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Database: UniProt
Entry: A0A151NHU5_ALLMI
LinkDB: A0A151NHU5_ALLMI
Original site: A0A151NHU5_ALLMI 
ID   A0A151NHU5_ALLMI        Unreviewed;      1992 AA.
AC   A0A151NHU5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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};
GN   ORFNames=Y1Q_0024143 {ECO:0000313|EMBL:KYO36392.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO36392.1};
RN   [1] {ECO:0000313|EMBL:KYO36392.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO36392.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA   Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA   Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA   Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA   Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA   McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA   Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA   Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA   Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA   Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical
CC       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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KYO36392.1}.
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DR   EMBL; AKHW03002956; KYO36392.1; -; Genomic_DNA.
DR   STRING; 8496.A0A151NHU5; -.
DR   eggNOG; KOG0161; Eukaryota.
DR   PhylomeDB; A0A151NHU5; -.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0060473; C:cortical granule; 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:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.5.340; -; 5.
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   PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR   PANTHER; PTHR45615:SF16; MYOSIN-9; 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; SM00015; IQ; 1.
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   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
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:UP000050525}.
FT   DOMAIN          56..109
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          113..808
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..708
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   REGION          1066..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1723..1753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1798..1821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1915..1992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1723..1742
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1798..1812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1915..1940
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1947..1962
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1969..1992
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1992 AA;  229940 MW;  B171EA7B8100F190 CRC64;
     MGGACSSGRG GSTRLETSQC RCVRGRQADA ENESLPGQKQ PPPPRLSPAD RRTQVPQYKP
     PWLREMSIKK NGFEAASIKE EAGDEAVVEL AENGKKIKVN KDDIQKMNPP KFSKVEDMAE
     LTCLNEASVL HNLKERYYSG LIYTYSGLFC VVINPYKNLP IYSEEIVDMY KGKKRHEMPP
     HIYAITDTAY RSMMQDREDQ SILCTGESGA GKTENTKKVI QYLAHVASSH KSKKDQGELE
     RQLLQANPIL EAFGNAKTVK NDNSSRFGKF IRINFDVNGY IVGANIETYL LEKSRAIRQA
     KEERTFHIFY YLLSGAGEHL KTDLLLEPYN KYRFLSNGHV TIPGQQDKDM FQETMEAMKI
     MGIPDDEQMG LLKVISGVLQ LGNIAFKKER NTDQASMPDN TAAQKVSHLL GINVTDFTRG
     ILTPRIKVGR DYVQKAQTKE QADFAIEALA KATYERMFRW LVMRINKALD KTKRQGASFI
     GILDIAGFEI FELNSFEQLC INYTNEKLQQ LFNHTMFILE QEEYQREGIE WNFIDFGLDL
     QPCIDLIEKP AGPPGILALL DEECWFPKAT DKSFVEKVMQ EQGSHPKFQK PKQLKDKADF
     CIIHYAGKVD YKADEWLMKN MDPLNDNIAT LLHQSSDKFV SELWKDVDRI VGLDQVAGMS
     ESALPGAFKT RKGMFRTVGQ LYKEQLAKLM ATLRNTNPNF VRCIIPNHEK KAGKLDPHLV
     LDQLRCNGVL EGIRICRQGF PNRVVFQEFR QRYEILTPNS IPKGFMDGKQ ACVLMIKALE
     LDPNLYRIGQ SKVFFRAGVL AHLEEERDLK ITDVIIGFQA CCRGYLARKA FAKRQQQLTA
     MKVLQRNCAA YLKLRNWQWW RLFTKVKPLL QVSRQEEEMM AKEEELVKVK EKQLAAENRL
     SEMETLQTQL MAEKMQLQEQ LQAETELCAE AEEIRARLTA KKQELEDICH DLEARVEEEE
     ERCQHLQIEK KKMQQNIQEL EEQLEEEESA RQKLQLEKVT TEAKVKKLEE DLIVLEDHNL
     KLGKEKKLLE DRISEFTTNL TEEEEKSKSL AKLKNKHEAM ITDLEERLRR EEKQRQELEK
     TRRKLEGDSG DLHDQIAELQ AQIAELKMQL AKKEEELQAA LARVEEESSQ KNMALKKIRE
     LESQITELQE DLESERAARN KAEKQKRDLG EELEALKTEL EDTLDSTAAQ QELRSKREQE
     VTLLKKTLDD EAKTHEAQIQ EMRQKHAQVV EELAEQLEQT KRVKANLEKA KQTLESDRAE
     LSNEVKVLLQ GKGDSEHKRK KVETQLQELQ VKFAEGERVR TELAEKVNKL QVELDNVTGL
     LNQSDSKSIK LAKDFSTLES QLQDTQELLQ EETRQKLSLS TKLKQMEDEK NSIKEQLEEE
     EEAKINLEKQ ISALHQQIAD MKKKVDDGLG CLEMVEEAKK KLQKDLEAMS QRYEEKAAAF
     DKLEKTKTRL QQELDDLTVD LDHQRQIVSN LEKKQKKFDQ LLAEEKNISA KYAEERDRAE
     AEAREKETKA LSLARALEEA MEQKAELERL NKQFRTEMED LMSSKDDVGK SVHELEKAKR
     ALEQQVEEMK TQLEELEDEL QATEDAKLRL EVNQQAMKAQ FERDLQGRDE QNEEKRKQLI
     RQVREMEVEL EDERKQRSIA VAARKKLEMD LKDLEGQIDS ANKNRDEAIK QLRKVQAQMK
     DCMRELDDTR TSREEILAQA KENEKKMKNM EAEMIHMQEE LAAAERAKRQ AQQERDELAD
     EIANSSGKGA LAMEEKRRLE ARIAQLEEEL EEEQGNTEMV NDRLKKANLQ VDQINADLNA
     ERSNAQKNEN ARQQMERQNK ELKVKLQEME GIMKSKYKSN ITALEAKIAQ LEEQLDSETK
     ERQAASKQVR RTEKKLKDIL LQVDDERRNA EQFKDQVDKS HVRLKQLKRQ LEEAEEEAQR
     ANAARRKLQR ELEDATETAD AMNREVSSLK SKLRRGDLPF VVPRRMGRKG TGECSDEEVD
     GKADAGDAKA TE
//
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