ID A0A3Q7RPS8_VULVU Unreviewed; 1254 AA.
AC A0A3Q7RPS8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tudor domain-containing protein 1 {ECO:0000313|RefSeq:XP_025847797.1};
GN Name=TDRD1 {ECO:0000313|RefSeq:XP_025847797.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025847797.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025847797.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025847797.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025847797.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_025847797.1; XM_025992012.1.
DR AlphaFoldDB; A0A3Q7RPS8; -.
DR STRING; 9627.ENSVVUP00000013294; -.
DR KEGG; vvp:112914798; -.
DR OrthoDB; 4266629at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd20408; Tudor_TDRD1_rpt1; 1.
DR CDD; cd20409; Tudor_TDRD1_rpt2; 1.
DR CDD; cd20410; Tudor_TDRD1_rpt3; 1.
DR Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 2.40.50.90; -; 4.
DR Gene3D; 6.10.140.2220; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047376; Tudor_TDRD1_rpt1.
DR InterPro; IPR047377; Tudor_TDRD1_rpt2.
DR InterPro; IPR047378; Tudor_TDRD1_rpt3.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF00567; TUDOR; 4.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00333; TUDOR; 4.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 4.
DR PROSITE; PS50304; TUDOR; 4.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 243..279
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 387..447
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 616..675
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 837..896
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 1064..1122
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 105..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1254 AA; 139612 MW; 542BB04768CF04CC CRC64;
MALGSKGSGC SIVNVNIPTS GAEIGGAFGG EKHTGGGPES GSDAWKQYMR RSTCTINYNL
GTLAALSPPV VINTSVNVKL PHNMISRNNL EASTCKMTEP FNFEKNENQL PAPDSLRSPG
GHANHPNFRL KSPDNGNKNN FLLCEQTKQY LASQEDSSVS SNPNSINGEV VGSKGDRKMS
AGNSVSPLNV GNRSPPKEVN NKPSNNVPPA KSKKVHKLVE NSLSINNSAL FNSLGPPLRS
TTCHRCGLFG SLRCSQCKQT YYCSIACQRR DWSAHSIVCK PVQQNFHKYE ASKSPFETKN
MEVKNESDYP LGVTKEIAIC TDKIMFSDLR SLQLRKTMEI KGTVTEFKHP SDFHVQLYSS
EVLEYMNQLS RSFKETYANM TQKEDYIPVK GEVCVAKYTV DQTWNRVIIQ EIDMLQKKAQ
VLYIDYGNEE IIPINRIHQL NRNIGLFPPC AIKCFVASVI PAEGNWSNEC VKTIKSLLME
QYCSIKIVDI LKEEVVTFAV DVMLPSSGKL LDDVLIEMGY GLKPKAQNSK KQSADPNDLE
DVGKMTAENK IVVDRSDLIP KVLTLNVGDE FCGVVAHIQT PEDFFCQQLQ SGHKLAELQA
SLSEYCGQVS PRSDFYPTIG DICCARFSED DQWYRASVLA YASEQSVLVG YVDYGNFEIL
SLTRLCPITP KLLELPMQAI KCVLAGVKPS LGIWTPEAIC LMKKIVQNKI IMVRVADKLE
NSSLVELVDK SVTPHLSIAQ ALRDAGFAVG ETGTLAEKPS VMKEANDPLG VEEKLNPLEW
TWVELAVDQT VDVVVCMMYS PGEFYCHVLQ EDALKKLNDL NKSLAEYCQQ KVPSDFKAEI
GRPCCASFAG DGNWYRALVK EILADGNIKV HFVDYGNMEE VTADELQMIP SKFLKLPFQG
IRCWLVDIQP RNKHWTEEAI ARFQTCVAGI KLQARVVEIT GQGLGIELTD LSTSYPRIIN
DVLIDEYLVL RTSSPHKDLT NNRSVGKHNL QVDVGLQAIS LAEQWRTIEL PVNKTVQASI
LEIVSPHLFY ALPSEIPGDQ ERLNILTAEL LEYCNTQKSQ LSYRPKIGDV CCAKYTNDDF
WYRAIVLGTS DAEVKVLYAD YGNLETLPLS RVQPISISHL ELPFQIIKCS LEGLMELNGS
CSQLVMELLK NFMLNQSVML SVKGITKNVH TVSVEKFSGN VTVNLADKLV TYGLAKSITS
KKQSTLSTEK LIKMNCCCTE LQKQVEKHEQ ILLFLLNNPT NQNKFIEMKK LLKS
//
