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Database: UniProt
Entry: A0A3Q3H118_KRYMA
LinkDB: A0A3Q3H118_KRYMA
Original site: A0A3Q3H118_KRYMA 
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
//
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