UniProt: A0A2G5UDS5

Database: UniProt
Entry: A0A2G5UDS5_9PELO

LinkDB:  A0A2G5UDS5_9PELO 
Original site:  A0A2G5UDS5_9PELO

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Ontology (6)   
   GO (6)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (3)   
   SMART (1)   
All databases (23)   

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ID   A0A2G5UDS5_9PELO        Unreviewed;      1291 AA.
AC   A0A2G5UDS5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Myosin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=Cnig_chr_IV.g16234 {ECO:0000313|EMBL:PIC37695.1};
GN   ORFNames=B9Z55_016234 {ECO:0000313|EMBL:PIC37695.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC37695.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC       {ECO:0000256|ARBA:ARBA00004657}.
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:PIC37695.1}.
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DR   EMBL; PDUG01000004; PIC37695.1; -; Genomic_DNA.
DR   STRING; 1611254.A0A2G5UDS5; -.
DR   Proteomes; UP000230233; Chromosome iv.
DR   GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR   GO; GO:0030016; C:myofibril; 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   CDD; cd21759; CBD_MYO6-like; 1.
DR   CDD; cd01382; MYSc_Myo6; 1.
DR   CDD; cd21958; MyUb_Myo6; 1.
DR   Gene3D; 1.10.10.820; -; 1.
DR   Gene3D; 1.20.58.530; -; 1.
DR   Gene3D; 3.30.70.1590; -; 1.
DR   Gene3D; 6.10.220.10; -; 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; IPR049016; MYO6_lever.
DR   InterPro; IPR032412; Myosin-VI_CBD.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR008989; Myosin_S1_N.
DR   InterPro; IPR036114; MYSc_Myo6.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR13140; MYOSIN; 1.
DR   PANTHER; PTHR13140:SF745; UNCONVENTIONAL MYOSIN-VI; 1.
DR   Pfam; PF21521; MYO6_lever; 1.
DR   Pfam; PF16521; Myosin-VI_CBD; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 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|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW   ProRule:PRU00782};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233}.
FT   DOMAIN          113..163
FT                   /note="Myosin N-terminal SH3-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51844"
FT   DOMAIN          167..876
FT                   /note="Myosin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS51456"
FT   REGION          1..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..778
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT   COILED          1015..1095
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        19..33
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         261..268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ   SEQUENCE   1291 AA;  147981 MW;  581D59862FAD9A6B CRC64;
     MLRTLGKRQK GGGTEPSAPP LSSKPPPDPS RNFEKPPDIP RSIEPVRRAP EPPRVYQNTR
     SSVITQPSEP ARRAPDPPST FRKPQASETI RPAEPTRRSE VPRQKQNDSL PPDFGRIVWI
     TDPEDGFRAA QIIDLSKSGF TLTLLNTKET VTRKYEEVFS SEDDPFKSVE DNCALMHLNE
     ATLLNNCRLR YKNGKIYSYV ANILISINPY QTIDGFYSTQ KIKEYRGKSL GQKEPHIYAI
     ADKSYREMRR HKKPQSIIVS GESGAGKTES QKSVLRYLCE NWGAEAGPIQ QRLLETNPIL
     EAFGNAKTLR NNNSSRFGKF VQIHFGEKGN VAGGYVSHYL LETSRICRQA SGERNYHIFY
     QLIAGTSPEL HNYLALEQPH CFNYLKNGFV GFFTHPNSNS STKIPKSRWS DSRFSQDSMV
     DDFLDFQRLE NALKLSGLKE KEIMFIWTTI AGVLHLGNIE FEENIGDSKG GCKVSGGSEG
     AVEQAARLLG LETMELKMGL CARIMQTKGG ARGTLIRVPL KSQEASAGRD ALSKAIYTKL
     FDWLVSRINQ SIPFEKSTHF IGVLDVAGFE FYAVNSFEQF CINFCNEKLQ NFFNERILKE
     EQALYEKEGL NVRKIEFVDN QDCIELFEMK SKGLFDLLDE EARLPTPSFK NFTKRAHEEN
     RKHFRLDTPR KSKVKSHREM RDDEGLLIRH YAGSVCYETK HFVEKNDDQL HNSLQILIEQ
     STSSLLVSLF PSSSDSIKSG NKLKSQSVGS KFKSQLSVLL KKLESTRTHF VRCIKPNNQM
     IPWQFDGSAI LSQLQCAGMT SVLKLMQDGF PSRTSFGDLY SSYQRNLPPK LARLDSRLFA
     KCLFRALGLD QHDFQFGLTK VFFRAGKFAE FDQMMRQDPE HMMSLINKVN DWLVKSRWRQ
     AQYAVWSVIK LKNKIAYRNA QVTKLQSMTR GYLARQKFSR QIAIYRKACN LLRNSKEIEK
     ILSHLNENSR AKWTSSAHLT IKDLEKLVSH VKLASVDQIE KAENAYEHYV KRVDSMILDL
     RRQQKSDEVE ELERKRREEE EKERVMKEEK ERLKRMEEQK ARIQKEHEAQ LVEQIKKAAK
     EKEENEKSAQ QEKLDAIVPN RLADSDGIAV VMSPESGSSS GNSTLKGKYD LAHWKYAELR
     DAINHSMDIN LLVACEEEFR RRLRIYNEWK SRNASKRDEP APARAPLSVY DASGSSRQCQ
     QRYFKYTFDA GAQLEFSFSG KTGMWYAHFS GEHIHRQITI RPSQMPQLMI AGRDDLQMCE
     LTLRETGLEQ KPGAEITEEE FENQWKMAGG N
//

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