ID W5N815_LEPOC Unreviewed; 949 AA.
AC W5N815;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=U2 snRNP-associated SURP motif-containing protein-like {ECO:0000313|Ensembl:ENSLOCP00000016774.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016774.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016774.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01007434; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01007436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7918.ENSLOCP00000016774; -.
DR Ensembl; ENSLOCT00000016804.1; ENSLOCP00000016774.1; ENSLOCG00000013596.1.
DR eggNOG; KOG0151; Eukaryota.
DR GeneTree; ENSGT00390000010687; -.
DR InParanoid; W5N815; -.
DR OMA; VTTNLYI; -.
DR Proteomes; UP000018468; Linkage group LG7.
DR Bgee; ENSLOCG00000013596; Expressed in larva and 13 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd21370; cwf21_SR140; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 6.10.140.420; -; 1.
DR Gene3D; 1.10.10.790; Surp module; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR013170; mRNA_splic_Cwf21_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR047488; SR140_cwf21.
DR InterPro; IPR000061; Surp.
DR InterPro; IPR035967; SWAP/Surp_sf.
DR PANTHER; PTHR23140; RNA PROCESSING PROTEIN LD23810P; 1.
DR PANTHER; PTHR23140:SF5; U2-ASSOCIATED SR140 PROTEIN-LIKE; 1.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF08312; cwf21; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF01805; Surp; 1.
DR SMART; SM01115; cwf21; 1.
DR SMART; SM00582; RPR; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00648; SWAP; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF109905; Surp module (SWAP domain); 1.
DR PROSITE; PS51391; CID; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50128; SURP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00176}.
FT DOMAIN 189..266
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 341..384
FT /note="SURP motif"
FT /evidence="ECO:0000259|PROSITE:PS50128"
FT DOMAIN 447..592
FT /note="CID"
FT /evidence="ECO:0000259|PROSITE:PS51391"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 106..133
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 707..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..949
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 108914 MW; 8AEC5732B3D61DF9 CRC64;
MTDRKVKTLG AKRPLSKKEQ EELKKKEEEK AAEVFEEFLA SFDSNDKSGV KTFVRGGIVN
ATKVEKSSEL ESNLVVCVTI HFNMEQRANK VTKVISDSQG FKKKAEEKKK SNLELFKEEL
KQIQEEREER YKRKKLTNEP GGYGDIDTLQ SRRSCKNTFA LCDNFVTCQP XAPLNPEVFD
DDTGAPQTTN LYIGCINPKM NEEMLCKEFG KYGPLASVKI MWPRTDEERT RVTNRGFVAF
MNRKDAERAL QALDGKSHVA LPRANDPNAL SVLKMTTPPP PSGLPFNAQP RERFRNQDFS
KPFNRSKEEF EKVMFPDYSN ETLSEAVVKV VIPTERNLLG LIHRMIEFVV REGPMFEAII
MNREKSNPEF RFLFENKSQE HVYYRWKLYS ILQGDPPNEW RTADFRMFRG GSLWRPPLLK
PYLHGDEDER EEPSSPSQEE EIKKGQLKAE HRDRLENTLR GLVARKEDIG NAMVFCLERA
EAAEEVVGCI AESLSILQTP LQKKIARLYL VSDILYNSCA KVANASYYRK YFEAKLPQIF
GDIGEAYRNI QARLQAEQFK QKIMSCFRAW EDWAIYPESY LIHLQNIFLG LVKPGEEVLD
RSEAQSPDLD GAPLEDVDGV PLENVDGSPM PNLPWDPASL DGTPVDDIDG VPLAPSVDDI
DGMPLQESSV SEKEKKLPHA RLTLSKWELV EDTEVIPQVN TESKWDNLED QNSDEDAIVG
QDTKEAAEDS EEDSSDMDSS SPSKYDAADL KTSLSSFDIS EGKRAKLREL ELKVMKFQDE
LESGHRPKKS GMTVQQQVEH YRNKLIQKEC EKDEQERREK GMQKTKERNK KEEKKDKAEE
RTKSKDKDKK RSKEMVQDRE KNRGRSEDEE KNRDRTDRYR GGSYSSPSKH PLLLGVTHSS
FSFSSFPRAK SKSPKKSKRS RSPSPSRRSW RSSSRSPHRS HKKSKKSKH
//
