ID A0A0C2MK68_THEKT Unreviewed; 647 AA.
AC A0A0C2MK68;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=E3 ubiquitin-protein ligase TRIM71 {ECO:0000313|EMBL:KII64780.1};
GN ORFNames=RF11_14505 {ECO:0000313|EMBL:KII64780.1};
OS Thelohanellus kitauei (Myxosporean).
OC Eukaryota; Metazoa; Cnidaria; Myxozoa; Myxosporea; Bivalvulida;
OC Platysporina; Myxobolidae; Thelohanellus.
OX NCBI_TaxID=669202 {ECO:0000313|EMBL:KII64780.1, ECO:0000313|Proteomes:UP000031668};
RN [1] {ECO:0000313|EMBL:KII64780.1, ECO:0000313|Proteomes:UP000031668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuqing {ECO:0000313|EMBL:KII64780.1};
RX PubMed=25381665; DOI=10.1093/gbe/evu247;
RA Yang Y., Xiong J., Zhou Z., Huo F., Miao W., Ran C., Liu Y., Zhang J.,
RA Feng J., Wang M., Wang M., Wang L., Yao B.;
RT "The genome of the myxosporean Thelohanellus kitauei shows adaptations to
RT nutrient acquisition within its fish host.";
RL Genome Biol. Evol. 6:3182-3198(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC {ECO:0000256|ARBA:ARBA00008518}.
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:KII64780.1}.
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DR EMBL; JWZT01004098; KII64780.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2MK68; -.
DR EnsemblMetazoa; KII64780; KII64780; RF11_14505.
DR OMA; LHQRKNT; -.
DR Proteomes; UP000031668; Unassembled WGS sequence.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR CDD; cd05819; NHL; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR047153; TRIM45/56/19.
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; PTHR25462; BONUS, ISOFORM C-RELATED; 1.
DR PANTHER; PTHR25462:SF266; TRANSCRIPTION INTERMEDIARY FACTOR 1-BETA; 1.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF01436; NHL; 2.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF15227; zf-C3HC4_4; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR PROSITE; PS51125; NHL; 2.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031668};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 15..60
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 111..158
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT REPEAT 316..416
FT /note="Filamin"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00087"
FT REPEAT 428..471
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
FT REPEAT 479..519
FT /note="NHL"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00504"
SQ SEQUENCE 647 AA; 74502 MW; 7F173ED168595900 CRC64;
MDKSLKEAFI EEFYCPICLD YFSDPVMLRC HHTFCSKCIG IFFKFSKKLT QWKLHCPLCR
SQCLVNCSPN DHPVKFLPNN YIVSSVVSKI KQIESQKIDN NDLEDLDHEE EKKPFCRLHQ
KNMIKYFCKN CQILVCRVCT IMNHREHELL FPHKVLVTHQ REISEQFDTL QSNHKKMDIA
LNTIQMTIGE IKSRYHEIVD QITKLIDARV VILNEQKQKL IKDLDSIVHY KLKKLAVQND
LIELEFGKSK IILNNAVNVL TEGEAIEKLQ LKSSLNQHIE SFNKLPVEPE EDDTIIFELP
ERATEMMIES LGIVEAKSTF AEISYASGEC LEETKVDNEA RFKVVARSNT GQLMKREGLL
NITIEGPNNT IVPSKITDKD TGEYEVTFRP MIKGKHKINI YLRGRPIQKS PFICNVVSYR
DYRDAQAKQV FGVYGTSNKE FKSPIGIVCD REGYLYISDC YNHRVQVFGP KGDNIYNHGS
PDCRKGYLSN PSGLAYCQQT NRIFICDTGN SRVQMLDLNN KPNEWFSQNT WCQTFVGSES
QISGPVKMPY GVAVSAQNQE IAITDTSINS VLIYSKEGKY ITSIGDKSGS NRVRKEHTQL
NCPCYVFYDP ENNLLHISDT KNNRVLIYDR RARSTRINFS ESKRNCF
//
