ID X6N0P3_RETFI Unreviewed; 779 AA.
AC X6N0P3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
DE Flags: Fragment;
GN ORFNames=RFI_17767 {ECO:0000313|EMBL:ETO19463.1};
OS Reticulomyxa filosa.
OC Eukaryota; Sar; Rhizaria; Retaria; Foraminifera; Monothalamids;
OC Reticulomyxidae; Reticulomyxa.
OX NCBI_TaxID=46433 {ECO:0000313|EMBL:ETO19463.1, ECO:0000313|Proteomes:UP000023152};
RN [1] {ECO:0000313|EMBL:ETO19463.1, ECO:0000313|Proteomes:UP000023152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24332546;
RA Glockner G., Hulsmann N., Schleicher M., Noegel A.A., Eichinger L.,
RA Gallinger C., Pawlowski J., Sierra R., Euteneuer U., Pillet L.,
RA Moustafa A., Platzer M., Groth M., Szafranski K., Schliwa M.;
RT "The Genome of the Foraminiferan Reticulomyxa filosa.";
RL Curr. Biol. 0:0-0(2013).
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:ETO19463.1}.
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DR EMBL; ASPP01013643; ETO19463.1; -; Genomic_DNA.
DR AlphaFoldDB; X6N0P3; -.
DR EnsemblProtists; ETO19463; ETO19463; RFI_17767.
DR OrthoDB; 1132597at2759; -.
DR Proteomes; UP000023152; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR36812:SF9; KED-LIKE PROTEIN; 1.
DR PANTHER; PTHR36812; NEUROFILAMENT TRIPLET M PROTEIN-LIKE PROTEIN; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000023152};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 377..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..373
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETO19463.1"
SQ SEQUENCE 779 AA; 88530 MW; D9C642FBE77C2ECE CRC64;
NNNNNNNNNN NNDNIPDIGY YAAPNQERRN DGYKDRYNPK YDATGYDWDE KSGNLIPLQD
LSSRGRATKD NREEKKEDGE DEKKAMESKT TTTTAAAAAG RGSMNVVRPI PPSMNLMDEI
TSSNDFSFEC MDCHSFDRNT NMFRWSVCRH EYSKECAIGV CVQHLTIQSL PFCVVPGCQQ
LLLDNEALIL LPSSFYNIYV NVCTNLGVTS SSSLINHDTF ATMTSSSIVN VNAQHLNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNSHC DDEKIEESKH ADGSTAPKNR PLSTLGSMSS
SLSKQQQQRQ QRDKPTSHCC SLCSKVLTTA AGNVKVVQLT ACGHEFCQPC LQRAIIDQME
LLNIFPPNCP TCRMELFFFY ACTNYLFCCF CFCFFFFLIG NNNNENKRLE SQDTDILIPE
FIKQEEEMQQ DRAAVDPLAG LPITPSDGDN LSYADSKSAG LNGHWKGPPP TSHGRRDKPP
PPKDEGIMSS SAIGADDEKK EEAESSWFSN RKDKEIATRC LTQECGEKVD NSQTLKFACR
RCRAVWCLAC KVEWHHGLTC EEYEHQLIHL SQRDMALAEI EKNSGLGYHA LTGHYYFSCY
HSVTSFFFFP LLIVWHTARV YIYVYMHICV YITCMYPRTH LFNKLNVLYA AWCAAAEGLS
YNETRQLLML QESGLLETKE DSYEPDNKFN HGHNNNGHTL NIMDEHMQLQ HLNELVETMT
ADDEKKSPDF SQQPEMTRCK RCNNVIEKRM QWDCPSCNQQ LLNQVQQGSI DHEEKISEA
//
