ID A0A151NUX6_ALLMI Unreviewed; 1090 AA.
AC A0A151NUX6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Tudor domain-containing protein 1 {ECO:0000313|EMBL:KYO40543.1};
GN Name=TDRD1 {ECO:0000313|EMBL:KYO40543.1};
GN ORFNames=Y1Q_0009568 {ECO:0000313|EMBL:KYO40543.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO40543.1};
RN [1] {ECO:0000313|EMBL:KYO40543.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO40543.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO40543.1}.
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DR EMBL; AKHW03001922; KYO40543.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151NUX6; -.
DR STRING; 8496.A0A151NUX6; -.
DR eggNOG; KOG2039; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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 Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 2.40.50.90; -; 4.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 81..117
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT DOMAIN 225..285
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 458..517
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 675..734
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT DOMAIN 895..953
FT /note="Tudor"
FT /evidence="ECO:0000259|PROSITE:PS50304"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1090 AA; 121963 MW; 9925E44989FB3481 CRC64;
MVNSFKQKEI GSEISDRMQT GNSVGTTSSK NSLVPSAGKT VSSDFHRAKQ KLHNSPENIL
SVNCDLKSHY PLVRFPRITT CHHCGLSGSL RCSQCKQTYY CSVDCQKKDW SSHVVVCKPV
KKNFKKNEEN AKPPGEIKKK VDFKGNLSPV DVVRTEDNIK KIMFSDLQDL ALKKAMEIQG
TVTEFRNPSE LYIQVYSPEV LEHIRTLTVK LKDCYANTVN EEEYVPVRGE VCVAKYFLDQ
TWNRVLVKEV DIVQKKALVL YIDYGNEENA SLLRIKQLHR DIDLFPPCAI KCSVANVPKE
GSWNKDFTSI ITPFMGERCS VAIADVLQEE MMTCFAVDVV IPSSGKRLGN ILLEMRSDLS
PKRSNNEQMH SEKSTLLKTD SEGNEGIMAE NKRLDHNNHL TIKAITLSVG DRFSGIVSHI
QNPEDFFCQQ LHNGRELAEL QATLCEYCNK IPSTSDFRPA VGDVCCAKFT EDNQWYRASI
ITYISEDTAL VGYIDYGNFE TLQITRLRPV VPKLLELPMQ AIKCTLAGLK PQLGTWPSEA
ISLMKQLVHN KVTTVRVMGK TDYSSVVEFT DESFTPINVS KHLIEAGYAM KESKALITAH
ETSNIGKEGN GDTVRKGNWT WVKLALKQTI NVIVCMLYSP GEFYCHILND DLNALNVLNK
SLAEYCQQAS APSFKPVRGE PCCAFFSGDG KWYRALVKDI SSDGAVKVQF VDYGNVEEVT
PDKLRQISFE FLKLPFQGIK CWLSGVKPVN KQWLPETIAQ FQMYTAGIKL QASIISLTKN
GAGLELIDNS TGCPRMISEM LICEQLTLKE VKTNKEVLLT KSADKKEWQE TSSSEQWKTI
KLPINKAISV RIVEVINPDL FYAMPSETKV DQDKLCTLMI ELAEYCSSCS SQSFKPKVGE
ACCAKFSGDG HWYRAVALQV SPSDVKVVYG DYGNTETLRF SKVMPITACH LKLPFQIIKC
SLAGIVQFDG DWSALVTDLP KTLASGKSVT VMVKGITENI HVVSVVKSFE NGNLNVADKL
VMESSAKPSA TGNPSILPQE HASETKCCCT ELRKQIEKHE QILLFLLNKC VDQDGLSEME
KMLERKVCLT
//
