ID A0A3Q1G966_9TELE Unreviewed; 2018 AA.
AC A0A3Q1G966;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Myosin-10 {ECO:0000313|Ensembl:ENSAPOP00000027101.1};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000027101.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000027101.1}
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; 80966.ENSAPOP00000027101; -.
DR Ensembl; ENSAPOT00000002036.1; ENSAPOP00000027101.1; ENSAPOG00000011552.1.
DR GeneTree; ENSGT00940000155159; -.
DR InParanoid; A0A3Q1G966; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000257200; 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:0070650; P:actin filament bundle distribution; IEA:Ensembl.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
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 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; 7.
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:UP000257200}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..825
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 703..725
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 973..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1735..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1817..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1903..2018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1970..1988
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 2018 AA; 234420 MW; DAFFDCED76B1D0C5 CRC64;
MSQRSGQEDP ERYLFVDRAV VYNPAAQADW TAKRLIWIPS ERHGFEAASI REERGDEVVV
ELAENGKKAV VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PPESPKPVKL QAQNAVSGPL FYGELERQLL
QANPILESFG NAKTVKNDNS SRFGKFIRIN FDVTGYIVGA NIETYLLEKS RAIRQAKDER
TFHIFYQLLA GAGEHLKSDL LLEGFNNYRF LSNGNIPIPG QQDKDNFHET MEAMHIMSFA
HEEILAMLKV VSSVLQFGNI VFKKERNTDQ ASMPDNTAAQ KLCHLLGMNV MEFTRAILSP
RIKVGRDYVQ KAQTKEQADF AVEALAKATY ERLFRWLVHR INKALDRTKR QGASFIGILD
IAGFEIFQLN SFEQLCINYT NEKLQQLFNH TMFILEQEEY QREGIEWSFI DFGLDLQPCI
DLIERPANPP GVLALLDEEC WFPKATDKTF VDKLIQEQGT HTKFQKPRQL KDKADFCIIH
YAGKVDYKAD EWLMKNMDPL NDNVATLLHQ STDKFVAELW KDEIQTIQRA SFYDNVTSLD
EPAVDRIVGL DQVAGMNETA FGATYKTKKG MFRTVGQLYK ESLTKLMATL RNTNPNFVRC
IIPNHEKRAG KLEPHLVLDQ LRCNGVLEGI RICRQGFPNR IVFQEFRQRY EILTPNAIPK
GFMDGKQACE RMIHALELDP NLFRIGQSKI FFRTGVLAHL EEERDLKITD IIIYFQSVCR
GYLARKAFAK KQQQLSALKV LQRNCAAYLK LRHWQWWRLF TKVKPLLQVT RQEEELQAKD
EELIKVKERQ LKVENEMVEM ERKHQQLVEE KNILAEQLHA ETELFAEAEE MRVRLLSRKQ
ELEEILHDLE SRVEEEEERN QSLQNEKKKM QSHIQDLEEQ LDEEEAARQK LQLDKVTAEA
KIKKMEEDIL LLEDQNSKFL KEKKLLEDRI VEMTSQLTEE EEKAKNLGKV KNKQEMMMVD
LEERLKKEEK TRQELEKAKR KLDAETTDLQ DQIAELQAQI EELKIQLAKK EEELQAALAR
SDEETVQKNN ALKQVRELQA QLAELQEDLE SEKMCRSKAE KLKRDLSEEL EALKTELEDT
LDTTAAQQEL RTKREQEVAE LKKAIDEETR NHEAQIQDMR QRHATALEEL SEQLDQAKRF
KANLEKNKQC LESDNKEMAC EVKSLQQAKT ESEHKRKKLE AQMQEFMTRA TEVERAKGEL
SERSHKLQTE LDNVSALLEE AEKKSVKLAK EVDNLNSKLQ DSEELRQEET RQKLNLSSQI
RQLELEKNTL LEQQEEDEEA RRSLEKQLQT VQAQVFETKK KLEDDVGAIE GLEEVKRKLQ
KDLELTSQRL EEKTMAMDKM EKTKNRLQQE LDDQLVDLDQ QRQIVSNLEK KQKKFDQMLA
EEKTISARYA EERDRAEAEA REKETKALSM ARALEEALEA KEELERFNKQ LRAEMEDLMS
SKDDVGKNVH ELEKSKRTLE QQVEEMRTQL EELEDELQAT EDAKLRLEVN MQAMKAQFDR
DLQARDEQGE EKKRALVKQV REMEAELEDE RKQRTLAIAA KKKLEMDLNE LEGQIEAANK
GRDEAIKQLR KLQAQMKDYQ RELEEARASR DEIFTQSKEN EKKLKSLEAE ILQLQEDHAA
SERARRHAEQ ERDELADEIS NSASGKSSLL DEKRRLEARI TQLEEELEEE QGNMELLNDR
FRKTTMQVDS LNTELAAERN TAQKSENARQ QMERQNKELK AKLAELEGAV KSKFKASITA
LEAKILQLEE QLEQEVKERA AANKIVRRTE KKLKEVMMQV EDERRHADQY KEQMEKANSR
MKQLKRQLEE AEEEATRANA SRRKLQRELD DATEASEGLT REVNSLKNRL RRGPVSSFSS
SRSGRRNLNL DGASVDMSDD DADSRAGDFN ETQTSNAE
//
