ID A0A3Q3H118_KRYMA Unreviewed; 1949 AA.
AC A0A3Q3H118;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Myosin-9 {ECO:0000256|ARBA:ARBA00039816};
DE AltName: Full=Myosin heavy chain 9 {ECO:0000256|ARBA:ARBA00041440};
DE AltName: Full=Myosin heavy chain, non-muscle IIa {ECO:0000256|ARBA:ARBA00042289};
DE AltName: Full=Non-muscle myosin heavy chain IIa {ECO:0000256|ARBA:ARBA00043098};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000029102.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000029102.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}. Cytoplasmic vesicle, secretory
CC vesicle, Cortical granule {ECO:0000256|ARBA:ARBA00037865}.
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; 37003.ENSKMAP00000029102; -.
DR Ensembl; ENSKMAT00000029465.1; ENSKMAP00000029102.1; ENSKMAG00000021559.1.
DR GeneTree; ENSGT00940000155421; -.
DR OMA; RCYFASK; -.
DR Proteomes; UP000264800; 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 CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.5.4820; -; 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 PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, NON-MUSCLE; 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}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000264800}.
FT DOMAIN 27..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 81..770
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 648..670
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1680..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1811..1949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1949 AA; 224795 MW; 43597B4074F1D3DA CRC64;
MSHSFDEKFL YVDKDLLNSP MAQADWAAKK LVWVPSEKHG FEAASVKEER GEEALVELAD
NGKKITVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LRERYFSGLI YTYSGLFCVV
VNPYKMLPIY SEKIIDMYKG KKRHEVPPHI YAIADNAYRN MMQDREDQSI LCTGESGAGK
TENTKKVIQY LAVVASSHKG KKDSSGELEK QLLQANPILE AFGNAKTIKN DNSSRFGKFI
RINFDVTGYI VGANIETYLL EKSRCIRQAK TERAFHIFYY MIAEDLLLES FSNYRFLSSG
HVQIPAQQDD EMFEETMEAM KIMGLTDEER IDILKVCSTV MQLGNIEFKK ERNQEQATMP
DNTAAQKVCH LQGINVTDFT RAILTPRIKV GREVVQKAQT KEQADFAVEA LAKAVYERLF
RWILGRVNKA LDKTKRQGAS FLGILDIAGF EIFEDNSFEQ LCINYTNEKL QQLFNHTMFI
LEQEEYQREG IEWNFIDFGL DLQPCIELIE RPNNPPGILA LLDEECWFPK ATDVSFVEKL
MNTQGNHMKF AKPKQLKDKT EFSILHYAGK VDYNATAWLT KNMDPLNDNV TSLLSNSSSQ
FVQDLWKDAD RVVGLDTIAK MTDSSMPSAS KTKKGMFRTV GQLYKESLAK LMTTLHNTQP
NFVRCIIPNH EKRAGKLDAH LVLEQLRCNG VLEGIRICRQ GFPNRIVFQE FRQRYEILAA
SAIPKGFMDG KQACCLMIKH LDLDPNLYRI GQSKIFFRTG VLAQLEEERD LKITVIIIAF
QAQARGFLAR KAFAKLQQQL TAMKVIQRNC AAYLKLRNWQ WWRLFTKVKP LLQVTRQEEE
MSLKEEELQK AKDVASKAEL FNSVLQIVEE RNALQEQLQA ETELYAEAEE MRVRLAAKKQ
ELEEILHEME ARLDEEEERA QTLLLDKKKM QQQMQELEEH LEEEEDARQK LQLEKVTCEG
KIKKLEDDIL VMEDHNNKLL KERKLLEERV ADFSANLAEE EEKSKNLTKL KNKHESMISE
LEVRLKKEEK TRQELDKAKR KLEAESNDLQ EQIADLQAQI SDLKAQLAKK DEELQNALAR
LEDEMAQKNN ALKKIRELEG HISDLQEDLD SERAARNKAE KIKRDLGEEL EALKSELEDT
LDTTATQQEL RAKREQEVTL LKRAIDDENR MHEAQIQEMR QKHTQAVEEL TEQLEQSKRV
KTNLEKAKQA LEKETSELTM EVRSLAQAKQ DGEHKRKKLE GQVVDLQSRF TDSEKQKAEL
SERCSKVTVE LESVTNLLNE AEGKNIKLSK DVNSLTSQLQ DSQELLAEET RQKLQISTKL
RQAEDDNHSL QEQLEEEMEA KRNVERHVST LNIQLSDAKK KLEEMSGNVE LLEEGKKRLQ
RDLEAANTQF EEKASAYDKL EKTKNRLQQE LEDTLMDLDN QRQIVSNLEK KQKKFDQMLA
EEKSISSKYA EERDRAEAEA REKETKALSL ARALEEAQDG REELERANKA LRVEMEDLIS
SKDDVGKNVH ELEKSKRALE AQVEEMKTQL EELEDELQAA EDAKLRLEVN MQALKAQFER
DLQGRDEMGE EKKRQLVKQV RELETELEDE RKQKAQAAAA KKKLETDMKD LEGQIETANK
GRDEAIKQLR KLQAQMKDFQ RELEDARAAR EEVLSTAKES ERKAKSLEAE LIQLQEELAS
AERARKQAEA ERDELSDELA SNTSGKSALA DEKRRLEAKI SQLEEELEEE QGNMEILNDR
LRKSSQQVEQ LNNELQTERS TSQKNESARQ QMERQNKELK AKLLEMENQV KSKFKSSISA
LEAKVAQLEE QLEDKQANAK SVRQKDKKLK DLMMQLEDER KQAEQYKDQA EKSTSRMKQL
KRQLEESEEE SQRATAARRK LQRELDEATE ANDAMSREVN SLKSKLRRGN EPSFGSVPRR
MGGGRRVVED ASEEEVDSQS DFNGTKASE
//