ID A0A1S3L6G6_SALSA Unreviewed; 2001 AA.
AC A0A1S3L6G6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Myosin-10-like isoform X5 {ECO:0000313|RefSeq:XP_013986385.1};
GN Name=LOC106564681 {ECO:0000313|RefSeq:XP_013986385.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_013986385.1};
RN [1] {ECO:0000313|RefSeq:XP_013986385.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_013986385.1};
RG RefSeq;
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 RefSeq; XP_013986385.1; XM_014130910.1.
DR GeneID; 106564681; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000087266; Chromosome ssa12.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; IEA:UniProtKB-SubCell.
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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR Gene3D; 1.10.10.820; -; 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; 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:UP000087266}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..806
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 684..706
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 953..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1721..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1798..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1883..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1721..1740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1938
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1955..1977
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 2001 AA; 231347 MW; 38BE45450143BA07 CRC64;
MAQRSGQEDP ERYLFVDRAV VCNPATQADW TAKKLVWIPS ERHGFEAASI REERGDEVVV
ELAENSKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
FCVVINPYKY LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAHVAS SHKGKKDHNI PVSPESPKPV KLQAENNNVG ELERQLLQAN
PILESFGNAK TVKNDNSSRF GKFIRINFDV TGYIVGANIE TYLLEKSRAV RQAKDERTFH
IFYQLLCGAG EHLRSDLLLE GFNSYRFLSN GNITVPGQQD KDNFQETMEA MHIMSFSHDE
ILAMLKVVSS VLQFGNIVFK KERNSDQASM PENTAAQKLC HLLGLNVMEF TRAILSPRIK
VGRDYVQKAQ TKEQADFAVE ALAKATYERL FRWLVHRINK ALDRTKRQGA SFIGILDIAG
FEIFQLNSFE QLCINYTNEK LQQLFNHTMF VLEQEEYQRE GIEWSFIDFG LDLQPCIDLI
ERPVSIRLAN PPGVLALLDE ECWFPKATDK TFIDKLVQEQ GTHSKFQKPR QLKDKADFCI
IHYAGKVDYK ADEWLMKNMD PLNDNVATLL NQSTDKFVAE LWKDVDRIVG LDQVAGMAET
TFGATYKTKK GMFRTVGQLY KESLTKLMAT LRNTNPNFVR CIIPNHEKKA GKLEPHLVLD
QLRCNGVLEG IRICRQGFPN RIVFQEFRQR YEILTPNAIP KGFMDGKQAC ERMIRALELD
SNLFRIGQSK IFFRTGVLAH LEEERDLKIT DIIIYFQSVC RGYLARKAFA KKQQQLSALK
VLQRNCAAYL KLRHWQWWRL FTKVKPLLQV TRQEEEMQAK DEELVKVKER QSKVEGELVD
MERKHQQLLE EKNILAEQLQ AETELFAEAE EMRARLAAKK QELEEILHDL ESRVEEEEER
NQSMQNEKKK MQSHIQDLEE QLDEEEAARQ KLQLEKVTAE AKIKKMEEDI LLLEDQNSKF
LKEKKLLDDR VAEMTSQLTE EEEKAKNLGK VKNKQEVMMV DLEECLKKEE KTRQELEKAK
RKLDAETTDL QDQIAELQAQ IEELKIQLAK KEEELQAALS RGDEEVAQKN NALKAVRELQ
AQLSELQEDL ESEKVSRNKA EKVKRDLSEE LEALKTELED TLDTTAAQQE LRTKREQEVA
ELKKAIDEET KNHESQVQEM RQRHSTALEE LSENLEQAKR FKSNLEKIKC TLESDNKELV
SEVKGLQQAK TESEHKRKKM DAQLQEFMAR ATEGERAKVE LADRTHKLQT ELDTVSALLE
DAEKKGIKLA KDSAGLESAL QDTQELLQEE TRQKLNLSSR IRQLEEDKST LQEQQEEDEE
ARRNLEKQLA TLQAQLFESR KKLDEDVGTL ESLEEVKRKL QKDMELTSQR LEEKASAFDK
MEKTKTRLQQ ELDDLMVDLD HQRTIVSNLE KKQKKFDQLL AEEKTISARY AEERDKAEAE
AREKETKALS IARALDEALE AKEEFERLNK QLRTEMEDLM SSKDDVGKSV HELEKSKRTL
EQQVEEMRTQ LEELEDELQA TEDGKLRLEV NMQAMKAQFD RDLQARDEQN EEKKRTLVKQ
VREMEAELED ERKQRALAVA AKKKLEMDLK DLEGQIEASN KARDEAIKQL RKLQAQMKDY
QRELEEARAS RDEIFAQSKE NEKKLKGLEA EILQLQEDLA ASERARRHAE QERDELADEI
SNSASGKSAL LDEKRRLEAR ISQLEEELEE EQSNMELLND RFRKTTMQVD ILNTELAGER
SAAQKSENAR QGMERQNKEL KAKLGELEGA VKSKFKAAIT ALEAKILQLE EQLEQEAKER
AAANKIVRRT EKKLKEVVIQ VEDERRHADQ YKEQMEKANS RMKQLKRQLE EAEEEATRAN
ASRRKLQREL DDATEASEGL TREVNTLKNR LRRGGPISFS SSRSGRSRQL QIDGTSVDNS
DDDADSRASD HNDTQASNQT E
//
