ID D8SXV1_SELML Unreviewed; 975 AA.
AC D8SXV1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=RanBP2-type domain-containing protein {ECO:0000259|PROSITE:PS50199};
GN ORFNames=SELMODRAFT_447225 {ECO:0000313|EMBL:EFJ10684.1};
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:EFJ10684.1, 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; GL377652; EFJ10684.1; -; Genomic_DNA.
DR RefSeq; XP_002988265.1; XM_002988219.1.
DR AlphaFoldDB; D8SXV1; -.
DR STRING; 88036.D8SXV1; -.
DR EnsemblPlants; EFJ10684; EFJ10684; SELMODRAFT_447225.
DR GeneID; 9662657; -.
DR Gramene; EFJ10684; EFJ10684; SELMODRAFT_447225.
DR KEGG; smo:SELMODRAFT_447225; -.
DR eggNOG; KOG4198; Eukaryota.
DR HOGENOM; CLU_304714_0_0_1; -.
DR InParanoid; D8SXV1; -.
DR OMA; RFTESQS; -.
DR OrthoDB; 228305at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 2.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23111:SF40; RNA-BINDING PROTEIN INVOLVED IN HETEROCHROMATIN ASSEMBLY-RELATED; 1.
DR PANTHER; PTHR23111; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00641; zf-RanBP; 2.
DR SMART; SM00547; ZnF_RBZ; 2.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 2.
DR PROSITE; PS01358; ZF_RANBP2_1; 2.
DR PROSITE; PS50199; ZF_RANBP2_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 395..424
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 428..457
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 87..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 56..83
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 115..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..860
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 105363 MW; 4740B7927B9857A5 CRC64;
MPALFGASRF LPTALGILST RCYTPGKSAA VSTEEEDAED GLMSLKERVK GKDGEIEALN
KSLKGEEEKT KSLKLENMKM AREMDKINSS TGRGASAGQR GKLSAKAAAA AMESDDESDF
SELDDSEIED ALGASTESEV EEDVASDSEL EKEFKKLESG SDSDFDVRAE NGKEVSDLSD
SEIEDVLASK QRVVGHRQTL DSSIGGEVMD AWRKFVALLK QKNYFKLNAE ELVKGEAAYE
SFSNIAEAFK RFSTERDDIL KMLPMGDLKV LASHPCPTTL RKAVNSGKRL RGFCNVEEAE
VCKSCSKKDD CSRAYLPPDS TASTSDALQY LFQFVVCTSE GSDFPEKTKT AVKNILRQLT
SLGAVSRDPT LPRDRQEVIA KPKTSRPQNE NYEMKPGDWK CVECDYINFC RNRHCRECHT
PRPPQDLRPG DWECPECRFV NFARNEECHD CKAERPDTVK VFHTIKGTKE KWEGSPEDFA
RQHTHLERKA KQAQGKYSDG LSDSDDDFKV APKRTTSLQN RRMASESESD LDEDSDDKDF
DVGSRKNLGK KQSKNDAWND DSDDDDDFTS SKRGGGQMRG RGRGAGFASR ASSLREDDGG
GRGRSFTSGR GRGGRASFAK DSEDDLDDSL DDSDDDDMPR RGARGGRGGS FTTRGGRGAR
GRGGGRFDSE DDSMDDLSDD DDDFGSSRGG RGRGARGRGR GGLRSRLDDD LDDDSDDVSE
DDRFSRGGRG GRGGARGALG RGSRFGHKKF DASDDASDLD SDDFLSEDDE PRFGRGRGRG
RGGGGRGRYG NGDDFSDESD DDGGGGGRFG GRGRGGGRFG SRGGGYGGRG GGYGDRDDFR
GGRGGYGDRD DFRGGRGGYG DRDGGFRGGR GGYGDRDGGG FRGGRGGFGD RDDFRGGRGG
RGGYGDRDDF RSGGGFRGGR GGRGGFGDRD DFRGGGGFRD RDDFGGGRGG GGGFRGGGRG
GFRGRGGSGF RGQDY
//
