ID A0A2D0PJP2_ICTPU Unreviewed; 1933 AA.
AC A0A2D0PJP2;
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_017305606.1};
GN Name=LOC108254798 {ECO:0000313|RefSeq:XP_017305606.1};
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_017305606.1};
RN [1] {ECO:0000313|RefSeq:XP_017305606.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017305606.1};
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_017305606.1; XM_017450117.3.
DR STRING; 7998.ENSIPUP00000027543; -.
DR GeneID; 108254798; -.
DR KEGG; ipu:108254798; -.
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; 4.
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..776
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 653..675
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1897..1933
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 1933 AA; 221831 MW; F326DB8280C0F38E CRC64;
MGDAEMECFG LAAIYLRKPE KERIEAQNKP FDAKTAVYVD EPTEIYLKGT LKSKEGGKAT
VETLDGKSIT VKEENIYPMN PPKFDKIEDM AMMTHLNEPT VLYNLKERYA AWMIYTYSGL
FCVTVNPYKW LPVYDAVVVA GYRGKKRVEA PPHIFSISDN AYQFMLTDRE NQSILITGES
GAGKTVNTKR VIQYFATIAV VGQKKAEPGK MQGSLEDQII AANPLLEAYG NAKTVRNDNS
SRFGKFIRIH FGQTGKLASA DIETYLLEKS RVTFQLCAER SYHIFYQLMT GHKPELLEAL
LITTNPYDYP MISQGEITVT SIDDVEEFVA TDTAIDILGF SADEKISIYK LTGAVMHHGT
MKFKQKQREE QAEPDGTEVA DKIAYLLGLN SADMLKALCC PRVKVGNEFV TKGQTVPQVN
NSVSALCKSI YEKMFLWMVL RINEMLATKH QREFYIGVLD IAGFEIFDYN SMEQLCINFT
NEKLQQFFNH HMFVLEQEEY KKEGIEWEFI DFGMDLASCI ELIEKPMGIF SILEEECMFP
KATNTTFKNK LYDQHLGKCA CFQKPKPAKG KAEAHFSLVH YAGTVDYNVN GWLDKNKDPL
NDSVVQLYQK SANKLLCLLY AAHGAADADT GGKKGKKKGG SFQTVSALFR ENLGKLMTNL
RSTHPHFVRC LIPNESKTPG LMENFLVIHQ LRCNGVLEGI RICRKGFPSR ILYADFKQRY
KVLNASVIPE GQFIDNKKAS EKLLGSIDVD HTQYKFGHTK VFFKAGLLGT LEEMRDDKLV
ALVTMIQALC RGFLMRTEFV KMMERRESIF TIQYNIRSFM NVKHWPWMKV YFKIKPLLKT
AETEKEMAAM KENFDKMKED LAKALAKKKE LEEKMVSLVQ EKNDLQLQVS AESENLSDAE
ERCEGLIKNK IQLEAKLKEI TERMEDEEEI NAELTAKKRK LEDECSELKK DIDDLELTLA
KVEKEKHATE NKVKNLTEEM TSQDESIVKL TKEKKALQEA HQQTLDDLQA EEDKVNTLTK
SKTKLEQQVD DLEGSLEQEK KLRMDLERAK RKLEGDLKMA QESIMDLEND KQQSDEKIKK
KDFEISHVLS RIEDEQSLGA QLQKKIKELQ ARIEELEEEI EAERAARAKV EKQRADLSRE
LEEISERLDE AGGATAAQIE MNKKREAEFQ KMRRDLEEST LQHEATAAAL RKKQADSVAE
LGEQIDNLQR VKQKLEKEKS EYKMEMDDLS SNMEAVAKSK ANLEKMCRTL EDQLSELKTK
NDEHVRQLND ISTQKARLQT ENGEFGRQLE EKEALVSQLT RGKQAYTQQI EELKRHIEEE
VKAKNALAHA VQSARHDCDL LREQFEEEQE AKAELQRGMS KANSEVAQWR TKYETDAIQR
TEELEEAKKK LAQRLQEAEE AIEAMNSKCA SLEKTKQRLQ GEVEDLMIDV ERANAVAATL
DKKQRNFDKV LAEWKQKYEE GQAELEGALK EARSLSTELF KMKNSYEEVL DHLETLKREN
KNLQQEISDL TEQVGETGKT IHELEKAKKT VEIEKSEIQT ALEEAEGTLE HEESKIVRIQ
LELTQVKSEI DRKLAEKDEE MEQIKRNSQR VIESMQTTLD AEIRSRNDAL RVKKKMEGDL
NEMEIQLSHA NRLAAEAQKQ LRNVQGQLKD AQLHLDDAVR GQEEMKEQVA MVERRNNLML
AEIEELRAAL EQTERGRKVA EQELVDASER VALLHSQNTS LINTKKKLEA ELVQIQGEVD
DTIQEARNAE EKAKKAITDA AMMAEELKKE QDTNAHMERM KKNLDITVKD LQHRLDEAES
LAMKGGKKQL QKLESRVREL ESEVEVEQRR SAESLKGVRK YERRVKELTY QTEEDKKNVS
RLQDLVDKLQ LKVKAYKRQA EDADEQANTH LSRYRKVQHE MEEAQERADI AESQVNKLRA
KSRDIGKGKQ VAE
//
