ID W5KHI1_ASTMX Unreviewed; 791 AA.
AC W5KHI1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Tudor domain-containing protein 3 {ECO:0000256|ARBA:ARBA00013421};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000007043.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000007043.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; W5KHI1; -.
DR STRING; 7994.ENSAMXP00000007043; -.
DR Ensembl; ENSAMXT00000007043.2; ENSAMXP00000007043.2; ENSAMXG00000006847.2.
DR eggNOG; KOG3683; Eukaryota.
DR GeneTree; ENSGT00940000155487; -.
DR HOGENOM; CLU_022646_0_0_1; -.
DR InParanoid; W5KHI1; -.
DR OrthoDB; 228723at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000006847; Expressed in embryo and 14 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR CDD; cd20413; Tudor_TDRD3; 1.
DR CDD; cd14282; UBA_TDRD3; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 2.40.50.770; RecQ-mediated genome instability protein Rmi1, C-terminal domain; 1.
DR InterPro; IPR042470; RMI1_N_C_sf.
DR InterPro; IPR013894; RMI1_OB.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047379; Tudor_TDRD3.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041915; UBA_TDRD3.
DR PANTHER; PTHR13681; SURVIVAL OF MOTOR NEURON-RELATED-SPLICING FACTOR 30-RELATED; 1.
DR PANTHER; PTHR13681:SF24; TUDOR DOMAIN-CONTAINING PROTEIN 3; 1.
DR Pfam; PF08585; RMI1_N_C; 1.
DR Pfam; PF00567; TUDOR; 1.
DR Pfam; PF00627; UBA; 1.
DR SMART; SM01161; DUF1767; 1.
DR SMART; SM00333; TUDOR; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50304; TUDOR; 1.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467}.
FT DOMAIN 289..329
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 695..755
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 87538 MW; 34E9DD8670CB22F2 CRC64;
MSELSAALGR EGWYLTEEGI EECKSSEKEK VTVTDIINVA LNSDLRPIGK SFLPADINSG
RVEKLEGPCV LQIQRIRNVS APKENEDSQA APRMLRVQMT DGQTMCTGLE FKHLSKISLN
TPPGTKVKLL GTVQMKNGLL LLDDSKIAVL GGEVDHMIEK WELQRSLAKH SRSNVGAEGG
PPPFLPFGQK CLRQEEVDSR TLDQRKTLQS SNAAKTASEN DEFEKQRIAA IAEIAKSKEM
RTFGGGGNAG SNLTNPGSSF KNRDTYQKRR EEREKTWTES KPEGVYRELV DERALRDIME
MGFNKEAARQ ALLDNNNNVE VALNALLTGV SQPKSAPVEA SRPPPRGKGR GRGRSRQDED
DEGGGGRPSG PSTLFDFLES KMGAFSIDDS KKPPPQKTQD HPGRMTFPNP ERIPRDAPQP
KQTNRNDGRP QRNDRPPRFQ RDGDFPKPGT TETTQPASSQ SQPQRWRDGE KGGRGGSERW
KDDRRDAKGG QMNITSSGNS RSKEQQQGSS GNFYQGSKDY GGPKGYQQVS RDMGPRAQEQ
VGGSDPLPFR KNQANGPLGP KALDWNVTVP DSKGRPEPHS RRKGKSDRPN SAHFDRNQEP
IGNLNSAYVP GGKDSTYFQD GGQGQFTKGG GNSNLYLQNG DSDHRRTGLI KPQSSGPPHK
SSNSHNSAPK KRSGPIKGQR GPEMGEPAEM SSQGCWKPGD QCLALYWEDN KFYRATIDAV
HPSGSTAVVV FSDYGNCEEV LLHNIKPLHM DMWDDDDVYY ENSLEFRRGG DGQPRRTRPT
QQYYQPPRAR D
//