN TKKVIQYLAH VASSHKGRKD HNIPGELERQ LLQANPILES FGNAKTVKND
NSSRFGKFIR INFDVTGYIV GANIETYLLE KSRAVRQAKD ERTFHIFYQL LAGAGEHLKS
DLLLENFTSY RFLSNGNIPI PGQQDKDIFQ DTMEAMRIMS FSHDEITAML RVVSSVLHFG
NIVFKKERNT DQASMPENTA AQKLCHLLGM NVMEFTRAIL TPRIKVGRDY VQKAQTKEQA
DFAVEALGKA TYERLFRWLV HRINKALDKT KRQGASFIGI LDIAGFEIFE LNSFEQLCIN
YTNEKLQQLF NHTMFILEQE EYQREGIEWS FIDFGLDLQP CIDLIERPTN PPGILALLDE
ECWFPKATDK SFVEKVGQEQ GTHPKFHKPK KLKDEADFCI MHYAGRVDYK ADEWLMKNMD
PLNDNVATLL HQSTDKFVAE LWKDVDRIVS LDQVAGMNET AFGSAYKTKK GMFRTVGQLY
KESLTKLMAT LRNTNPNFVR CIIPNHEKRA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN
RIVFQEFRQR YEILTPNAIP KGFMDGKQAC ERMIQALELD PNLFRIGQSK IFFRAGVLAH
LEEERDLKIT DIIIYFQAVC RGYLARKAFA KKQQQLSALR VLQRNCAAYL KLRHWQWWRL
FTKVKPLLQV TRQEEEMQAK DEELIKVKEK QNKVETELVE MERKHQQLLE EKNILAEQLQ
AETELCAEAE EMRARLAAKK QELEEILHDL EARVEEEEER NQGMQNEKKK MQVHIQDLEE
QLDEEEAARQ KLQLEKVTAE AKMKKMEEDI LLLEDQNSKF MKEKKLLEDR VNEITSRLTE
EEEKAKNLGK TKNKQEMMMV DLEERLKKEE KTRQELEKAK RKLDTETSDL QDQITELQAQ
IDELKLQLAK KEEELQAAQA RSDEEAAQKN NALKQVRELQ AQLAELQEDL EAEKLARNKA
EKLKRDLSEE LEALKTELED TLDTTAAQQE LRTKREQEVA ELKKAIDEET KNHESLIQDM
RQRHSTALEE LSEQLEQAKR FKSNLEKSKQ TQENTNKELA NEVRGLQQTK SDSEHKRKKL
EAQVQEVTAR VTEVERSKVE LADRSHKLQA ELDNVSMFLE DAEKKGIKLG KDVASLESQL
QDTQELLQEE TRQKLNLSSR VRQLEEEKSS LQEQQEEEEE ARRNLEKQLT TVQAQMTETK
KKLEDDVGTM EGLEEVKRKL QKDMENTAQR LEEKAIAFDK LEKTKTRLQQ ELDDLTVDLD
HQRQTVSNLE KKQKKFDQML AEEKNVSARF AEERDRAEAE AREKETRALA LTRALDEALE
SKEELERLNK QLRAEMEDLM SSKDDVGKNV HELEKSKRGM EQQLEEMKTQ LEELEDELQA
TEDAKLRLEV NMQAMKAQFE RDLQGKDEMG EEKKRQLVKQ VRELEAELED ERKQKVLAVA
AKKKMEMDLK DLEAQIEAAN KARDEAIKQL RKLQAQMKDY QRELDEARAS RDEIFAQSKE
NEKKLKNLEA EILQLQEDLA ASERARRHAE QERDEFADEI ANSVSGKSAL LEEKRKLEAR
IVQLEEELEE EQSNMELLND RFRKTTMQVD TLSMELAGER SSAQKSESAR QQLERQNKEL
KLKLQELEGA VKSKYKAAIA ALEAKIAQLE EQLEQEAKER AAANKTVRRT EKKLKEVFMQ
VEDERRHADQ YKEQMEKANS RMKQLKRQLE EAEEEAQRAN ANRRKLQREL EDATESADAM
NREVNALKSR LRRGGPISFP SGRTGRRVTQ VEGASLELSD DDGTTSDSKA NEVNEASTPS
PQGE
//
