ID A0A2D0PKM5_ICTPU Unreviewed; 1935 AA.
AC A0A2D0PKM5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Myosin heavy chain, fast skeletal muscle {ECO:0000313|RefSeq:XP_017305605.1};
GN Name=LOC108254796 {ECO:0000313|RefSeq:XP_017305605.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017305605.1};
RN [1] {ECO:0000313|RefSeq:XP_017305605.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017305605.1};
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_017305605.1; XM_017450116.3.
DR STRING; 7998.ENSIPUP00000028391; -.
DR GeneID; 108254796; -.
DR KEGG; ipu:108254796; -.
DR OrthoDB; 2877572at2759; -.
DR Proteomes; UP000221080; Chromosome 21.
DR GO; GO:0030016; C:myofibril; 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:0048731; P:system development; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 6.
DR Gene3D; 1.20.5.370; -; 4.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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 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:SF44; MYOSIN-13; 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; 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 32..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..779
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 656..678
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1908..1935
FT /note="Disordered"
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 1935 AA; 221871 MW; 9FC586FB8E060381 CRC64;
MGDGEMECFG PAAIFLRKPE RERIESQNKP FDAKTAYFVS EPSEMYLKGV LQSKEGGKAT
VKTLCGKTLT VKEDDIFPMN PPKFDKIEDM AMMTHLNEPA VLYNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYDAVVVT AYRGKKRVEA PPHIFSISDN AYQFMLTDRE NQSILITGES
GAGKTVNTKR VIQYFATIAV SGQKKTEPTP GKMQGSLEDQ IIAANPLLEA YGNAKTVRND
NSSRFGKFIR IHFGTTGKLA SADIETYLLE KSRVTFQLSA ERSYHIFYQL MTGHKPELLE
ALLITTNPYD YPMISQGEIT VKSINDVEEF IATDTAIDIL GFTADEKINI YKLTGAVVHH
GNMKFKQKQR EEQAEPDGTE VADKIAYLIG LNSADMLKAL CYPRVKVGNE FVTKGQTVPQ
VNNAVSALCK SIYEKMFLWM VIRINEMLDT KQPRQFFIGV LDIAGFEIFD FNSLEQLCIN
FTNEKLQQFF NHHMFVLEQE EYKKEGIEWE FIDFGMDLAA CIELIEKPMG IFSILEEECM
FPKATDTSFK NKLHDQHLGK SAAFQKPKPA KGKAEAHFSL VHYAGTVDYN IVGWLDKNKD
PLNDSVVQLY QKSANKLLCF LYVAHASAEA ESGGKKGGKK KGGSFQTVSA LFRENLGKLM
TNLRSTHPHF VRCLIPNESK TPGLMENFLV IHQLRCNGVL EGIRICRKGF PSRILYGDFK
QRYKVLNASV IPEGQFIDNK KASEKLLGSI DVDHTQYKFG HTKVFFKAGL LGTLEEMRDD
KLAELVTMTQ ALCRGFLMRR EFIKMMERRE AIFAIQYNIR SFMNVKHWPW MKLYFKIKPL
LKSAETEKEM AAMKENFDKM KEDLTKALAK KKELEEKMVS LLQEKNDLQL QVAAESENLS
DAEERCEGLI KSKIQLEAKL KETNERLEDE EEINAELTAK KRKLEDECSE LKKDIDDLEL
TLAKVEKEKH ATENKVKNLT EEMTSQDEAI AKLSKEKKAL QEAHQQTLDD LQAEEDKVNT
LTKSKTKLEQ QVDDLEGSLE QEKKLRMDLE RAKRKLEGDL KLAQESIMDL ENDKQQSDEK
IKRKDFEVSQ LLGKIEDEQS LGAQLQKKIK ELQARIEELE EEIEAERAAR AKVEKQRADL
SRELEEISER LEEAGGATAA QIEMNKKREA EFQKLRRDLE ESTLQHEATA AALRKKQADS
VAELGEQIDN LQRVKQKLEK EKSEYKMEID DLASNLEAVA KSKSNLEKMC RTLEDQLSEL
KTRNDEHTRQ LNDVNAQKAR LQTENGEFGR QLEEKEALVS QLTRGKQAHT QQIEELKRQI
EEEVKAKNAL AHSVQSARHD CDLLREQFEE EQEAKAELQR AMSKANSEVA QWRTKYETDA
IQRTEELEEA KKKLAQRLQE AEETIEAVNS KCASLEKTKQ RLQGEVEDLM IDVERANALA
ANLDKKQRNF DKVLAEWKQK YEEGQAELEG AQKEARSLST ELFKMKNSYE EALDHLETLK
RENKNLQQEI SDLTEQLGET GKTIHELEKS KKTVETEKSE IQTALEEAEG TLEHEESKIL
RVQLELTQVK SEIDRKLAEK DEEMEQIKRN SQRVIESMQT TLDSEVRSRN DALRVKKKME
GDLNEMEIQL SHANRQAAEA QKQLRNVQGQ LKDAQLHLDE AIRGQEDMKE QVAMVERRNN
LMLAEIEELR AALEQTERGR KVAEQELVDA SERVTLLHSQ NTSLINTKKK LEADLVQIQG
EVEDTVQEAR NAEEKAKKAI TDAAMMAEEL KKEQDTSAHL ERMKKNLEVT VKDLQHRLDE
AENLAMKGGK KQLQKLEARV RELESEVEAE QRRGADAVKG VRKYERRVKE LTYQTEEDKK
NVNRLQDLVD KLQLKVKAYK RQAEEAEEQA NTHLSRYRKV QHELEEAQER ADIAESQVNK
LRAKSRDIGK GKEAE
//
