ID M7BIA1_CHEMY Unreviewed; 692 AA.
AC M7BIA1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=E3 ubiquitin-protein ligase TRAF7 {ECO:0000313|EMBL:EMP36914.1};
GN ORFNames=UY3_05894 {ECO:0000313|EMBL:EMP36914.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36914.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB523472; EMP36914.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BIA1; -.
DR STRING; 8469.M7BIA1; -.
DR eggNOG; KOG0274; Eukaryota.
DR eggNOG; KOG0297; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16644; mRING-HC-C3HC3D_TRAF7; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR19848:SF8; E3 UBIQUITIN-PROTEIN LIGASE TRAF7; 1.
DR PANTHER; PTHR19848; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF00400; WD40; 4.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00184; RING; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 171..205
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 383..415
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 426..465
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 546..585
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 586..629
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 77365 MW; 7CEF3214DD61CE58 CRC64;
MESTEVSRHA SEHQDLLTKV SSQDQDPGLL ADATVTNQDS SPTLKSLVIV YYRAKTIRAL
LLQPRSQEPL LVKGAAKNLK CFFCFKADGT NTFKQHRRTP SSSSTLTYSP RDEDDGMPPI
STPRRSDSAI SVRSLHSESN MSLRSTFSLH EEEEEPEPLV FAEQPSVKLC CQLCCSVFKD
PVITTCGHTF CRRCALTSEK CPVDNAKLTV VVNNIAVAEQ IGELFIHCKY GASSKPAAFE
VDPHGCPFTI KLSARKCTFI GNQDTYETHL EMCKFEGLKE FLQQTDDRFH EMQVAMAQKD
QEIAFLRSML GKLSEKIDQL EKNLELKFDV LDENQSKLSE DLMEFRRDAS MLNDELSHIN
ARLNMGILGS YDPQQIFKCK GTFVGHQGPV WCLCVYSIGD LLFSGSSDKT IKVWDTCTTY
KCQKTLEGHD GIVLALCIQG NKLYSGSADC TIIVWDIQTL QKVNTIRAHD NPVCTLVSSH
NMLFSGSLKA IKVWDIVGTE LKLKKELTGL NHWVRALVAS QNYLYSGSYQ TIKIWDIRNL
ECVHVLQTSG GSVYSIAVTN HHIVCGTYEN LIHVWDIESK EQVRTLTGHV GTVYALAVIS
TPDQTKVFSA SYDRSLRVWS MDNMICTQTL LRHQGSVTAL AVSRGRLFSG AVDSTVKEQT
SSKHHEPFNI QNSQNNIGGT EAQKSREKHQ DA
//
