ID A0A151MYK3_ALLMI Unreviewed; 1238 AA.
AC A0A151MYK3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Myosin motor domain-containing protein {ECO:0000259|PROSITE:PS51456};
GN ORFNames=Y1Q_0016948 {ECO:0000313|EMBL:KYO29643.1};
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:KYO29643.1};
RN [1] {ECO:0000313|EMBL:KYO29643.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO29643.1};
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 -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC {ECO:0000256|ARBA:ARBA00011364}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000256|ARBA:ARBA00004575}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004575}; Nucleoplasmic side
CC {ECO:0000256|ARBA:ARBA00004575}.
CC -!- SIMILARITY: Belongs to the NAB family. {ECO:0000256|ARBA:ARBA00008864}.
CC -!- SIMILARITY: Belongs to the NEMP family.
CC {ECO:0000256|ARBA:ARBA00005748}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:KYO29643.1}.
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DR EMBL; AKHW03004587; KYO29643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151MYK3; -.
DR STRING; 8496.A0A151MYK3; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:InterPro.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.20.120.2010; NAB conserved domain 2; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR006989; NAB_co-repressor_dom.
DR InterPro; IPR006988; Nab_N.
DR InterPro; IPR038398; NCD2_sf.
DR InterPro; IPR019358; NEMP_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF291; UNCONVENTIONAL MYOSIN-IA; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF04904; NCD1; 1.
DR Pfam; PF04905; NCD2; 1.
DR Pfam; PF10225; NEMP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 396..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 757..1238
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 90..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 850..857
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1238 AA; 137843 MW; F43B849ACB6BFB82 CRC64;
MALPRTLGEL QLYRVLQRAN LLSYYETFIQ QGGDDVRQLC EAGEEEFLEI MALVGMAAKP
LHVRRLQKAL REWAAHPGLF GPPAPALPAR VPPVLPDVPL EPRSPSPPSP EQDEEGSTSP
GEPEALEPAL VRAVAEGVER LLPGGPRAAA EPEPGALQRV GRRLARAVGH VFQMDDGDRR
KAGEIRRLSA IYGRGEGRRR EGRRLSLQEL TINEAAAQFC LRDQSLLLRR VELFSLARQP
GEVRKSYWGS VQTWAWCHAG ACGSAVPDNL PLPRAAAAPG AVIPLQEGRP HHNNVSRQFC
FNNALPPTWR DIWTRMQIRV NSTRALRVTQ ADSEADLREL EQFSIWNLLS SLFKEKINDT
YIGLDLYSPQ TCLRVELPEP DTTYSVIVLR WFDPKLFLVF FLGLLLFFCG DVLSRSQLFY
YSAGISVGLL ASLLILIYVV SRVMPKKSPI YLLLVGGWSF SLYLIQLVFK NLREIGRGYW
QYGLGYLLLV GLGSFAVCYR YGPLEDERSI RLLAWALQLL GLLLMYAGIQ IRPMALAFVA
TAVGTKYLEY PLQWGYAAYR MARRAATKPS PPRLLTEEEY RAQGEAETRR ALEELRSYCN
SPDFSAWTVV SRIQSPKRFA DFVGGASHLT PNEVSVHEQE YGLGGSYLEG QLFEEEDEAE
DTPVPPSPSA YLVQVPELWG RARSPLSFAV SGLPQQGRKE GWCREAGPAR LSEPWTAPSQ
PGPCLPQAAL FLPSFGSPRA GTRARAMEAD PPVLATVGVG DLVLLDPLSE ESLLSNLRER
FLHKEIYTYI GNVVISVNPY CPLPIYSAEM VEQYCNGNFY ALKPHIYAIA EDAYSSLRDR
DRDQCILITG ESGAGKTEAS KLVMSYVAAV CSKGAEVTKV KEQLLQSNPV LEAFGNAKTI
RNNNSSRFGK YMDVEFDFKG EPLGGLISNY LLEKSRVVQH VKNERNFHIF YQLLAGASDP
LLKRLKLQRD CRHHGYLGDE DPRLPGMDDA TNFQAVQDAM RIIGFSEAEV TQLLEVTAVV
LKLGDLQLSS QFQASGMEAC GIQNMQVLRD ICELIGLRES VLEQALCSRT MEAKQEKVVT
ALSVAQGYFG RDALAKNIYS RLFDWLVTRI NESIQVTTGE RRKVMGVLDI YGFEIVKDNS
FEQFIINYCN EKLQQIFILM TLKEEQEEYF REGIAWTPVT FFDNGIICDL IESVWGAVMG
ALGWLAGGEG PWGCPCWVSP SCNSAGSKGQ GRDPGAAG
//
