ID D8QUJ8_SELML Unreviewed; 550 AA.
AC D8QUJ8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=RING-CH-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SELMODRAFT_404192 {ECO:0000313|EMBL:EFJ35886.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ35886.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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DR EMBL; GL377567; EFJ35886.1; -; Genomic_DNA.
DR RefSeq; XP_002962423.1; XM_002962377.1.
DR AlphaFoldDB; D8QUJ8; -.
DR STRING; 88036.D8QUJ8; -.
DR EnsemblPlants; EFJ35886; EFJ35886; SELMODRAFT_404192.
DR Gramene; EFJ35886; EFJ35886; SELMODRAFT_404192.
DR KEGG; smo:SELMODRAFT_404192; -.
DR eggNOG; KOG1609; Eukaryota.
DR HOGENOM; CLU_495590_0_0_1; -.
DR InParanoid; D8QUJ8; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006301; P:postreplication repair; IEA:InterPro.
DR GO; GO:0006513; P:protein monoubiquitination; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR039577; Rad18.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14134; E3 UBIQUITIN-PROTEIN LIGASE RAD18; 1.
DR PANTHER; PTHR14134:SF3; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF12906; RINGv; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 139..202
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 429..492
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 376..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..351
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 376..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 61613 MW; 64C350F0382F1C04 CRC64;
MVANILTKPL DKSTFQGLRK MLGMEPDKYP PILQHSTIGV LPKRLVIAIF HLSMVENHTL
QRSKPSFTIG NDPGTISNPG LLEFKLGDIP CLPGSIVSAV GRSYGDQDMA DSDAPWPLLR
HDAPAIACSL AAEIESNTCP ICFELMKSPT YSPILLYPCG HTFCAKVCTN RIINGDLLVP
RLGQCLEIHT VTNRKKTCPY CRQRIVSQAL NLSLQKLINN FVALQKNPAP AHQSFDHGAQ
SQYGEKLRQA ETRSRILQCA LANSVEAKAK LARDIADAQR KVVQLESREQ ETKVRLEKVN
LEYHRVLSEI RENQDNLATL QKYQDEETAK VNLIQETLKN LRKEYLLMED AVAPQAQASP
PLPPQVLVLI KEESLTASPH HENERRPKES AESSSPVVVI ITVQEQQPSC SYDSSKPQEI
ATAASSAQQQ QHHELVCRVC QLGSPEVRGE LMELACVCKD DLAVAHRRCA EAWFQIRGNR
RCEICGKIVT NITLKRGMWS RVTRIINPER KKLFTWNADD STLQVSGNRE KGERTNWDTQ
PSKNARDVIE
//
