ID Q2TAE0_XENLA Unreviewed; 622 AA.
AC Q2TAE0;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:AAI10974.1};
DE Flags: Fragment;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAI10974.1};
RN [1] {ECO:0000313|EMBL:AAI10974.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAI10974.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; BC110973; AAI10974.1; -; mRNA.
DR AlphaFoldDB; Q2TAE0; -.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd19800; Bbox2_xNF7-like; 1.
DR CDD; cd13733; SPRY_PRY_C-I_1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF286; E3 UBIQUITIN-PROTEIN LIGASE TRIM69; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 158..198
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 232..273
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 428..622
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 353..380
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 103..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAI10974.1"
SQ SEQUENCE 622 AA; 69615 MW; 030DD2513E2E4982 CRC64;
ADSNQEDSAA GDEEEGPGSG QNKAEENEVV TVGSTYPCKK ADGSLHDAEV VKTRMNKQLG
KEEYYVHYIG LNRRQNEWVD KTRLVLTKAE VKEEAKDEAS GNNQEMADAT EQANGNTPQG
QKRKLEEQEP ETKKTKVEAA PNSSLVGPAG DFAEELTCHL CVELFKDPVM VECGHNFCKA
CIEKAWAGQD SFSCPECKEV INDKKYTINR ALANLVKKTA TAPVIPAEKK EKPLENCPEH
DERLKLYCKD DGTLGCIICR DSLKHVSHNF LPILDAVAVY REQLAAIVAP LEASLKVSEQ
VVSQQNEKIV QHKNNICEYK DHIVAEFERM HEFLEEREKV LLAQLQEQGD GLLKEMEQNM
VKMQENIDGI KKTIAVAKDR VDENDSISFL TDIKAFIDKC LEQQREVVSS SGNTLLSKEL
CQGTFKGPIQ YILWKEIKKA IVPYLSPMLL DPSTAHPNLI LSDGLTSVKY GDNKLSVPDN
PKRFSQCILV LGSVGFDSGR HYWEVDVGDK TAWDVGMASE SSNRKGKIKL NPKNGYWAIW
LRNGNAYKAL ESPSKTLVLA SKPHKIGVYV DYEGGMISFY NADDMTPIYT FNATFTEKLY
PYLSPFLHDS GRNAEPLRLV HN
//
