ID A0A3B4XXQ3_SERLL Unreviewed; 1939 AA.
AC A0A3B4XXQ3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Myosin-10-like {ECO:0000313|Ensembl:ENSSLDP00000023345.1};
GN Name=MYH10 {ECO:0000313|Ensembl:ENSSLDP00000023345.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000023345.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000023345.1}
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 STRING; 1841481.ENSSLDP00000023345; -.
DR Ensembl; ENSSLDT00000024098.1; ENSSLDP00000023345.1; ENSSLDG00000018182.1.
DR GeneTree; ENSGT00940000155159; -.
DR Proteomes; UP000261360; 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; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 4.
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; 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 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..773
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 651..673
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1033..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1262..1286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1879..1905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1939 AA; 225525 MW; E817025F41AEB443 CRC64;
MSHRSGQEDP ERYLFVDRAV VYNPATQADW TAKKLVWVPS ERHGFEAASI REERGEEVQV
ELAENGKKVV INKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQGES GAGKTENTKK
VIQYLAHVAS SHKGRKDHNI PGELERQLLQ ANPILESFGN AKTVKNDNSS RFGKFIRINF
DVTGYIVGAN IETYLLEKSR AIRQAKDERT FHIFYRLLAG AGEHLRTDLL LEGFNNYRFL
SNGNIPIPGQ QDKENFQETM EAMHIMSFNH EEIVCMLKVV SAVLQFGNIV FKKERNTDQA
SMPENTAAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK AQTKEQADFA VEALAKATYE
RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS FEQLCINYTN EKLQQLFNHT
MFILEQEEYQ REGIEWSFID FGLDLQPCID LIERPNNPPG ILALLDEECW FPKATDKTFV
DKVLQEQGTH TKFQKPRQLK DKADFCIIHY AGRVDYKADE WLMKNMDPLN DNVATLLHQS
TDKFVAELWK DVDRIVGLDQ VAGMNETAFG AAYKTKKGMF RTVGQLYKEQ LSKLMATLRN
TNPNFVRCII PNHEKRAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRIV FQEFRQRYEI
LTPNAIPKGF MDGKQACERM IQALELDGNL FRIGQSKIFF RAGVLAHLEE ERDLKITDII
IYFQAVCRGY LARKAFAKKQ QQLSALKVLQ RNCAAYLKLR HWQWWRLFTK VKPLLQVTRQ
EEEMQAKDEE LVKVKEKQTK VEGELVEMER KHQQLVEEKN ILAEQLQAET ELFAEAEEMR
ARLASKKQEL EEILHDLESR LEEEEERNQG LQNEKKKMQS HIQDLEEQLD EEEAARQKLQ
LEKVTAEAKM KKYEEDILLL EDQNSKFLKE KKLMEDRINE VNSLLAEEEE KAKNLGKIKN
KQEMMMVDLE ERLKKEEKTR QELEKAKRKL DGETSDFQDQ ISELQAQVEE QKVQMGKKEE
EQQMMQARGE DEVSQKNNAL KQVRELQAQL SELQEDLESE KQSRNKAEKL KRDLSEELEA
LKTELEDTLD TTAAQQELRT KREQEVAELK KAIDEETKNH EAQIQEMRQR HGTALEELSE
QLEQAKRFKA NLEKTKQSQE SANKELASEV KTLQQAKTES EHKRKKLEAQ LQEFMARVTE
GERAKGELAE RSHKLQTELD NVSAMLEDSE RKGIKTAKDV AGLESQLQDS QELLQEETRQ
KLNLSSRIRQ LEEEKNALQE QQEEDEEARK NLEKQMLTLQ AQLSESKKKL EDDVGTIDSL
EEVKKKLQKD LELGSQRLEE KTIAFEKMEK TKTRLQQELD DLTVDLDHQR QIVSNLEKKQ
KKFDQMLAEE KSISARYAEE RDRAEAEARE KETKALSMTR ALDEALEAKE ELERVNKQLR
AEMEDLMSSK DDVGKNVHEL EKSKRTLEQQ LEEMKTQLEE LEDELQATED AKLRLEVNMQ
AMKAQYERDL QGRDDQNDEK KRALVKQVRE MEAELEDERK QRGLAVAAKK KLEMDLKDIE
GHIEGANKAR DEAIKQLRKL QAQMKDYQRE LEDARASRDD IFAISKENEK KLKSLEAEIV
QLHEDLAASE RGRRHAEQER DELQDEISNS TSGKSALMDE KRRLEARIAQ LEEELEEEQG
NMELLNDRFR KTTMQVDTLT TELSAERSTA QKSENARQQL ERQNKELRAK LGELEGSVKN
RFKASITALE AKIAQLEEQL EQEAKERATA NKIVRRTEKK LKEICMQVED ERRHADQFKE
QVEKASSRMK QLKRQLEEAE EEATRANASR RKLQRELDDA TEASEGLSRE VHTLKNRLRY
GVVDKTPTIC QSPFILLLY
//
