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Database: UniProt
Entry: A0A401PQ00_SCYTO
LinkDB: A0A401PQ00_SCYTO
Original site: A0A401PQ00_SCYTO 
ID   A0A401PQ00_SCYTO        Unreviewed;       529 AA.
AC   A0A401PQ00;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=RanBP2-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=scyTo_0020333 {ECO:0000313|EMBL:GCB75191.1};
OS   Scyliorhinus torazame (Cloudy catshark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC   Scyliorhinus.
OX   NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB75191.1, ECO:0000313|Proteomes:UP000288216};
RN   [1] {ECO:0000313|EMBL:GCB75191.1, ECO:0000313|Proteomes:UP000288216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RRM TET family.
CC       {ECO:0000256|ARBA:ARBA00008448}.
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:GCB75191.1}.
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DR   EMBL; BFAA01016284; GCB75191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401PQ00; -.
DR   STRING; 75743.A0A401PQ00; -.
DR   OMA; NYHGNYG; -.
DR   Proteomes; UP000288216; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd12535; RRM_FUS_TAF15; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR034870; TET_fam.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR23238; RNA BINDING PROTEIN; 1.
DR   PANTHER; PTHR23238:SF5; RNA-BINDING PROTEIN FUS; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00176}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          268..354
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          423..454
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   REGION          1..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   529 AA;  53263 MW;  78151842AAB5E898 CRC64;
     MASNAADLGN YGQSAPQSYG AYNAQPSQGG YTQPPPQGYS HQSYSGYGQS TDTSAYSQSG
     SYGASYNQAQ AAGYGSQPPA QGYSHSNQGG YGSAGYGSAQ ASQGSYGQQS SYPGYGQQTA
     ATTSPSSYGG ANSQSTTYGQ PQGSGYGHQQ SSYGQQQQQS SYGQQPSSYG QQQGSYGQQP
     GGYQAQQGGY GQQGQYSGSG GGDNRGRGRG GYSRGGGFDR GGGRGGRGGR GGGMGGGERG
     GFTKFGGPRD QGPGAPNPGS DQDNSDNNTI FVQGLGDSVT VETVAEYFKQ IGVIKLNKRT
     GQPMINLYTD RETGKLKGEA TVSFDDPPSA KAAIDWFDGK EFSGNMIKVS FATRRTEFNR
     GGLRGGGRGV GGGRGAPMGR GGFGGGGGGG GGGGAGGGGP RGGFSGSGGG GGGGGGSGGG
     QQRAGDWKCT NPTCGNINFS WRNECNQCKS PKPEGAGGPP PMGGFGGDRG GGGERGNRGG
     FERGGGYRGR GGDRGGFRGR GGDRGGYGMG AGKMDSRSDH RQDRRERPY
//
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