ID A0A2Y9RLR1_TRIMA Unreviewed; 1707 AA.
AC A0A2Y9RLR1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Unconventional myosin-XVIIIa isoform X3 {ECO:0000313|RefSeq:XP_023595392.1};
GN Name=LOC101354113 {ECO:0000313|RefSeq:XP_023595392.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023595392.1};
RN [1] {ECO:0000313|RefSeq:XP_023595392.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR RefSeq; XP_023595392.1; XM_023739624.1.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
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 CDD; cd01386; MYSc_Myo18; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 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; 4.10.270.10; Myosin, subunit A; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 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; IPR002928; Myosin_tail.
DR InterPro; IPR036064; MYSc_Myo18.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF13; UNCONVENTIONAL MYOSIN-XVIIIA; 1.
DR Pfam; PF00063; Myosin_head; 2.
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; 1.
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|PROSITE-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:UP000248480}.
FT DOMAIN 18..70
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..854
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 392..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1520..1569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 918..1015
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1606..1629
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1682..1707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 167..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1707 AA; 194387 MW; ED14D0D51CE29423 CRC64;
MRAKTEEQIA AEEAWYETEK VWLVHKDGFS LASQLKSEEL SLPEGKVRVK LDHDGAILDV
DEDDVEKANA PSCDRLEDLA SLVYLNESSV LHTLRQRYGA SLLHTYAGPS LLVLSPRGAP
AVYSEKVMHM FKGCRREDMA PHIYAVAQNA YRAMLMSRQD QSIILLGSSG SGKTTSCQHL
VQYLATIAGT SGNKVFSVEK WQALYTLLEA FGNSPTILNG NATRFSQILS LDFDQAGQVA
SASIQTMLLE KLRVARRPAG EATFNIFYYL LACGDDTLRT ELHLNHLAEN SVFGIVPLAK
PEEKQKAAQQ FSKLQTAMKV LGISPDEQKA CWFILAAIYH LGAAGATKEA AEAGHRQFAR
HEWAQKAAYL LGCSLEELSS AIFKHQHKGG TLQRSTSFRQ GPEESSLGDG TGPKLSALEC
LEGMASGLYS ELFTLLISLV NRALKSSQHS LCSMMIVDTP GFQNPEQGGS ARGASFEELC
HNYAQDRLQR LFHERTFVQE LERYKEENVE LAFDDLDPAT DDSVAAVDQA SHQSLVRSLA
RTDEARGLLW LLEEEALVPG ATEDALLERL FSYYGPQEGD KKGPSPLLRS SKPHHFLLGH
SHGTNWVEYN VAGWLSYTKQ NPATQNAPRL LQDSQKKIIS NLFLGRAGST TVLSGSIAGL
EGGSQLALRR ATSMRKTFTT GMAAVKKKSL CIQVKLQVDA LIDTIKKSKL HFVHCFLPVA
EGWAGEPRSA SSRRVSSSSE LDLPSGDHCE AGLLQLDLPL LRAQLRGSRL LDAMRMYRQG
YPDHMVFSEF RRRFDVLAPH LTKKHGRNYI VVDERRAVEE LLESLDLEKS SCCMGLSRVF
FRAGTLARLE EQRDEQTSRN LTLFQAACRG YLSRQHFKKR KIQDLAIRCV QKNIKKNKGV
KDWPWWKLFT TVRPLIEVQL SEEQIRNKDE EIQQLRSKLE KVEKERNELR LNSDRLETRI
SELTSELTDE RNTGESASQL LDAETAERLR AEKEMKELQT QYDALKKQME VMEMEVIEAR
LIRAAEINGE VDDDAGGEWR LKYERAMREV DFTKKRLQQE FEDKLEVEQQ NKRQLERRLG
DLQADSDESQ RALQQLKKKC QRLTAELQDT KLHLEGQQVR NHELEKKQRR FDSELSQAHD
EAQREKLQRE KLQREKDMLL AEAFSLKQQM EEKDMDIAGF TQKVVSLEAE LQDISSQESK
DEASLAKVKK QLRDLEAKVK DQEEELDEQA GTIQMLEQAK LRLEMEMERM RQTHSKEMES
RDEEVEEARQ SCQKKLKQME VQLEEEYEDK QKVLRDKREL ESKLTALSDQ VNQRDFESEK
RLRKDLKRTK ALLADAQIML DHLKNNAPSK REIAQLKNQL EESEFTCAAA VKARKAMEVE
IEDLHLQIGD ITKAKTALEE QLSRLQREKN EIQNRLEEDQ EDMNELMKKH KAAVAQASRD
LAQMNDLQAQ LEEANKEKQE LQEKLQALQS QVEFLEQSMV DKSLVSRQEA KIRELETRLE
FERTQVKRLE SLASRLKENM EKLTEERDQR IAAENREKEQ NKRLQRQLRD TKEEMGELAR
KEAEASRKKH ELEMDLGSLE AANQSLQADL KLAFKRIGDL QAAIEDEMES DENEDLINSE
GDSDVDSELE DRVDGVKSWL SKNKGPSKAA SDDGSLKSSS PTSYWKPLAP DRSDDEHDPL
NSTSRPQYSH NYLSDSDTEA RLTETNA
//
