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Database: UniProt
Entry: A0A2D0RBG2_ICTPU
LinkDB: A0A2D0RBG2_ICTPU
Original site: A0A2D0RBG2_ICTPU 
ID   A0A2D0RBG2_ICTPU        Unreviewed;      1117 AA.
AC   A0A2D0RBG2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Tudor domain-containing protein 7B isoform X1 {ECO:0000313|RefSeq:XP_017327887.1};
GN   Name=tdrd7b {ECO:0000313|RefSeq:XP_017327887.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017327887.1};
RN   [1] {ECO:0000313|RefSeq:XP_017327887.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017327887.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the TDRD7 family.
CC       {ECO:0000256|ARBA:ARBA00007740}.
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DR   RefSeq; XP_017327887.1; XM_017472398.3.
DR   AlphaFoldDB; A0A2D0RBG2; -.
DR   GeneID; 108267899; -.
DR   KEGG; ipu:108267899; -.
DR   CTD; 100004703; -.
DR   OrthoDB; 5403690at2759; -.
DR   Proteomes; UP000221080; Chromosome 7.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   CDD; cd09974; LOTUS_3_TDRD7; 1.
DR   CDD; cd20429; Tudor_TDRD7_rpt3; 1.
DR   Gene3D; 2.30.30.140; -; 3.
DR   Gene3D; 2.40.50.90; -; 3.
DR   Gene3D; 3.30.420.610; LOTUS domain-like; 3.
DR   InterPro; IPR041966; LOTUS-like.
DR   InterPro; IPR025605; OST-HTH/LOTUS_dom.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR037978; TDRD7_LOTUS_3.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047449; Tudor_TDRD7_rpt3.
DR   PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22948:SF29; TUDOR DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF12872; OST-HTH; 2.
DR   Pfam; PF00567; TUDOR; 3.
DR   SMART; SM00333; TUDOR; 3.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 3.
DR   PROSITE; PS51644; HTH_OST; 3.
DR   PROSITE; PS50304; TUDOR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          2..75
FT                   /note="HTH OST-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51644"
FT   DOMAIN          241..311
FT                   /note="HTH OST-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51644"
FT   DOMAIN          359..429
FT                   /note="HTH OST-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51644"
FT   DOMAIN          517..575
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          112..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..894
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  125978 MW;  30A2EAEA3D2DD5A0 CRC64;
     MVDEEAVKKI LRTVLQSRSS ISLSCLQAEY KELTGETIPH KQLGHTTVDA LLHSMPSLVQ
     LDRNRSGEVM CYAAVGNEKA NITKLVARQH AAKKTGRPQM VNCQLRVKPI SPLALNAKPR
     TSLRQPEYRS RQGRGSSRTV SMRETQPDGR GSKVHNTPPN MPSRRGSLPS DKYDRARHPE
     SPLQIQTFTF FRSDKRMTLP SRFQKEVHTH LSRNPQQSHT PSNLNESTPP SKPRTQISLY
     SPKLVQSRLK EVLSKHSNGF WVSKLPQLYR ELYKQELPSE ALKDLEQWTH ICTVEKPCSS
     KSQELLLYPA KDVSQSTNTY SLEMTHFPDM HFPSPPKPQK VSRKPKNNTS SQLASPKALP
     EDLKQNLAEL LLKYSSGLWA HALPKLYQDT YKTNLPEYVL DNLPLLSDIC TIDYPVPDNP
     KRAILYVKVL EDENCNQTDS AELKAREEAG RRLSSQSVPP LLIPREEYPS VLVVEASSTN
     SVVLRYIGEA YSKAQEKLED DMKEFYRQDN TRKPLISLSS GQLTAAIAEE EEEILRAQVC
     EVKSDKVKVY YVDHGFSDVI SKSKLLELHE KFFKLPFQAT KCKLAGLEAF AQEPAVLKKF
     DSMASGKILL AEILEREDIP LMVLYDTSQE DDININASCL KALQEKSFES PLQINSAYMN
     VSVTSVCSDG MFYCQLPSSG LTKLSEILEK TESYFRNQVT SESLVSRPFC GKGCLARYKG
     KWSRVEITNL HGSRVLDILF VDVGVQASVE VIELREIPHP FLRDLISIPP QAVKCCLTDL
     PVSVGCWTPD AVQWLKDTAI HCSDCSLKIV KVEESKRLAH VYLFTNKNFQ DLNHSLNRQL
     ANSDLWKHQD DVFLSSQGSL KSSTRTTSSN TPTTAPTTIP TPSTGTSSPR TNRACKAPHT
     PKRLAPHLGS SSILSGSLTL PPVLELPQMG QNMDIYVSVA CHPGHFVLQP WQDMYKLVVL
     MEEMILYYNK TDEKPLTVEK NQVYAAKVEN NWHRVLVKGV LSNGLVSVYE LDYGKHELVS
     CTVLRPLIQE FRQLPFQGIT AQLAGVKSRQ WSEEASIVFR NHVEKKAMVA QVESVQEAEQ
     PWDRKLTVYL VDTSQEDSDI WVHDLMAEFT DELTKAA
//
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