ID A0A2K5MIV9_CERAT Unreviewed; 1114 AA.
AC A0A2K5MIV9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tudor domain containing 1 {ECO:0000313|Ensembl:ENSCATP00000025146.1};
GN Name=TDRD1 {ECO:0000313|Ensembl:ENSCATP00000025146.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000025146.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000025146.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5MIV9; -.
DR Ensembl; ENSCATT00000049376.1; ENSCATP00000025146.1; ENSCATG00000035999.1.
DR GeneTree; ENSGT00940000158754; -.
DR OMA; EYCSAQK; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000035999; Expressed in heart and 1 other cell type or tissue.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20408; Tudor_TDRD1_rpt1; 1.
DR CDD; cd20409; Tudor_TDRD1_rpt2; 1.
DR CDD; cd20410; Tudor_TDRD1_rpt3; 1.
DR CDD; cd20411; Tudor_TDRD1_rpt4; 1.
DR Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 2.40.50.90; -; 3.
DR Gene3D; 6.10.140.2220; -; 1.
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 PANTHER; PTHR22948:SF29; TUDOR DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00567; TUDOR; 4.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00333; TUDOR; 4.
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 Differentiation {ECO:0000256|ARBA:ARBA00022871};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 170..206
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 313..373
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 542..601
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 763..822
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 991..1049
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 125019 MW; 41C43B05B8833609 CRC64;
MNVKSPFSMM SRNNLEVPPS KMTEPFNFEK NENKLPPHES LRSPGTLPNH PNFRLKSSEN
GNKKNNFLLC EQTKQYLASQ EDSSVSSKPN GINGEVAGSK GDRKKLPAGN SVPSPSVESN
SPPKEVNTKP GNNVRPAKSK KLNKLVENSL SINNPGLFTS LGPPLRSTTC HRCGLFGSLR
CSQCKQTYYC STACQRRDWS AHSIVCKPVQ PNFHKLEDNK SSIETKDVEV NNKSDCPLGV
TKEIAIWAER IMFSDLRSLQ LKKTMEIKGT VTEFKHPGDF YVQLYSSEVL EYMNQLSASL
KETYANMHEK DYIPVKGEVC IAKYTVDQTW NRVIIQNVDV QQKKAHVLYV DYGNEEIIPL
NRIYHLNRNI DLFPPCAIKC FVANVIPAEG NWSDDCIKAT KPLLMEQYCS IKIVDILEEE
VVTFAVEVEL PNSGKLLDHV LIEMGYGLKP NGQDSKKENA DQSDPEDVGK MTTENKIVVD
KSDLIPKVLT LNVGDKFCGV VAHIQTPEDF FCQQLQSGRK LAELQASLSK YCGQLPPRSD
FYPAIGDICC AQFSEDDQWY RASVLAYASE ESVLVGYVDY GNFEILSLMR LCPIIPKLLE
LPMQAIKCVL AGVKPSLGIW TPEAICLMKK LVQNKIITVK VVDKLENSSL VELIDKSETP
HVSVSRVLID AGFAVGEQRM VTDKPSDVKE DSVPLGVEGK VDPLEWTWVE LAVDQTVDVV
VCVIYSPGEF YCHVLKEDDL KKLNDLNKSL AEHCQQKLPN GFKAEIGQPC CAFFAGDGNW
YRALVKEILP NGNVKVHFVD YGNIEEVTAD ELRMISSTFL NLPFQGIRCR LADIQSRNKH
WSKEAITRFQ MCVAGVKLQA RVVEVTENGT GVELTDLSTR YPRIISDVLI DELLVLKSAS
PHKDLPDDRL VNKHELQVHI QGLQATASAE QWKTIELPVN KTVQANVLEI ISPNLFYALP
NGMPENQEKL CILTAELLEY CNAPKSRPPY RPRIGDACCA KYTSDDFWYR AVVLGTSDTD
VEVLYADYGN IETVPLCRVQ PITSSHLALP FQIIRCSLEE KMYRMKCCCT ELQKQVEKHE
HILLFLLNNS TNQNKFIEMK KLLKKTASLG GKPL
//
