ID A0A452I2Y5_9SAUR Unreviewed; 1973 AA.
AC A0A452I2Y5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Myosin-11 {ECO:0000256|ARBA:ARBA00040393};
DE AltName: Full=Myosin heavy chain 11 {ECO:0000256|ARBA:ARBA00042406};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000021895.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000021895.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Muscle contraction. {ECO:0000256|ARBA:ARBA00037488}.
CC -!- SUBUNIT: Muscle myosin is a hexameric protein that consists of 2 heavy
CC chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC regulatory light chain subunits (MLC-2).
CC {ECO:0000256|ARBA:ARBA00038612}.
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 Ensembl; ENSGAGT00000024937.1; ENSGAGP00000021890.1; ENSGAGG00000016067.1.
DR Ensembl; ENSGAGT00000024942.1; ENSGAGP00000021895.1; ENSGAGG00000016067.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.370; -; 1.
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 InterPro; IPR014751; XRCC4-like_C.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF23; MYOSIN-11; 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; 5.
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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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:UP000291020}.
FT DOMAIN 31..81
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 85..783
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 661..683
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1862..1973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 847..1281
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1862..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1946..1973
FT /note="Basic and acidic 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 1973 AA; 228257 MW; D665BA6DEB279646 CRC64;
MAQKTQLSDD EKFLFVDKNI LNSPLAQADW TAKRLVWVPS EKQGFEAASI KEEKGDEVLV
ELAENGKKIT ISKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLRERYF SGLIYTYSGL
FCVVVNPYKY LPIYSDKIID MYKGKKRHEM PPHIYAIADT AYRSMLQDRE DQSILCTGES
GAGKTENTKK VIQYLAFVAS SHKGKKDTSI TGELEKQLLQ ANPILEAFGN AKTVKNDNSS
RFGKFIRINF DVTGYIVGAN IETYLLEKSR AIRQARDERT FHIFYYMIAG TGEQMKKDLL
LESFNNYTFL SNGHVPIPGQ QDDEMFQETL EAMTIMGFSE EEQLAMLKVV SSVLQLGNII
FKKERNTDQA SMPDDTAAQK VCHLMGINVT DFTRAILTPR IKVGRDVVQK AQTKEQADFA
VEALAKATYE RLFRWILTRV NKALDKTKRQ GASFLGILDI AGFEIFEVNS FEQLCINYTN
EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCIE LIERPNNPPG VLALLDEECW
FPKATDTSFV EKLCQEQGSH AKFQKPKQLK DKTEFSIIHY AGRVNYSATA WLTKNMDPLN
DNVTSLLNQS SDKFVADLWK DVDRIVGLDQ MAKMTESSLP SSSKTKKGMF RTVGQLYKEQ
LTKLMTTLRN TNPNFVRCII PNHEKRAGKL DAHLVLEQLR CNGVLEGIRI CRQGFPNRIV
FQEFRQRYEI LASNAIPKGF MDGKQACILM IKALELDANL YRIGQSKIFF RTGVLAHLEE
ERDLKITDII IAFQAQSRGY LARKAFAKKQ QQLTAMRVIQ RNCSAYLKLR NWQWWRLFTK
VKPLLQVTRQ EEEMQAKDEE LQRTKERQQK AESELKELEL KHNQLCEEKN LLQEQLQAET
ELYAEAEEMR VRLAAKKQEL EEILHEMEAR IEEEEERSHQ LQTEKKKMQQ QMLDLEDQLE
EEEAARQKLQ LEKVTAEAKI KKMEDDILVM DDQNNKLTKE RKLLEERISD LTTNLAEEEE
KAKNLTKLKN KHESMISELE VRLKKEEKSR QELEKTKRKL EGDASDLHEQ IADLQAQIAE
LKMQLAKKEE ELQAALARLE DEIAQKNNAL KKIRELEGHI SDLQEDLDSE RAARNKAEKH
KRDLSEELEA LKTELEDTLD STATQQELRA KREQEVTVLK RALDEETRTH EAQVQEMRQK
HTQAVEELTE QLEQFKRAKV NLDKTKQTLE KENADLNTEI RSLTQAKQDV EYKKKKLEVQ
LQELQSKYTD GERIRVELNE KVHKLQVEVE NVTGLLSDAE TKAIKLTKDV ASLGSQLQDT
QELLQEETRQ KLTITTKLRQ LEAENNSLQE QLEEEAEAKQ NLERHISTLT VQLSDSKKKL
QEYTSTIESM EEGKKKFQKE IEGLTQQFEE KAASYDKLEK TKNRLQQELD DLIVDLDNQR
QLVSNLEKKQ KKFDQMLAEE KNISSKYADE RDRAEAEARE KETKALSLAR ALEEALEAKE
ELERTNKLLK AEMEDLVSSK DDVGKNVHDL EKSKRALEQQ VEEMKTQLEE LEDELQATED
AKLRLEVNMQ ALKGQFERDL QARDEQNEEK RRQLLKQLHE YETELEDERK QRGLATAAKK
KLEVDIKDLE GQVDSANKAR EEAIKQLRKL QSQMKDFQRE LDDARASREE IFATARENEK
KAKNLEAELM QLQEDLAAAE RARKHADLEK EELAEELANA ASGRTSLQDE KRRLEARISQ
LEEELEEEQG NMEAMSDRFR KAVQQSEQLN NELVTERTVA QKNESARQQL ERQNKELKAK
LQEMEGAVKS KFKATIASLE AKIAQLEEQV EQESREKQVT AKTLRQKDKK LKEVLLQVED
ERKQAEQYKD QADKSTARVK QLKRQLEEAE EEAQRINANR RKLQRELDEA AESNEAMGRE
MATLKSKLRR GNEPASFAPS RRSGGRRIIE NAEGSEEEAD SRDGDFNGTK ASE
//
