ID A0A151N5B1_ALLMI Unreviewed; 661 AA.
AC A0A151N5B1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=RNA-binding protein EWS isoform B {ECO:0000313|EMBL:KYO31789.1};
GN Name=EWSR1 {ECO:0000313|EMBL:KYO31789.1};
GN ORFNames=Y1Q_0022857 {ECO:0000313|EMBL:KYO31789.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO31789.1};
RN [1] {ECO:0000313|EMBL:KYO31789.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO31789.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:KYO31789.1}.
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DR EMBL; AKHW03004053; KYO31789.1; -; Genomic_DNA.
DR RefSeq; XP_014449104.1; XM_014593618.2.
DR AlphaFoldDB; A0A151N5B1; -.
DR GeneID; 102561474; -.
DR CTD; 2130; -.
DR OrthoDB; 162112at2759; -.
DR Proteomes; UP000050525; 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; cd12533; RRM_EWS; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 1.
DR InterPro; IPR034869; EWS_RRM.
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:SF3; RNA-BINDING PROTEIN EWS; 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:UP000050525};
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 360..446
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 516..547
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT REGION 122..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 68898 MW; BDC2740B53D45E96 CRC64;
MASTDYSTYS QAAAQQGYSA YAAQPAQGYA QTTQTYGQQS YGTYGQPTDV NYTQAQTTAT
YGQTAYATSY GQPPTGYTTP TAPPAYSQPV QGYGTAAYDA TTATVTTTQA SYAAQSPYGT
QPAYPAYGQQ PATSAPARPQ DGSKPVETSQ PQSSTAGYSQ PSLGYGQSNY SYPQVPGSYP
MQPVTAPPSY PPTSYSSTQP SSYDQSTYSQ QSSYGQPSTY GQQTSYGQQS SYGQQPPTSY
PPPTGSYSQA PSQYSQPSSS YGQQSSFRQD HPSSMNVYGQ ESGGYSGPGE NRNMSGPDNR
GRGRGGFDRG GMSRGGRGGG RGGMGAGERG GFNKPGGPME EGPDLDLGPS VDPDEDSDNS
SVYVQGLNDN VTLEELADFF KQCGVVKMNK RTGQPMINLY IDKETGKPKG DATVSYDDPS
TAKAAIEWFD GKDFQGNKLK VTLTRKKPPM NSMRGGMPQR EQRGMPPPLR GGPGGPGGPS
GPMGRMGGRG GDRGGFSSRG PRGSRGNSSG GNVQHRAGDW QCPNPGCGNQ NFAWRTECNQ
CKAPKPEGFL PPPFPPPGGD RGRGGPGGMR GGRGGLMDRG GPGGMFRGGR GGDRGGFRGG
RGMDRGGFGG GGGGGGRRGG PGGPPGPLME QMGGGGRGGR RGGPGKMDKG EHRQERRDRP
Y
//
