ID B4MXF5_DROWI Unreviewed; 226 AA.
AC B4MXF5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Tudor domain-containing protein {ECO:0000259|SMART:SM00333};
GN Name=Dwil\GK19792 {ECO:0000313|EMBL:EDW76724.1};
GN ORFNames=Dwil_GK19792 {ECO:0000313|EMBL:EDW76724.1};
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW76724.1, ECO:0000313|Proteomes:UP000007798};
RN [1] {ECO:0000313|EMBL:EDW76724.1, ECO:0000313|Proteomes:UP000007798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000256|ARBA:ARBA00004216}. Nucleus, gem
CC {ECO:0000256|ARBA:ARBA00034695}.
CC -!- SIMILARITY: Belongs to the SMN family. {ECO:0000256|ARBA:ARBA00005371}.
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DR EMBL; CH963876; EDW76724.1; -; Genomic_DNA.
DR RefSeq; XP_002065738.1; XM_002065702.2.
DR AlphaFoldDB; B4MXF5; -.
DR SMR; B4MXF5; -.
DR STRING; 7260.B4MXF5; -.
DR EnsemblMetazoa; FBtr0250443; FBpp0248935; FBgn0221790.
DR GeneID; 6643117; -.
DR KEGG; dwi:6643117; -.
DR eggNOG; KOG4327; Eukaryota.
DR HOGENOM; CLU_077852_0_0_1; -.
DR InParanoid; B4MXF5; -.
DR OMA; FHTGYYH; -.
DR OrthoDB; 4110955at2759; -.
DR PhylomeDB; B4MXF5; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0015030; C:Cajal body; IEA:EnsemblMetazoa.
DR GO; GO:0071254; C:cytoplasmic U snRNP body; IEA:EnsemblMetazoa.
DR GO; GO:0097504; C:Gemini of coiled bodies; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IEA:EnsemblMetazoa.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0034730; C:SmD-containing SMN-Sm protein complex; IEA:EnsemblMetazoa.
DR GO; GO:0032797; C:SMN complex; IEA:EnsemblMetazoa.
DR GO; GO:0034718; C:SMN-Gemin2 complex; IEA:EnsemblMetazoa.
DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR GO; GO:0051393; F:alpha-actinin binding; IEA:EnsemblMetazoa.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0097113; P:AMPA glutamate receptor clustering; IEA:EnsemblMetazoa.
DR GO; GO:0045175; P:basal protein localization; IEA:EnsemblMetazoa.
DR GO; GO:0007417; P:central nervous system development; IEA:EnsemblMetazoa.
DR GO; GO:0051276; P:chromosome organization; IEA:EnsemblMetazoa.
DR GO; GO:1990194; P:cytoplasmic U snRNP body assembly; IEA:EnsemblMetazoa.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:EnsemblMetazoa.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:EnsemblMetazoa.
DR GO; GO:0002164; P:larval development; IEA:EnsemblMetazoa.
DR GO; GO:0008345; P:larval locomotory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0035149; P:lumen formation, open tracheal system; IEA:EnsemblMetazoa.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:EnsemblMetazoa.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR GO; GO:0048601; P:oocyte morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0033962; P:P-body assembly; IEA:EnsemblMetazoa.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IEA:EnsemblMetazoa.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; IEA:EnsemblMetazoa.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IEA:EnsemblMetazoa.
DR GO; GO:0048863; P:stem cell differentiation; IEA:EnsemblMetazoa.
DR GO; GO:0017145; P:stem cell division; IEA:EnsemblMetazoa.
DR GO; GO:0072089; P:stem cell proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0072553; P:terminal button organization; IEA:EnsemblMetazoa.
DR CDD; cd22852; SMN_C; 1.
DR CDD; cd20398; Tudor_SMN; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR040424; Smn1.
DR InterPro; IPR047313; SMN_C.
DR InterPro; IPR010304; SMN_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047298; Tudor_SMN_eumet.
DR PANTHER; PTHR39267:SF1; SURVIVAL MOTOR NEURON PROTEIN; 1.
DR PANTHER; PTHR39267; SURVIVAL MOTOR NEURON-LIKE PROTEIN 1; 1.
DR Pfam; PF06003; SMN_Tudor; 1.
DR Pfam; PF20635; SMN_YG-box; 1.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000007798}.
FT DOMAIN 67..125
FT /note="Tudor"
FT /evidence="ECO:0000259|SMART:SM00333"
FT REGION 45..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 226 AA; 24902 MW; 198E78F462A7AB99 CRC64;
MSDEANTLAW DDTLLMKTYD ESVNLAREAL ARRLADYTNK QEAAEAASGV ADNKTESATN
DSVSPETVYK VGDFARATYT DGLDYEGSIV SINDLTGTCV LRYCGYENEQ EVLLTDLLPS
WGKKTRREQF VQAKAELDQE EARPKNVSKK PTKIPGLVMP PMPFMPPMPF VPPIINPAGN
TIEGEQDFVA MLTAWYMSGY YTGFYQGKKD ANKKNQSGAG PSAAKK
//
