ID D2V1P1_NAEGR Unreviewed; 693 AA.
AC D2V1P1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=RING finger domain-containing protein {ECO:0000313|EMBL:EFC49196.1};
GN ORFNames=NAEGRDRAFT_56808 {ECO:0000313|EMBL:EFC49196.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC49196.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC49196.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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DR EMBL; GG738848; EFC49196.1; -; Genomic_DNA.
DR RefSeq; XP_002681940.1; XM_002681894.1.
DR AlphaFoldDB; D2V1P1; -.
DR STRING; 5762.D2V1P1; -.
DR EnsemblProtists; EFC49196; EFC49196; NAEGRDRAFT_56808.
DR GeneID; 8855198; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_56808; -.
DR eggNOG; KOG2164; Eukaryota.
DR InParanoid; D2V1P1; -.
DR OMA; QFHITEY; -.
DR OrthoDB; 125113at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16536; RING-HC_RNF10; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039739; MAG2/RNF10.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12983; RING FINGER 10 FAMILY MEMBER; 1.
DR PANTHER; PTHR12983:SF9; RING FINGER PROTEIN 10; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 255..297
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 556..590
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 68..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..184
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 80993 MW; EBCA6EC64C8CA6D5 CRC64;
MSQTSQAAAT DELNPHIQLD NQNKVVVEEE TCLDHHHDDV NIEESLESTI EHYHDEIEEN
EVVADNDDHH QQHSDLNQQK NKNRKNKPKK VFPASQFFIA NQSKSNEEAN LVETNDDHDE
EEYFHSEEPE LAYHYKGHSF IVNKTAYKPN SNSGNGSSSS NTNNKNNKSK KQHHHNHSHH
HKYNNYYQRP KTKEEFVLAN FHFVLRPLSQ SNTNFINQQF HITEYNNGKF DADTLVDWDT
IELVIQQTHD ENQECPICLD TFKAPKMTKC GHVFCYPCIL RHVALGETNY RKCPLCNESV
YIDALRSVRV EYRKKYKEND KMNLVLLKRD KKLIIPDLVS ELNTTKEGVQ SKDLPTIYPV
DGDSESAKFS RFNVTYDISQ ILEKELADLD NSLKTSESAA ESEFIVLAKD QVLQRKKDWL
EWTKTHLAKG KPTQPKNKSS QKPEVSQATE KKEVEDYWYY QSSDCQMIFL HPLCSKMLIH
EFQDYSNFPT NLNDCPILEI ETVELNEELR RRYPVLKHVP CGCYISLVEI DMRNIVSKET
INTFIKDIKH RKYRRDEKVR MRIREEQEEK KNEEKRKEEE RLARERLIQE LHISNFPELI
STPPPVNSDF HFPTTLKTVT PVQQQQQPEK KQKKPNDWSK RKQQIDITQS VASSSVQLQG
DWAKKTNTNT TTKNVSTSSG KKDDFPSIKS KKK
//
